PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
20006435-1	2010	A brief review is conducted on the application of vegetable oils in the treatment of PAH-contaminated soils.	Plant Oils	50-64	phenylalanine hydroxylase	Homo sapiens	85-88
20346485-11	2010	The anthracene/phenanthrene and benzo[a]anthracene/chrysene ratios in the winter were significantly lower than those in the summer, which indicate that there might be long-range transported PAH input to Guangzhou in the winter.	anthracene	4-14	phenylalanine hydroxylase	Homo sapiens	190-193
20346485-11	2010	The anthracene/phenanthrene and benzo[a]anthracene/chrysene ratios in the winter were significantly lower than those in the summer, which indicate that there might be long-range transported PAH input to Guangzhou in the winter.	phenanthrene	15-27	phenylalanine hydroxylase	Homo sapiens	190-193
20346485-11	2010	The anthracene/phenanthrene and benzo[a]anthracene/chrysene ratios in the winter were significantly lower than those in the summer, which indicate that there might be long-range transported PAH input to Guangzhou in the winter.	anthracene	40-50	phenylalanine hydroxylase	Homo sapiens	190-193
20346485-11	2010	The anthracene/phenanthrene and benzo[a]anthracene/chrysene ratios in the winter were significantly lower than those in the summer, which indicate that there might be long-range transported PAH input to Guangzhou in the winter.	chrysene	51-59	phenylalanine hydroxylase	Homo sapiens	190-193
20078130-1	2010	In this article, we discuss in situ polymer gelation in microfluidic channels from electrostatically mediated interactions when reactant streams of a linear cationic polymer (poly(allylamine hydrochloride, PAH) and a multivalent anion (sodium citrate) are subjected to shear flow.	Polymers	36-43	phenylalanine hydroxylase	Homo sapiens	206-209
20078130-1	2010	In this article, we discuss in situ polymer gelation in microfluidic channels from electrostatically mediated interactions when reactant streams of a linear cationic polymer (poly(allylamine hydrochloride, PAH) and a multivalent anion (sodium citrate) are subjected to shear flow.	Polymers	166-173	phenylalanine hydroxylase	Homo sapiens	206-209
20078130-7	2010	The gelation of PAH begins with the formation of colloidal aggregates of PAH and citrate, which then combine under shear flow to form noncontinuous or continuous gels.	Citric Acid	81-88	phenylalanine hydroxylase	Homo sapiens	16-19
19913839-1	2010	Conflicting results have been reported concerning the efficacy of tetrahydrobiopterin (BH4), the cofactor of phenylalanine hydroxylase, for reducing phenylalanine (Phe) concentration in phenylketonuria (PKU).	sapropterin	66-85	phenylalanine hydroxylase	Homo sapiens	109-134
19913839-1	2010	Conflicting results have been reported concerning the efficacy of tetrahydrobiopterin (BH4), the cofactor of phenylalanine hydroxylase, for reducing phenylalanine (Phe) concentration in phenylketonuria (PKU).	sapropterin	87-90	phenylalanine hydroxylase	Homo sapiens	109-134
19913839-1	2010	Conflicting results have been reported concerning the efficacy of tetrahydrobiopterin (BH4), the cofactor of phenylalanine hydroxylase, for reducing phenylalanine (Phe) concentration in phenylketonuria (PKU).	Phenylalanine	164-167	phenylalanine hydroxylase	Homo sapiens	109-134
20230191-0	2010	Post-translational activation of human phenylalanine 4-monooxygenase from an endobiotic to a xenobiotic enzyme by reactive oxygen and reactive nitrogen species.	reactive oxygen and reactive nitrogen species	114-159	phenylalanine hydroxylase	Homo sapiens	39-68
20230191-1	2010	An investigation into the post-translational activation of cDNA-expressed human phenylalanine 4-monooxygenase and human hepatic cytosolic fraction phenylalanine 4-monooxygenase activity with respect to both endobiotic metabolism and xenobiotic metabolism revealed that the reactive oxygen species (hydrogen peroxide and hydroxyl radical) and reactive nitrogen species (nitric oxide and peroxynitrite) could elicit the post-translational activation of the enzyme with respect to both of these biotransformation reactions.	Reactive Oxygen Species	273-296	phenylalanine hydroxylase	Homo sapiens	80-109
20230191-1	2010	An investigation into the post-translational activation of cDNA-expressed human phenylalanine 4-monooxygenase and human hepatic cytosolic fraction phenylalanine 4-monooxygenase activity with respect to both endobiotic metabolism and xenobiotic metabolism revealed that the reactive oxygen species (hydrogen peroxide and hydroxyl radical) and reactive nitrogen species (nitric oxide and peroxynitrite) could elicit the post-translational activation of the enzyme with respect to both of these biotransformation reactions.	Reactive Oxygen Species	273-296	phenylalanine hydroxylase	Homo sapiens	147-176
20230191-1	2010	An investigation into the post-translational activation of cDNA-expressed human phenylalanine 4-monooxygenase and human hepatic cytosolic fraction phenylalanine 4-monooxygenase activity with respect to both endobiotic metabolism and xenobiotic metabolism revealed that the reactive oxygen species (hydrogen peroxide and hydroxyl radical) and reactive nitrogen species (nitric oxide and peroxynitrite) could elicit the post-translational activation of the enzyme with respect to both of these biotransformation reactions.	radical	329-336	phenylalanine hydroxylase	Homo sapiens	80-109
20230191-1	2010	An investigation into the post-translational activation of cDNA-expressed human phenylalanine 4-monooxygenase and human hepatic cytosolic fraction phenylalanine 4-monooxygenase activity with respect to both endobiotic metabolism and xenobiotic metabolism revealed that the reactive oxygen species (hydrogen peroxide and hydroxyl radical) and reactive nitrogen species (nitric oxide and peroxynitrite) could elicit the post-translational activation of the enzyme with respect to both of these biotransformation reactions.	radical	329-336	phenylalanine hydroxylase	Homo sapiens	147-176
20230191-1	2010	An investigation into the post-translational activation of cDNA-expressed human phenylalanine 4-monooxygenase and human hepatic cytosolic fraction phenylalanine 4-monooxygenase activity with respect to both endobiotic metabolism and xenobiotic metabolism revealed that the reactive oxygen species (hydrogen peroxide and hydroxyl radical) and reactive nitrogen species (nitric oxide and peroxynitrite) could elicit the post-translational activation of the enzyme with respect to both of these biotransformation reactions.	Reactive Nitrogen Species	342-367	phenylalanine hydroxylase	Homo sapiens	80-109
20230191-1	2010	An investigation into the post-translational activation of cDNA-expressed human phenylalanine 4-monooxygenase and human hepatic cytosolic fraction phenylalanine 4-monooxygenase activity with respect to both endobiotic metabolism and xenobiotic metabolism revealed that the reactive oxygen species (hydrogen peroxide and hydroxyl radical) and reactive nitrogen species (nitric oxide and peroxynitrite) could elicit the post-translational activation of the enzyme with respect to both of these biotransformation reactions.	Reactive Nitrogen Species	342-367	phenylalanine hydroxylase	Homo sapiens	147-176
20230191-1	2010	An investigation into the post-translational activation of cDNA-expressed human phenylalanine 4-monooxygenase and human hepatic cytosolic fraction phenylalanine 4-monooxygenase activity with respect to both endobiotic metabolism and xenobiotic metabolism revealed that the reactive oxygen species (hydrogen peroxide and hydroxyl radical) and reactive nitrogen species (nitric oxide and peroxynitrite) could elicit the post-translational activation of the enzyme with respect to both of these biotransformation reactions.	Nitric Oxide	369-381	phenylalanine hydroxylase	Homo sapiens	80-109
20230191-1	2010	An investigation into the post-translational activation of cDNA-expressed human phenylalanine 4-monooxygenase and human hepatic cytosolic fraction phenylalanine 4-monooxygenase activity with respect to both endobiotic metabolism and xenobiotic metabolism revealed that the reactive oxygen species (hydrogen peroxide and hydroxyl radical) and reactive nitrogen species (nitric oxide and peroxynitrite) could elicit the post-translational activation of the enzyme with respect to both of these biotransformation reactions.	Nitric Oxide	369-381	phenylalanine hydroxylase	Homo sapiens	147-176
20230191-1	2010	An investigation into the post-translational activation of cDNA-expressed human phenylalanine 4-monooxygenase and human hepatic cytosolic fraction phenylalanine 4-monooxygenase activity with respect to both endobiotic metabolism and xenobiotic metabolism revealed that the reactive oxygen species (hydrogen peroxide and hydroxyl radical) and reactive nitrogen species (nitric oxide and peroxynitrite) could elicit the post-translational activation of the enzyme with respect to both of these biotransformation reactions.	Peroxynitrous Acid	386-399	phenylalanine hydroxylase	Homo sapiens	80-109
20230191-1	2010	An investigation into the post-translational activation of cDNA-expressed human phenylalanine 4-monooxygenase and human hepatic cytosolic fraction phenylalanine 4-monooxygenase activity with respect to both endobiotic metabolism and xenobiotic metabolism revealed that the reactive oxygen species (hydrogen peroxide and hydroxyl radical) and reactive nitrogen species (nitric oxide and peroxynitrite) could elicit the post-translational activation of the enzyme with respect to both of these biotransformation reactions.	Peroxynitrous Acid	386-399	phenylalanine hydroxylase	Homo sapiens	147-176
20230191-3	2010	These effects were shown to occur at activator concentrations known to exist in physiological situations and, hence, suggest that reactive oxygen and reactive nitrogen species may cause, and may be involved with, the post-translational activation of phenylalanine 4-monooxygenase within the human body.	reactive oxygen and reactive nitrogen species	130-175	phenylalanine hydroxylase	Homo sapiens	250-279
20556201-7	2010	On the other hand, all three inhibitors appear to be uncompetitive versus the cofactor 6-methyltetrahydropterin, which is not only consistent with the structural data but also indicate that the hydroxylation reaction follows an ordered binding mechanism in which a productive complex is formed only if tryptophan binds only after pterin, similar to the kinetic mechanisms of tyrosine and phenylalanine hydroxylase.	6-methyltetrahydropterin	87-111	phenylalanine hydroxylase	Homo sapiens	388-413
20556201-7	2010	On the other hand, all three inhibitors appear to be uncompetitive versus the cofactor 6-methyltetrahydropterin, which is not only consistent with the structural data but also indicate that the hydroxylation reaction follows an ordered binding mechanism in which a productive complex is formed only if tryptophan binds only after pterin, similar to the kinetic mechanisms of tyrosine and phenylalanine hydroxylase.	Pterins	105-111	phenylalanine hydroxylase	Homo sapiens	388-413
19844955-9	2010	The current results demonstrate a lag in excretion of urinary 8-OHdG relative to 1-OHP and 3-PHBaP after dietary PAH exposure.	8-ohdg	62-68	phenylalanine hydroxylase	Homo sapiens	113-116
19844955-9	2010	The current results demonstrate a lag in excretion of urinary 8-OHdG relative to 1-OHP and 3-PHBaP after dietary PAH exposure.	3-phbap	91-98	phenylalanine hydroxylase	Homo sapiens	113-116
19844955-10	2010	These relationships highlight the importance of sampling time when assessing PAH-related DNA lesions through urinary 8-OHdG.	8-ohdg	117-123	phenylalanine hydroxylase	Homo sapiens	77-80
20036649-12	2010	In school children, PAH levels also correlated significantly with 8-OHdG levels, DNA strand breaks and DNA repair capacity.	8-ohdg	66-72	phenylalanine hydroxylase	Homo sapiens	20-23
20187763-1	2010	AIM: Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe), and production of the phenylketonuria disease.	Phenylalanine	186-199	phenylalanine hydroxylase	Homo sapiens	5-30
20187763-1	2010	AIM: Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe), and production of the phenylketonuria disease.	Phenylalanine	186-199	phenylalanine hydroxylase	Homo sapiens	32-35
20187763-1	2010	AIM: Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe), and production of the phenylketonuria disease.	Phenylalanine	186-199	phenylalanine hydroxylase	Homo sapiens	78-81
20187763-1	2010	AIM: Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe), and production of the phenylketonuria disease.	Phenylalanine	186-199	phenylalanine hydroxylase	Homo sapiens	78-81
20187763-1	2010	AIM: Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe), and production of the phenylketonuria disease.	Phenylalanine	5-8	phenylalanine hydroxylase	Homo sapiens	32-35
20187763-1	2010	AIM: Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe), and production of the phenylketonuria disease.	Phenylalanine	5-8	phenylalanine hydroxylase	Homo sapiens	78-81
20187763-1	2010	AIM: Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe), and production of the phenylketonuria disease.	Phenylalanine	5-8	phenylalanine hydroxylase	Homo sapiens	78-81
19925861-2	2010	They may relate to a diminished conversion of phe to tyrosine (tyr) by the enzyme phenylalanine-hydroxylase (PAH).	Phenylalanine	46-49	phenylalanine hydroxylase	Homo sapiens	82-107
19925861-2	2010	They may relate to a diminished conversion of phe to tyrosine (tyr) by the enzyme phenylalanine-hydroxylase (PAH).	Phenylalanine	46-49	phenylalanine hydroxylase	Homo sapiens	109-112
19925861-2	2010	They may relate to a diminished conversion of phe to tyrosine (tyr) by the enzyme phenylalanine-hydroxylase (PAH).	Tyrosine	53-61	phenylalanine hydroxylase	Homo sapiens	82-107
19925861-2	2010	They may relate to a diminished conversion of phe to tyrosine (tyr) by the enzyme phenylalanine-hydroxylase (PAH).	Tyrosine	53-61	phenylalanine hydroxylase	Homo sapiens	109-112
19925861-2	2010	They may relate to a diminished conversion of phe to tyrosine (tyr) by the enzyme phenylalanine-hydroxylase (PAH).	Tyrosine	53-56	phenylalanine hydroxylase	Homo sapiens	82-107
19925861-2	2010	They may relate to a diminished conversion of phe to tyrosine (tyr) by the enzyme phenylalanine-hydroxylase (PAH).	Tyrosine	53-56	phenylalanine hydroxylase	Homo sapiens	109-112
19925861-3	2010	PAH is rate-limiting in the biosynthesis of dopamine, and impaired PAH activity is reflected by an increased phe to tyr ratio (phe/tyr).	Dopamine	44-52	phenylalanine hydroxylase	Homo sapiens	0-3
19925861-3	2010	PAH is rate-limiting in the biosynthesis of dopamine, and impaired PAH activity is reflected by an increased phe to tyr ratio (phe/tyr).	Phenylalanine	109-112	phenylalanine hydroxylase	Homo sapiens	67-70
19925861-3	2010	PAH is rate-limiting in the biosynthesis of dopamine, and impaired PAH activity is reflected by an increased phe to tyr ratio (phe/tyr).	Tyrosine	116-119	phenylalanine hydroxylase	Homo sapiens	67-70
19925861-3	2010	PAH is rate-limiting in the biosynthesis of dopamine, and impaired PAH activity is reflected by an increased phe to tyr ratio (phe/tyr).	Phenylalanine	127-130	phenylalanine hydroxylase	Homo sapiens	67-70
19925861-3	2010	PAH is rate-limiting in the biosynthesis of dopamine, and impaired PAH activity is reflected by an increased phe to tyr ratio (phe/tyr).	Tyrosine	131-134	phenylalanine hydroxylase	Homo sapiens	67-70
19925861-12	2010	ART was found to decrease phe/tyr and this change could indicate and influence on PAH activity.	Phenylalanine	26-29	phenylalanine hydroxylase	Homo sapiens	82-85
19925861-12	2010	ART was found to decrease phe/tyr and this change could indicate and influence on PAH activity.	Tyrosine	30-33	phenylalanine hydroxylase	Homo sapiens	82-85
19817864-6	2010	In similar microcosms incubated also with naphthalene or phenanthrene, analysis of the 16S rRNA gene sequences (DNA and cDNA) with denaturing gradient gel electrophoresis and clone libraries indicated that the PAH-degrading communities were dominated by Cycloclasticus spp., confirming their universal key role in degradation of low-molecular-weight PAHs in marine environments.	naphthalene	42-53	phenylalanine hydroxylase	Homo sapiens	210-213
20063067-1	2010	Phenylketonuria (PKU) is an inherited metabolic disease characterized by phenylalanine (Phe) accumulation due to defects in the enzyme phenylalanine hydroxylase (PAH).	Phenylalanine	73-86	phenylalanine hydroxylase	Homo sapiens	135-160
20063067-1	2010	Phenylketonuria (PKU) is an inherited metabolic disease characterized by phenylalanine (Phe) accumulation due to defects in the enzyme phenylalanine hydroxylase (PAH).	Phenylalanine	73-86	phenylalanine hydroxylase	Homo sapiens	162-165
20063067-1	2010	Phenylketonuria (PKU) is an inherited metabolic disease characterized by phenylalanine (Phe) accumulation due to defects in the enzyme phenylalanine hydroxylase (PAH).	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	135-160
20063067-1	2010	Phenylketonuria (PKU) is an inherited metabolic disease characterized by phenylalanine (Phe) accumulation due to defects in the enzyme phenylalanine hydroxylase (PAH).	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	162-165
20063067-3	2010	Some individuals with PKU respond to tetrahydrobiopterin (BH4) treatment, the natural cofactor of PAH, by a reduction in blood Phe concentrations.We tested 12 patients with PKU, 8-29 years of age, all carrying the common Y414C mutation in the PAH gene.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	98-101
20063067-3	2010	Some individuals with PKU respond to tetrahydrobiopterin (BH4) treatment, the natural cofactor of PAH, by a reduction in blood Phe concentrations.We tested 12 patients with PKU, 8-29 years of age, all carrying the common Y414C mutation in the PAH gene.	sapropterin	58-61	phenylalanine hydroxylase	Homo sapiens	98-101
20063067-3	2010	Some individuals with PKU respond to tetrahydrobiopterin (BH4) treatment, the natural cofactor of PAH, by a reduction in blood Phe concentrations.We tested 12 patients with PKU, 8-29 years of age, all carrying the common Y414C mutation in the PAH gene.	sapropterin	58-61	phenylalanine hydroxylase	Homo sapiens	243-246
20063067-3	2010	Some individuals with PKU respond to tetrahydrobiopterin (BH4) treatment, the natural cofactor of PAH, by a reduction in blood Phe concentrations.We tested 12 patients with PKU, 8-29 years of age, all carrying the common Y414C mutation in the PAH gene.	Phenylalanine	127-130	phenylalanine hydroxylase	Homo sapiens	98-101
19922977-0	2010	1-Hydroxypyrene and 3-hydroxybenzo[a]pyrene as biomarkers of exposure to PAH in various environmental exposure situations.	1-hydroxypyrene	0-15	phenylalanine hydroxylase	Homo sapiens	73-76
19922977-0	2010	1-Hydroxypyrene and 3-hydroxybenzo[a]pyrene as biomarkers of exposure to PAH in various environmental exposure situations.	3-hydroxybenzo(a)pyrene	20-43	phenylalanine hydroxylase	Homo sapiens	73-76
19969441-1	2010	The method of stagnation point optical reflectometry was applied for investigation of adsorption of bovine serum albumin (BSA) on previously formed poly(allylamine hydrochloride)/poly(sodium 4-styrenesulphonate) (PAH/PSS) multilayer with PAH being a terminal layer.	polyallylamine	148-178	phenylalanine hydroxylase	Homo sapiens	213-216
19969441-1	2010	The method of stagnation point optical reflectometry was applied for investigation of adsorption of bovine serum albumin (BSA) on previously formed poly(allylamine hydrochloride)/poly(sodium 4-styrenesulphonate) (PAH/PSS) multilayer with PAH being a terminal layer.	polyallylamine	148-178	phenylalanine hydroxylase	Homo sapiens	238-241
19969441-1	2010	The method of stagnation point optical reflectometry was applied for investigation of adsorption of bovine serum albumin (BSA) on previously formed poly(allylamine hydrochloride)/poly(sodium 4-styrenesulphonate) (PAH/PSS) multilayer with PAH being a terminal layer.	poly(sodium 4-styrenesulphonate)	179-211	phenylalanine hydroxylase	Homo sapiens	213-216
20134300-2	2009	Phenylketonuria (PKU) is an autosomal recessive disorder of phenylalanine (Phe) metabolism characterized by a deficiency of the hepatic enzyme, phenylalanine hydroxylase, an enzyme responsible for the conversion of phenylalanine to tyrosine, and elevated levels of Phe and Phe metabolite.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	144-169
19817864-6	2010	In similar microcosms incubated also with naphthalene or phenanthrene, analysis of the 16S rRNA gene sequences (DNA and cDNA) with denaturing gradient gel electrophoresis and clone libraries indicated that the PAH-degrading communities were dominated by Cycloclasticus spp., confirming their universal key role in degradation of low-molecular-weight PAHs in marine environments.	phenanthrene	57-69	phenylalanine hydroxylase	Homo sapiens	210-213
20389002-0	2010	Electrochemical degradation of PAH compounds in process water: a kinetic study on model solutions and a proof of concept study on runoff water from harbour sediment purification.	Water	56-61	phenylalanine hydroxylase	Homo sapiens	31-34
20389002-0	2010	Electrochemical degradation of PAH compounds in process water: a kinetic study on model solutions and a proof of concept study on runoff water from harbour sediment purification.	Water	137-142	phenylalanine hydroxylase	Homo sapiens	31-34
20389002-6	2010	Decreased current densities from 200 to 15 mA cm(-2) in the NaCl electrolyte also decreased the removal rates, but significantly enhanced the current efficiencies of the PAH oxidation, based on a defined current efficiency constant, k(q).	Sodium Chloride	60-64	phenylalanine hydroxylase	Homo sapiens	170-173
20560550-3	2009	(PAH/PGA) films emerged as the most dense films with the lowest hydration (29%) and the highest COO(-) molar density.	Prostaglandins A	5-8	phenylalanine hydroxylase	Homo sapiens	1-4
20560550-4	2009	In addition, PAH is greatly in excess in these films (3 PAH monomers per PGA monomer).	Prostaglandins A	73-76	phenylalanine hydroxylase	Homo sapiens	13-16
20560550-6	2009	All of the films could be cross-linked in a tunable manner, but PAH/PGA exhibited the highest absolute number of amide bonds created, approximately 7 times more than for (PLL/HA) and (CHI/HA) films.	Prostaglandins A	68-71	phenylalanine hydroxylase	Homo sapiens	64-67
20560550-6	2009	All of the films could be cross-linked in a tunable manner, but PAH/PGA exhibited the highest absolute number of amide bonds created, approximately 7 times more than for (PLL/HA) and (CHI/HA) films.	Amides	113-118	phenylalanine hydroxylase	Homo sapiens	64-67
19194782-10	2009	The different phenylalanine tolerance in pregnancies with PKU-affected and non-affected fetuses suggests that PAH genotype and metabolic situation of the fetus influence maternal metabolic control.	Phenylalanine	14-27	phenylalanine hydroxylase	Homo sapiens	110-113
19747868-2	2009	Phe tolerance (mg phe/kg body weight/day) is the amount of phe those with PKU can consume and maintain acceptable blood phe levels; it requires individual assessment because of varying phenylalanine hydroxylase activity.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	185-210
20134300-2	2009	Phenylketonuria (PKU) is an autosomal recessive disorder of phenylalanine (Phe) metabolism characterized by a deficiency of the hepatic enzyme, phenylalanine hydroxylase, an enzyme responsible for the conversion of phenylalanine to tyrosine, and elevated levels of Phe and Phe metabolite.	Phenylalanine	60-73	phenylalanine hydroxylase	Homo sapiens	144-169
20134300-2	2009	Phenylketonuria (PKU) is an autosomal recessive disorder of phenylalanine (Phe) metabolism characterized by a deficiency of the hepatic enzyme, phenylalanine hydroxylase, an enzyme responsible for the conversion of phenylalanine to tyrosine, and elevated levels of Phe and Phe metabolite.	Tyrosine	232-240	phenylalanine hydroxylase	Homo sapiens	144-169
20134300-2	2009	Phenylketonuria (PKU) is an autosomal recessive disorder of phenylalanine (Phe) metabolism characterized by a deficiency of the hepatic enzyme, phenylalanine hydroxylase, an enzyme responsible for the conversion of phenylalanine to tyrosine, and elevated levels of Phe and Phe metabolite.	Phenylalanine	75-78	phenylalanine hydroxylase	Homo sapiens	144-169
20134300-2	2009	Phenylketonuria (PKU) is an autosomal recessive disorder of phenylalanine (Phe) metabolism characterized by a deficiency of the hepatic enzyme, phenylalanine hydroxylase, an enzyme responsible for the conversion of phenylalanine to tyrosine, and elevated levels of Phe and Phe metabolite.	Phenylalanine	75-78	phenylalanine hydroxylase	Homo sapiens	144-169
19560382-4	2009	During this period the animals provide an in vivo model which can be used to study the regulatory effects of phenylalanine on PAH, and for related pediatric metabolic disease in humans; from birth to youth.	Phenylalanine	109-122	phenylalanine hydroxylase	Homo sapiens	126-129
19653802-1	2009	Phenylalanine 4-monooxygenase is the key enzyme in the sulfoxidation of the thioether drug S-carboxymethyl-l-cysteine and its thioether metabolites, S-methyl-l-cysteine, N-acetyl-S-carboxymethyl-l-cysteine and N-acetyl-S-methyl-l-cysteine in humans, and a number of other mammalian species.	Sulfides	76-85	phenylalanine hydroxylase	Homo sapiens	0-29
19653802-1	2009	Phenylalanine 4-monooxygenase is the key enzyme in the sulfoxidation of the thioether drug S-carboxymethyl-l-cysteine and its thioether metabolites, S-methyl-l-cysteine, N-acetyl-S-carboxymethyl-l-cysteine and N-acetyl-S-methyl-l-cysteine in humans, and a number of other mammalian species.	Carbocysteine	93-117	phenylalanine hydroxylase	Homo sapiens	0-29
19653802-1	2009	Phenylalanine 4-monooxygenase is the key enzyme in the sulfoxidation of the thioether drug S-carboxymethyl-l-cysteine and its thioether metabolites, S-methyl-l-cysteine, N-acetyl-S-carboxymethyl-l-cysteine and N-acetyl-S-methyl-l-cysteine in humans, and a number of other mammalian species.	Sulfides	126-135	phenylalanine hydroxylase	Homo sapiens	0-29
19653802-1	2009	Phenylalanine 4-monooxygenase is the key enzyme in the sulfoxidation of the thioether drug S-carboxymethyl-l-cysteine and its thioether metabolites, S-methyl-l-cysteine, N-acetyl-S-carboxymethyl-l-cysteine and N-acetyl-S-methyl-l-cysteine in humans, and a number of other mammalian species.	S-methylcysteine	149-168	phenylalanine hydroxylase	Homo sapiens	0-29
19653802-1	2009	Phenylalanine 4-monooxygenase is the key enzyme in the sulfoxidation of the thioether drug S-carboxymethyl-l-cysteine and its thioether metabolites, S-methyl-l-cysteine, N-acetyl-S-carboxymethyl-l-cysteine and N-acetyl-S-methyl-l-cysteine in humans, and a number of other mammalian species.	N-acetyl-S-(2-carboxymethyl)cysteine	170-205	phenylalanine hydroxylase	Homo sapiens	0-29
19653802-1	2009	Phenylalanine 4-monooxygenase is the key enzyme in the sulfoxidation of the thioether drug S-carboxymethyl-l-cysteine and its thioether metabolites, S-methyl-l-cysteine, N-acetyl-S-carboxymethyl-l-cysteine and N-acetyl-S-methyl-l-cysteine in humans, and a number of other mammalian species.	N-Acetyl-S-methyl-L-cysteine	210-238	phenylalanine hydroxylase	Homo sapiens	0-29
19653802-3	2009	Differences in K(m), V(max) and CL(E) of S-carboxymethyl-l-cysteine have been seen in HepG2 cells and human and mouse cDNA expressed phenylalanine 4-monooxygenase when compared to both rat and human hepatic cytosolic fractions.	Carbocysteine	41-67	phenylalanine hydroxylase	Homo sapiens	133-162
19345005-1	2009	Potassium permanganate, widely used in water treatment, has shown its applicability to reduce PAH contamination in groundwater and soils.	Potassium Permanganate	0-22	phenylalanine hydroxylase	Homo sapiens	94-97
19557660-1	2009	Phenylketonuria (PKU) is an autosomal recessive inborn error of phenylalanine (Phe) metabolism resulting from deficiency of phenylalanine hydroxylase (PAH).	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	151-154
19345005-1	2009	Potassium permanganate, widely used in water treatment, has shown its applicability to reduce PAH contamination in groundwater and soils.	Water	39-44	phenylalanine hydroxylase	Homo sapiens	94-97
19345005-6	2009	We showed that treatment with potassium permanganate significantly reduced PAH concentration, but pyrene was more recalcitrant than phenanthrene.	Potassium Permanganate	30-52	phenylalanine hydroxylase	Homo sapiens	75-78
19356845-0	2009	Remediation of PAH spiked soils: concentrated H2O2 treatment/continuous hot water extraction-oxidation.	Hydrogen Peroxide	46-50	phenylalanine hydroxylase	Homo sapiens	15-18
19356845-3	2009	Acenaphthene (the most soluble PAH) is completely removed with treatment A regardless of the operating conditions used.	acenaphthene	0-12	phenylalanine hydroxylase	Homo sapiens	31-34
19225966-10	2009	The results indicate that exposure to PAH or possibly other compounds in cooking-oil fumes may cause oxidative DNA damage.	Oils	81-84	phenylalanine hydroxylase	Homo sapiens	38-41
21255289-2	2009	To evaluate the thermodynamic constraints on methanogenic PAH degradation we have estimated the Gibbs free energy values for naphthalene, phenanthrene, anthracene, pyrene and chrysene in the aqueous phase, and used these values to evaluate several possible routes whereby PAHs may be converted to methane.	naphthalene	125-136	phenylalanine hydroxylase	Homo sapiens	58-61
21255289-2	2009	To evaluate the thermodynamic constraints on methanogenic PAH degradation we have estimated the Gibbs free energy values for naphthalene, phenanthrene, anthracene, pyrene and chrysene in the aqueous phase, and used these values to evaluate several possible routes whereby PAHs may be converted to methane.	phenanthrene	138-150	phenylalanine hydroxylase	Homo sapiens	58-61
21255289-2	2009	To evaluate the thermodynamic constraints on methanogenic PAH degradation we have estimated the Gibbs free energy values for naphthalene, phenanthrene, anthracene, pyrene and chrysene in the aqueous phase, and used these values to evaluate several possible routes whereby PAHs may be converted to methane.	anthracene	152-162	phenylalanine hydroxylase	Homo sapiens	58-61
21255289-2	2009	To evaluate the thermodynamic constraints on methanogenic PAH degradation we have estimated the Gibbs free energy values for naphthalene, phenanthrene, anthracene, pyrene and chrysene in the aqueous phase, and used these values to evaluate several possible routes whereby PAHs may be converted to methane.	pyrene	164-170	phenylalanine hydroxylase	Homo sapiens	58-61
21255289-2	2009	To evaluate the thermodynamic constraints on methanogenic PAH degradation we have estimated the Gibbs free energy values for naphthalene, phenanthrene, anthracene, pyrene and chrysene in the aqueous phase, and used these values to evaluate several possible routes whereby PAHs may be converted to methane.	chrysene	175-183	phenylalanine hydroxylase	Homo sapiens	58-61
21255289-4	2009	Per mole of methane produced this is 27-35 kJ mol(-1), indicating that PAH-based methanogenesis is exergonic.	Methane	12-19	phenylalanine hydroxylase	Homo sapiens	71-74
21255289-5	2009	We evaluated the energetics of three potential PAH degradation routes: oxidation to H(2)/CO(2), complete conversion to acetate, or incomplete oxidation to H(2) plus acetate.	h(2)	84-88	phenylalanine hydroxylase	Homo sapiens	47-50
21255289-6	2009	Depending on the in situ conditions the energetically most favourable pathway for the PAH-degrading organisms is oxidation to H(2)/CO(2) or conversion into acetate.	h(2)	126-130	phenylalanine hydroxylase	Homo sapiens	86-89
21255289-6	2009	Depending on the in situ conditions the energetically most favourable pathway for the PAH-degrading organisms is oxidation to H(2)/CO(2) or conversion into acetate.	co(2)	131-136	phenylalanine hydroxylase	Homo sapiens	86-89
21255289-6	2009	Depending on the in situ conditions the energetically most favourable pathway for the PAH-degrading organisms is oxidation to H(2)/CO(2) or conversion into acetate.	Acetates	156-163	phenylalanine hydroxylase	Homo sapiens	86-89
21255289-8	2009	This may be because the kinetic theory of optimal length of metabolic pathways suggests that PAH degraders may have evolved towards incomplete oxidation to acetate plus H(2) as the optimal pathway.	Acetates	156-163	phenylalanine hydroxylase	Homo sapiens	93-96
21255289-8	2009	This may be because the kinetic theory of optimal length of metabolic pathways suggests that PAH degraders may have evolved towards incomplete oxidation to acetate plus H(2) as the optimal pathway.	h(2)	169-173	phenylalanine hydroxylase	Homo sapiens	93-96
19403296-6	2009	Single-breath diffusion capacity for carbon monoxide (DL(CO)) was also decreased in PAH patients.	Carbon Monoxide	37-52	phenylalanine hydroxylase	Homo sapiens	84-87
19513811-1	2009	Tetrahydrobiopterin (BH(4)) cofactor loading is a standard procedure to differentiate defects of BH(4) metabolism from phenylalanine hydroxylase (PAH) deficiency.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	119-144
19513811-1	2009	Tetrahydrobiopterin (BH(4)) cofactor loading is a standard procedure to differentiate defects of BH(4) metabolism from phenylalanine hydroxylase (PAH) deficiency.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	146-149
19394257-1	2009	Specific mutations in the gene encoding phenylalanine hydroxylase (PAH), located on chromosome 12q22-24.1, are linked to tetrahydrobiopterin (BH4; sapropterin)-responsive phenylketonuria (PKU).	sapropterin	121-140	phenylalanine hydroxylase	Homo sapiens	40-65
19403296-1	2009	BACKGROUND: Although previous studies have shown that peripheral airway obstruction can occur in idiopathic PAH (IPAH), pulmonary function tests have not been well-studied in patients with PAH associated with congenital heart disease (CHD-PAH) and connective tissue disease (CTD-PAH).	ipah	113-117	phenylalanine hydroxylase	Homo sapiens	108-111
19394257-1	2009	Specific mutations in the gene encoding phenylalanine hydroxylase (PAH), located on chromosome 12q22-24.1, are linked to tetrahydrobiopterin (BH4; sapropterin)-responsive phenylketonuria (PKU).	sapropterin	121-140	phenylalanine hydroxylase	Homo sapiens	67-70
19394257-1	2009	Specific mutations in the gene encoding phenylalanine hydroxylase (PAH), located on chromosome 12q22-24.1, are linked to tetrahydrobiopterin (BH4; sapropterin)-responsive phenylketonuria (PKU).	sapropterin	142-145	phenylalanine hydroxylase	Homo sapiens	40-65
19394257-1	2009	Specific mutations in the gene encoding phenylalanine hydroxylase (PAH), located on chromosome 12q22-24.1, are linked to tetrahydrobiopterin (BH4; sapropterin)-responsive phenylketonuria (PKU).	sapropterin	142-145	phenylalanine hydroxylase	Homo sapiens	67-70
19394257-1	2009	Specific mutations in the gene encoding phenylalanine hydroxylase (PAH), located on chromosome 12q22-24.1, are linked to tetrahydrobiopterin (BH4; sapropterin)-responsive phenylketonuria (PKU).	sapropterin	147-158	phenylalanine hydroxylase	Homo sapiens	40-65
19394257-1	2009	Specific mutations in the gene encoding phenylalanine hydroxylase (PAH), located on chromosome 12q22-24.1, are linked to tetrahydrobiopterin (BH4; sapropterin)-responsive phenylketonuria (PKU).	sapropterin	147-158	phenylalanine hydroxylase	Homo sapiens	67-70
19394257-4	2009	We investigated the predictive value of BH4-responsive PAH mutations in Croatian population.	sapropterin	40-43	phenylalanine hydroxylase	Homo sapiens	55-58
19394257-11	2009	With regard to the predicted relative PAH activity of recombinantly expressed mutant alleles, there was a significant (p<0.002) difference between BH4-responders and non-responders.	sapropterin	150-153	phenylalanine hydroxylase	Homo sapiens	38-41
19013712-0	2009	Combined column and cell flotation process for the treatment of PAH contaminated hazardous wastes produced by an aluminium production plant.	Aluminum	113-122	phenylalanine hydroxylase	Homo sapiens	64-67
19013712-1	2009	The aluminium electrolytic plants generate PAH and fluoride contaminated wastes which are usually classified as hazardous material.	Aluminum	4-13	phenylalanine hydroxylase	Homo sapiens	43-46
19013712-3	2009	A flotation cell process was previously developed to remove PAH from these aluminium industry wastes.	Aluminum	75-84	phenylalanine hydroxylase	Homo sapiens	60-63
19489646-2	2009	We have previously shown that the Fe(II) site in phenylalanine hydroxylase (PAH) converts from six-coordinate (6C) to five-coordinate (5C) only when both substrate + cofactor are bound.	ammonium ferrous sulfate	34-40	phenylalanine hydroxylase	Homo sapiens	49-74
19489646-2	2009	We have previously shown that the Fe(II) site in phenylalanine hydroxylase (PAH) converts from six-coordinate (6C) to five-coordinate (5C) only when both substrate + cofactor are bound.	ammonium ferrous sulfate	34-40	phenylalanine hydroxylase	Homo sapiens	76-79
19234759-2	2009	BH4 is an essential cofactor not only for phenylalanine hydroxylase, but also for tyrosine and two tryptophan hydroxylases, three nitric oxide synthases, and glyceryl-ether monooxygenase.	sapropterin	0-3	phenylalanine hydroxylase	Homo sapiens	42-67
18937293-1	2009	Recessive mutations in the phenylalanine hydroxylase (PAH) gene predispose to phenylketonuria (PKU) in conjunction with dietary exposure to phenylalanine.	Phenylalanine	27-40	phenylalanine hydroxylase	Homo sapiens	54-57
19302510-5	2009	The median concentration of PAH ranged from 0.14 (lowest, anthracene) to 31.18 microg g(-1) [dibenz(a,h)anthracene] in kajal sample and from not detectable concentration (naphthalene) to 197.47 microg g(-1) of benzo(a)pyrene in surma sample.	anthracene	58-68	phenylalanine hydroxylase	Homo sapiens	28-31
19302510-5	2009	The median concentration of PAH ranged from 0.14 (lowest, anthracene) to 31.18 microg g(-1) [dibenz(a,h)anthracene] in kajal sample and from not detectable concentration (naphthalene) to 197.47 microg g(-1) of benzo(a)pyrene in surma sample.	1,2,5,6-dibenzanthracene	93-114	phenylalanine hydroxylase	Homo sapiens	28-31
19302510-5	2009	The median concentration of PAH ranged from 0.14 (lowest, anthracene) to 31.18 microg g(-1) [dibenz(a,h)anthracene] in kajal sample and from not detectable concentration (naphthalene) to 197.47 microg g(-1) of benzo(a)pyrene in surma sample.	Benzo(a)pyrene	210-224	phenylalanine hydroxylase	Homo sapiens	28-31
19440493-1	2009	BACKGROUND: Polycyclic aromatic hydrocarbons (PAHs) may increase breast cancer risk, and the association may be modified by inherited differences in deactivation of PAH intermediates by glutathione S-transferases (GSTs).	Polycyclic Aromatic Hydrocarbons	12-44	phenylalanine hydroxylase	Homo sapiens	46-49
19444284-0	2009	A limited spectrum of phenylalanine hydroxylase mutations is observed in phenylketonuria patients in western Poland and implications for treatment with 6R tetrahydrobiopterin.	sapropterin	152-174	phenylalanine hydroxylase	Homo sapiens	22-47
19281164-1	2009	The nonheme iron enzyme phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase catalyze the hydroxylation of their aromatic amino acid substrates using a tetrahydropterin as the source of electrons.	Iron	12-16	phenylalanine hydroxylase	Homo sapiens	24-49
19281164-1	2009	The nonheme iron enzyme phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase catalyze the hydroxylation of their aromatic amino acid substrates using a tetrahydropterin as the source of electrons.	Amino Acids, Aromatic	136-155	phenylalanine hydroxylase	Homo sapiens	24-49
19281164-1	2009	The nonheme iron enzyme phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase catalyze the hydroxylation of their aromatic amino acid substrates using a tetrahydropterin as the source of electrons.	tetrahydropterin	175-191	phenylalanine hydroxylase	Homo sapiens	24-49
19208488-1	2009	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase (PAH) gene, leading to deficient conversion of phenylalanine (Phe) to tyrosine and accumulation of toxic levels of Phe.	Phenylalanine	52-65	phenylalanine hydroxylase	Homo sapiens	79-82
19208488-1	2009	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase (PAH) gene, leading to deficient conversion of phenylalanine (Phe) to tyrosine and accumulation of toxic levels of Phe.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	52-77
19208488-1	2009	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase (PAH) gene, leading to deficient conversion of phenylalanine (Phe) to tyrosine and accumulation of toxic levels of Phe.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	79-82
19208488-1	2009	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase (PAH) gene, leading to deficient conversion of phenylalanine (Phe) to tyrosine and accumulation of toxic levels of Phe.	Tyrosine	148-156	phenylalanine hydroxylase	Homo sapiens	52-77
19208488-1	2009	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase (PAH) gene, leading to deficient conversion of phenylalanine (Phe) to tyrosine and accumulation of toxic levels of Phe.	Tyrosine	148-156	phenylalanine hydroxylase	Homo sapiens	79-82
19208488-1	2009	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase (PAH) gene, leading to deficient conversion of phenylalanine (Phe) to tyrosine and accumulation of toxic levels of Phe.	Phenylalanine	140-143	phenylalanine hydroxylase	Homo sapiens	52-77
19208488-1	2009	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase (PAH) gene, leading to deficient conversion of phenylalanine (Phe) to tyrosine and accumulation of toxic levels of Phe.	Phenylalanine	140-143	phenylalanine hydroxylase	Homo sapiens	79-82
19208488-4	2009	The observation of clinically significant reductions in blood Phe levels in a subset of patients with PKU following oral administration of 6R-tetrahydrobiopterin dihydrochloride (BH(4)), a cofactor of PAH, raises the prospect of oral pharmacotherapy for PKU.	Phenylalanine	62-65	phenylalanine hydroxylase	Homo sapiens	201-204
19208488-4	2009	The observation of clinically significant reductions in blood Phe levels in a subset of patients with PKU following oral administration of 6R-tetrahydrobiopterin dihydrochloride (BH(4)), a cofactor of PAH, raises the prospect of oral pharmacotherapy for PKU.	sapropterin	139-177	phenylalanine hydroxylase	Homo sapiens	201-204
19036622-0	2009	The activity of wild type and mutant phenylalanine hydroxylase with respect to the C-oxidation of phenylalanine and the S-oxidation of S-carboxymethyl-L-cysteine.	Carbocysteine	135-161	phenylalanine hydroxylase	Homo sapiens	37-62
19276420-1	2009	Experiments were performed to investigate the activity of hepatic Phe hydroxylase (PAH) and plasma amino acid concentrations under conditions of Phe imbalance or toxicity in chicks fed on experimental diets from 7 to 14 or 16 d of age.	Phenylalanine	66-69	phenylalanine hydroxylase	Homo sapiens	83-86
19276420-4	2009	Correcting the imbalance by adding 1.12% Phe to the diet prevented the growth impairment and increased the activity of PAH.	Phenylalanine	41-44	phenylalanine hydroxylase	Homo sapiens	119-122
19276420-7	2009	The activity of PAH was not significantly affected by 2% Phe, but it increased in chicks fed the corrected diet.	Phenylalanine	57-60	phenylalanine hydroxylase	Homo sapiens	16-19
19276420-11	2009	The addition of Phe significantly increased hepatic PAH activity, but there was no detectable main effect of the IAA - Phe and no interaction.	Phenylalanine	16-19	phenylalanine hydroxylase	Homo sapiens	52-55
19276420-13	2009	We conclude that hepatic PAH activity in chicks variably increases in response to Phe or a 10% dietary supplement of indispensable amino acids including Phe but does not increase in response to IAA - Phe when the amino acids are added to a diet that is marginally adequate in Phe.	Phenylalanine	82-85	phenylalanine hydroxylase	Homo sapiens	25-28
19276420-13	2009	We conclude that hepatic PAH activity in chicks variably increases in response to Phe or a 10% dietary supplement of indispensable amino acids including Phe but does not increase in response to IAA - Phe when the amino acids are added to a diet that is marginally adequate in Phe.	Phenylalanine	153-156	phenylalanine hydroxylase	Homo sapiens	25-28
19276420-13	2009	We conclude that hepatic PAH activity in chicks variably increases in response to Phe or a 10% dietary supplement of indispensable amino acids including Phe but does not increase in response to IAA - Phe when the amino acids are added to a diet that is marginally adequate in Phe.	Phenylalanine	153-156	phenylalanine hydroxylase	Homo sapiens	25-28
19276420-13	2009	We conclude that hepatic PAH activity in chicks variably increases in response to Phe or a 10% dietary supplement of indispensable amino acids including Phe but does not increase in response to IAA - Phe when the amino acids are added to a diet that is marginally adequate in Phe.	Phenylalanine	153-156	phenylalanine hydroxylase	Homo sapiens	25-28
19350915-0	2009	Measurement of freely dissolved PAH concentrations in sediment beds using passive sampling with low-density polyethylene strips.	Polyethylene	108-120	phenylalanine hydroxylase	Homo sapiens	32-35
19123805-5	2009	Films constituted by more than nine PSS/PAH bilayers are still permeable to hexacyanoferrate(II) ions, Fe(CN)(6)4-, whatever the nature of the supporting salt anion.	hexacyanoferrate II	76-92	phenylalanine hydroxylase	Homo sapiens	40-43
19123805-5	2009	Films constituted by more than nine PSS/PAH bilayers are still permeable to hexacyanoferrate(II) ions, Fe(CN)(6)4-, whatever the nature of the supporting salt anion.	Iron	103-105	phenylalanine hydroxylase	Homo sapiens	40-43
18937047-2	2009	Biochemical characterization of mutant PAH enzymes p.D143G, p.R155H, p.L348V, p.R408W and p.P416Q included determination of specific activity, substrate activation, V(max), K(m) for (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)), K (d) for BH(4), and protein stabilization by BH(4).	sapropterin	182-224	phenylalanine hydroxylase	Homo sapiens	39-42
18977496-10	2009	These results indicate that the overall decreased PAH concentrations are likely to be due to evaporation, photoxidation and tidal flushing of the residual oil in these impacted sites.	Oils	155-158	phenylalanine hydroxylase	Homo sapiens	50-53
18801694-6	2009	The rate constants of PAH degradation increase when the water solubility, the vapour pressure and the Henry"s law constant increase.	Water	56-61	phenylalanine hydroxylase	Homo sapiens	22-25
19007315-6	2009	Two tetrahydrobiopterin analogues, N(5)-methyltetrahydrobiopterin and 4-aminotetrahydrobiopterin, had a similar impact on glyceryl ether monooxygenase activity, as has already been shown for phenylalanine hydroxylase.	n(5)-methyltetrahydrobiopterin	35-65	phenylalanine hydroxylase	Homo sapiens	191-216
19007315-6	2009	Two tetrahydrobiopterin analogues, N(5)-methyltetrahydrobiopterin and 4-aminotetrahydrobiopterin, had a similar impact on glyceryl ether monooxygenase activity, as has already been shown for phenylalanine hydroxylase.	4-amino-tetrahydrobiopterin	70-96	phenylalanine hydroxylase	Homo sapiens	191-216
19627172-1	2009	Sapropterin dihydrochloride (Kuvan)) is a synthetic formulation of the active 6R-isomer of tetrahydrobiopterin, a naturally occurring co-factor for phenylalanine hydroxylase.	sapropterin	0-27	phenylalanine hydroxylase	Homo sapiens	148-173
19627172-1	2009	Sapropterin dihydrochloride (Kuvan)) is a synthetic formulation of the active 6R-isomer of tetrahydrobiopterin, a naturally occurring co-factor for phenylalanine hydroxylase.	sapropterin	29-34	phenylalanine hydroxylase	Homo sapiens	148-173
19627172-1	2009	Sapropterin dihydrochloride (Kuvan)) is a synthetic formulation of the active 6R-isomer of tetrahydrobiopterin, a naturally occurring co-factor for phenylalanine hydroxylase.	sapropterin	91-110	phenylalanine hydroxylase	Homo sapiens	148-173
19016342-1	2009	BACKGROUND: Tetrahydrobiopterin (BH(4)) loading has been performed for many years in patients detected by newborn screening for hyperphenylalaninaemia (HPA) to distinguish BH(4) cofactor synthesis or recycling defects from phenylalanine hydroxylase (PAH)-deficient HPA.	sapropterin	12-31	phenylalanine hydroxylase	Homo sapiens	223-248
19238985-7	2009	The most dominant PAH species monitored were fluoranthene and pyrene.	fluoranthene	45-57	phenylalanine hydroxylase	Homo sapiens	18-21
19238985-7	2009	The most dominant PAH species monitored were fluoranthene and pyrene.	pyrene	62-68	phenylalanine hydroxylase	Homo sapiens	18-21
19007315-3	2009	The seven other tetrahydrobiopterin-dependent enzymes can be divided in the family of aromatic amino acid hydroxylases - comprising phenylalanine hydroxylase, tyrosine hydroxylase and the two tryptophan hydroxylases - and into the three nitric oxide synthases.	sapropterin	16-35	phenylalanine hydroxylase	Homo sapiens	132-157
19007315-5	2009	1,10-Phenanthroline, an inhibitor of non-heme iron-dependent enzymes, was able to potently block glyceryl ether monooxygenase as well as phenylalanine hydroxylase, but had no effect on inducible nitric oxide synthase.	1,10-phenanthroline	0-19	phenylalanine hydroxylase	Homo sapiens	137-162
19007315-6	2009	Two tetrahydrobiopterin analogues, N(5)-methyltetrahydrobiopterin and 4-aminotetrahydrobiopterin, had a similar impact on glyceryl ether monooxygenase activity, as has already been shown for phenylalanine hydroxylase.	sapropterin	4-23	phenylalanine hydroxylase	Homo sapiens	191-216
23045014-2	2009	PAH is a non-heme-iron-dependent protein that normally catalyzes the C-oxidation of phenylalanine (Phe) to tyrosine (Tyr) in the presence of BH(4), utilizing molecular dioxygen as an additional substrate.	Phenylalanine	99-102	phenylalanine hydroxylase	Homo sapiens	0-3
23045014-2	2009	PAH is a non-heme-iron-dependent protein that normally catalyzes the C-oxidation of phenylalanine (Phe) to tyrosine (Tyr) in the presence of BH(4), utilizing molecular dioxygen as an additional substrate.	Tyrosine	107-115	phenylalanine hydroxylase	Homo sapiens	0-3
23045014-2	2009	PAH is a non-heme-iron-dependent protein that normally catalyzes the C-oxidation of phenylalanine (Phe) to tyrosine (Tyr) in the presence of BH(4), utilizing molecular dioxygen as an additional substrate.	Tyrosine	117-120	phenylalanine hydroxylase	Homo sapiens	0-3
23045014-2	2009	PAH is a non-heme-iron-dependent protein that normally catalyzes the C-oxidation of phenylalanine (Phe) to tyrosine (Tyr) in the presence of BH(4), utilizing molecular dioxygen as an additional substrate.	Oxygen	168-176	phenylalanine hydroxylase	Homo sapiens	0-3
23045014-4	2009	Like the cytochrome P450 system, PAH is able to oxidize both aliphatic and aromatic carbon centers in addition to undertaking the S-oxidation of aliphatic thioethers (including the two mucoactive drugs S-carboxymethyl-L-cysteine and S-methyl-L-cysteine).	Carbon	84-90	phenylalanine hydroxylase	Homo sapiens	33-36
23045014-4	2009	Like the cytochrome P450 system, PAH is able to oxidize both aliphatic and aromatic carbon centers in addition to undertaking the S-oxidation of aliphatic thioethers (including the two mucoactive drugs S-carboxymethyl-L-cysteine and S-methyl-L-cysteine).	aliphatic	61-70	phenylalanine hydroxylase	Homo sapiens	33-36
23045014-4	2009	Like the cytochrome P450 system, PAH is able to oxidize both aliphatic and aromatic carbon centers in addition to undertaking the S-oxidation of aliphatic thioethers (including the two mucoactive drugs S-carboxymethyl-L-cysteine and S-methyl-L-cysteine).	Sulfides	155-165	phenylalanine hydroxylase	Homo sapiens	33-36
23045014-4	2009	Like the cytochrome P450 system, PAH is able to oxidize both aliphatic and aromatic carbon centers in addition to undertaking the S-oxidation of aliphatic thioethers (including the two mucoactive drugs S-carboxymethyl-L-cysteine and S-methyl-L-cysteine).	Carbocysteine	202-228	phenylalanine hydroxylase	Homo sapiens	33-36
23045014-4	2009	Like the cytochrome P450 system, PAH is able to oxidize both aliphatic and aromatic carbon centers in addition to undertaking the S-oxidation of aliphatic thioethers (including the two mucoactive drugs S-carboxymethyl-L-cysteine and S-methyl-L-cysteine).	S-methylcysteine	233-252	phenylalanine hydroxylase	Homo sapiens	33-36
19323589-1	2009	UNLABELLED: Sapropterin dihydrochloride (Kuvan), hereafter referred to as sapropterin, is a synthetic formulation of the active 6R-isomer of tetrahydrobiopterin, a naturally occurring cofactor for phenylalanine hydroxylase.	sapropterin	12-39	phenylalanine hydroxylase	Homo sapiens	197-222
19323589-1	2009	UNLABELLED: Sapropterin dihydrochloride (Kuvan), hereafter referred to as sapropterin, is a synthetic formulation of the active 6R-isomer of tetrahydrobiopterin, a naturally occurring cofactor for phenylalanine hydroxylase.	sapropterin	41-46	phenylalanine hydroxylase	Homo sapiens	197-222
19323589-1	2009	UNLABELLED: Sapropterin dihydrochloride (Kuvan), hereafter referred to as sapropterin, is a synthetic formulation of the active 6R-isomer of tetrahydrobiopterin, a naturally occurring cofactor for phenylalanine hydroxylase.	sapropterin	74-85	phenylalanine hydroxylase	Homo sapiens	197-222
19323589-1	2009	UNLABELLED: Sapropterin dihydrochloride (Kuvan), hereafter referred to as sapropterin, is a synthetic formulation of the active 6R-isomer of tetrahydrobiopterin, a naturally occurring cofactor for phenylalanine hydroxylase.	sapropterin	141-160	phenylalanine hydroxylase	Homo sapiens	197-222
19036622-1	2009	The involvement of the enzyme, phenylalanine hydroxylase (PAH), in the S-oxidation of S-carboxymethyl-L-cysteine (SCMC) is now firmly established in man and rat.	Carbocysteine	86-112	phenylalanine hydroxylase	Homo sapiens	31-56
19036622-1	2009	The involvement of the enzyme, phenylalanine hydroxylase (PAH), in the S-oxidation of S-carboxymethyl-L-cysteine (SCMC) is now firmly established in man and rat.	Carbocysteine	86-112	phenylalanine hydroxylase	Homo sapiens	58-61
19036622-1	2009	The involvement of the enzyme, phenylalanine hydroxylase (PAH), in the S-oxidation of S-carboxymethyl-L-cysteine (SCMC) is now firmly established in man and rat.	Carbocysteine	114-118	phenylalanine hydroxylase	Homo sapiens	31-56
19036622-1	2009	The involvement of the enzyme, phenylalanine hydroxylase (PAH), in the S-oxidation of S-carboxymethyl-L-cysteine (SCMC) is now firmly established in man and rat.	Carbocysteine	114-118	phenylalanine hydroxylase	Homo sapiens	58-61
19036622-2	2009	However, the underlying role of the molecular genetics of PAH in dictating and influencing the S-oxidation polymorphism of SCMC metabolism is as yet unknown.	Carbocysteine	123-127	phenylalanine hydroxylase	Homo sapiens	58-61
19036622-3	2009	In this work we report that the S-oxidation of SCMC was dramatically reduced in the tetrahydrobiopterin (BH(4)) responsive mutant PAH proteins (I65T, R68S, R261Q, V388M and Y414C) with these enzymes possessing between 1.2% and 2.0% of the wild type PAH activity when SCMC was used as substrate.	Carbocysteine	47-51	phenylalanine hydroxylase	Homo sapiens	130-133
19036622-3	2009	In this work we report that the S-oxidation of SCMC was dramatically reduced in the tetrahydrobiopterin (BH(4)) responsive mutant PAH proteins (I65T, R68S, R261Q, V388M and Y414C) with these enzymes possessing between 1.2% and 2.0% of the wild type PAH activity when SCMC was used as substrate.	Carbocysteine	47-51	phenylalanine hydroxylase	Homo sapiens	249-252
19036622-3	2009	In this work we report that the S-oxidation of SCMC was dramatically reduced in the tetrahydrobiopterin (BH(4)) responsive mutant PAH proteins (I65T, R68S, R261Q, V388M and Y414C) with these enzymes possessing between 1.2% and 2.0% of the wild type PAH activity when SCMC was used as substrate.	sapropterin	84-103	phenylalanine hydroxylase	Homo sapiens	130-133
19036622-3	2009	In this work we report that the S-oxidation of SCMC was dramatically reduced in the tetrahydrobiopterin (BH(4)) responsive mutant PAH proteins (I65T, R68S, R261Q, V388M and Y414C) with these enzymes possessing between 1.2% and 2.0% of the wild type PAH activity when SCMC was used as substrate.	sapropterin	84-103	phenylalanine hydroxylase	Homo sapiens	249-252
19036622-3	2009	In this work we report that the S-oxidation of SCMC was dramatically reduced in the tetrahydrobiopterin (BH(4)) responsive mutant PAH proteins (I65T, R68S, R261Q, V388M and Y414C) with these enzymes possessing between 1.2% and 2.0% of the wild type PAH activity when SCMC was used as substrate.	Carbocysteine	267-271	phenylalanine hydroxylase	Homo sapiens	130-133
19036622-4	2009	These same mutant proteins express between 23% and 76% of the wild type PAH activity when phenylalanine was used as the substrate.	Phenylalanine	90-103	phenylalanine hydroxylase	Homo sapiens	72-75
19036622-5	2009	The PAH mutant proteins (R158Q, I174T and R408W) that result in the classical phenylketonuria (PKU) phenotype expressing 0.2-1.8% of the wild type PAH activity when using phenylalanine as substrate were found to have <0.1% of the wild type PAH activity when SCMC was used as the substrate.	Phenylalanine	171-184	phenylalanine hydroxylase	Homo sapiens	4-7
19036622-5	2009	The PAH mutant proteins (R158Q, I174T and R408W) that result in the classical phenylketonuria (PKU) phenotype expressing 0.2-1.8% of the wild type PAH activity when using phenylalanine as substrate were found to have <0.1% of the wild type PAH activity when SCMC was used as the substrate.	Phenylalanine	171-184	phenylalanine hydroxylase	Homo sapiens	147-150
19036622-5	2009	The PAH mutant proteins (R158Q, I174T and R408W) that result in the classical phenylketonuria (PKU) phenotype expressing 0.2-1.8% of the wild type PAH activity when using phenylalanine as substrate were found to have <0.1% of the wild type PAH activity when SCMC was used as the substrate.	Phenylalanine	171-184	phenylalanine hydroxylase	Homo sapiens	147-150
19036622-5	2009	The PAH mutant proteins (R158Q, I174T and R408W) that result in the classical phenylketonuria (PKU) phenotype expressing 0.2-1.8% of the wild type PAH activity when using phenylalanine as substrate were found to have <0.1% of the wild type PAH activity when SCMC was used as the substrate.	Carbocysteine	261-265	phenylalanine hydroxylase	Homo sapiens	4-7
19036622-5	2009	The PAH mutant proteins (R158Q, I174T and R408W) that result in the classical phenylketonuria (PKU) phenotype expressing 0.2-1.8% of the wild type PAH activity when using phenylalanine as substrate were found to have <0.1% of the wild type PAH activity when SCMC was used as the substrate.	Carbocysteine	261-265	phenylalanine hydroxylase	Homo sapiens	147-150
19036622-5	2009	The PAH mutant proteins (R158Q, I174T and R408W) that result in the classical phenylketonuria (PKU) phenotype expressing 0.2-1.8% of the wild type PAH activity when using phenylalanine as substrate were found to have <0.1% of the wild type PAH activity when SCMC was used as the substrate.	Carbocysteine	261-265	phenylalanine hydroxylase	Homo sapiens	147-150
19036622-6	2009	Mutations that result in PAH proteins retaining some residual PAH activity with phenylalanine as substrate have <2.0% residual activity when SCMC was used as a substrate.	Phenylalanine	80-93	phenylalanine hydroxylase	Homo sapiens	25-28
19036622-6	2009	Mutations that result in PAH proteins retaining some residual PAH activity with phenylalanine as substrate have <2.0% residual activity when SCMC was used as a substrate.	Phenylalanine	80-93	phenylalanine hydroxylase	Homo sapiens	62-65
19036622-6	2009	Mutations that result in PAH proteins retaining some residual PAH activity with phenylalanine as substrate have <2.0% residual activity when SCMC was used as a substrate.	Carbocysteine	144-148	phenylalanine hydroxylase	Homo sapiens	25-28
19036622-6	2009	Mutations that result in PAH proteins retaining some residual PAH activity with phenylalanine as substrate have <2.0% residual activity when SCMC was used as a substrate.	Carbocysteine	144-148	phenylalanine hydroxylase	Homo sapiens	62-65
19036622-7	2009	This investigation has led to the hypothesis that the S-oxidation polymorphism in man is a consequence of an individual carrying one mutant PAH allele which has resulted in the loss of the ability of the residual PAH protein to undertake the S-oxidation of SCMC in vivo.	Carbocysteine	257-261	phenylalanine hydroxylase	Homo sapiens	140-143
19036622-7	2009	This investigation has led to the hypothesis that the S-oxidation polymorphism in man is a consequence of an individual carrying one mutant PAH allele which has resulted in the loss of the ability of the residual PAH protein to undertake the S-oxidation of SCMC in vivo.	Carbocysteine	257-261	phenylalanine hydroxylase	Homo sapiens	213-216
18701209-4	2008	Oxidative stress resulting from chronic immune activation and inflammation could impair activity of phenylalanine (4)-hydroxylase (PAH) and thus give rise to increased phenylalanine concentrations.	Phenylalanine	100-113	phenylalanine hydroxylase	Homo sapiens	131-134
18701209-8	2008	The phenylalanine to tyrosine ratio (phe/tyr), an estimate of PAH activity, correlated somewhat stronger with sTNF-R75 (rs=0.549; p<0.01) and neopterin (rs=0.497; p=0.01).	Phenylalanine	4-17	phenylalanine hydroxylase	Homo sapiens	62-65
18701209-8	2008	The phenylalanine to tyrosine ratio (phe/tyr), an estimate of PAH activity, correlated somewhat stronger with sTNF-R75 (rs=0.549; p<0.01) and neopterin (rs=0.497; p=0.01).	Tyrosine	21-29	phenylalanine hydroxylase	Homo sapiens	62-65
18701209-8	2008	The phenylalanine to tyrosine ratio (phe/tyr), an estimate of PAH activity, correlated somewhat stronger with sTNF-R75 (rs=0.549; p<0.01) and neopterin (rs=0.497; p=0.01).	Phenylalanine	4-7	phenylalanine hydroxylase	Homo sapiens	62-65
18701209-8	2008	The phenylalanine to tyrosine ratio (phe/tyr), an estimate of PAH activity, correlated somewhat stronger with sTNF-R75 (rs=0.549; p<0.01) and neopterin (rs=0.497; p=0.01).	Neopterin	145-154	phenylalanine hydroxylase	Homo sapiens	62-65
18701209-11	2008	The relationship between oxidative stress marker isoprostane-8 and phenylalanine as well as sTNF-R75 concentrations suggests a link between reactive oxygen species formed during chronic immune activation and inflammation and the decline of PAH activity, which might underlie the increase of phe/tyr (248 words).	isoprostane-8	49-62	phenylalanine hydroxylase	Homo sapiens	240-243
18701209-11	2008	The relationship between oxidative stress marker isoprostane-8 and phenylalanine as well as sTNF-R75 concentrations suggests a link between reactive oxygen species formed during chronic immune activation and inflammation and the decline of PAH activity, which might underlie the increase of phe/tyr (248 words).	Phenylalanine	67-80	phenylalanine hydroxylase	Homo sapiens	240-243
18701209-11	2008	The relationship between oxidative stress marker isoprostane-8 and phenylalanine as well as sTNF-R75 concentrations suggests a link between reactive oxygen species formed during chronic immune activation and inflammation and the decline of PAH activity, which might underlie the increase of phe/tyr (248 words).	Reactive Oxygen Species	140-163	phenylalanine hydroxylase	Homo sapiens	240-243
18701209-11	2008	The relationship between oxidative stress marker isoprostane-8 and phenylalanine as well as sTNF-R75 concentrations suggests a link between reactive oxygen species formed during chronic immune activation and inflammation and the decline of PAH activity, which might underlie the increase of phe/tyr (248 words).	Tyrosine	295-298	phenylalanine hydroxylase	Homo sapiens	240-243
19005598-0	2008	Theoretical studies on the carcinogenic activity of diol epoxide derivatives of PAH: proton affinity and aromaticity as decisive descriptors.	diol epoxide	52-64	phenylalanine hydroxylase	Homo sapiens	80-83
19904458-5	2008	The BH4 responsiveness seems to be regulated in mild PKU by PAH mutations, and affected by the BH4 dose and administration period.	sapropterin	4-7	phenylalanine hydroxylase	Homo sapiens	60-63
18769885-2	2008	Rescue of the enzyme activity of several recombinant hPAH mutant forms (I65T, R261Q, R270K and V388M) by low molecular weight compounds namely glycerol, trimethylamine N-oxide (TMAO) and sodium 4-phenylbutyrate (4-PB) was investigated using a prokaryotic expression model.	Glycerol	143-151	phenylalanine hydroxylase	Homo sapiens	53-57
18974895-8	2008	The PAH profiles were clearly dominated by phenanthrene.	phenanthrene	43-55	phenylalanine hydroxylase	Homo sapiens	4-7
18353549-5	2008	PAH homologue distributions of the three selected sintering process areas were significantly different from that of the outdoor environment suggesting that PAHs found in the sintering workplace atmospheres were mainly contributed by process fugitives.	Polycyclic Aromatic Hydrocarbons	156-160	phenylalanine hydroxylase	Homo sapiens	0-3
18941584-6	2008	Prenatal PAH exposure was measured by PAH-DNA adducts (benzo[a]pyrene-DNA) in umbilical cord blood.	Benzo(a)pyrene	55-69	phenylalanine hydroxylase	Homo sapiens	9-12
18941584-6	2008	Prenatal PAH exposure was measured by PAH-DNA adducts (benzo[a]pyrene-DNA) in umbilical cord blood.	Benzo(a)pyrene	55-69	phenylalanine hydroxylase	Homo sapiens	38-41
18270801-2	2008	According to the concentrations in the core three groups of PAHs may be distinguished: (1) relatively stable concentrations of PAHs within the whole studied time interval; (2) very low concentrations in sediments accumulated before intensive anthropogenic impact (from 19th century up to the 1920s) following a slight increase and (3) an overall increase in PAH concentrations since the 1920s up to the present.	Polycyclic Aromatic Hydrocarbons	127-131	phenylalanine hydroxylase	Homo sapiens	60-63
19068615-1	2008	To obtain the temporal and spatial distribution and partition of PAH between water and particles in coastal area, water samples were collected from the Pearl River Estuary in July 2002 (summer) and April 2003 (spring) and polycyclic aromatic hydrocarbons (PAHs) were analysed with GC-MS in the present study.	Water	77-82	phenylalanine hydroxylase	Homo sapiens	65-68
19068615-2	2008	Total PAH concentrations in water samples were higher in spring (c(p): 4.0-39.1 ng/L; c(w): 15.9-184.2 ng/L) than in summer (c(p): 2.6-26.6 ng/L; c(w): 13.0-28.3 ng/L).	Water	28-33	phenylalanine hydroxylase	Homo sapiens	6-9
19068615-3	2008	Suspended particle matter (SPM) content, photogradation and riverine discharge were the major factors controlling the PAH concentrations in water.	Water	140-145	phenylalanine hydroxylase	Homo sapiens	118-121
19068615-7	2008	The partition coefficient (Kp) increased with the particular organic carbon content of SPM and salinity of water and decreased with the SPM content of samples, which were consistent with the PAH partition theory.	Carbon	69-75	phenylalanine hydroxylase	Homo sapiens	191-194
19068615-7	2008	The partition coefficient (Kp) increased with the particular organic carbon content of SPM and salinity of water and decreased with the SPM content of samples, which were consistent with the PAH partition theory.	Water	107-112	phenylalanine hydroxylase	Homo sapiens	191-194
23045014-2	2009	PAH is a non-heme-iron-dependent protein that normally catalyzes the C-oxidation of phenylalanine (Phe) to tyrosine (Tyr) in the presence of BH(4), utilizing molecular dioxygen as an additional substrate.	Heme	13-17	phenylalanine hydroxylase	Homo sapiens	0-3
23045014-2	2009	PAH is a non-heme-iron-dependent protein that normally catalyzes the C-oxidation of phenylalanine (Phe) to tyrosine (Tyr) in the presence of BH(4), utilizing molecular dioxygen as an additional substrate.	Iron	18-22	phenylalanine hydroxylase	Homo sapiens	0-3
23045014-2	2009	PAH is a non-heme-iron-dependent protein that normally catalyzes the C-oxidation of phenylalanine (Phe) to tyrosine (Tyr) in the presence of BH(4), utilizing molecular dioxygen as an additional substrate.	Phenylalanine	84-97	phenylalanine hydroxylase	Homo sapiens	0-3
18608740-0	2008	Enzyme kinetic and molecular modelling studies of sulphur-containing substrates of phenylalanine 4-monooxygenase.	Sulfur	50-57	phenylalanine hydroxylase	Homo sapiens	83-112
18608740-1	2008	Previous investigations into the binding of substrates/cofactors to the PAH active site have only concentrated on Phe, thienylalanine and BH(4).	Phenylalanine	114-117	phenylalanine hydroxylase	Homo sapiens	72-75
18608740-1	2008	Previous investigations into the binding of substrates/cofactors to the PAH active site have only concentrated on Phe, thienylalanine and BH(4).	3-(2-Thienyl)-dl-alanine	119-133	phenylalanine hydroxylase	Homo sapiens	72-75
18608740-2	2008	This is the first reported investigation to model aliphatic thioether amino acid substrates to PAH.	thioether amino acid	60-80	phenylalanine hydroxylase	Homo sapiens	95-98
18608740-4	2008	The xenobiotic thioether substrates (SMC and SCMC) were predicted to be poor substrates for PAH by the molecular modelling investigation and this has now been confirmed by the in vitro enzyme kinetic data.	Sulfides	15-24	phenylalanine hydroxylase	Homo sapiens	92-95
18608740-4	2008	The xenobiotic thioether substrates (SMC and SCMC) were predicted to be poor substrates for PAH by the molecular modelling investigation and this has now been confirmed by the in vitro enzyme kinetic data.	Carbocysteine	45-49	phenylalanine hydroxylase	Homo sapiens	92-95
18608740-5	2008	However, reaction phenotyping investigations have found that PAH was the major enzyme involved in the metabolism of SCMC in vitro and in vivo.	Carbocysteine	116-120	phenylalanine hydroxylase	Homo sapiens	61-64
18281132-3	2008	With increasing concentration of rhamnolipids, the PAH content in ryegrass roots initially increased and then decreased, while the PAH content in ryegrass shoots did not change.	rhamnolipid	33-45	phenylalanine hydroxylase	Homo sapiens	51-54
18281132-3	2008	With increasing concentration of rhamnolipids, the PAH content in ryegrass roots initially increased and then decreased, while the PAH content in ryegrass shoots did not change.	rhamnolipid	33-45	phenylalanine hydroxylase	Homo sapiens	131-134
18281132-5	2008	The increase of permeability of ryegrass root cells with the increase of rhamnolipid concentration may lead to the initial enhancement of PAH content in ryegrass roots, and the decrease of PAH adsorption onto the root surface with further increase of rhamnolipids led to the decrease of PAH content in ryegrass roots.	rhamnolipid	73-84	phenylalanine hydroxylase	Homo sapiens	138-141
18808160-1	2008	In this study, a magnetic-sensitive microcapsule was prepared using Fe 3O 4/poly(allylamine) (Fe 3O 4/PAH) polyelectrolyte to construct the shell.	polyallylamine	76-92	phenylalanine hydroxylase	Homo sapiens	94-105
18769885-2	2008	Rescue of the enzyme activity of several recombinant hPAH mutant forms (I65T, R261Q, R270K and V388M) by low molecular weight compounds namely glycerol, trimethylamine N-oxide (TMAO) and sodium 4-phenylbutyrate (4-PB) was investigated using a prokaryotic expression model.	trimethyloxamine	153-175	phenylalanine hydroxylase	Homo sapiens	53-57
18769885-2	2008	Rescue of the enzyme activity of several recombinant hPAH mutant forms (I65T, R261Q, R270K and V388M) by low molecular weight compounds namely glycerol, trimethylamine N-oxide (TMAO) and sodium 4-phenylbutyrate (4-PB) was investigated using a prokaryotic expression model.	trimethyloxamine	177-181	phenylalanine hydroxylase	Homo sapiens	53-57
18769885-2	2008	Rescue of the enzyme activity of several recombinant hPAH mutant forms (I65T, R261Q, R270K and V388M) by low molecular weight compounds namely glycerol, trimethylamine N-oxide (TMAO) and sodium 4-phenylbutyrate (4-PB) was investigated using a prokaryotic expression model.	4-phenylbutyric acid	187-210	phenylalanine hydroxylase	Homo sapiens	53-57
18769885-2	2008	Rescue of the enzyme activity of several recombinant hPAH mutant forms (I65T, R261Q, R270K and V388M) by low molecular weight compounds namely glycerol, trimethylamine N-oxide (TMAO) and sodium 4-phenylbutyrate (4-PB) was investigated using a prokaryotic expression model.	4-phenylbutyric acid	212-216	phenylalanine hydroxylase	Homo sapiens	53-57
18769885-6	2008	Since the addition of the studied compounds to the medium did not change the expression level of E. Coli molecular chaperones we postulate that glycerol and TMAO rescue results from a direct stabilizing effect of the newly synthesized mutant hPAH enzymes.	trimethyloxamine	157-161	phenylalanine hydroxylase	Homo sapiens	242-246
18163176-5	2008	Increased phenylalanine implies insufficient conversion by phenylalanine (4)-hydroxylase (PAH).	Phenylalanine	10-23	phenylalanine hydroxylase	Homo sapiens	59-88
18163176-5	2008	Increased phenylalanine implies insufficient conversion by phenylalanine (4)-hydroxylase (PAH).	Phenylalanine	10-23	phenylalanine hydroxylase	Homo sapiens	90-93
18163176-7	2008	This assumption is further supported by the correlation found between higher neopterin concentrations and higher phenylalanine to tyrosine ratio, which estimates efficacy of PAH.	Neopterin	77-86	phenylalanine hydroxylase	Homo sapiens	174-177
18163176-7	2008	This assumption is further supported by the correlation found between higher neopterin concentrations and higher phenylalanine to tyrosine ratio, which estimates efficacy of PAH.	Phenylalanine	113-126	phenylalanine hydroxylase	Homo sapiens	174-177
18163176-7	2008	This assumption is further supported by the correlation found between higher neopterin concentrations and higher phenylalanine to tyrosine ratio, which estimates efficacy of PAH.	Tyrosine	130-138	phenylalanine hydroxylase	Homo sapiens	174-177
18489080-3	2008	Alternatively, aldo-keto reductases (AKRs) convert intermediate PAH trans-dihydrodiols to o-quinones, which cause DNA damage by generating reactive oxygen species (ROS).	Reactive Oxygen Species	164-167	phenylalanine hydroxylase	Homo sapiens	64-67
18460651-3	2008	CePAH presents similar molecular and kinetic properties to human PAH [S(0.5)(L-Phe) approximately 150 microM; K(m) for tetrahydrobiopterin (BH(4)) approximately 35 microM and comparable V(max)], but cePAH is devoid of positive cooperativity for L-Phe, an important regulatory mechanism of mammalian PAH that protects the nervous system from excess L-Phe.	Phenylalanine	77-82	phenylalanine hydroxylase	Homo sapiens	2-5
18460651-3	2008	CePAH presents similar molecular and kinetic properties to human PAH [S(0.5)(L-Phe) approximately 150 microM; K(m) for tetrahydrobiopterin (BH(4)) approximately 35 microM and comparable V(max)], but cePAH is devoid of positive cooperativity for L-Phe, an important regulatory mechanism of mammalian PAH that protects the nervous system from excess L-Phe.	Phenylalanine	77-82	phenylalanine hydroxylase	Homo sapiens	65-68
18460651-3	2008	CePAH presents similar molecular and kinetic properties to human PAH [S(0.5)(L-Phe) approximately 150 microM; K(m) for tetrahydrobiopterin (BH(4)) approximately 35 microM and comparable V(max)], but cePAH is devoid of positive cooperativity for L-Phe, an important regulatory mechanism of mammalian PAH that protects the nervous system from excess L-Phe.	sapropterin	119-138	phenylalanine hydroxylase	Homo sapiens	2-5
18165874-0	2008	Effect of incubation conditions on the enrichment of pyrene-degrading bacteria identified by stable-isotope probing in an aged, PAH-contaminated soil.	pyrene	53-59	phenylalanine hydroxylase	Homo sapiens	128-131
18538294-1	2008	A significant share of patients with phenylalanine hydroxylase (PAH) deficiency benefits from pharmacological doses of tetrahydrobiopterin (BH(4)), the natural PAH cofactor.	sapropterin	119-138	phenylalanine hydroxylase	Homo sapiens	37-62
18538294-1	2008	A significant share of patients with phenylalanine hydroxylase (PAH) deficiency benefits from pharmacological doses of tetrahydrobiopterin (BH(4)), the natural PAH cofactor.	sapropterin	119-138	phenylalanine hydroxylase	Homo sapiens	64-67
18538294-1	2008	A significant share of patients with phenylalanine hydroxylase (PAH) deficiency benefits from pharmacological doses of tetrahydrobiopterin (BH(4)), the natural PAH cofactor.	sapropterin	119-138	phenylalanine hydroxylase	Homo sapiens	160-163
18313659-1	2008	Urinary monohydroxy polycyclic aromatic hydrocarbons (OH-PAHs) are a class of PAH metabolites used as biomarkers for assessing human exposure to PAHs.	monohydroxy polycyclic aromatic hydrocarbons	8-52	phenylalanine hydroxylase	Homo sapiens	57-60
18313659-5	2008	The geometric mean for 1-hydroxypyrene (1-PYR)--the most commonly used biomarker for PAH exposure--was 49.6 ng/L urine, or 46.4 ng/g creatinine.	1-hydroxypyrene	23-46	phenylalanine hydroxylase	Homo sapiens	85-88
18313659-9	2008	The correlation coefficients between 1-PYR and other metabolites ranging from 0.17 to 0.63 support the use of 1-PYR as a useful surrogate representing PAH exposure.	1-hydroxypyrene	37-42	phenylalanine hydroxylase	Homo sapiens	151-154
18313659-9	2008	The correlation coefficients between 1-PYR and other metabolites ranging from 0.17 to 0.63 support the use of 1-PYR as a useful surrogate representing PAH exposure.	1-hydroxypyrene	110-115	phenylalanine hydroxylase	Homo sapiens	151-154
18688457-11	2008	The best reflection of the PAH losses was observed in the case of fluoranthene, anthracene and indeno[1,2,3-cd]pyrene.	fluoranthene	66-78	phenylalanine hydroxylase	Homo sapiens	27-30
18688457-11	2008	The best reflection of the PAH losses was observed in the case of fluoranthene, anthracene and indeno[1,2,3-cd]pyrene.	anthracene	80-90	phenylalanine hydroxylase	Homo sapiens	27-30
18688457-11	2008	The best reflection of the PAH losses was observed in the case of fluoranthene, anthracene and indeno[1,2,3-cd]pyrene.	indeno(1,2,3-cd)pyrene	95-117	phenylalanine hydroxylase	Homo sapiens	27-30
18482855-0	2008	Development of a model for assessment of phenylalanine hydroxylase activity in newborns with phenylketonuria receiving tetrahydrobiopterin: a potential for practical implementation.	sapropterin	119-138	phenylalanine hydroxylase	Homo sapiens	41-66
18589972-1	2008	We investigated enrichment with salicylate as a method to stimulate the degradation of polycyclic aromatic hydrocarbons (PAHs) by a microbial communityfrom a bioreactortreating PAH-contaminated soil.	Salicylates	32-42	phenylalanine hydroxylase	Homo sapiens	121-124
18589972-1	2008	We investigated enrichment with salicylate as a method to stimulate the degradation of polycyclic aromatic hydrocarbons (PAHs) by a microbial communityfrom a bioreactortreating PAH-contaminated soil.	Polycyclic Aromatic Hydrocarbons	87-119	phenylalanine hydroxylase	Homo sapiens	121-124
18589992-8	2008	The mean content of the particle-bound total-PAHs/-BaPeqs and the PAH/BaPeq-derived carcinogenic potency followed the order nano > ultrafine > fine > coarse.	bapeqs	51-57	phenylalanine hydroxylase	Homo sapiens	45-48
18589992-8	2008	The mean content of the particle-bound total-PAHs/-BaPeqs and the PAH/BaPeq-derived carcinogenic potency followed the order nano > ultrafine > fine > coarse.	bapeq	51-56	phenylalanine hydroxylase	Homo sapiens	45-48
18489080-0	2008	The pattern of p53 mutations caused by PAH o-quinones is driven by 8-oxo-dGuo formation while the spectrum of mutations is determined by biological selection for dominance.	8-ohdg	67-77	phenylalanine hydroxylase	Homo sapiens	39-42
18489080-2	2008	P4501A1/P4501B1 plus epoxide hydrolase activate PAH to (+/-)- anti-benzo[ a]pyrene diol epoxide ((+/-)- anti-BPDE), which causes bulky DNA adducts.	pyrene diol epoxide	76-95	phenylalanine hydroxylase	Homo sapiens	48-51
18489080-9	2008	Nanomolar concentrations of PAH o-quinones generated 8-oxo-dGuo (detected by HPLC-ECD) in a concentration dependent manner that correlated in a linear fashion with mutagenic frequency.	o-quinones	32-42	phenylalanine hydroxylase	Homo sapiens	28-31
18489080-9	2008	Nanomolar concentrations of PAH o-quinones generated 8-oxo-dGuo (detected by HPLC-ECD) in a concentration dependent manner that correlated in a linear fashion with mutagenic frequency.	8-ohdg	53-63	phenylalanine hydroxylase	Homo sapiens	28-31
18489080-2	2008	P4501A1/P4501B1 plus epoxide hydrolase activate PAH to (+/-)- anti-benzo[ a]pyrene diol epoxide ((+/-)- anti-BPDE), which causes bulky DNA adducts.	7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide	109-113	phenylalanine hydroxylase	Homo sapiens	48-51
18489080-12	2008	However, mutations at guanine bases observed with either PAH-treatment occurred randomly throughout the DNA-binding domain of p53.	Guanine	22-29	phenylalanine hydroxylase	Homo sapiens	57-60
18489080-3	2008	Alternatively, aldo-keto reductases (AKRs) convert intermediate PAH trans-dihydrodiols to o-quinones, which cause DNA damage by generating reactive oxygen species (ROS).	o-quinones	90-100	phenylalanine hydroxylase	Homo sapiens	64-67
18489080-3	2008	Alternatively, aldo-keto reductases (AKRs) convert intermediate PAH trans-dihydrodiols to o-quinones, which cause DNA damage by generating reactive oxygen species (ROS).	Reactive Oxygen Species	139-162	phenylalanine hydroxylase	Homo sapiens	64-67
32907124-5	2008	Charged polysaccharides form soluble complexes or coacervates with proteins depending on pH, ionic strength, and biopolymer charge distribution.	Polysaccharides	8-23	phenylalanine hydroxylase	Homo sapiens	89-91
18470301-5	2008	PAH-DNA adducts (specifically benzo[a]pyrene adducts) provided a biologically relevant measure of PAH exposure.	Benzo(a)pyrene	30-44	phenylalanine hydroxylase	Homo sapiens	0-3
18470301-5	2008	PAH-DNA adducts (specifically benzo[a]pyrene adducts) provided a biologically relevant measure of PAH exposure.	Benzo(a)pyrene	30-44	phenylalanine hydroxylase	Homo sapiens	98-101
18177348-3	2008	The central role of tyrosinase as the key enzyme in initiation of melanogenesis has been closely associated with the 6BH4 dependent phenylalanine hydroxylase (PAH) and tyrosine hydroxylase isoform I (THI) providing evidence for an old concept of the three enzyme theory in the initiation of the pigmentation process.	6bh4	117-121	phenylalanine hydroxylase	Homo sapiens	132-157
18493213-6	2008	RESULTS: From birth to screening test, the amount of Phe tolerated ranged from 704 to 1620 mg, according to the class of PAH deficiency.	Phenylalanine	53-56	phenylalanine hydroxylase	Homo sapiens	121-124
32907124-5	2008	Charged polysaccharides form soluble complexes or coacervates with proteins depending on pH, ionic strength, and biopolymer charge distribution.	coacervates	50-61	phenylalanine hydroxylase	Homo sapiens	89-91
18272200-8	2008	A closer examination of individual PAH results indicated that both techniques overestimated the availability of large molecules with logK(ow)>6 suggesting a biological mechanism limiting uptake of larger PAHs which seems to be related to the molecular size of compounds.	Polycyclic Aromatic Hydrocarbons	207-211	phenylalanine hydroxylase	Homo sapiens	35-38
18385878-4	2008	The total PAH concentrations (2- to 6-ring parent and alkylated PAHs, including the 16 US EPA PAHs) were less than 150 microg kg(-1) dry weight and their composition indicated a predominantly pyrolytic input to the basin in 2002.	Polycyclic Aromatic Hydrocarbons	64-68	phenylalanine hydroxylase	Homo sapiens	10-13
17977740-6	2007	In patients suffering from phenylketonuria the hydroxylation of phenylalanine to tyrosine is defective due to lack of phenylalanine hydroxylase.	Phenylalanine	64-77	phenylalanine hydroxylase	Homo sapiens	118-143
18566668-1	2008	Phenylketonuria (PKU) is an autosomal recessive inborn error of phenylalanine (Phe) metabolism resulting from deficiency of phenylalanine hydroxylase (PAH).	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	151-154
18210214-1	2008	BACKGROUND: A significant percentage of patients with hyperphenylalaninaemia (HPA) due to primary deficiency of the phenylalanine hydroxylase enzyme (PAH) respond to a dose of tetrahydrobiopterin (BH(4)) with an increased rate of phenylalanine (Phe) disposal.	sapropterin	176-195	phenylalanine hydroxylase	Homo sapiens	150-153
18210214-1	2008	BACKGROUND: A significant percentage of patients with hyperphenylalaninaemia (HPA) due to primary deficiency of the phenylalanine hydroxylase enzyme (PAH) respond to a dose of tetrahydrobiopterin (BH(4)) with an increased rate of phenylalanine (Phe) disposal.	Phenylalanine	116-129	phenylalanine hydroxylase	Homo sapiens	150-153
18210214-1	2008	BACKGROUND: A significant percentage of patients with hyperphenylalaninaemia (HPA) due to primary deficiency of the phenylalanine hydroxylase enzyme (PAH) respond to a dose of tetrahydrobiopterin (BH(4)) with an increased rate of phenylalanine (Phe) disposal.	Phenylalanine	245-248	phenylalanine hydroxylase	Homo sapiens	150-153
18212372-0	2008	Phenylalanine requirement, imbalance, and dietary excess in one-week-old chicks: growth and phenylalanine hydroxylase activity.	Phenylalanine	0-13	phenylalanine hydroxylase	Homo sapiens	92-117
18212372-7	2008	The activities of the major hepatic enzyme of Phe catabolism, Phe hydroxylase (PAH), were significantly higher than that of chicks fed the basal diet when the chicks were fed the diets containing IAA - Phe plus 1.1% Phe (P > or = 0.05) but not when chicks were fed the diet containing IAA - Phe alone.	iaa - phe	196-205	phenylalanine hydroxylase	Homo sapiens	46-77
18212372-7	2008	The activities of the major hepatic enzyme of Phe catabolism, Phe hydroxylase (PAH), were significantly higher than that of chicks fed the basal diet when the chicks were fed the diets containing IAA - Phe plus 1.1% Phe (P > or = 0.05) but not when chicks were fed the diet containing IAA - Phe alone.	iaa - phe	196-205	phenylalanine hydroxylase	Homo sapiens	79-82
18212372-7	2008	The activities of the major hepatic enzyme of Phe catabolism, Phe hydroxylase (PAH), were significantly higher than that of chicks fed the basal diet when the chicks were fed the diets containing IAA - Phe plus 1.1% Phe (P > or = 0.05) but not when chicks were fed the diet containing IAA - Phe alone.	Phenylalanine	46-49	phenylalanine hydroxylase	Homo sapiens	79-82
18212372-7	2008	The activities of the major hepatic enzyme of Phe catabolism, Phe hydroxylase (PAH), were significantly higher than that of chicks fed the basal diet when the chicks were fed the diets containing IAA - Phe plus 1.1% Phe (P > or = 0.05) but not when chicks were fed the diet containing IAA - Phe alone.	iaa - phe	288-297	phenylalanine hydroxylase	Homo sapiens	46-77
18212372-7	2008	The activities of the major hepatic enzyme of Phe catabolism, Phe hydroxylase (PAH), were significantly higher than that of chicks fed the basal diet when the chicks were fed the diets containing IAA - Phe plus 1.1% Phe (P > or = 0.05) but not when chicks were fed the diet containing IAA - Phe alone.	iaa - phe	288-297	phenylalanine hydroxylase	Homo sapiens	79-82
18212372-8	2008	The activity of PAH in chicks given the excess (2%) Phe was nearly 4 times the activity of PAH in chicks given the basal diet.	Phenylalanine	52-55	phenylalanine hydroxylase	Homo sapiens	16-19
18212372-8	2008	The activity of PAH in chicks given the excess (2%) Phe was nearly 4 times the activity of PAH in chicks given the basal diet.	Phenylalanine	52-55	phenylalanine hydroxylase	Homo sapiens	91-94
18212372-9	2008	Adding IAA - Phe to the diet containing excess Phe also resulted in higher PAH activity than was observed in chicks fed the basal diet, although the activity was significantly lower than observed for chicks receiving the diet containing excess Phe alone (P > or = 0.05).	iaa - phe	7-16	phenylalanine hydroxylase	Homo sapiens	75-78
18212372-9	2008	Adding IAA - Phe to the diet containing excess Phe also resulted in higher PAH activity than was observed in chicks fed the basal diet, although the activity was significantly lower than observed for chicks receiving the diet containing excess Phe alone (P > or = 0.05).	Phenylalanine	13-16	phenylalanine hydroxylase	Homo sapiens	75-78
18212372-9	2008	Adding IAA - Phe to the diet containing excess Phe also resulted in higher PAH activity than was observed in chicks fed the basal diet, although the activity was significantly lower than observed for chicks receiving the diet containing excess Phe alone (P > or = 0.05).	Phenylalanine	47-50	phenylalanine hydroxylase	Homo sapiens	75-78
18212372-10	2008	It is concluded that hepatic PAH activity in chicks increases primarily in response to its substrate, Phe.	Phenylalanine	102-105	phenylalanine hydroxylase	Homo sapiens	29-32
32907201-0	2008	pH-Responsive polymers: synthesis, properties and applications.	Polymers	14-22	phenylalanine hydroxylase	Homo sapiens	0-2
32907201-1	2008	pH-Responsive polymers are systems whose solubility, volume, and chain conformation can be manipulated by changes in pH, co-solvent, and electrolytes.	Polymers	14-22	phenylalanine hydroxylase	Homo sapiens	0-2
32907201-1	2008	pH-Responsive polymers are systems whose solubility, volume, and chain conformation can be manipulated by changes in pH, co-solvent, and electrolytes.	Polymers	14-22	phenylalanine hydroxylase	Homo sapiens	117-119
18198853-2	2008	It has been found that the reaction mechanism of this haptotropic migration can either occur in a single step or stepwise depending on the interaction between the orbitals of the Cr(CO)3 and the PAH fragments.	Cr(CO)3	179-186	phenylalanine hydroxylase	Homo sapiens	195-198
19326770-3	2008	In pooled female human hepatic cytosolic fractions the calculated K(m) and V(max) for substrate (SCMC) activated PAH was 16.22 +/- 11.31 mM and 0.87 +/- 0.41 nmoles x min(-1) mg(-1).	Carbocysteine	97-101	phenylalanine hydroxylase	Homo sapiens	113-116
19326770-6	2008	A linear correlation was seen in the production of Tyr and SCMC R/S S-oxide in 20 individual female hepatic cytosolic fractions for both substrate and lysophosphatidylcholine activated PAH (r(s) > 0.96).	Tyrosine	51-54	phenylalanine hydroxylase	Homo sapiens	185-188
17935162-2	2008	Tetrahydrobiopterin (BH(4))-responsive hyperphenylalaninemia has been recently described as a variant of PAH deficiency caused by specific mutations in the PAH gene.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	105-108
17935162-2	2008	Tetrahydrobiopterin (BH(4))-responsive hyperphenylalaninemia has been recently described as a variant of PAH deficiency caused by specific mutations in the PAH gene.	sapropterin	21-27	phenylalanine hydroxylase	Homo sapiens	105-108
17977740-6	2007	In patients suffering from phenylketonuria the hydroxylation of phenylalanine to tyrosine is defective due to lack of phenylalanine hydroxylase.	Tyrosine	81-89	phenylalanine hydroxylase	Homo sapiens	118-143
18049780-5	2007	In the gaseous phase, naphthalene (67-89%) was the most abundant PAH in all of the exhaust samples.	naphthalene	22-33	phenylalanine hydroxylase	Homo sapiens	65-68
18049780-7	2007	Pyrene is the most abundant particulate PAH in the Chinese restaurants (14-49%) while its contribution was much lower in the Western cooking style restaurants (10-22%).	pyrene	0-6	phenylalanine hydroxylase	Homo sapiens	40-43
17884650-0	2007	Effects of tetrahydrobiopterin and phenylalanine on in vivo human phenylalanine hydroxylase by phenylalanine breath test.	sapropterin	11-30	phenylalanine hydroxylase	Homo sapiens	66-91
17884650-0	2007	Effects of tetrahydrobiopterin and phenylalanine on in vivo human phenylalanine hydroxylase by phenylalanine breath test.	Phenylalanine	35-48	phenylalanine hydroxylase	Homo sapiens	66-91
17884650-1	2007	BH(4) administration results in the reduction of blood phenylalanine level in patients with tetrahydrobiopterin (BH(4))-responsive phenylalanine hydroxylase (PAH) deficiency.	sapropterin	92-111	phenylalanine hydroxylase	Homo sapiens	131-156
32900105-0	2007	The performance of poly(styrene)-block-poly(2-vinyl pyridine)-block-poly(styrene) triblock copolymers as pH-driven actuators.	poly(styrene)-block-poly(2-vinyl pyridine)-block-poly(styrene) triblock copolymers	19-101	phenylalanine hydroxylase	Homo sapiens	105-107
19326770-6	2008	A linear correlation was seen in the production of Tyr and SCMC R/S S-oxide in 20 individual female hepatic cytosolic fractions for both substrate and lysophosphatidylcholine activated PAH (r(s) > 0.96).	scmc r	59-65	phenylalanine hydroxylase	Homo sapiens	185-188
19326770-6	2008	A linear correlation was seen in the production of Tyr and SCMC R/S S-oxide in 20 individual female hepatic cytosolic fractions for both substrate and lysophosphatidylcholine activated PAH (r(s) > 0.96).	Oxides	68-75	phenylalanine hydroxylase	Homo sapiens	185-188
19326770-6	2008	A linear correlation was seen in the production of Tyr and SCMC R/S S-oxide in 20 individual female hepatic cytosolic fractions for both substrate and lysophosphatidylcholine activated PAH (r(s) > 0.96).	Lysophosphatidylcholines	151-174	phenylalanine hydroxylase	Homo sapiens	185-188
19326770-7	2008	Inhibitor studies found that the specific chemical and antibody inhibitors of PAH reduced the production of Tyr and SCMC R/S S-oxide in these in vitro PAH assays.	Tyrosine	108-111	phenylalanine hydroxylase	Homo sapiens	78-81
19326770-7	2008	Inhibitor studies found that the specific chemical and antibody inhibitors of PAH reduced the production of Tyr and SCMC R/S S-oxide in these in vitro PAH assays.	Tyrosine	108-111	phenylalanine hydroxylase	Homo sapiens	151-154
19326770-7	2008	Inhibitor studies found that the specific chemical and antibody inhibitors of PAH reduced the production of Tyr and SCMC R/S S-oxide in these in vitro PAH assays.	scmc r	116-122	phenylalanine hydroxylase	Homo sapiens	78-81
19326770-7	2008	Inhibitor studies found that the specific chemical and antibody inhibitors of PAH reduced the production of Tyr and SCMC R/S S-oxide in these in vitro PAH assays.	scmc r	116-122	phenylalanine hydroxylase	Homo sapiens	151-154
19326770-7	2008	Inhibitor studies found that the specific chemical and antibody inhibitors of PAH reduced the production of Tyr and SCMC R/S S-oxide in these in vitro PAH assays.	Oxides	123-132	phenylalanine hydroxylase	Homo sapiens	78-81
19326770-7	2008	Inhibitor studies found that the specific chemical and antibody inhibitors of PAH reduced the production of Tyr and SCMC R/S S-oxide in these in vitro PAH assays.	Oxides	123-132	phenylalanine hydroxylase	Homo sapiens	151-154
19326770-8	2008	An investigation of the mechanism of interaction of SCMC with PAH indicated that the drug was a competitive inhibitor of the aromatic C-oxidation of Phe with a calculated K(i) of 17.23 +/- 4.15 mM.	Carbocysteine	52-56	phenylalanine hydroxylase	Homo sapiens	62-65
19326770-8	2008	An investigation of the mechanism of interaction of SCMC with PAH indicated that the drug was a competitive inhibitor of the aromatic C-oxidation of Phe with a calculated K(i) of 17.23 +/- 4.15 mM.	Phenylalanine	149-152	phenylalanine hydroxylase	Homo sapiens	62-65
19326770-9	2008	The requirement of BH4 as cofactor and the lack of effect of the specific tyrosine hydroxylase, tryptophan hydroxylase and nitric oxide synthase inhibitors on the S-oxidation of SCMC all indicate that PAH was the enzyme responsible for this biotransformation reaction in human hepatic cytosolic fractions.	Carbocysteine	178-182	phenylalanine hydroxylase	Homo sapiens	201-204
18022071-1	2007	BACKGROUND: Sildenafil is a selective inhibitor of phosphodiesterase type 5 (PDE5), and has been shown to improve 6-minute walk distance (SMWD) and World Health Organization (WHO) functional class in patients with idiopathic pulmonary arterial hypertension (iPAH) and PAH associated with connective tissue disease or with repaired congenital systemic-to-pulmonary shunts.	Sildenafil Citrate	12-22	phenylalanine hydroxylase	Homo sapiens	259-262
17968763-1	2007	Phenylketonuria (PKU) and mild hyperphenylalaninemia (HPA) are genetic disorders characterized by a deficiency in phenylalanine hydroxylase (PAH), resulting in intellectual impairment if not treated with dietary restriction of phenylalanine intake.	Phenylalanine	36-49	phenylalanine hydroxylase	Homo sapiens	141-144
17968763-2	2007	Sapropterin dihydrochloride (Kuvan) is an orally active synthetic form of (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4; a cofactor for PAH) that has received Orphan Drug status and Fast Track designation for the treatment of PKU.	sapropterin	0-27	phenylalanine hydroxylase	Homo sapiens	138-141
17968763-2	2007	Sapropterin dihydrochloride (Kuvan) is an orally active synthetic form of (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4; a cofactor for PAH) that has received Orphan Drug status and Fast Track designation for the treatment of PKU.	sapropterin	29-34	phenylalanine hydroxylase	Homo sapiens	138-141
17968763-2	2007	Sapropterin dihydrochloride (Kuvan) is an orally active synthetic form of (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4; a cofactor for PAH) that has received Orphan Drug status and Fast Track designation for the treatment of PKU.	sapropterin	74-116	phenylalanine hydroxylase	Homo sapiens	138-141
17968763-2	2007	Sapropterin dihydrochloride (Kuvan) is an orally active synthetic form of (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4; a cofactor for PAH) that has received Orphan Drug status and Fast Track designation for the treatment of PKU.	sapropterin	118-121	phenylalanine hydroxylase	Homo sapiens	138-141
18022071-3	2007	METHODS: We studied 14 patients on long-term subcutaneous treprostinil for PAH (from a cohort of 51 patients [27%]), who wished to discontinue treatment because of injection-site pain.	treprostinil	58-70	phenylalanine hydroxylase	Homo sapiens	75-78
17603758-1	2007	The response to tetrahydrobiopterin (BH4) in patients with phenylalanine hydroxylase (PAH, EC 1.14.16.1) deficiency (OMIM 261600) has been widely reported.	sapropterin	16-35	phenylalanine hydroxylase	Homo sapiens	59-84
17603758-1	2007	The response to tetrahydrobiopterin (BH4) in patients with phenylalanine hydroxylase (PAH, EC 1.14.16.1) deficiency (OMIM 261600) has been widely reported.	sapropterin	16-35	phenylalanine hydroxylase	Homo sapiens	86-89
17603758-1	2007	The response to tetrahydrobiopterin (BH4) in patients with phenylalanine hydroxylase (PAH, EC 1.14.16.1) deficiency (OMIM 261600) has been widely reported.	sapropterin	37-40	phenylalanine hydroxylase	Homo sapiens	59-84
17603758-1	2007	The response to tetrahydrobiopterin (BH4) in patients with phenylalanine hydroxylase (PAH, EC 1.14.16.1) deficiency (OMIM 261600) has been widely reported.	sapropterin	37-40	phenylalanine hydroxylase	Homo sapiens	86-89
17603758-6	2007	Of particular interest were positive responses in two patients with classic PKU, and in one patient with mutations of the phenylalanine hydroxylase (PAH) gene that have not to date been reported to be BH4-responsive (p.S303A and p.G46S).	sapropterin	201-204	phenylalanine hydroxylase	Homo sapiens	122-147
17603758-6	2007	Of particular interest were positive responses in two patients with classic PKU, and in one patient with mutations of the phenylalanine hydroxylase (PAH) gene that have not to date been reported to be BH4-responsive (p.S303A and p.G46S).	sapropterin	201-204	phenylalanine hydroxylase	Homo sapiens	149-152
17443661-5	2007	The PAH enzyme converts phenylalanine to tyrosine in the presence of molecular oxygen and catalytic amounts of tetrahydrobiopterin (BH4), its nonprotein cofactor.	Phenylalanine	24-37	phenylalanine hydroxylase	Homo sapiens	4-7
17570467-5	2007	Two- and 3-ring PAHs (methylnaphthalene, fluorene, phenanthrene and anthracene) were the main compounds found in most sites, although total PAH concentrations showed relatively low levels compared with other human-impacted areas in Antarctica.	1-methylnaphthalene	22-39	phenylalanine hydroxylase	Homo sapiens	16-19
17570467-5	2007	Two- and 3-ring PAHs (methylnaphthalene, fluorene, phenanthrene and anthracene) were the main compounds found in most sites, although total PAH concentrations showed relatively low levels compared with other human-impacted areas in Antarctica.	fluorene	41-49	phenylalanine hydroxylase	Homo sapiens	16-19
17570467-5	2007	Two- and 3-ring PAHs (methylnaphthalene, fluorene, phenanthrene and anthracene) were the main compounds found in most sites, although total PAH concentrations showed relatively low levels compared with other human-impacted areas in Antarctica.	phenanthrene	51-63	phenylalanine hydroxylase	Homo sapiens	16-19
17570467-5	2007	Two- and 3-ring PAHs (methylnaphthalene, fluorene, phenanthrene and anthracene) were the main compounds found in most sites, although total PAH concentrations showed relatively low levels compared with other human-impacted areas in Antarctica.	anthracene	68-78	phenylalanine hydroxylase	Homo sapiens	16-19
17443661-5	2007	The PAH enzyme converts phenylalanine to tyrosine in the presence of molecular oxygen and catalytic amounts of tetrahydrobiopterin (BH4), its nonprotein cofactor.	Tyrosine	41-49	phenylalanine hydroxylase	Homo sapiens	4-7
17443661-5	2007	The PAH enzyme converts phenylalanine to tyrosine in the presence of molecular oxygen and catalytic amounts of tetrahydrobiopterin (BH4), its nonprotein cofactor.	Oxygen	79-85	phenylalanine hydroxylase	Homo sapiens	4-7
17443661-5	2007	The PAH enzyme converts phenylalanine to tyrosine in the presence of molecular oxygen and catalytic amounts of tetrahydrobiopterin (BH4), its nonprotein cofactor.	sapropterin	111-130	phenylalanine hydroxylase	Homo sapiens	4-7
17443661-5	2007	The PAH enzyme converts phenylalanine to tyrosine in the presence of molecular oxygen and catalytic amounts of tetrahydrobiopterin (BH4), its nonprotein cofactor.	sapropterin	132-135	phenylalanine hydroxylase	Homo sapiens	4-7
17627389-0	2007	Mutations in the regulatory domain of phenylalanine hydroxylase and response to tetrahydrobiopterin.	sapropterin	80-99	phenylalanine hydroxylase	Homo sapiens	38-63
17658743-0	2007	Interaction energies between tetrahydrobiopterin analogues and aromatic residues in tyrosine hydroxylase and phenylalanine hydroxylase.	sapropterin	29-48	phenylalanine hydroxylase	Homo sapiens	109-134
17658743-2	2007	The residues phenylalanine 254 and tyrosine 325 similarly aid in binding BH4 in phenylalanine hydroxylase.	Phenylalanine	13-26	phenylalanine hydroxylase	Homo sapiens	80-105
17658743-2	2007	The residues phenylalanine 254 and tyrosine 325 similarly aid in binding BH4 in phenylalanine hydroxylase.	Tyrosine	35-43	phenylalanine hydroxylase	Homo sapiens	80-105
17658743-2	2007	The residues phenylalanine 254 and tyrosine 325 similarly aid in binding BH4 in phenylalanine hydroxylase.	sapropterin	73-76	phenylalanine hydroxylase	Homo sapiens	80-105
17565982-6	2007	PAH is a key enzyme in the metabolic pathway of phenylalanine.	Phenylalanine	48-61	phenylalanine hydroxylase	Homo sapiens	0-3
17680344-1	2007	In recent years several studies on tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency have been published.	sapropterin	35-54	phenylalanine hydroxylase	Homo sapiens	72-97
17680344-1	2007	In recent years several studies on tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency have been published.	sapropterin	56-59	phenylalanine hydroxylase	Homo sapiens	72-97
17627389-2	2007	The present study was aimed at understanding the effect of BH4 on mutations in the regulatory domain of phenylalanine hydroxylase (PAH).	sapropterin	59-62	phenylalanine hydroxylase	Homo sapiens	104-129
17445838-2	2007	Populations exposed to environmental air pollution show increased levels of PAH DNA adducts and it has been postulated that another contributing cause of carcinogenicity by environmental air pollution may be the production of reactive oxygen species following oxidative stress leading to oxidative DNA damage.	Reactive Oxygen Species	226-249	phenylalanine hydroxylase	Homo sapiens	76-79
17616875-3	2007	The total PAH levels in water samples from all the sampling stations (except at station WB 11), were sufficiently high (> 10 microg/L) to cause acute toxicity to the exposed organisms.	Water	24-29	phenylalanine hydroxylase	Homo sapiens	10-13
17445838-7	2007	The interesting finding from this study was the significant negative correlation between the level of 8-oxodG adducts and the level of total PAH (bulky) and B[a]P DNA adducts implying that the repair of oxidative DNA damage may be enhanced.	8-ohdg	102-109	phenylalanine hydroxylase	Homo sapiens	141-144
17381124-4	2007	The main difference between these two classes of cachacas is in the quantitative profile of the most potent carcinogenic PAH, benzo[a]pyrene, which is more abundant in cachaca produced from burned sugar cane crops (4.54 x 10(-2) microg L(-1)) than in cachaca produced from nonburned crops (9.02 x 10(-3) microg L(-1)).	Benzo(a)pyrene	126-140	phenylalanine hydroxylase	Homo sapiens	121-124
17554422-0	2007	Prediction of PAH biodegradation in field contaminated soils using a cyclodextrin extraction technique.	Cyclodextrins	69-81	phenylalanine hydroxylase	Homo sapiens	14-17
17554422-5	2007	The amounts of PAHs degraded by the catabolic activity of the indigenous microflora in each of the soils were correlated with HPCD-extractable PAH concentrations.	2-Hydroxypropyl-beta-cyclodextrin	126-130	phenylalanine hydroxylase	Homo sapiens	15-18
17513427-3	2007	Phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase all require tetrahydrobiopterin (BH4) as a cofactor.	sapropterin	88-107	phenylalanine hydroxylase	Homo sapiens	0-25
17513427-3	2007	Phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase all require tetrahydrobiopterin (BH4) as a cofactor.	sapropterin	109-112	phenylalanine hydroxylase	Homo sapiens	0-25
17557244-1	2007	OBJECTIVE: To analyze characteristics of different hyperphenylalaninemia (HPA) and to discuss the clinical difference between southern and northern Chinese patients with tetrahydrobiopterin (BH4) responsive phenylalanine hydroxylase (PAH) deficiency.	sapropterin	170-189	phenylalanine hydroxylase	Homo sapiens	207-232
17557244-1	2007	OBJECTIVE: To analyze characteristics of different hyperphenylalaninemia (HPA) and to discuss the clinical difference between southern and northern Chinese patients with tetrahydrobiopterin (BH4) responsive phenylalanine hydroxylase (PAH) deficiency.	sapropterin	170-189	phenylalanine hydroxylase	Homo sapiens	234-237
17557244-1	2007	OBJECTIVE: To analyze characteristics of different hyperphenylalaninemia (HPA) and to discuss the clinical difference between southern and northern Chinese patients with tetrahydrobiopterin (BH4) responsive phenylalanine hydroxylase (PAH) deficiency.	sapropterin	191-194	phenylalanine hydroxylase	Homo sapiens	207-232
17557244-1	2007	OBJECTIVE: To analyze characteristics of different hyperphenylalaninemia (HPA) and to discuss the clinical difference between southern and northern Chinese patients with tetrahydrobiopterin (BH4) responsive phenylalanine hydroxylase (PAH) deficiency.	sapropterin	191-194	phenylalanine hydroxylase	Homo sapiens	234-237
17557244-8	2007	RESULTS: (1)Among the 108 HPA cases, 36 patients (33.3%) were BH4 responsive PAH deficiency, 49 (45.4%) were non-BH4 no responsive phenylketonuria (PKU)and 23(21.3%)were BH4 deficiency (BH4D).	sapropterin	62-65	phenylalanine hydroxylase	Homo sapiens	77-80
17557244-9	2007	The Phe concentration of patients with BH4 responsive PAH deficiency decreased by 49.24% and 65.35% at 8 h and 24 h after oral BH4, 23 in southern group and 13 in northern group among 36 patients.	Phenylalanine	4-7	phenylalanine hydroxylase	Homo sapiens	54-57
17557244-9	2007	The Phe concentration of patients with BH4 responsive PAH deficiency decreased by 49.24% and 65.35% at 8 h and 24 h after oral BH4, 23 in southern group and 13 in northern group among 36 patients.	sapropterin	39-42	phenylalanine hydroxylase	Homo sapiens	54-57
17557244-9	2007	The Phe concentration of patients with BH4 responsive PAH deficiency decreased by 49.24% and 65.35% at 8 h and 24 h after oral BH4, 23 in southern group and 13 in northern group among 36 patients.	sapropterin	127-130	phenylalanine hydroxylase	Homo sapiens	54-57
17557244-11	2007	CONCLUSION: Most of mild and moderate HPA patients affected by PAH deficiency show plasma Phe concentration decrease >30% in 24 h after oral BH4 20 mg/kg, few are classic PKU.	Phenylalanine	90-93	phenylalanine hydroxylase	Homo sapiens	63-66
17557244-11	2007	CONCLUSION: Most of mild and moderate HPA patients affected by PAH deficiency show plasma Phe concentration decrease >30% in 24 h after oral BH4 20 mg/kg, few are classic PKU.	sapropterin	144-147	phenylalanine hydroxylase	Homo sapiens	63-66
17408607-1	2007	BACKGROUND: Tetrahydrobiopterin (BH4), cofactor of phenylalanine hydroxylase, can be used to treat a subset of phenylketonuria (PKU) patients as it results in a reduction in blood phenylalanine levels.	sapropterin	12-31	phenylalanine hydroxylase	Homo sapiens	51-76
17408607-1	2007	BACKGROUND: Tetrahydrobiopterin (BH4), cofactor of phenylalanine hydroxylase, can be used to treat a subset of phenylketonuria (PKU) patients as it results in a reduction in blood phenylalanine levels.	sapropterin	33-36	phenylalanine hydroxylase	Homo sapiens	51-76
17382369-0	2007	Ozone pre-treatment as improver of PAH removal during anaerobic digestion of urban sludge.	Ozone	0-5	phenylalanine hydroxylase	Homo sapiens	35-38
17382369-7	2007	Finally, addition of tyloxapol before sludge ozone pre-treatment had antagonist effects on PAH removal during anaerobic digestion: negative impact on anaerobic ecosystem activity and improvement of PAH bioaccessibility (particularly the PAHs with the highest octanol water partition coefficients).	tyloxapol	21-30	phenylalanine hydroxylase	Homo sapiens	91-94
17382369-7	2007	Finally, addition of tyloxapol before sludge ozone pre-treatment had antagonist effects on PAH removal during anaerobic digestion: negative impact on anaerobic ecosystem activity and improvement of PAH bioaccessibility (particularly the PAHs with the highest octanol water partition coefficients).	tyloxapol	21-30	phenylalanine hydroxylase	Homo sapiens	198-201
17071945-4	2007	Benzo(g,h,i)perylene (BghiP), an indicator of automobile exhaust emission, was the predominant PAH.	1,12-benzoperylene	0-20	phenylalanine hydroxylase	Homo sapiens	95-98
17071945-4	2007	Benzo(g,h,i)perylene (BghiP), an indicator of automobile exhaust emission, was the predominant PAH.	1,12-benzoperylene	22-27	phenylalanine hydroxylase	Homo sapiens	95-98
17258279-2	2007	The results indicated a significant contribution of tobacco smoke to the PAH contamination of milk: the condensate contained in the cigarettes smoked daily by each subject was strongly related with the polynuclear hydrocarbon content (R(2)=0.92, P<0.005).	Hydrocarbons	214-225	phenylalanine hydroxylase	Homo sapiens	73-76
17169401-5	2007	For the aqueous PAH-solutions, we observed reduced light inhibition values for the miniaturised bioassay when using black microplates made of polypropylene (PP) and polystyrene (PS) compared to the standard LUMIStox test.	Polypropylenes	142-155	phenylalanine hydroxylase	Homo sapiens	16-19
17258279-5	2007	The risk evaluation due to PAH ingestion via breast milk was assessed on the basis of the acceptable daily intake of Benzo(a)pyrene in drinking water, evidencing that a hazard cannot be excluded for heavy smokers residing in urban areas.	Benzo(a)pyrene	117-131	phenylalanine hydroxylase	Homo sapiens	27-30
17169401-5	2007	For the aqueous PAH-solutions, we observed reduced light inhibition values for the miniaturised bioassay when using black microplates made of polypropylene (PP) and polystyrene (PS) compared to the standard LUMIStox test.	Polystyrenes	165-176	phenylalanine hydroxylase	Homo sapiens	16-19
17169401-5	2007	For the aqueous PAH-solutions, we observed reduced light inhibition values for the miniaturised bioassay when using black microplates made of polypropylene (PP) and polystyrene (PS) compared to the standard LUMIStox test.	Polystyrenes	178-180	phenylalanine hydroxylase	Homo sapiens	16-19
17365288-6	2007	The products obtained by the solar radiation of PAH after extraction to DCM were mainly ketone and hydroxyl derivatives.	Hydroxyl Radical	99-107	phenylalanine hydroxylase	Homo sapiens	48-51
17454117-0	2007	Polycyclic aromatic hydrocarbons (PAHs) in meat products and estimated PAH intake by children and the general population in Estonia.	Polycyclic Aromatic Hydrocarbons	0-32	phenylalanine hydroxylase	Homo sapiens	34-37
16676991-0	2006	EPR and UV-vis studies of the nitric oxide adducts of bacterial phenylalanine hydroxylase: effects of cofactor and substrate on the iron environment.	Nitric Oxide	30-42	phenylalanine hydroxylase	Homo sapiens	64-89
17207845-0	2007	Co-variations of bacterial composition and catabolic genes related to PAH degradation in a produced water treatment system consisting of successive anoxic and aerobic units.	Water	100-105	phenylalanine hydroxylase	Homo sapiens	70-73
17207845-6	2007	The existence of nahAc and C23O genes in the influent and the high similarity of genotype between the influent and the two sludge samples suggested that bacteria existing in the influent contributed to PAH removal and bacteria harboring PAH catabolic genes were enriched in the sludge.	nahac	17-22	phenylalanine hydroxylase	Homo sapiens	202-205
17162569-2	2007	The degradation rates of PAH were in the order: acenaphthene > fluorene > phenanthrene > anthracene > pyrene.	acenaphthene	48-60	phenylalanine hydroxylase	Homo sapiens	25-28
17162569-2	2007	The degradation rates of PAH were in the order: acenaphthene > fluorene > phenanthrene > anthracene > pyrene.	fluorene	66-74	phenylalanine hydroxylase	Homo sapiens	25-28
17162569-2	2007	The degradation rates of PAH were in the order: acenaphthene > fluorene > phenanthrene > anthracene > pyrene.	phenanthrene	80-92	phenylalanine hydroxylase	Homo sapiens	25-28
17162569-2	2007	The degradation rates of PAH were in the order: acenaphthene > fluorene > phenanthrene > anthracene > pyrene.	anthracene	98-108	phenylalanine hydroxylase	Homo sapiens	25-28
17162569-2	2007	The degradation rates of PAH were in the order: acenaphthene > fluorene > phenanthrene > anthracene > pyrene.	pyrene	114-120	phenylalanine hydroxylase	Homo sapiens	25-28
17162569-4	2007	Comparison of the PAH degradation rates under three reducing conditions showed the following order: sulfate-reducing conditions > methanogenic conditions > nitrate-reducing conditions.	Sulfates	100-107	phenylalanine hydroxylase	Homo sapiens	18-21
17162569-4	2007	Comparison of the PAH degradation rates under three reducing conditions showed the following order: sulfate-reducing conditions > methanogenic conditions > nitrate-reducing conditions.	Nitrates	162-169	phenylalanine hydroxylase	Homo sapiens	18-21
17162569-5	2007	The addition of electron donors (acetate, lactate and pyruvate) enhanced PAH degradation under methanogenic and sulfate-reducing conditions.	Acetates	33-40	phenylalanine hydroxylase	Homo sapiens	73-76
17162569-5	2007	The addition of electron donors (acetate, lactate and pyruvate) enhanced PAH degradation under methanogenic and sulfate-reducing conditions.	Lactic Acid	42-49	phenylalanine hydroxylase	Homo sapiens	73-76
17162569-5	2007	The addition of electron donors (acetate, lactate and pyruvate) enhanced PAH degradation under methanogenic and sulfate-reducing conditions.	Pyruvic Acid	54-62	phenylalanine hydroxylase	Homo sapiens	73-76
17162569-5	2007	The addition of electron donors (acetate, lactate and pyruvate) enhanced PAH degradation under methanogenic and sulfate-reducing conditions.	Sulfates	112-119	phenylalanine hydroxylase	Homo sapiens	73-76
17162569-6	2007	However, the addition of acetate, lactate or pyruvate inhibited PAH degradation under nitrate-reducing conditions.	Acetates	25-32	phenylalanine hydroxylase	Homo sapiens	64-67
17162569-6	2007	However, the addition of acetate, lactate or pyruvate inhibited PAH degradation under nitrate-reducing conditions.	Lactic Acid	34-41	phenylalanine hydroxylase	Homo sapiens	64-67
17162569-6	2007	However, the addition of acetate, lactate or pyruvate inhibited PAH degradation under nitrate-reducing conditions.	Pyruvic Acid	45-53	phenylalanine hydroxylase	Homo sapiens	64-67
17162569-6	2007	However, the addition of acetate, lactate or pyruvate inhibited PAH degradation under nitrate-reducing conditions.	Nitrates	86-93	phenylalanine hydroxylase	Homo sapiens	64-67
17162569-7	2007	The addition of heavy metals, nonylphenol and phthalate esters (PAEs) inhibited PAH degradation.	nonylphenol	30-41	phenylalanine hydroxylase	Homo sapiens	80-83
17162569-7	2007	The addition of heavy metals, nonylphenol and phthalate esters (PAEs) inhibited PAH degradation.	phthalate esters	46-62	phenylalanine hydroxylase	Homo sapiens	80-83
17162569-7	2007	The addition of heavy metals, nonylphenol and phthalate esters (PAEs) inhibited PAH degradation.	phenyl-2-aminoethyl sulfide	64-68	phenylalanine hydroxylase	Homo sapiens	80-83
17162569-8	2007	Our results show that sulfate-reducing bacteria, methanogen and eubacteria are involved in the degradation of PAH; sulfate-reducing bacteria constitute a major microbial component in PAH degradation.	Sulfates	22-29	phenylalanine hydroxylase	Homo sapiens	110-113
17162569-8	2007	Our results show that sulfate-reducing bacteria, methanogen and eubacteria are involved in the degradation of PAH; sulfate-reducing bacteria constitute a major microbial component in PAH degradation.	Sulfates	22-29	phenylalanine hydroxylase	Homo sapiens	183-186
17162569-8	2007	Our results show that sulfate-reducing bacteria, methanogen and eubacteria are involved in the degradation of PAH; sulfate-reducing bacteria constitute a major microbial component in PAH degradation.	Sulfates	115-122	phenylalanine hydroxylase	Homo sapiens	110-113
17162569-8	2007	Our results show that sulfate-reducing bacteria, methanogen and eubacteria are involved in the degradation of PAH; sulfate-reducing bacteria constitute a major microbial component in PAH degradation.	Sulfates	115-122	phenylalanine hydroxylase	Homo sapiens	183-186
16842825-0	2006	Molecular and stable carbon isotopic characterization of PAH contaminants at McMurdo Station, Antarctica.	Carbon	21-27	phenylalanine hydroxylase	Homo sapiens	57-60
16564118-4	2006	The efficacy of the HPCD-extraction technique for the estimation of PAH microbial availability in soil is demonstrated in the presence of co-contaminants that have been aged for the duration of the experiment together in the soil.	2-Hydroxypropyl-beta-cyclodextrin	20-24	phenylalanine hydroxylase	Homo sapiens	68-71
16564118-6	2006	Overall, a single HPCD-extraction technique proved accurate and reproducible for the estimation of PAH bioavailability from soil.	2-Hydroxypropyl-beta-cyclodextrin	18-22	phenylalanine hydroxylase	Homo sapiens	99-102
16765994-0	2006	The importance of arginine mutation for the evolutionary structure and function of phenylalanine hydroxylase gene.	Arginine	18-26	phenylalanine hydroxylase	Homo sapiens	83-108
16765994-4	2006	In many countries, Arginine mutations have the highest frequency among PAH gene mutations in PKU patients.	Arginine	19-27	phenylalanine hydroxylase	Homo sapiens	71-74
16765994-6	2006	In our analyses, we have detected that a majority of mutations causing a change in arginine and other amino acids concentrated in exon 7 comprising the catalytic domain (residues 143-410) of PAH gene.	Arginine	83-91	phenylalanine hydroxylase	Homo sapiens	191-194
16765994-8	2006	Therefore, the role of arginine amino acid in PAH gene is rather remarkable in that it shows the role of amino acids in the protein/RNA interaction that has started in the evolutionary process and is still preserved and maintained in the motif formation of active domain structure due to its strong binding properties.	arginine amino acid	23-42	phenylalanine hydroxylase	Homo sapiens	46-49
16916019-8	2006	Polyethylene strips proved to be an excellent, low-cost tool for determining the PAH patterns in a large watershed.	Polyethylene	0-12	phenylalanine hydroxylase	Homo sapiens	81-84
17365288-5	2007	Deuterium water also hastened the decomposition of PAH.	Deuterium	0-9	phenylalanine hydroxylase	Homo sapiens	51-54
17365288-5	2007	Deuterium water also hastened the decomposition of PAH.	Water	10-15	phenylalanine hydroxylase	Homo sapiens	51-54
17365288-6	2007	The products obtained by the solar radiation of PAH after extraction to DCM were mainly ketone and hydroxyl derivatives.	dcm	72-75	phenylalanine hydroxylase	Homo sapiens	48-51
17365288-6	2007	The products obtained by the solar radiation of PAH after extraction to DCM were mainly ketone and hydroxyl derivatives.	Ketones	88-94	phenylalanine hydroxylase	Homo sapiens	48-51
17157453-8	2007	Urinary 1-hydroxypyrene, a metabolite of PAH, was also significantly higher, while PAH-DNA adducts in lymphocytes were five-fold higher in Bangkok school children than rural school children.	1-hydroxypyrene	8-23	phenylalanine hydroxylase	Homo sapiens	41-44
17157453-13	2007	Genetic polymorphisms have been detected in glutathione-S-transferases (GSTs) and cytochrome P450 (CYP450) enzymes involved in the metabolism of benzene and PAHs, but these polymorphisms had no significant effects on the biomarkers of PAH exposure.	Benzene	145-152	phenylalanine hydroxylase	Homo sapiens	157-160
32680266-1	2007	Colloids with graduated fluorescence intensities were fabricated by means of layer-wise adsorption of fluorescein isothiocyanate-labelled poly(allyl amine hydrochloride) (FITC-PAH) together with poly(styrene sulfonate) (PSS) on silica particles.	polyallylamine	138-169	phenylalanine hydroxylase	Homo sapiens	176-179
17112485-1	2007	Phenylketonuria (PKU) is a common genetic disorder in humans that arises from deficient activity of phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine.	Tyrosine	184-192	phenylalanine hydroxylase	Homo sapiens	100-125
16950911-9	2006	We also cultivated isolates from the polluted sediments that could transform the model PAH compound, phenanthrene.	phenanthrene	101-113	phenylalanine hydroxylase	Homo sapiens	87-90
16527332-7	2006	The concentration of PAH decreased in the order chrysene > benzo(b)fluoranthene > fluoranthene.	chrysene	48-56	phenylalanine hydroxylase	Homo sapiens	21-24
16527332-7	2006	The concentration of PAH decreased in the order chrysene > benzo(b)fluoranthene > fluoranthene.	benzo(b)	62-70	phenylalanine hydroxylase	Homo sapiens	21-24
16527332-7	2006	The concentration of PAH decreased in the order chrysene > benzo(b)fluoranthene > fluoranthene.	fluoranthene	70-82	phenylalanine hydroxylase	Homo sapiens	21-24
16527332-7	2006	The concentration of PAH decreased in the order chrysene > benzo(b)fluoranthene > fluoranthene.	fluoranthene	88-100	phenylalanine hydroxylase	Homo sapiens	21-24
17051797-2	2006	Organic carbon and PAH transfer from coal tar particles to water was investigated with closed-looped laboratory column experiments run at various particle sizes and temperatures.	Water	59-64	phenylalanine hydroxylase	Homo sapiens	19-22
16935936-0	2006	Specific interaction of the diastereomers 7(R)- and 7(S)-tetrahydrobiopterin with phenylalanine hydroxylase: implications for understanding primapterinuria and vitiligo.	7(r)- and 7(s)-tetrahydrobiopterin	42-76	phenylalanine hydroxylase	Homo sapiens	82-107
16935936-1	2006	Pterin-4a-carbinolamine dehydratase (PCD) is an essential component of the phenylalanine hydroxylase (PAH) system, catalyzing the regeneration of the essential cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin [6(R)BH4].	sapropterin	183-211	phenylalanine hydroxylase	Homo sapiens	75-100
16935936-1	2006	Pterin-4a-carbinolamine dehydratase (PCD) is an essential component of the phenylalanine hydroxylase (PAH) system, catalyzing the regeneration of the essential cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin [6(R)BH4].	sapropterin	183-211	phenylalanine hydroxylase	Homo sapiens	102-105
16935936-1	2006	Pterin-4a-carbinolamine dehydratase (PCD) is an essential component of the phenylalanine hydroxylase (PAH) system, catalyzing the regeneration of the essential cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin [6(R)BH4].	sapropterin	213-220	phenylalanine hydroxylase	Homo sapiens	75-100
16935936-1	2006	Pterin-4a-carbinolamine dehydratase (PCD) is an essential component of the phenylalanine hydroxylase (PAH) system, catalyzing the regeneration of the essential cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin [6(R)BH4].	sapropterin	213-220	phenylalanine hydroxylase	Homo sapiens	102-105
16935936-2	2006	Mutations in PCD or its deactivation by hydrogen peroxide result in the generation of 7(R,S)BH4, which is a potent inhibitor of PAH that has been implicated in primapterinuria, a variant form of phenylketonuria, and in the skin depigmentation disorder vitiligo.	Hydrogen Peroxide	40-57	phenylalanine hydroxylase	Homo sapiens	128-131
16935936-2	2006	Mutations in PCD or its deactivation by hydrogen peroxide result in the generation of 7(R,S)BH4, which is a potent inhibitor of PAH that has been implicated in primapterinuria, a variant form of phenylketonuria, and in the skin depigmentation disorder vitiligo.	7(r,s)bh4	86-95	phenylalanine hydroxylase	Homo sapiens	128-131
16935936-4	2006	Both 7(R)- and 7(S)BH4 function as poor cofactors for PAH, whereas only 7(S)BH4 acts as a potent competitive inhibitor vs. 6(R)BH4 (Ki=2.3-4.9 microM).	sapropterin	19-22	phenylalanine hydroxylase	Homo sapiens	54-57
16935936-4	2006	Both 7(R)- and 7(S)BH4 function as poor cofactors for PAH, whereas only 7(S)BH4 acts as a potent competitive inhibitor vs. 6(R)BH4 (Ki=2.3-4.9 microM).	7(s)bh4	15-22	phenylalanine hydroxylase	Homo sapiens	54-57
16935936-5	2006	Kinetic and binding studies, as well as characterization of the pterin-enzyme complexes by fluorescence spectroscopy, revealed that the inhibitory effects of 7(R,S)BH4 on PAH are in fact specifically based on 7(S)BH4 binding.	7(r,s)bh4	158-167	phenylalanine hydroxylase	Homo sapiens	171-174
16935936-5	2006	Kinetic and binding studies, as well as characterization of the pterin-enzyme complexes by fluorescence spectroscopy, revealed that the inhibitory effects of 7(R,S)BH4 on PAH are in fact specifically based on 7(S)BH4 binding.	7(s)bh4	209-216	phenylalanine hydroxylase	Homo sapiens	171-174
16935936-6	2006	The molecular dynamics simulated structures of the pterin-PAH complexes indicate that 7(S)BH4 inhibition is due to its interaction with the polar region at the pterin binding site close to Ser-251, whereas its low efficiency as cofactor is related to a suboptimal positioning toward the catalytic iron.	Pterins	51-57	phenylalanine hydroxylase	Homo sapiens	58-61
16935936-6	2006	The molecular dynamics simulated structures of the pterin-PAH complexes indicate that 7(S)BH4 inhibition is due to its interaction with the polar region at the pterin binding site close to Ser-251, whereas its low efficiency as cofactor is related to a suboptimal positioning toward the catalytic iron.	sapropterin	87-93	phenylalanine hydroxylase	Homo sapiens	58-61
16935936-6	2006	The molecular dynamics simulated structures of the pterin-PAH complexes indicate that 7(S)BH4 inhibition is due to its interaction with the polar region at the pterin binding site close to Ser-251, whereas its low efficiency as cofactor is related to a suboptimal positioning toward the catalytic iron.	Pterins	160-166	phenylalanine hydroxylase	Homo sapiens	58-61
16935936-6	2006	The molecular dynamics simulated structures of the pterin-PAH complexes indicate that 7(S)BH4 inhibition is due to its interaction with the polar region at the pterin binding site close to Ser-251, whereas its low efficiency as cofactor is related to a suboptimal positioning toward the catalytic iron.	Serine	189-192	phenylalanine hydroxylase	Homo sapiens	58-61
16935936-6	2006	The molecular dynamics simulated structures of the pterin-PAH complexes indicate that 7(S)BH4 inhibition is due to its interaction with the polar region at the pterin binding site close to Ser-251, whereas its low efficiency as cofactor is related to a suboptimal positioning toward the catalytic iron.	Iron	297-301	phenylalanine hydroxylase	Homo sapiens	58-61
16935936-8	2006	Taken together, our results identified structural determinants for the specific regulation of PAH and TH by 7(S)BH4, which in turn aid in the understanding of primapterinuria and acute vitiligo.	7(s)bh4	108-115	phenylalanine hydroxylase	Homo sapiens	94-97
16917891-8	2006	Examination of a representative region in exon 12 (and also in exon 7) in the PAH gene shows that 5 mC is restricted to cytosines in CpG dinucleotides in the hypermutable codons.	Methylcholanthrene	100-102	phenylalanine hydroxylase	Homo sapiens	78-81
16917891-8	2006	Examination of a representative region in exon 12 (and also in exon 7) in the PAH gene shows that 5 mC is restricted to cytosines in CpG dinucleotides in the hypermutable codons.	cytidylyl-3'-5'-guanosine	133-150	phenylalanine hydroxylase	Homo sapiens	78-81
16455197-3	2006	Main target of the study was to find out a method with which the PAH concentrations could be decreased below the Finnish guideline level for total PAHs.	Polycyclic Aromatic Hydrocarbons	147-151	phenylalanine hydroxylase	Homo sapiens	65-68
16721748-0	2006	Induction of the transferrin receptor gene by benzo[a]pyrene in breast cancer MCF-7 cells: potential as a biomarker of PAH exposure.	Benzo(a)pyrene	46-60	phenylalanine hydroxylase	Homo sapiens	119-122
16721748-4	2006	Using a GeneMAP CancerArray, we analyzed in breast cancer MCF-7 cells the temporal effects of the AhR agonist benzo[a]pyrene (B[a]P), which is a prototype PAH and known environmental carcinogen.	Benzo(a)pyrene	110-124	phenylalanine hydroxylase	Homo sapiens	155-158
16613835-6	2006	We exposed mouse (NMRI) E18 mandibular first and second molar explants to 7,12-dimethylbenz[a]anthracene (DMBA), a toxic PAH compound, in organ culture for 7 or 12 days.	7,12-dimethylbenz[a	74-93	phenylalanine hydroxylase	Homo sapiens	121-124
16613835-6	2006	We exposed mouse (NMRI) E18 mandibular first and second molar explants to 7,12-dimethylbenz[a]anthracene (DMBA), a toxic PAH compound, in organ culture for 7 or 12 days.	anthracene	94-104	phenylalanine hydroxylase	Homo sapiens	121-124
16613835-6	2006	We exposed mouse (NMRI) E18 mandibular first and second molar explants to 7,12-dimethylbenz[a]anthracene (DMBA), a toxic PAH compound, in organ culture for 7 or 12 days.	9,10-Dimethyl-1,2-benzanthracene	106-110	phenylalanine hydroxylase	Homo sapiens	121-124
16246473-4	2006	A factor analysis of the 18 different operational conditions under investigation indicated that the optimal operational conditions for degradation of PAHs occurred at MC 60%, S:GW 0.8:1 and T 38 degrees C. Thus, it is recommended to maintain operational conditions during in-vessel composting of PAH-solid waste close to these values.	Methylcholanthrene	167-169	phenylalanine hydroxylase	Homo sapiens	150-153
16246473-4	2006	A factor analysis of the 18 different operational conditions under investigation indicated that the optimal operational conditions for degradation of PAHs occurred at MC 60%, S:GW 0.8:1 and T 38 degrees C. Thus, it is recommended to maintain operational conditions during in-vessel composting of PAH-solid waste close to these values.	glycyltryptophan	177-179	phenylalanine hydroxylase	Homo sapiens	150-153
16676991-0	2006	EPR and UV-vis studies of the nitric oxide adducts of bacterial phenylalanine hydroxylase: effects of cofactor and substrate on the iron environment.	Iron	132-136	phenylalanine hydroxylase	Homo sapiens	64-89
16676991-1	2006	Phenylalanine hydroxylase from Chromobacterium violaceum (cPAH), which catalyzes phenylalanine oxidation to tyrosine, is homologous to the catalytic domain of eukaryotic PAHs.	Phenylalanine	81-94	phenylalanine hydroxylase	Homo sapiens	0-25
16676991-1	2006	Phenylalanine hydroxylase from Chromobacterium violaceum (cPAH), which catalyzes phenylalanine oxidation to tyrosine, is homologous to the catalytic domain of eukaryotic PAHs.	Tyrosine	108-116	phenylalanine hydroxylase	Homo sapiens	0-25
16423549-2	2006	In the cytoplasm it is an enzyme required for the regeneration of tetrahydrobiopterin, an essential cofactor for phenylalanine hydroxylase.	sapropterin	66-85	phenylalanine hydroxylase	Homo sapiens	113-138
16584268-1	2006	Multilayered manganese oxide nanocomposites intercalated with strong (poly(diallyldimethylammonium) chloride, PDDA) and weak (poly(allylamine hydrochloride), PAH) polyelectrolytes can be produced on polycrystalline platinum electrode in a thin film form by a simple, one-step electrochemical route.	manganese oxide	13-28	phenylalanine hydroxylase	Homo sapiens	158-161
16584268-4	2006	The layered film prepared with PAH has a larger polymer content (PAH/Mn molar ratio of 0.98) than that (PDDA/Mn molar ratio of 0.43) made with PDDA because of the smaller charging degree of PAH, exhibiting a larger interlayer distance (1.19 nm).	Polymers	48-55	phenylalanine hydroxylase	Homo sapiens	31-34
16584268-5	2006	The interlayer PAH contains neutral (-NH2) and positively charged (-NH3(+)) amine groups, and the -NH3(+) groups are associated with Cl- (to generate -NH3(+) Cl- ion pairs) as well as the negatively charged manganese oxide layers.	Amines	76-81	phenylalanine hydroxylase	Homo sapiens	15-18
16584268-5	2006	The interlayer PAH contains neutral (-NH2) and positively charged (-NH3(+)) amine groups, and the -NH3(+) groups are associated with Cl- (to generate -NH3(+) Cl- ion pairs) as well as the negatively charged manganese oxide layers.	manganese oxide	207-222	phenylalanine hydroxylase	Homo sapiens	15-18
16584268-8	2006	On the contrary, the layered PAH/MnO(x) film showed a good electrochemical response due to the redox reaction of Mn3+/Mn4+ couple with no change in the structure.	manganese(III) acetate dihydrate	113-117	phenylalanine hydroxylase	Homo sapiens	29-32
16584268-8	2006	On the contrary, the layered PAH/MnO(x) film showed a good electrochemical response due to the redox reaction of Mn3+/Mn4+ couple with no change in the structure.	Manganese	118-121	phenylalanine hydroxylase	Homo sapiens	29-32
16584268-9	2006	X-ray photoelectron spectroscopy revealed that, in this case, excess negative charges generated on the manganese oxide layers upon reduction can be balanced by the protons being released from the -NH3(+) Cl- sites in the interlayer PAH; the Cl- anions becoming unnecessary are inevitably excluded from the interlayer, and vice versa upon oxidation.	manganese oxide	103-118	phenylalanine hydroxylase	Homo sapiens	232-235
16584268-9	2006	X-ray photoelectron spectroscopy revealed that, in this case, excess negative charges generated on the manganese oxide layers upon reduction can be balanced by the protons being released from the -NH3(+) Cl- sites in the interlayer PAH; the Cl- anions becoming unnecessary are inevitably excluded from the interlayer, and vice versa upon oxidation.	Ammonia	197-200	phenylalanine hydroxylase	Homo sapiens	232-235
16504182-0	2006	Analysis of the effect of tetrahydrobiopterin on PAH gene expression in hepatoma cells.	sapropterin	26-45	phenylalanine hydroxylase	Homo sapiens	49-52
16646466-7	2006	Models of PAH adsorption using structures from molecular mechanics and energies from ab initio calculations do produce water-soot partitioning energies that correlate well with observed log(K(d)) values.	Water	119-124	phenylalanine hydroxylase	Homo sapiens	10-13
16504182-1	2006	Tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency is a recently recognized variant of phenylketonuria, with a probable multifactorial molecular basis.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	37-62
16504182-1	2006	Tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency is a recently recognized variant of phenylketonuria, with a probable multifactorial molecular basis.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	64-67
16504182-1	2006	Tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency is a recently recognized variant of phenylketonuria, with a probable multifactorial molecular basis.	sapropterin	21-24	phenylalanine hydroxylase	Homo sapiens	37-62
16504182-1	2006	Tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency is a recently recognized variant of phenylketonuria, with a probable multifactorial molecular basis.	sapropterin	21-24	phenylalanine hydroxylase	Homo sapiens	64-67
16504182-2	2006	In this study we have investigated the effect of BH4 on PAH gene expression in human hepatoma.	sapropterin	49-52	phenylalanine hydroxylase	Homo sapiens	56-59
16504182-3	2006	Our results show that increased BH4 levels result in an enhancement of PAH activity and PAH protein, due to longer turnover rates, while PAH mRNA levels remain unchanged.	sapropterin	32-35	phenylalanine hydroxylase	Homo sapiens	71-74
16504182-3	2006	Our results show that increased BH4 levels result in an enhancement of PAH activity and PAH protein, due to longer turnover rates, while PAH mRNA levels remain unchanged.	sapropterin	32-35	phenylalanine hydroxylase	Homo sapiens	88-91
16504182-3	2006	Our results show that increased BH4 levels result in an enhancement of PAH activity and PAH protein, due to longer turnover rates, while PAH mRNA levels remain unchanged.	sapropterin	32-35	phenylalanine hydroxylase	Homo sapiens	88-91
16504182-4	2006	This was confirmed for mutant PAH proteins (A309V, V388M and Y414C) associated to in vivo BH4 responsiveness, validating previous studies.	sapropterin	90-93	phenylalanine hydroxylase	Homo sapiens	30-33
16504182-5	2006	We can conclude that there is no effect of the cofactor on PAH gene transcription, probably being the chemical chaperone effect of BH4 stabilizing mutant PAH proteins the major underlying mechanism of the response.	sapropterin	131-134	phenylalanine hydroxylase	Homo sapiens	154-157
16402341-4	2006	Cumulatively these findings suggested that TD was related to phenylalanine metabolism and thus that sequence variants in the gene for phenylalanine hydroxylase (PAH), the rate-limiting enzyme in the catabolism of phenylalanine, could be associated with TD susceptibility.	Phenylalanine	61-74	phenylalanine hydroxylase	Homo sapiens	134-159
16219457-6	2006	A major finding was that the application of {PSS/PAH} films as thin as 12 nm can drastically improve the sensor performance over uncoated sensors based on calcium alginate microspheres.	Alginates	155-171	phenylalanine hydroxylase	Homo sapiens	49-52
16402341-4	2006	Cumulatively these findings suggested that TD was related to phenylalanine metabolism and thus that sequence variants in the gene for phenylalanine hydroxylase (PAH), the rate-limiting enzyme in the catabolism of phenylalanine, could be associated with TD susceptibility.	Phenylalanine	61-74	phenylalanine hydroxylase	Homo sapiens	161-164
16143554-10	2005	To understand the mechanism of response to BH4, the kinetics and stability of mutant PAH were studied.	sapropterin	43-46	phenylalanine hydroxylase	Homo sapiens	85-88
16253218-2	2006	We demonstrated PAH mutational spectrum from patients with PKU, including 10 novel and 3 tetrahydrobiopterin (BH(4))-responsive mutations.	sapropterin	89-108	phenylalanine hydroxylase	Homo sapiens	16-19
16253218-3	2006	In this study, 11 PAH missense mutations, including 6 novel mutations (P69S, G103S, L293M, G332V, S391I, A447P) found in our previous study, 2 mutations common in east Asian patients with PKU (R243Q, R413P), and 3 tetrahydrobiopterin (BH(4))-responsive mutations (R53H, R241C, R408Q) have been functionally and structurally analyzed.	sapropterin	214-233	phenylalanine hydroxylase	Homo sapiens	18-21
16550150-10	2006	Advances in treatment: a study published in 2002 showed that some patients deficient in phenylalanine hydroxylase are sensitive to pharmacological doses of tetrahydrobiopterin (BH4), a cofactor of this "enzyme essential to the transformation of phenylalanine into tyrosine.	sapropterin	156-175	phenylalanine hydroxylase	Homo sapiens	88-113
16550150-10	2006	Advances in treatment: a study published in 2002 showed that some patients deficient in phenylalanine hydroxylase are sensitive to pharmacological doses of tetrahydrobiopterin (BH4), a cofactor of this "enzyme essential to the transformation of phenylalanine into tyrosine.	sapropterin	177-180	phenylalanine hydroxylase	Homo sapiens	88-113
16550150-10	2006	Advances in treatment: a study published in 2002 showed that some patients deficient in phenylalanine hydroxylase are sensitive to pharmacological doses of tetrahydrobiopterin (BH4), a cofactor of this "enzyme essential to the transformation of phenylalanine into tyrosine.	Tyrosine	264-272	phenylalanine hydroxylase	Homo sapiens	88-113
16489829-2	2006	It has been shown in a previous paper that phospholipid vesicles can be incorporated without spontaneous bilayer rupture into poly-L-glutamic acid/poly(allylamine) (PGA/PAH) multilayered polyelectrolyte films.	Phospholipids	43-55	phenylalanine hydroxylase	Homo sapiens	169-172
16489829-2	2006	It has been shown in a previous paper that phospholipid vesicles can be incorporated without spontaneous bilayer rupture into poly-L-glutamic acid/poly(allylamine) (PGA/PAH) multilayered polyelectrolyte films.	Polyglutamic Acid	126-146	phenylalanine hydroxylase	Homo sapiens	169-172
16489829-2	2006	It has been shown in a previous paper that phospholipid vesicles can be incorporated without spontaneous bilayer rupture into poly-L-glutamic acid/poly(allylamine) (PGA/PAH) multilayered polyelectrolyte films.	polyallylamine	147-163	phenylalanine hydroxylase	Homo sapiens	169-172
16470264-3	2006	The PAH, the Forties crude and diesel oil equivalent concentrations were generally higher in sediment of fine grain size and higher organic carbon concentration.	Carbon	140-146	phenylalanine hydroxylase	Homo sapiens	4-7
16601866-1	2006	A fall in blood phenylalanine (Phe) after tetrahydrobiopterin (BH(4)) administration is a common trait in phenylalanine hydroxylase (PAH, EC 1.14.16.1) deficiency (McKusick 261600).	Phenylalanine	16-29	phenylalanine hydroxylase	Homo sapiens	106-131
16601866-1	2006	A fall in blood phenylalanine (Phe) after tetrahydrobiopterin (BH(4)) administration is a common trait in phenylalanine hydroxylase (PAH, EC 1.14.16.1) deficiency (McKusick 261600).	Phenylalanine	16-29	phenylalanine hydroxylase	Homo sapiens	133-136
16601866-1	2006	A fall in blood phenylalanine (Phe) after tetrahydrobiopterin (BH(4)) administration is a common trait in phenylalanine hydroxylase (PAH, EC 1.14.16.1) deficiency (McKusick 261600).	Phenylalanine	31-34	phenylalanine hydroxylase	Homo sapiens	106-131
16601866-1	2006	A fall in blood phenylalanine (Phe) after tetrahydrobiopterin (BH(4)) administration is a common trait in phenylalanine hydroxylase (PAH, EC 1.14.16.1) deficiency (McKusick 261600).	Phenylalanine	31-34	phenylalanine hydroxylase	Homo sapiens	133-136
16601866-1	2006	A fall in blood phenylalanine (Phe) after tetrahydrobiopterin (BH(4)) administration is a common trait in phenylalanine hydroxylase (PAH, EC 1.14.16.1) deficiency (McKusick 261600).	sapropterin	42-61	phenylalanine hydroxylase	Homo sapiens	106-131
16601866-1	2006	A fall in blood phenylalanine (Phe) after tetrahydrobiopterin (BH(4)) administration is a common trait in phenylalanine hydroxylase (PAH, EC 1.14.16.1) deficiency (McKusick 261600).	sapropterin	42-61	phenylalanine hydroxylase	Homo sapiens	133-136
15936235-0	2005	The activity of wild-type and mutant phenylalanine hydroxylase and its regulation by phenylalanine and tetrahydrobiopterin at physiological and pathological concentrations: an isothermal titration calorimetry study.	sapropterin	103-122	phenylalanine hydroxylase	Homo sapiens	37-62
15936235-1	2005	The activity of phenylalanine hydroxylase (PAH) is regulated by the levels of both the substrate (L-Phe) and the natural cofactor (6R)-tetrahydrobiopterin (BH4).	Phenylalanine	98-103	phenylalanine hydroxylase	Homo sapiens	16-41
15936235-1	2005	The activity of phenylalanine hydroxylase (PAH) is regulated by the levels of both the substrate (L-Phe) and the natural cofactor (6R)-tetrahydrobiopterin (BH4).	sapropterin	130-154	phenylalanine hydroxylase	Homo sapiens	16-41
15936235-1	2005	The activity of phenylalanine hydroxylase (PAH) is regulated by the levels of both the substrate (L-Phe) and the natural cofactor (6R)-tetrahydrobiopterin (BH4).	sapropterin	156-159	phenylalanine hydroxylase	Homo sapiens	16-41
16165389-0	2005	Spanish BH4-responsive phenylalanine hydroxylase-deficient patients: evolution of seven patients on long-term treatment with tetrahydrobiopterin.	sapropterin	8-11	phenylalanine hydroxylase	Homo sapiens	23-48
16165389-0	2005	Spanish BH4-responsive phenylalanine hydroxylase-deficient patients: evolution of seven patients on long-term treatment with tetrahydrobiopterin.	sapropterin	125-144	phenylalanine hydroxylase	Homo sapiens	23-48
16165389-1	2005	A novel subtype of patients with mutations in the phenylalanine hydroxylase (PAH) gene that show a positive response during a tetrahydrobiopterin (BH4) loading test has recently been recognized.	sapropterin	126-145	phenylalanine hydroxylase	Homo sapiens	50-75
16165389-1	2005	A novel subtype of patients with mutations in the phenylalanine hydroxylase (PAH) gene that show a positive response during a tetrahydrobiopterin (BH4) loading test has recently been recognized.	sapropterin	126-145	phenylalanine hydroxylase	Homo sapiens	77-80
16165389-1	2005	A novel subtype of patients with mutations in the phenylalanine hydroxylase (PAH) gene that show a positive response during a tetrahydrobiopterin (BH4) loading test has recently been recognized.	sapropterin	147-150	phenylalanine hydroxylase	Homo sapiens	50-75
16165389-1	2005	A novel subtype of patients with mutations in the phenylalanine hydroxylase (PAH) gene that show a positive response during a tetrahydrobiopterin (BH4) loading test has recently been recognized.	sapropterin	147-150	phenylalanine hydroxylase	Homo sapiens	77-80
16165389-3	2005	In our unit, we performed BH4 overload tests in 50 PAH-deficient patients.	sapropterin	26-29	phenylalanine hydroxylase	Homo sapiens	51-54
16831323-13	2006	CONCLUSIONS: PAH is a common complication of CTDs, which occurs often in the forth year after initial CTD manifestations and is earlier in patients with SLE or MCTD, compared to those with pSS.	beta-cyclodextrin tetradecasulfate	45-49	phenylalanine hydroxylase	Homo sapiens	13-16
15996733-7	2006	A good correlation existed between the benzo[a]pyrene level and the total PAH concentration (r=0.97), making benzo[a]pyrene a potential molecular marker for PAH pollution.	Benzo(a)pyrene	39-53	phenylalanine hydroxylase	Homo sapiens	74-77
15996733-7	2006	A good correlation existed between the benzo[a]pyrene level and the total PAH concentration (r=0.97), making benzo[a]pyrene a potential molecular marker for PAH pollution.	Benzo(a)pyrene	39-53	phenylalanine hydroxylase	Homo sapiens	157-160
15996733-7	2006	A good correlation existed between the benzo[a]pyrene level and the total PAH concentration (r=0.97), making benzo[a]pyrene a potential molecular marker for PAH pollution.	Benzo(a)pyrene	109-123	phenylalanine hydroxylase	Homo sapiens	74-77
15996733-7	2006	A good correlation existed between the benzo[a]pyrene level and the total PAH concentration (r=0.97), making benzo[a]pyrene a potential molecular marker for PAH pollution.	Benzo(a)pyrene	109-123	phenylalanine hydroxylase	Homo sapiens	157-160
16853967-1	2005	A series of Cr-incorporated PKU-1 molecular sieves (Cr-PKU-1) were synthesized by using boric acid as a flux, and the physicochemical properties were characterized by XRD, ICP, SEM, XPS, UV-vis, and NH3-TPD methods.	boric acid	88-98	phenylalanine hydroxylase	Homo sapiens	28-33
16853967-2	2005	The morphology of Cr-PKU-1 is a needlelike hexagonal prism with uniform size of about 2 microm in diameter and 20-50 microm in length.	Chromium	18-20	phenylalanine hydroxylase	Homo sapiens	21-26
16853967-3	2005	XRD and UV-vis provide direct evidence that Cr ions have been successfully incorporated into the framework of PKU-1.	Chromium	44-46	phenylalanine hydroxylase	Homo sapiens	110-115
16853967-4	2005	NH3-TPD shows a dramatic increase of acidic sites in the Cr-PKU-1 in comparison with PKU-1, indicating that the Cr incorporation can significantly modify the acidity of the compound.	Chromium	57-59	phenylalanine hydroxylase	Homo sapiens	60-65
16853967-4	2005	NH3-TPD shows a dramatic increase of acidic sites in the Cr-PKU-1 in comparison with PKU-1, indicating that the Cr incorporation can significantly modify the acidity of the compound.	Chromium	112-114	phenylalanine hydroxylase	Homo sapiens	60-65
16853967-4	2005	NH3-TPD shows a dramatic increase of acidic sites in the Cr-PKU-1 in comparison with PKU-1, indicating that the Cr incorporation can significantly modify the acidity of the compound.	Chromium	112-114	phenylalanine hydroxylase	Homo sapiens	85-90
16853967-5	2005	In addition, the incorporated Cr ions may act as redox centers, thus catalytic performance of Cr-PKU-1 molecular sieve was investigated by the selective oxidation of styrene under mild reaction conditions.	Chromium	30-32	phenylalanine hydroxylase	Homo sapiens	97-102
16853967-5	2005	In addition, the incorporated Cr ions may act as redox centers, thus catalytic performance of Cr-PKU-1 molecular sieve was investigated by the selective oxidation of styrene under mild reaction conditions.	Styrene	166-173	phenylalanine hydroxylase	Homo sapiens	97-102
16640195-1	2005	Phenylketonuria (PKU) is a genetic disorder caused by a partial or complete mutation of the enzyme phenylalanine hydroxylase (PHA), fact that produces high levels of phenylalanine in blood resulting in mental retardation if not diagnosed during the neonatal period.	Phenylalanine	99-112	phenylalanine hydroxylase	Homo sapiens	126-129
16183315-1	2005	Tetrahydrobiopterin (BH4) responsive hyperphenylalaninemia (HPA) with a mutant phenylalanine hydroxylase (PAH) gene was found during neonatal screening for PKU.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	79-104
16143554-11	2005	We found that mutant PAH responds with increase in the residual enzyme activity following BH4 administration.	sapropterin	90-93	phenylalanine hydroxylase	Homo sapiens	21-24
16183315-1	2005	Tetrahydrobiopterin (BH4) responsive hyperphenylalaninemia (HPA) with a mutant phenylalanine hydroxylase (PAH) gene was found during neonatal screening for PKU.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	106-109
16183315-1	2005	Tetrahydrobiopterin (BH4) responsive hyperphenylalaninemia (HPA) with a mutant phenylalanine hydroxylase (PAH) gene was found during neonatal screening for PKU.	sapropterin	21-24	phenylalanine hydroxylase	Homo sapiens	79-104
16183315-1	2005	Tetrahydrobiopterin (BH4) responsive hyperphenylalaninemia (HPA) with a mutant phenylalanine hydroxylase (PAH) gene was found during neonatal screening for PKU.	sapropterin	21-24	phenylalanine hydroxylase	Homo sapiens	106-109
16242984-1	2005	Tetrahydrobiopterin (BH4), the natural cofactor of phenylalanine hydroxylase (EC 1.14.16.1), can reduce blood phenylalanine (Phe) in BH4 sensitive patients with hyperphenylalaninemia (McKuisick 261600).	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	51-76
16198137-0	2005	Incidence of BH4-responsiveness in phenylalanine-hydroxylase-deficient Italian patients.	sapropterin	13-16	phenylalanine hydroxylase	Homo sapiens	35-60
16242984-1	2005	Tetrahydrobiopterin (BH4), the natural cofactor of phenylalanine hydroxylase (EC 1.14.16.1), can reduce blood phenylalanine (Phe) in BH4 sensitive patients with hyperphenylalaninemia (McKuisick 261600).	sapropterin	21-24	phenylalanine hydroxylase	Homo sapiens	51-76
16242984-1	2005	Tetrahydrobiopterin (BH4), the natural cofactor of phenylalanine hydroxylase (EC 1.14.16.1), can reduce blood phenylalanine (Phe) in BH4 sensitive patients with hyperphenylalaninemia (McKuisick 261600).	Phenylalanine	125-128	phenylalanine hydroxylase	Homo sapiens	51-76
16290003-1	2005	Patients with tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency may benefit from BH4 therapy instead or in addition to the low-phenylalanine diet.	sapropterin	14-33	phenylalanine hydroxylase	Homo sapiens	51-76
16242984-1	2005	Tetrahydrobiopterin (BH4), the natural cofactor of phenylalanine hydroxylase (EC 1.14.16.1), can reduce blood phenylalanine (Phe) in BH4 sensitive patients with hyperphenylalaninemia (McKuisick 261600).	sapropterin	133-136	phenylalanine hydroxylase	Homo sapiens	51-76
16290003-1	2005	Patients with tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency may benefit from BH4 therapy instead or in addition to the low-phenylalanine diet.	sapropterin	35-38	phenylalanine hydroxylase	Homo sapiens	51-76
16219508-0	2005	Enhancement of PAH biomineralization rates by cyclodextrins under Fe(III)-reducing conditions.	Cyclodextrins	46-59	phenylalanine hydroxylase	Homo sapiens	15-18
16290003-1	2005	Patients with tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency may benefit from BH4 therapy instead or in addition to the low-phenylalanine diet.	sapropterin	111-114	phenylalanine hydroxylase	Homo sapiens	51-76
16290004-0	2005	Stimulation of hepatic phenylalanine hydroxylase activity but not Pah-mRNA expression upon oral loading of tetrahydrobiopterin in normal mice.	sapropterin	107-126	phenylalanine hydroxylase	Homo sapiens	23-48
16262324-4	2005	On the 50 kDa substrates, PSS/PDADMAC films containing 3.5 bilayers exhibit a 95% rejection of SO(4)(2-) and a chloride/sulfate selectivity of 27, whereas 4.5-bilayer PSS/PAH coatings show a glucose/raffinose selectivity of 100.	Diallyldimethylammonium chloride	30-37	phenylalanine hydroxylase	Homo sapiens	171-174
16262324-5	2005	Pure water flux for [PSS/PAH](3)PSS-coated membranes at 4.8 bar is 1.6 m(3)/(m(2)day), which is more than 2-fold higher than that through a commercial 500 Da membrane.	Water	5-10	phenylalanine hydroxylase	Homo sapiens	25-28
16219508-0	2005	Enhancement of PAH biomineralization rates by cyclodextrins under Fe(III)-reducing conditions.	ferric sulfate	66-73	phenylalanine hydroxylase	Homo sapiens	15-18
16328660-5	2005	Densities of phenanthrene degraders reflected previous PAH exposure, whereas pyrene degraders were detected only in the most polluted soils.	phenanthrene	13-25	phenylalanine hydroxylase	Homo sapiens	55-58
16328660-3	2005	We estimated the PAH degradation capacity of 13 soils ranging from pristine locations (total PAHs approximately 0.1 mg kg(-1)) to heavily polluted industrial sites (total PAHs approximately 400 mg kg(-1)).	Polycyclic Aromatic Hydrocarbons	93-97	phenylalanine hydroxylase	Homo sapiens	17-20
16328660-7	2005	The time to 10% mineralization of added (14)C phenanthrene and (14)C pyrene was inversely correlated with the PAH content of the soils.	phenanthrene	46-58	phenylalanine hydroxylase	Homo sapiens	110-113
16328660-7	2005	The time to 10% mineralization of added (14)C phenanthrene and (14)C pyrene was inversely correlated with the PAH content of the soils.	pyrene	69-75	phenylalanine hydroxylase	Homo sapiens	110-113
16328660-11	2005	Mineralization of phenanthrene and pyrene by all Danish soils suggests that soil microbial communities of inhabited areas possess a sufficiently high PAH degradation capacity to question the value of bioaugmentation with specific PAH degraders for bioremediation.	phenanthrene	18-30	phenylalanine hydroxylase	Homo sapiens	150-153
16328660-11	2005	Mineralization of phenanthrene and pyrene by all Danish soils suggests that soil microbial communities of inhabited areas possess a sufficiently high PAH degradation capacity to question the value of bioaugmentation with specific PAH degraders for bioremediation.	pyrene	35-41	phenylalanine hydroxylase	Homo sapiens	150-153
16245837-3	2005	A profile comparison of the PAH mixture--using benzo[a]pyrene (B[a]P) relative abundance ratios (PAH/B[a]P)--for the cascade impactor filters indicated the formation of a sampling artifact.	Benzo(a)pyrene	47-61	phenylalanine hydroxylase	Homo sapiens	28-31
16245837-4	2005	Overall, the PAH stability scale generated in this study agrees with those produced experimentally for ozone and nitrogen dioxides or developed using other in situ measurement techniques.	Nitrogen	113-121	phenylalanine hydroxylase	Homo sapiens	13-16
15763632-2	2005	PAH exposure was estimated by the urinary excretion of 1-hydroxypyrene (1-OHP), whereas the regulatory effects were assessed by the caffeine metabolic ratio (CMR).	1-hydroxypyrene	55-70	phenylalanine hydroxylase	Homo sapiens	0-3
16087477-8	2005	The PAH exposure at workplaces was mainly composed of volatile compounds, particularly naphthalene, suggesting low exposure through the respiratory tract and a low effect of PAH in ROS induction.	naphthalene	87-98	phenylalanine hydroxylase	Homo sapiens	4-7
16087477-8	2005	The PAH exposure at workplaces was mainly composed of volatile compounds, particularly naphthalene, suggesting low exposure through the respiratory tract and a low effect of PAH in ROS induction.	ros	181-184	phenylalanine hydroxylase	Homo sapiens	4-7
16087477-8	2005	The PAH exposure at workplaces was mainly composed of volatile compounds, particularly naphthalene, suggesting low exposure through the respiratory tract and a low effect of PAH in ROS induction.	ros	181-184	phenylalanine hydroxylase	Homo sapiens	174-177
26641900-4	2005	This method provides results for H2/PAH interactions in close agreement with MP2 and higher-level ab initio methods.	Hydrogen	33-35	phenylalanine hydroxylase	Homo sapiens	36-39
16089392-1	2005	In a previous paper (Michel, M.; Vautier, D.; Voegel, J.-C.; Schaaf, P.; Ball, V. Langmuir 2004, 20, 4835), we showed that phospholipid vesicles can be incorporated into poly(glutamic-acid)/poly(allylamine) (PGA/PAH) multilayered polyelectrolyte films built by the alternated dipping of a surface in polyanion and polycation solutions.	Phospholipids	123-135	phenylalanine hydroxylase	Homo sapiens	212-215
16096991-3	2005	Furthermore, it was found that enzyme within PAH/PSS- and crosslinked PAH/PAA-coated spheres retained more than 84 and 60% of initial activity, respectively, after three months, whereas uncoated and PDDA/PSS-coated microspheres retained less than 20%.	paa	74-77	phenylalanine hydroxylase	Homo sapiens	70-73
15963939-3	2005	Using (6R)-tetrahydrobiopterin as electron donor in the phenylalanine hydroxylase (PAH) reaction, a stable stoichiometry of 1:1 was obtained between the amount of oxygen consumed and the tyrosine formation.	sapropterin	6-30	phenylalanine hydroxylase	Homo sapiens	56-81
15963939-3	2005	Using (6R)-tetrahydrobiopterin as electron donor in the phenylalanine hydroxylase (PAH) reaction, a stable stoichiometry of 1:1 was obtained between the amount of oxygen consumed and the tyrosine formation.	sapropterin	6-30	phenylalanine hydroxylase	Homo sapiens	83-86
15963939-3	2005	Using (6R)-tetrahydrobiopterin as electron donor in the phenylalanine hydroxylase (PAH) reaction, a stable stoichiometry of 1:1 was obtained between the amount of oxygen consumed and the tyrosine formation.	Oxygen	163-169	phenylalanine hydroxylase	Homo sapiens	56-81
15963939-3	2005	Using (6R)-tetrahydrobiopterin as electron donor in the phenylalanine hydroxylase (PAH) reaction, a stable stoichiometry of 1:1 was obtained between the amount of oxygen consumed and the tyrosine formation.	Oxygen	163-169	phenylalanine hydroxylase	Homo sapiens	83-86
15963939-3	2005	Using (6R)-tetrahydrobiopterin as electron donor in the phenylalanine hydroxylase (PAH) reaction, a stable stoichiometry of 1:1 was obtained between the amount of oxygen consumed and the tyrosine formation.	Tyrosine	187-195	phenylalanine hydroxylase	Homo sapiens	56-81
15963939-3	2005	Using (6R)-tetrahydrobiopterin as electron donor in the phenylalanine hydroxylase (PAH) reaction, a stable stoichiometry of 1:1 was obtained between the amount of oxygen consumed and the tyrosine formation.	Tyrosine	187-195	phenylalanine hydroxylase	Homo sapiens	83-86
15963939-7	2005	Furthermore, the amount of H(2)O(2) produced in the reaction catalyzed by R158Q PAH was about four times higher than the amount produced by the wild-type PAH, demonstrating a possible pathogenetic mechanism of the mutant enzyme.	Hydrogen Peroxide	27-35	phenylalanine hydroxylase	Homo sapiens	80-83
15963939-7	2005	Furthermore, the amount of H(2)O(2) produced in the reaction catalyzed by R158Q PAH was about four times higher than the amount produced by the wild-type PAH, demonstrating a possible pathogenetic mechanism of the mutant enzyme.	Hydrogen Peroxide	27-35	phenylalanine hydroxylase	Homo sapiens	154-157
16124286-6	2005	Average atmospheric wet deposition PAH fluxes at the seven sites ranged from 0.40 (cyclopenta[cd]pyrene) to 140 (methylphenanthrenes) ng m(-2) d(-1).	cyclopenta(c,d)pyrene	83-103	phenylalanine hydroxylase	Homo sapiens	35-38
16124286-6	2005	Average atmospheric wet deposition PAH fluxes at the seven sites ranged from 0.40 (cyclopenta[cd]pyrene) to 140 (methylphenanthrenes) ng m(-2) d(-1).	methylphenanthrenes	113-132	phenylalanine hydroxylase	Homo sapiens	35-38
15895215-5	2005	The proposed method combined with a partial-least-square (PLS) treatment was tested for quantitative analysis of mixtures of four PAH in a spiked drinking water.	Water	155-160	phenylalanine hydroxylase	Homo sapiens	130-133
15962938-16	2005	These data showed that the production of 8-oxo-dGuo was dependent on Cu(II)/Cu(I) catalyzed redox cycling of PAH o-quinones to produce ROS and that the immediate oxidant was not hydroxyl radical or Cu(I)OOH and that it is more likely (1)O(2), which can produce a 4,8-endoperoxide-dGuo intermediate.	4,8-endoperoxide-dguo	263-284	phenylalanine hydroxylase	Homo sapiens	109-112
15895215-0	2005	Detection and quantification of PAH in drinking water by front-face fluorimetry on a solid sorbent and PLS analysis.	Drinking Water	39-53	phenylalanine hydroxylase	Homo sapiens	32-35
15962938-0	2005	Formation of 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-oxo-dGuo) by PAH o-quinones: involvement of reactive oxygen species and copper(II)/copper(I) redox cycling.	8-ohdg	13-48	phenylalanine hydroxylase	Homo sapiens	65-68
15962938-0	2005	Formation of 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-oxo-dGuo) by PAH o-quinones: involvement of reactive oxygen species and copper(II)/copper(I) redox cycling.	8-ohdg	50-60	phenylalanine hydroxylase	Homo sapiens	65-68
15962938-0	2005	Formation of 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-oxo-dGuo) by PAH o-quinones: involvement of reactive oxygen species and copper(II)/copper(I) redox cycling.	o-quinones	69-79	phenylalanine hydroxylase	Homo sapiens	65-68
15962938-0	2005	Formation of 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-oxo-dGuo) by PAH o-quinones: involvement of reactive oxygen species and copper(II)/copper(I) redox cycling.	Reactive Oxygen Species	96-119	phenylalanine hydroxylase	Homo sapiens	65-68
15962938-0	2005	Formation of 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-oxo-dGuo) by PAH o-quinones: involvement of reactive oxygen species and copper(II)/copper(I) redox cycling.	Copper	124-130	phenylalanine hydroxylase	Homo sapiens	65-68
15962938-0	2005	Formation of 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-oxo-dGuo) by PAH o-quinones: involvement of reactive oxygen species and copper(II)/copper(I) redox cycling.	Copper	135-141	phenylalanine hydroxylase	Homo sapiens	65-68
15962938-3	2005	Spectrophotometric assays showed that NADPH caused PAH o-quinones to enter futile redox cycles, which result in the depletion of excess cofactor.	NADP	38-43	phenylalanine hydroxylase	Homo sapiens	51-54
15962938-9	2005	HPLC-ECD analysis revealed that in the presence of NADPH and Cu(II), submicromolar concentrations of PAH o-quinones generated >60.0 8-oxo-dGuo adducts/10(5) dGuo.	NADP	51-56	phenylalanine hydroxylase	Homo sapiens	101-104
15962938-9	2005	HPLC-ECD analysis revealed that in the presence of NADPH and Cu(II), submicromolar concentrations of PAH o-quinones generated >60.0 8-oxo-dGuo adducts/10(5) dGuo.	cu(ii)	61-67	phenylalanine hydroxylase	Homo sapiens	101-104
15962938-9	2005	HPLC-ECD analysis revealed that in the presence of NADPH and Cu(II), submicromolar concentrations of PAH o-quinones generated >60.0 8-oxo-dGuo adducts/10(5) dGuo.	8-ohdg	135-145	phenylalanine hydroxylase	Homo sapiens	101-104
15962938-9	2005	HPLC-ECD analysis revealed that in the presence of NADPH and Cu(II), submicromolar concentrations of PAH o-quinones generated >60.0 8-oxo-dGuo adducts/10(5) dGuo.	2-amino-9-[(2R,3S,4S,5R)-3-deuterio-4-hydroxy-5-(hydroxymethyl)oxolan-2-yl]-1H-purin-6-one	141-145	phenylalanine hydroxylase	Homo sapiens	101-104
15962938-11	2005	The formation of 8-oxo-dGuo by PAH o-quinones was concentration-dependent.	8-ohdg	17-27	phenylalanine hydroxylase	Homo sapiens	31-34
15962938-16	2005	These data showed that the production of 8-oxo-dGuo was dependent on Cu(II)/Cu(I) catalyzed redox cycling of PAH o-quinones to produce ROS and that the immediate oxidant was not hydroxyl radical or Cu(I)OOH and that it is more likely (1)O(2), which can produce a 4,8-endoperoxide-dGuo intermediate.	8-ohdg	41-51	phenylalanine hydroxylase	Homo sapiens	109-112
15962938-16	2005	These data showed that the production of 8-oxo-dGuo was dependent on Cu(II)/Cu(I) catalyzed redox cycling of PAH o-quinones to produce ROS and that the immediate oxidant was not hydroxyl radical or Cu(I)OOH and that it is more likely (1)O(2), which can produce a 4,8-endoperoxide-dGuo intermediate.	cu(ii)	69-75	phenylalanine hydroxylase	Homo sapiens	109-112
15962938-16	2005	These data showed that the production of 8-oxo-dGuo was dependent on Cu(II)/Cu(I) catalyzed redox cycling of PAH o-quinones to produce ROS and that the immediate oxidant was not hydroxyl radical or Cu(I)OOH and that it is more likely (1)O(2), which can produce a 4,8-endoperoxide-dGuo intermediate.	Copper	69-71	phenylalanine hydroxylase	Homo sapiens	109-112
15962938-16	2005	These data showed that the production of 8-oxo-dGuo was dependent on Cu(II)/Cu(I) catalyzed redox cycling of PAH o-quinones to produce ROS and that the immediate oxidant was not hydroxyl radical or Cu(I)OOH and that it is more likely (1)O(2), which can produce a 4,8-endoperoxide-dGuo intermediate.	Reactive Oxygen Species	135-138	phenylalanine hydroxylase	Homo sapiens	109-112
15962938-16	2005	These data showed that the production of 8-oxo-dGuo was dependent on Cu(II)/Cu(I) catalyzed redox cycling of PAH o-quinones to produce ROS and that the immediate oxidant was not hydroxyl radical or Cu(I)OOH and that it is more likely (1)O(2), which can produce a 4,8-endoperoxide-dGuo intermediate.	cu(i)ooh	198-206	phenylalanine hydroxylase	Homo sapiens	109-112
15917086-0	2005	The active site residue tyrosine 325 influences iron binding and coupling efficiency in human phenylalanine hydroxylase.	Tyrosine	24-32	phenylalanine hydroxylase	Homo sapiens	94-119
15917086-0	2005	The active site residue tyrosine 325 influences iron binding and coupling efficiency in human phenylalanine hydroxylase.	Iron	48-52	phenylalanine hydroxylase	Homo sapiens	94-119
15917086-1	2005	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4))-dependent enzyme that catalyzes the hydroxylation of l-Phe to l-Tyr.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	0-25
15917086-1	2005	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4))-dependent enzyme that catalyzes the hydroxylation of l-Phe to l-Tyr.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	27-30
15917086-1	2005	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4))-dependent enzyme that catalyzes the hydroxylation of l-Phe to l-Tyr.	sapropterin	58-63	phenylalanine hydroxylase	Homo sapiens	0-25
15917086-1	2005	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4))-dependent enzyme that catalyzes the hydroxylation of l-Phe to l-Tyr.	sapropterin	58-63	phenylalanine hydroxylase	Homo sapiens	27-30
15917086-1	2005	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4))-dependent enzyme that catalyzes the hydroxylation of l-Phe to l-Tyr.	Phenylalanine	118-123	phenylalanine hydroxylase	Homo sapiens	0-25
15917086-1	2005	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4))-dependent enzyme that catalyzes the hydroxylation of l-Phe to l-Tyr.	Phenylalanine	118-123	phenylalanine hydroxylase	Homo sapiens	27-30
15917086-1	2005	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4))-dependent enzyme that catalyzes the hydroxylation of l-Phe to l-Tyr.	Tyrosine	127-132	phenylalanine hydroxylase	Homo sapiens	0-25
15917086-1	2005	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4))-dependent enzyme that catalyzes the hydroxylation of l-Phe to l-Tyr.	Tyrosine	127-132	phenylalanine hydroxylase	Homo sapiens	27-30
15917086-13	2005	On the other hand, compared to wild-type PAH, Y325L shows reduced specific activity, decreased coupling efficiency and decreased iron content.	Iron	129-133	phenylalanine hydroxylase	Homo sapiens	41-44
15917086-16	2005	Tyr325 thus appears to have an important role ensuring stoichiometric binding of iron, correct geometry of the complexes with substrate and cofactor and, consequently, a right coupling efficiency of the PAH reaction.	Iron	81-85	phenylalanine hydroxylase	Homo sapiens	203-206
15926592-2	2005	The removal of PAH compounds was evaluated with a model feed (toluene, naphthalene, and dibenzothiophene)that approached the composition of diesel fuel.	Toluene	62-69	phenylalanine hydroxylase	Homo sapiens	15-18
15926592-2	2005	The removal of PAH compounds was evaluated with a model feed (toluene, naphthalene, and dibenzothiophene)that approached the composition of diesel fuel.	naphthalene	71-82	phenylalanine hydroxylase	Homo sapiens	15-18
15926592-2	2005	The removal of PAH compounds was evaluated with a model feed (toluene, naphthalene, and dibenzothiophene)that approached the composition of diesel fuel.	dibenzothiophene	88-104	phenylalanine hydroxylase	Homo sapiens	15-18
15924746-1	2005	OBJECTIVE: Tetrahydrobiopterin (BH(4)) responsive phenylalanine hydroxylase (PAH) deficiency is one of the forms of phenylketonuria (PKU).	sapropterin	11-30	phenylalanine hydroxylase	Homo sapiens	50-75
15763632-2	2005	PAH exposure was estimated by the urinary excretion of 1-hydroxypyrene (1-OHP), whereas the regulatory effects were assessed by the caffeine metabolic ratio (CMR).	Oxaliplatin	72-77	phenylalanine hydroxylase	Homo sapiens	0-3
15504500-5	2004	Phenanthrene was the prevalent PAH in all air samples tested, with concentrations up to 17.6 ng.m(-3), followed by fluorene, fluoranthene and pyrene present mostly in the gaseous phase.	phenanthrene	0-12	phenylalanine hydroxylase	Homo sapiens	31-34
15878743-1	2005	Phenylketonuria (PKU) is an autossomal recessive disease caused by phenylalanine-4-hydroxylase deficiency, which is a liver-specific enzyme that catalyzes the hydroxylation of l-phenylalanine (Phe) to l-tyrosine (Tyr).	Phenylalanine	176-191	phenylalanine hydroxylase	Homo sapiens	67-94
15878743-1	2005	Phenylketonuria (PKU) is an autossomal recessive disease caused by phenylalanine-4-hydroxylase deficiency, which is a liver-specific enzyme that catalyzes the hydroxylation of l-phenylalanine (Phe) to l-tyrosine (Tyr).	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	67-94
15878743-1	2005	Phenylketonuria (PKU) is an autossomal recessive disease caused by phenylalanine-4-hydroxylase deficiency, which is a liver-specific enzyme that catalyzes the hydroxylation of l-phenylalanine (Phe) to l-tyrosine (Tyr).	Tyrosine	201-211	phenylalanine hydroxylase	Homo sapiens	67-94
15878743-1	2005	Phenylketonuria (PKU) is an autossomal recessive disease caused by phenylalanine-4-hydroxylase deficiency, which is a liver-specific enzyme that catalyzes the hydroxylation of l-phenylalanine (Phe) to l-tyrosine (Tyr).	Tyrosine	213-216	phenylalanine hydroxylase	Homo sapiens	67-94
15807618-1	2005	We show, in this paper that multivalent ferrocyanide anions can penetrate into exponentially growing (PGA/PAH)n multilayer films whatever the nature of the last deposited layer.	ferrocyanide anions	40-59	phenylalanine hydroxylase	Homo sapiens	106-109
15807618-1	2005	We show, in this paper that multivalent ferrocyanide anions can penetrate into exponentially growing (PGA/PAH)n multilayer films whatever the nature of the last deposited layer.	Polyglutamic Acid	102-105	phenylalanine hydroxylase	Homo sapiens	106-109
15807618-3	2005	However, the contact of this film with a poly(allylamine) (PAH) or a poly(L-glutamic acid) (PGA) solution leads to the release of ferrocyanide ions from the multilayer.	polyallylamine	41-57	phenylalanine hydroxylase	Homo sapiens	59-62
15807618-3	2005	However, the contact of this film with a poly(allylamine) (PAH) or a poly(L-glutamic acid) (PGA) solution leads to the release of ferrocyanide ions from the multilayer.	hexacyanoferrate II	130-142	phenylalanine hydroxylase	Homo sapiens	59-62
15807618-6	2005	When the film is then brought in contact with a PAH solution, the PAH chains from the solution are expected to strongly interact with the ferrocyanide ions and thus induce a diffusion mechanism of the multivalent anions out of the film, the film/solution interface playing the role of a sink for these ions.	hexacyanoferrate II	138-150	phenylalanine hydroxylase	Homo sapiens	48-51
15807618-6	2005	When the film is then brought in contact with a PAH solution, the PAH chains from the solution are expected to strongly interact with the ferrocyanide ions and thus induce a diffusion mechanism of the multivalent anions out of the film, the film/solution interface playing the role of a sink for these ions.	hexacyanoferrate II	138-150	phenylalanine hydroxylase	Homo sapiens	66-69
15773496-0	2005	Comment on "addition of carbon sorbents to reduce PCB and PAH bioavailability in marine sediments: physicochemical tests".	Carbon	24-30	phenylalanine hydroxylase	Homo sapiens	58-61
15965718-0	2005	Dissolved oxygen saturation controls PAH biodegradation in freshwater estuary sediments.	Oxygen	10-16	phenylalanine hydroxylase	Homo sapiens	37-40
15965718-6	2005	PAH mineralization correlated with bottom water DO saturation above 70% (r(2) > 0.99).	Water	42-47	phenylalanine hydroxylase	Homo sapiens	0-3
15965718-7	2005	These results suggest that the proportional utilization of PAH carbon to natural organic carbon is as much as three orders of magnitude higher during cooler months, when water temperatures are lower and DO % saturation is higher.	Carbon	63-69	phenylalanine hydroxylase	Homo sapiens	59-62
15965718-7	2005	These results suggest that the proportional utilization of PAH carbon to natural organic carbon is as much as three orders of magnitude higher during cooler months, when water temperatures are lower and DO % saturation is higher.	Carbon	89-95	phenylalanine hydroxylase	Homo sapiens	59-62
15965718-8	2005	Infusion of cooler, well-oxygenated water to the water column overlying contaminated sediments during the summer months may stimulate PAH metabolism preferentially over non-PAH organic matter.	Water	36-41	phenylalanine hydroxylase	Homo sapiens	134-137
15965718-8	2005	Infusion of cooler, well-oxygenated water to the water column overlying contaminated sediments during the summer months may stimulate PAH metabolism preferentially over non-PAH organic matter.	Water	36-41	phenylalanine hydroxylase	Homo sapiens	173-176
15816606-2	2005	MATERIALS AND METHODS: To investigate the role of polycyclic aromatic hydrocarbons (PAHs) in the etiology of ESCC in northeastern Iran, we measured urine 1-hydroxypyrene glucuronide (1-OHPG), a stable PAH metabolite, in 99 inhabitants of this area.	Polycyclic Aromatic Hydrocarbons	50-82	phenylalanine hydroxylase	Homo sapiens	84-87
16046863-1	2005	Phenylketonuria (PKU) is an inherited disease causing increased levels of phenylalanine in body fluids due to deficiency of hepatic phenylalanine hydroxylase (PAH) or other enzymes involved in the phenylalanine metabolism.	Phenylalanine	74-87	phenylalanine hydroxylase	Homo sapiens	159-162
16046863-1	2005	Phenylketonuria (PKU) is an inherited disease causing increased levels of phenylalanine in body fluids due to deficiency of hepatic phenylalanine hydroxylase (PAH) or other enzymes involved in the phenylalanine metabolism.	Phenylalanine	132-145	phenylalanine hydroxylase	Homo sapiens	159-162
16046863-2	2005	With the long-term goal of using gene transfer to the skin to remove phenylalanine, we have previously shown that overexpression of PAH, catalyzing the hydroxylation of phenylalanine, and GTP cyclohydrolase (GTP-CH), involved in the formation of the necessary cofactor BH4,are required.	Phenylalanine	69-82	phenylalanine hydroxylase	Homo sapiens	132-135
16046863-2	2005	With the long-term goal of using gene transfer to the skin to remove phenylalanine, we have previously shown that overexpression of PAH, catalyzing the hydroxylation of phenylalanine, and GTP cyclohydrolase (GTP-CH), involved in the formation of the necessary cofactor BH4,are required.	sapropterin	269-272	phenylalanine hydroxylase	Homo sapiens	132-135
16086552-1	2005	The role of phenylalanine 4-monooxygenase (PAH) in the S-oxidation of S-carboxymethyl-L-cysteine (SCMC) in the rat has now been well established in rat cytosolic fractions in vitro.	p-Aminohippuric Acid	43-46	phenylalanine hydroxylase	Homo sapiens	12-41
16086552-1	2005	The role of phenylalanine 4-monooxygenase (PAH) in the S-oxidation of S-carboxymethyl-L-cysteine (SCMC) in the rat has now been well established in rat cytosolic fractions in vitro.	Carbocysteine	70-96	phenylalanine hydroxylase	Homo sapiens	12-41
16086552-1	2005	The role of phenylalanine 4-monooxygenase (PAH) in the S-oxidation of S-carboxymethyl-L-cysteine (SCMC) in the rat has now been well established in rat cytosolic fractions in vitro.	Carbocysteine	98-102	phenylalanine hydroxylase	Homo sapiens	12-41
15626640-5	2005	In contrast, colon digests of these PAH compounds displayed estrogenicity, equivalent to 0.31, 2.14, 2.70, and 1.48 nmol 17alpha-ethynylestradiol (EE2), respectively.	Ethinyl Estradiol	121-145	phenylalanine hydroxylase	Homo sapiens	36-39
15626640-5	2005	In contrast, colon digests of these PAH compounds displayed estrogenicity, equivalent to 0.31, 2.14, 2.70, and 1.48 nmol 17alpha-ethynylestradiol (EE2), respectively.	Ethinyl Estradiol	147-150	phenylalanine hydroxylase	Homo sapiens	36-39
15626640-7	2005	Liquid chromatography-mass spectrometry analysis confirmed the microbial PAH transformation by the detection of PAH metabolites 1-hydroxypyrene and 7-hydroxybenzo(a)pyrene in colon digests of pyrene and benzo(a)pyrene.	1-hydroxypyrene	128-143	phenylalanine hydroxylase	Homo sapiens	73-76
15626640-7	2005	Liquid chromatography-mass spectrometry analysis confirmed the microbial PAH transformation by the detection of PAH metabolites 1-hydroxypyrene and 7-hydroxybenzo(a)pyrene in colon digests of pyrene and benzo(a)pyrene.	1-hydroxypyrene	128-143	phenylalanine hydroxylase	Homo sapiens	112-115
15626640-7	2005	Liquid chromatography-mass spectrometry analysis confirmed the microbial PAH transformation by the detection of PAH metabolites 1-hydroxypyrene and 7-hydroxybenzo(a)pyrene in colon digests of pyrene and benzo(a)pyrene.	7-Hydroxybenzo(a)pyrene	148-171	phenylalanine hydroxylase	Homo sapiens	73-76
15626640-7	2005	Liquid chromatography-mass spectrometry analysis confirmed the microbial PAH transformation by the detection of PAH metabolites 1-hydroxypyrene and 7-hydroxybenzo(a)pyrene in colon digests of pyrene and benzo(a)pyrene.	7-Hydroxybenzo(a)pyrene	148-171	phenylalanine hydroxylase	Homo sapiens	112-115
15626640-7	2005	Liquid chromatography-mass spectrometry analysis confirmed the microbial PAH transformation by the detection of PAH metabolites 1-hydroxypyrene and 7-hydroxybenzo(a)pyrene in colon digests of pyrene and benzo(a)pyrene.	pyrene	137-143	phenylalanine hydroxylase	Homo sapiens	73-76
15626640-7	2005	Liquid chromatography-mass spectrometry analysis confirmed the microbial PAH transformation by the detection of PAH metabolites 1-hydroxypyrene and 7-hydroxybenzo(a)pyrene in colon digests of pyrene and benzo(a)pyrene.	pyrene	137-143	phenylalanine hydroxylase	Homo sapiens	112-115
15626640-7	2005	Liquid chromatography-mass spectrometry analysis confirmed the microbial PAH transformation by the detection of PAH metabolites 1-hydroxypyrene and 7-hydroxybenzo(a)pyrene in colon digests of pyrene and benzo(a)pyrene.	Benzo(a)pyrene	157-171	phenylalanine hydroxylase	Homo sapiens	73-76
15626640-7	2005	Liquid chromatography-mass spectrometry analysis confirmed the microbial PAH transformation by the detection of PAH metabolites 1-hydroxypyrene and 7-hydroxybenzo(a)pyrene in colon digests of pyrene and benzo(a)pyrene.	Benzo(a)pyrene	157-171	phenylalanine hydroxylase	Homo sapiens	112-115
15626640-8	2005	Furthermore, we show that colon digests of a PAH-contaminated soil (simulated ingestion dose of 5 g/day) displayed estrogenic activity equivalent to 0.58 nmol EE2, whereas stomach or small intestine digests did not.	Ethinyl Estradiol	159-162	phenylalanine hydroxylase	Homo sapiens	45-48
15626640-10	2005	Moreover, because PAH toxicity is also linked to estrogenicity of the compounds, the PAH bioactivation potency of colon microbiota suggests that current risk assessment may underestimate the risk from ingested PAHs.	Polycyclic Aromatic Hydrocarbons	210-214	phenylalanine hydroxylase	Homo sapiens	85-88
15595771-8	2004	In addition, comparison to NMR results previously reported allows for conclusions about the mobility of the solvent in the multilayers: the average rotational correlation time of the water molecules in the polyelectrolyte layers decreases upon addition of PSS and increases upon addition of PAH.	Water	183-188	phenylalanine hydroxylase	Homo sapiens	291-294
15926592-0	2005	Removal of PAH compounds from liquid fuels by Pd catalysts.	Palladium	46-48	phenylalanine hydroxylase	Homo sapiens	11-14
15504500-9	2004	The most abundant nitrated PAH derivatives were nitronaphthalenes, which were present exclusively in the vapor phase; 9-nitroanthracene, 9-nitrophenantrene and 3-nitrofluoranthene were associated mostly with particulate matter (PM(10)).	nitronaphthalenes	48-65	phenylalanine hydroxylase	Homo sapiens	27-30
15557004-1	2004	Phenylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently shown normalization of blood phenylalanine levels upon oral administration of the PAH cofactor tetrahydrobiopterin [(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)].	sapropterin	198-217	phenylalanine hydroxylase	Homo sapiens	185-188
15557004-1	2004	Phenylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently shown normalization of blood phenylalanine levels upon oral administration of the PAH cofactor tetrahydrobiopterin [(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)].	sapropterin	219-261	phenylalanine hydroxylase	Homo sapiens	47-72
15557004-1	2004	Phenylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently shown normalization of blood phenylalanine levels upon oral administration of the PAH cofactor tetrahydrobiopterin [(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)].	sapropterin	219-261	phenylalanine hydroxylase	Homo sapiens	74-77
15557004-1	2004	Phenylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently shown normalization of blood phenylalanine levels upon oral administration of the PAH cofactor tetrahydrobiopterin [(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)].	sapropterin	219-261	phenylalanine hydroxylase	Homo sapiens	185-188
15557004-1	2004	Phenylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently shown normalization of blood phenylalanine levels upon oral administration of the PAH cofactor tetrahydrobiopterin [(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)].	sapropterin	263-266	phenylalanine hydroxylase	Homo sapiens	47-72
15557004-1	2004	Phenylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently shown normalization of blood phenylalanine levels upon oral administration of the PAH cofactor tetrahydrobiopterin [(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)].	sapropterin	263-266	phenylalanine hydroxylase	Homo sapiens	74-77
15557004-1	2004	Phenylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently shown normalization of blood phenylalanine levels upon oral administration of the PAH cofactor tetrahydrobiopterin [(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)].	sapropterin	263-266	phenylalanine hydroxylase	Homo sapiens	185-188
15556637-0	2004	Tetrahydrobiopterin protects phenylalanine hydroxylase activity in vivo: implications for tetrahydrobiopterin-responsive hyperphenylalaninemia.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	29-54
15557004-0	2004	Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations.	sapropterin	47-66	phenylalanine hydroxylase	Homo sapiens	108-133
15557004-1	2004	Phenylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently shown normalization of blood phenylalanine levels upon oral administration of the PAH cofactor tetrahydrobiopterin [(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)].	Phenylalanine	47-60	phenylalanine hydroxylase	Homo sapiens	74-77
15557004-1	2004	Phenylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently shown normalization of blood phenylalanine levels upon oral administration of the PAH cofactor tetrahydrobiopterin [(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)].	Phenylalanine	47-60	phenylalanine hydroxylase	Homo sapiens	185-188
15557004-1	2004	Phenylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently shown normalization of blood phenylalanine levels upon oral administration of the PAH cofactor tetrahydrobiopterin [(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)].	sapropterin	198-217	phenylalanine hydroxylase	Homo sapiens	47-72
15557004-1	2004	Phenylketonuria patients harboring a subset of phenylalanine hydroxylase (PAH) mutations have recently shown normalization of blood phenylalanine levels upon oral administration of the PAH cofactor tetrahydrobiopterin [(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)].	sapropterin	198-217	phenylalanine hydroxylase	Homo sapiens	74-77
15556637-1	2004	The natural cofactor of phenylalanine hydroxylase (PAH), tetrahydrobiopterin (BH4), regulates the enzyme activity as well as being essential in catalysis.	sapropterin	57-76	phenylalanine hydroxylase	Homo sapiens	24-49
15556637-1	2004	The natural cofactor of phenylalanine hydroxylase (PAH), tetrahydrobiopterin (BH4), regulates the enzyme activity as well as being essential in catalysis.	sapropterin	57-76	phenylalanine hydroxylase	Homo sapiens	51-54
15556637-1	2004	The natural cofactor of phenylalanine hydroxylase (PAH), tetrahydrobiopterin (BH4), regulates the enzyme activity as well as being essential in catalysis.	sapropterin	78-81	phenylalanine hydroxylase	Homo sapiens	24-49
15556637-1	2004	The natural cofactor of phenylalanine hydroxylase (PAH), tetrahydrobiopterin (BH4), regulates the enzyme activity as well as being essential in catalysis.	sapropterin	78-81	phenylalanine hydroxylase	Homo sapiens	51-54
15537293-2	2004	The feasibility of SPE (solid-phase extraction) and SPME (solid-phase microextraction) for the determination of PAH in drinking water samples has been evaluated.	Water	128-133	phenylalanine hydroxylase	Homo sapiens	112-115
15556637-2	2004	BH4-responsive PAH deficiency is a variant of hyperphenylalaninemia or phenylketonuria (PKU) caused by mutations in the human PAH gene that respond to oral BH4 loading by stimulating enzyme activity and therefore lowering serum phenylalanine.	sapropterin	0-3	phenylalanine hydroxylase	Homo sapiens	15-18
15556637-2	2004	BH4-responsive PAH deficiency is a variant of hyperphenylalaninemia or phenylketonuria (PKU) caused by mutations in the human PAH gene that respond to oral BH4 loading by stimulating enzyme activity and therefore lowering serum phenylalanine.	sapropterin	0-3	phenylalanine hydroxylase	Homo sapiens	126-129
15556637-2	2004	BH4-responsive PAH deficiency is a variant of hyperphenylalaninemia or phenylketonuria (PKU) caused by mutations in the human PAH gene that respond to oral BH4 loading by stimulating enzyme activity and therefore lowering serum phenylalanine.	sapropterin	156-159	phenylalanine hydroxylase	Homo sapiens	15-18
15556637-2	2004	BH4-responsive PAH deficiency is a variant of hyperphenylalaninemia or phenylketonuria (PKU) caused by mutations in the human PAH gene that respond to oral BH4 loading by stimulating enzyme activity and therefore lowering serum phenylalanine.	sapropterin	156-159	phenylalanine hydroxylase	Homo sapiens	126-129
15556637-2	2004	BH4-responsive PAH deficiency is a variant of hyperphenylalaninemia or phenylketonuria (PKU) caused by mutations in the human PAH gene that respond to oral BH4 loading by stimulating enzyme activity and therefore lowering serum phenylalanine.	Phenylalanine	51-64	phenylalanine hydroxylase	Homo sapiens	15-18
15556637-2	2004	BH4-responsive PAH deficiency is a variant of hyperphenylalaninemia or phenylketonuria (PKU) caused by mutations in the human PAH gene that respond to oral BH4 loading by stimulating enzyme activity and therefore lowering serum phenylalanine.	Phenylalanine	51-64	phenylalanine hydroxylase	Homo sapiens	126-129
15556637-3	2004	Here, we showed in a coupled transcription-translation in vitro assay that upon expression in the presence of BH4, wild-type PAH enzyme activity was enhanced.	sapropterin	110-113	phenylalanine hydroxylase	Homo sapiens	125-128
15556637-5	2004	The rate of hepatic PAH enzyme activity increased significantly with BH4 content without affecting gene expression or Pah-mRNA stability.	sapropterin	69-72	phenylalanine hydroxylase	Homo sapiens	20-23
15556637-6	2004	These results indicate that BH4 has a chaperon-like effect on PAH synthesis and/or is a protecting cofactor against enzyme auto-inactivation and degradation also in vivo.	sapropterin	28-31	phenylalanine hydroxylase	Homo sapiens	62-65
15556637-7	2004	Our findings thus contribute to the understanding of the regulation of PAH by its cofactor BH4 on an additional level and provide a molecular explanation for cofactor-responsive PKU.	sapropterin	91-94	phenylalanine hydroxylase	Homo sapiens	71-74
15488581-3	2004	PAH in organic extracts were analyzed by gas chromatography-mass spectrometry (GC-MS) and 25 individual target PAH summed to get the total PAH concentration in each water sample.	Water	165-170	phenylalanine hydroxylase	Homo sapiens	0-3
15319459-0	2004	In vivo studies of phenylalanine hydroxylase by phenylalanine breath test: diagnosis of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency.	sapropterin	88-107	phenylalanine hydroxylase	Homo sapiens	19-44
15493924-0	2004	Thermodynamic characterization of the binding of tetrahydropterins to phenylalanine hydroxylase.	tetrahydropterin	49-66	phenylalanine hydroxylase	Homo sapiens	70-95
15493924-1	2004	Phenylalanine hydroxylase (PAH) is the key enzyme in the catabolism of L-Phe.	Phenylalanine	71-76	phenylalanine hydroxylase	Homo sapiens	0-25
15459954-1	2004	A subtype of phenylalanine hydroxylase (PAH) deficiency that responds to cofactor (tetrahydrobiopterin, BH4) supplementation has been associated with phenylketonuria (PKU) mutations.	sapropterin	83-102	phenylalanine hydroxylase	Homo sapiens	13-38
15459954-1	2004	A subtype of phenylalanine hydroxylase (PAH) deficiency that responds to cofactor (tetrahydrobiopterin, BH4) supplementation has been associated with phenylketonuria (PKU) mutations.	sapropterin	104-107	phenylalanine hydroxylase	Homo sapiens	13-38
15319459-1	2004	Tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency is characterized by reduction of blood phenylalanine level after a BH4-loading test.	sapropterin	147-150	phenylalanine hydroxylase	Homo sapiens	37-62
15319459-1	2004	Tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency is characterized by reduction of blood phenylalanine level after a BH4-loading test.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	37-62
15319459-1	2004	Tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency is characterized by reduction of blood phenylalanine level after a BH4-loading test.	sapropterin	21-24	phenylalanine hydroxylase	Homo sapiens	37-62
15543751-4	2004	Sediment treated with 3.4 wt % activated carbon showed 92% and 84% reductions in aqueous equilibrium PCB and PAH concentrations, 77% and 83% reductions in PCB and PAH uptake by semipermeable membrane devices (SPMD), respectively, and reductions in PCB flux to overlying water in quiescent systems up to 89%.	Carbon	41-47	phenylalanine hydroxylase	Homo sapiens	109-112
15543751-4	2004	Sediment treated with 3.4 wt % activated carbon showed 92% and 84% reductions in aqueous equilibrium PCB and PAH concentrations, 77% and 83% reductions in PCB and PAH uptake by semipermeable membrane devices (SPMD), respectively, and reductions in PCB flux to overlying water in quiescent systems up to 89%.	Carbon	41-47	phenylalanine hydroxylase	Homo sapiens	163-166
15543751-0	2004	Addition of carbon sorbents to reduce PCB and PAH bioavailability in marine sediments: physicochemical tests.	Carbon	12-18	phenylalanine hydroxylase	Homo sapiens	46-49
12744702-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	0-25
15313177-0	2004	Human phenylalanine hydroxylase is activated by H2O2: a novel mechanism for increasing the L-tyrosine supply for melanogenesis in melanocytes.	Hydrogen Peroxide	48-52	phenylalanine hydroxylase	Homo sapiens	6-31
15313177-0	2004	Human phenylalanine hydroxylase is activated by H2O2: a novel mechanism for increasing the L-tyrosine supply for melanogenesis in melanocytes.	Tyrosine	91-101	phenylalanine hydroxylase	Homo sapiens	6-31
15313177-1	2004	Epidermal phenylalanine hydroxylase (PAH) produces L-tyrosine from the essential amino acid L-phenylalanine supporting melanogenesis in human melanocytes.	Tyrosine	51-61	phenylalanine hydroxylase	Homo sapiens	10-35
15313177-1	2004	Epidermal phenylalanine hydroxylase (PAH) produces L-tyrosine from the essential amino acid L-phenylalanine supporting melanogenesis in human melanocytes.	Tyrosine	51-61	phenylalanine hydroxylase	Homo sapiens	37-40
15313177-1	2004	Epidermal phenylalanine hydroxylase (PAH) produces L-tyrosine from the essential amino acid L-phenylalanine supporting melanogenesis in human melanocytes.	essential amino acid l-phenylalanine	71-107	phenylalanine hydroxylase	Homo sapiens	10-35
15313177-1	2004	Epidermal phenylalanine hydroxylase (PAH) produces L-tyrosine from the essential amino acid L-phenylalanine supporting melanogenesis in human melanocytes.	essential amino acid l-phenylalanine	71-107	phenylalanine hydroxylase	Homo sapiens	37-40
15313177-3	2004	Since UVB generates also H(2)O(2), we here asked the question whether this reactive oxygen species could influence the activity of pure recombinant human PAH.	Reactive Oxygen Species	75-98	phenylalanine hydroxylase	Homo sapiens	154-157
15313177-7	2004	PAH was still activated by H(2)O(2) in the presence of the electron donor/cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin despite slow oxidation of this cofactor.	Hydrogen Peroxide	27-35	phenylalanine hydroxylase	Homo sapiens	0-3
15313177-7	2004	PAH was still activated by H(2)O(2) in the presence of the electron donor/cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin despite slow oxidation of this cofactor.	sapropterin	83-125	phenylalanine hydroxylase	Homo sapiens	0-3
15313177-9	2004	Hence, generation of H(2)O(2) by UVB can activate epidermal PAH leading to an increased L-tyrosine pool for melanogenesis.	Tyrosine	88-98	phenylalanine hydroxylase	Homo sapiens	60-63
15276721-5	2004	The measured PAH concentrations in sediments and soils (224-4222 ng/g), runoff water (8.3 microg/l) and air particles (2.3 microg/m(3)) are discussed in relation to concentrations and patterns found in the surface water bodies.	Water	214-219	phenylalanine hydroxylase	Homo sapiens	13-16
15276721-7	2004	The atmospheric PAH deposition to water bodies in the city area of Hangzhou was estimated to be 530 tons/a, while the contribution of surface runoff water was estimated to be 30.7 tons/a.	Water	34-39	phenylalanine hydroxylase	Homo sapiens	16-19
15464430-1	2004	Tetrahydrobiopterin (BH4) responsiveness in patients with mutations in the phenylalanine hydroxylase (PAH) gene is a recently recognized subtype of hyperphenylalaninemia characterized by a positive BH4 loading test.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	75-100
15464430-1	2004	Tetrahydrobiopterin (BH4) responsiveness in patients with mutations in the phenylalanine hydroxylase (PAH) gene is a recently recognized subtype of hyperphenylalaninemia characterized by a positive BH4 loading test.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	102-105
15464430-1	2004	Tetrahydrobiopterin (BH4) responsiveness in patients with mutations in the phenylalanine hydroxylase (PAH) gene is a recently recognized subtype of hyperphenylalaninemia characterized by a positive BH4 loading test.	sapropterin	21-24	phenylalanine hydroxylase	Homo sapiens	75-100
15464430-1	2004	Tetrahydrobiopterin (BH4) responsiveness in patients with mutations in the phenylalanine hydroxylase (PAH) gene is a recently recognized subtype of hyperphenylalaninemia characterized by a positive BH4 loading test.	sapropterin	21-24	phenylalanine hydroxylase	Homo sapiens	102-105
15464430-1	2004	Tetrahydrobiopterin (BH4) responsiveness in patients with mutations in the phenylalanine hydroxylase (PAH) gene is a recently recognized subtype of hyperphenylalaninemia characterized by a positive BH4 loading test.	sapropterin	198-201	phenylalanine hydroxylase	Homo sapiens	75-100
15464430-1	2004	Tetrahydrobiopterin (BH4) responsiveness in patients with mutations in the phenylalanine hydroxylase (PAH) gene is a recently recognized subtype of hyperphenylalaninemia characterized by a positive BH4 loading test.	sapropterin	198-201	phenylalanine hydroxylase	Homo sapiens	102-105
15464430-3	2004	This underscores the importance of identifying BH4-responsive patients in each population, establishing the association with specific PAH mutations.	sapropterin	47-50	phenylalanine hydroxylase	Homo sapiens	134-137
15135070-2	2004	Tyrosine-, tryptophan- and phenylalanine hydroxylase (TH, TPH and PAH, respectively) were transiently activated at low urea concentrations and rapidly inactivated in >3 M urea.	Urea	119-123	phenylalanine hydroxylase	Homo sapiens	66-69
15135070-2	2004	Tyrosine-, tryptophan- and phenylalanine hydroxylase (TH, TPH and PAH, respectively) were transiently activated at low urea concentrations and rapidly inactivated in >3 M urea.	Urea	174-178	phenylalanine hydroxylase	Homo sapiens	66-69
15135070-5	2004	Furthermore, the urea-induced aggregation of hPAH was 100-fold higher than for hTH.	Urea	17-21	phenylalanine hydroxylase	Homo sapiens	45-49
15096628-1	2004	Phosphorylation of phenylalanine hydroxylase (PAH) at Ser16 by cAMP-dependent protein kinase increases the basal activity of the enzyme and its resistance to tryptic proteolysis.	Cyclic AMP	63-67	phenylalanine hydroxylase	Homo sapiens	19-44
15013699-8	2004	This pilot study demonstrates the presence of PAH-DNA adducts in archived paraffin-embedded endoscopic esophageal biopsy samples that are close to 20 years old, and suggests that an appropriate set of archived samples could be used to prospectively correlate PAH-DNA adduct formation with risk of esophageal cancer development.	Paraffin	74-82	phenylalanine hydroxylase	Homo sapiens	46-49
14681498-0	2004	Long-term treatment and diagnosis of tetrahydrobiopterin-responsive hyperphenylalaninemia with a mutant phenylalanine hydroxylase gene.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	104-129
14681498-2	2004	A total of 12 patients who met the criteria for tetrahydrobiopterin (BH(4))-responsive hyperphenylalaninemia (HPA) with a mutant phenylalanine hydroxylase (PAH) (EC 1.14.16.1) gene were recruited at 12 medical centers in Japan between June 1995 and July 2001.	sapropterin	48-67	phenylalanine hydroxylase	Homo sapiens	129-154
14681498-2	2004	A total of 12 patients who met the criteria for tetrahydrobiopterin (BH(4))-responsive hyperphenylalaninemia (HPA) with a mutant phenylalanine hydroxylase (PAH) (EC 1.14.16.1) gene were recruited at 12 medical centers in Japan between June 1995 and July 2001.	sapropterin	48-67	phenylalanine hydroxylase	Homo sapiens	156-159
14637340-4	2004	Aspen wood-water sorption coefficients, Kww, were linearly correlated to octanol-water partition coefficients and the molecular weight of the studied PAH compounds.	Water	11-16	phenylalanine hydroxylase	Homo sapiens	150-153
14637340-4	2004	Aspen wood-water sorption coefficients, Kww, were linearly correlated to octanol-water partition coefficients and the molecular weight of the studied PAH compounds.	Octanols	73-80	phenylalanine hydroxylase	Homo sapiens	150-153
14726806-12	2004	Mapping the mutations that responded to BH4 on the PAH enzyme showed that mutations were in the catalytic, regulatory, oligomerization, and BH4 binding domains.	sapropterin	40-43	phenylalanine hydroxylase	Homo sapiens	51-54
14726806-12	2004	Mapping the mutations that responded to BH4 on the PAH enzyme showed that mutations were in the catalytic, regulatory, oligomerization, and BH4 binding domains.	sapropterin	140-143	phenylalanine hydroxylase	Homo sapiens	51-54
14726806-14	2004	CONCLUSION: The data presented suggest higher than anticipated number of PKU mutations respond to BH4, and such mutations are on all the domains of PAH.	sapropterin	98-101	phenylalanine hydroxylase	Homo sapiens	148-151
14728991-1	2004	Tetrahydrobiopterin (BH(4)) is a required cofactor for the enzymatic activity of phenylalanine hydroxylase (PAH) and is synthesized de novo from GTP in several tissues.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	81-106
14728991-1	2004	Tetrahydrobiopterin (BH(4)) is a required cofactor for the enzymatic activity of phenylalanine hydroxylase (PAH) and is synthesized de novo from GTP in several tissues.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	108-111
14728991-1	2004	Tetrahydrobiopterin (BH(4)) is a required cofactor for the enzymatic activity of phenylalanine hydroxylase (PAH) and is synthesized de novo from GTP in several tissues.	sapropterin	21-26	phenylalanine hydroxylase	Homo sapiens	81-106
14728991-1	2004	Tetrahydrobiopterin (BH(4)) is a required cofactor for the enzymatic activity of phenylalanine hydroxylase (PAH) and is synthesized de novo from GTP in several tissues.	sapropterin	21-26	phenylalanine hydroxylase	Homo sapiens	108-111
14728991-1	2004	Tetrahydrobiopterin (BH(4)) is a required cofactor for the enzymatic activity of phenylalanine hydroxylase (PAH) and is synthesized de novo from GTP in several tissues.	Guanosine Triphosphate	145-148	phenylalanine hydroxylase	Homo sapiens	108-111
14741785-1	2004	Phenylketonuria (PKU) is a disease in which phenylalanine and phenylalanine-derived metabolites build up to neurotoxic levels due to mutations in the phenylalanine hydroxylase gene (PAH).	Phenylalanine	44-57	phenylalanine hydroxylase	Homo sapiens	150-175
14741785-1	2004	Phenylketonuria (PKU) is a disease in which phenylalanine and phenylalanine-derived metabolites build up to neurotoxic levels due to mutations in the phenylalanine hydroxylase gene (PAH).	Phenylalanine	44-57	phenylalanine hydroxylase	Homo sapiens	182-185
14741785-1	2004	Phenylketonuria (PKU) is a disease in which phenylalanine and phenylalanine-derived metabolites build up to neurotoxic levels due to mutations in the phenylalanine hydroxylase gene (PAH).	Phenylalanine	62-75	phenylalanine hydroxylase	Homo sapiens	150-175
14741785-1	2004	Phenylketonuria (PKU) is a disease in which phenylalanine and phenylalanine-derived metabolites build up to neurotoxic levels due to mutations in the phenylalanine hydroxylase gene (PAH).	Phenylalanine	62-75	phenylalanine hydroxylase	Homo sapiens	182-185
14741785-5	2004	Three recombinantly produced PAH enzymes were reacted with activated PEG species, with the aim of developing a stable and active PKU enzyme replacement.	Polyethylene Glycols	69-72	phenylalanine hydroxylase	Homo sapiens	29-32
14741785-8	2004	All PEG-derivatized PAH species retained catalytic activity, and, at low numbers of PEG molecules attached, these PEGylated PAH proteins were found to be more active and more stable than their non-derivatized PAH counterparts.	Polyethylene Glycols	4-7	phenylalanine hydroxylase	Homo sapiens	20-23
14741785-8	2004	All PEG-derivatized PAH species retained catalytic activity, and, at low numbers of PEG molecules attached, these PEGylated PAH proteins were found to be more active and more stable than their non-derivatized PAH counterparts.	Polyethylene Glycols	4-7	phenylalanine hydroxylase	Homo sapiens	124-127
14741785-8	2004	All PEG-derivatized PAH species retained catalytic activity, and, at low numbers of PEG molecules attached, these PEGylated PAH proteins were found to be more active and more stable than their non-derivatized PAH counterparts.	Polyethylene Glycols	4-7	phenylalanine hydroxylase	Homo sapiens	124-127
14741785-8	2004	All PEG-derivatized PAH species retained catalytic activity, and, at low numbers of PEG molecules attached, these PEGylated PAH proteins were found to be more active and more stable than their non-derivatized PAH counterparts.	Polyethylene Glycols	84-87	phenylalanine hydroxylase	Homo sapiens	124-127
14741785-8	2004	All PEG-derivatized PAH species retained catalytic activity, and, at low numbers of PEG molecules attached, these PEGylated PAH proteins were found to be more active and more stable than their non-derivatized PAH counterparts.	Polyethylene Glycols	84-87	phenylalanine hydroxylase	Homo sapiens	124-127
14654659-6	2003	Maternal IQ increased, and the assigned phenylalanine (Phe) levels decreased with decreasing severity of PAH genotype.	Phenylalanine	55-58	phenylalanine hydroxylase	Homo sapiens	105-108
14654665-5	2003	Also, with the aid of recent crystal structure determinations of co-factor and substrate analogs bound at the PAH active site, the recently discovered tetrahydrobiopterin-responsive PKU/HPA genotypes can be mapped onto the PAH structure, providing a molecular basis for this tetrahydrobiopterin response.	sapropterin	151-170	phenylalanine hydroxylase	Homo sapiens	110-113
14654665-5	2003	Also, with the aid of recent crystal structure determinations of co-factor and substrate analogs bound at the PAH active site, the recently discovered tetrahydrobiopterin-responsive PKU/HPA genotypes can be mapped onto the PAH structure, providing a molecular basis for this tetrahydrobiopterin response.	sapropterin	151-170	phenylalanine hydroxylase	Homo sapiens	223-226
14654665-5	2003	Also, with the aid of recent crystal structure determinations of co-factor and substrate analogs bound at the PAH active site, the recently discovered tetrahydrobiopterin-responsive PKU/HPA genotypes can be mapped onto the PAH structure, providing a molecular basis for this tetrahydrobiopterin response.	sapropterin	275-294	phenylalanine hydroxylase	Homo sapiens	110-113
14654665-5	2003	Also, with the aid of recent crystal structure determinations of co-factor and substrate analogs bound at the PAH active site, the recently discovered tetrahydrobiopterin-responsive PKU/HPA genotypes can be mapped onto the PAH structure, providing a molecular basis for this tetrahydrobiopterin response.	sapropterin	275-294	phenylalanine hydroxylase	Homo sapiens	223-226
14568534-0	2003	2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding.	sapropterin	117-136	phenylalanine hydroxylase	Homo sapiens	69-94
14568534-0	2003	2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding.	2-thienylalanine	141-164	phenylalanine hydroxylase	Homo sapiens	69-94
14568534-0	2003	2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding.	Norleucine	168-180	phenylalanine hydroxylase	Homo sapiens	69-94
14568534-1	2003	The crystal structures of the catalytic domain of human phenylalanine hydroxylase (hPheOH) in complex with the physiological cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) and the substrate analogues 3-(2-thienyl)-L-alanine (THA) or L-norleucine (NLE) have been determined at 2.0A resolution.	sapropterin	134-176	phenylalanine hydroxylase	Homo sapiens	56-81
14568534-1	2003	The crystal structures of the catalytic domain of human phenylalanine hydroxylase (hPheOH) in complex with the physiological cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) and the substrate analogues 3-(2-thienyl)-L-alanine (THA) or L-norleucine (NLE) have been determined at 2.0A resolution.	2-thienylalanine	213-236	phenylalanine hydroxylase	Homo sapiens	56-81
14568534-1	2003	The crystal structures of the catalytic domain of human phenylalanine hydroxylase (hPheOH) in complex with the physiological cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) and the substrate analogues 3-(2-thienyl)-L-alanine (THA) or L-norleucine (NLE) have been determined at 2.0A resolution.	tha	238-241	phenylalanine hydroxylase	Homo sapiens	56-81
14568534-1	2003	The crystal structures of the catalytic domain of human phenylalanine hydroxylase (hPheOH) in complex with the physiological cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) and the substrate analogues 3-(2-thienyl)-L-alanine (THA) or L-norleucine (NLE) have been determined at 2.0A resolution.	Norleucine	246-258	phenylalanine hydroxylase	Homo sapiens	56-81
14568534-1	2003	The crystal structures of the catalytic domain of human phenylalanine hydroxylase (hPheOH) in complex with the physiological cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) and the substrate analogues 3-(2-thienyl)-L-alanine (THA) or L-norleucine (NLE) have been determined at 2.0A resolution.	Norleucine	260-263	phenylalanine hydroxylase	Homo sapiens	56-81
12919719-9	2003	These results may suggest an association between levels of the exposure biomarker 1-OH-P and presence of the CYP1A1*2A genotype, a potential genetic susceptibility biomarker which might be useful in identifying individuals at higher risk among people exposed to high PAH levels in diesel exhaust.	Oxaliplatin	82-88	phenylalanine hydroxylase	Homo sapiens	267-270
12860366-11	2003	The increase in the ratio between PHE and TYR suggests inhibition of the enzyme phenylalanine hydroxylase.	Phenylalanine	34-37	phenylalanine hydroxylase	Homo sapiens	80-105
12860366-11	2003	The increase in the ratio between PHE and TYR suggests inhibition of the enzyme phenylalanine hydroxylase.	Tyrosine	42-45	phenylalanine hydroxylase	Homo sapiens	80-105
15060071-1	2004	Phenylalanine hydroxylase (PAH) is generally considered to undergo a large and reversible conformational transition upon l-Phe binding, which is closely linked to the substrate-induced catalytic activation of this hysteretic enzyme.	Phenylalanine	121-126	phenylalanine hydroxylase	Homo sapiens	0-25
15060071-1	2004	Phenylalanine hydroxylase (PAH) is generally considered to undergo a large and reversible conformational transition upon l-Phe binding, which is closely linked to the substrate-induced catalytic activation of this hysteretic enzyme.	Phenylalanine	121-126	phenylalanine hydroxylase	Homo sapiens	27-30
15060071-3	2004	On this basis, single-site mutagenesis of key residues in these regions of the human PAH tetramer was performed in the present study, and their functional impact was measured by steady-state kinetics and the global conformational transition as assessed by surface plasmon resonance and intrinsic tryptophan fluorescence spectroscopy.	Tryptophan	296-306	phenylalanine hydroxylase	Homo sapiens	85-88
15060071-4	2004	A strong correlation (r(2) = 0.93-0.96) was observed between the l-Phe-induced global conformational transition and V(max) values for wild-type human PAH and the mutant forms K113P, N223D, N426D, and N32D, in contrast to the substitution T427P, which resulted in a tetrameric form with no kinetic cooperativity.	Phenylalanine	65-70	phenylalanine hydroxylase	Homo sapiens	150-153
15803720-2	2004	Cell adhesive patterns were created on cell resistant multilayer films composed of poly(acrylic acid) and polyacrylamide through polymer-on-polymer stamping of poly(allylamine hydrochloride) PAH and subsequent reaction of the amine functional groups with an adhesion ligand containing RGD (Arg-Gly-Asp).	carbopol 940	83-101	phenylalanine hydroxylase	Homo sapiens	191-194
15803720-2	2004	Cell adhesive patterns were created on cell resistant multilayer films composed of poly(acrylic acid) and polyacrylamide through polymer-on-polymer stamping of poly(allylamine hydrochloride) PAH and subsequent reaction of the amine functional groups with an adhesion ligand containing RGD (Arg-Gly-Asp).	polyacrylamide	106-120	phenylalanine hydroxylase	Homo sapiens	191-194
15803720-2	2004	Cell adhesive patterns were created on cell resistant multilayer films composed of poly(acrylic acid) and polyacrylamide through polymer-on-polymer stamping of poly(allylamine hydrochloride) PAH and subsequent reaction of the amine functional groups with an adhesion ligand containing RGD (Arg-Gly-Asp).	Polymers	129-136	phenylalanine hydroxylase	Homo sapiens	191-194
15803720-2	2004	Cell adhesive patterns were created on cell resistant multilayer films composed of poly(acrylic acid) and polyacrylamide through polymer-on-polymer stamping of poly(allylamine hydrochloride) PAH and subsequent reaction of the amine functional groups with an adhesion ligand containing RGD (Arg-Gly-Asp).	Polymers	140-147	phenylalanine hydroxylase	Homo sapiens	191-194
15159646-6	2004	This report demonstrates that when discordant phenotypes occur in a family, without protein loading or phenylalanine tolerance test, complete analysis of the PAH gene may be performed in order to support the diagnosis and assist in accurate genetic counselling and patient management.	Phenylalanine	103-116	phenylalanine hydroxylase	Homo sapiens	158-161
12836060-1	2003	We describe six children with tetrahydrobiopterin (BH(4)) responsive phenylalanine hydroxylase (PAH) deficiency.	sapropterin	30-49	phenylalanine hydroxylase	Homo sapiens	69-94
12836060-1	2003	We describe six children with tetrahydrobiopterin (BH(4)) responsive phenylalanine hydroxylase (PAH) deficiency.	sapropterin	30-49	phenylalanine hydroxylase	Homo sapiens	96-99
12836060-1	2003	We describe six children with tetrahydrobiopterin (BH(4)) responsive phenylalanine hydroxylase (PAH) deficiency.	sapropterin	51-56	phenylalanine hydroxylase	Homo sapiens	69-94
12836060-1	2003	We describe six children with tetrahydrobiopterin (BH(4)) responsive phenylalanine hydroxylase (PAH) deficiency.	sapropterin	51-56	phenylalanine hydroxylase	Homo sapiens	96-99
12836060-6	2003	Previous in vitro studies have demonstrated that BH(4) inhibits PAH tetramers but activates PAH dimers.	sapropterin	49-54	phenylalanine hydroxylase	Homo sapiens	64-67
12836060-6	2003	Previous in vitro studies have demonstrated that BH(4) inhibits PAH tetramers but activates PAH dimers.	sapropterin	49-54	phenylalanine hydroxylase	Homo sapiens	92-95
12854704-6	2003	The octanol-air partition coefficient (K(OA)) derived model provides a good description of PAH soil-air partitioning coefficients (K(P)) below the inversion layer but underpredicts them in the area dominated by deposition of long-range transported aerosols without inputs of organic matter from local vegetation.	Octanols	4-11	phenylalanine hydroxylase	Homo sapiens	91-94
12744702-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	27-30
12744702-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate.	Phenylalanine	110-125	phenylalanine hydroxylase	Homo sapiens	0-25
12744702-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate.	Phenylalanine	110-125	phenylalanine hydroxylase	Homo sapiens	27-30
12744702-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate.	Phenylalanine	127-132	phenylalanine hydroxylase	Homo sapiens	0-25
12744702-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate.	Phenylalanine	127-132	phenylalanine hydroxylase	Homo sapiens	27-30
12744702-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate.	Tyrosine	137-147	phenylalanine hydroxylase	Homo sapiens	0-25
12744702-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate.	Tyrosine	137-147	phenylalanine hydroxylase	Homo sapiens	27-30
12744702-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate.	Oxygen	154-162	phenylalanine hydroxylase	Homo sapiens	0-25
12744702-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate.	Oxygen	154-162	phenylalanine hydroxylase	Homo sapiens	27-30
12744702-8	2003	By doing so, 6R-BH(4) facilitates an interaction between Glu21 and the active site iron, further pulling the N-terminal into the active site of PAH and blocking the L-Phe binding site.	6r-bh	13-18	phenylalanine hydroxylase	Homo sapiens	144-147
12873431-0	2003	L-[1-13C] phenylalanine breath test reflects phenylalanine hydroxylase activity of the whole liver.	-[1-13c	1-8	phenylalanine hydroxylase	Homo sapiens	45-70
12714182-1	2003	Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene (12q22-q24) resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe) and production of the phenylketonuria (PKU) disease.	Phenylalanine	193-206	phenylalanine hydroxylase	Homo sapiens	0-25
12873431-5	2003	Subsequently, we examined the relationship between the results of PBT and PAH activity.	(E)-2-(pent-3-en-1-yn-1-yl)thiophene	66-69	phenylalanine hydroxylase	Homo sapiens	74-77
12873431-7	2003	The results of PBT %13C dose h(-1) correlated with the PAH activity/liver, with correlation coefficients at 30, 45, and 60 min of more than 0.7, and the maximum correlation was at 30 min (r = 0.821, P < 0.0001).	(E)-2-(pent-3-en-1-yn-1-yl)thiophene	15-18	phenylalanine hydroxylase	Homo sapiens	55-58
12873431-7	2003	The results of PBT %13C dose h(-1) correlated with the PAH activity/liver, with correlation coefficients at 30, 45, and 60 min of more than 0.7, and the maximum correlation was at 30 min (r = 0.821, P < 0.0001).	13c	20-23	phenylalanine hydroxylase	Homo sapiens	55-58
12873431-8	2003	%13C cumulative excretion correlated with the PAH activity/liver with correlation coefficients of more than 0.7 after 45 min.	13c	1-4	phenylalanine hydroxylase	Homo sapiens	46-49
12873431-10	2003	CONCLUSION: PBT values reflect PAH activity in the whole liver and, in particular, the % dose h(-1) at 30 min after oral administration highly correlates with PAH activity, providing an important indicator for monitoring changes in whole liver PAH activity.	(E)-2-(pent-3-en-1-yn-1-yl)thiophene	12-15	phenylalanine hydroxylase	Homo sapiens	31-34
12873431-10	2003	CONCLUSION: PBT values reflect PAH activity in the whole liver and, in particular, the % dose h(-1) at 30 min after oral administration highly correlates with PAH activity, providing an important indicator for monitoring changes in whole liver PAH activity.	(E)-2-(pent-3-en-1-yn-1-yl)thiophene	12-15	phenylalanine hydroxylase	Homo sapiens	159-162
12873431-10	2003	CONCLUSION: PBT values reflect PAH activity in the whole liver and, in particular, the % dose h(-1) at 30 min after oral administration highly correlates with PAH activity, providing an important indicator for monitoring changes in whole liver PAH activity.	(E)-2-(pent-3-en-1-yn-1-yl)thiophene	12-15	phenylalanine hydroxylase	Homo sapiens	159-162
12714182-1	2003	Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene (12q22-q24) resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe) and production of the phenylketonuria (PKU) disease.	Phenylalanine	193-206	phenylalanine hydroxylase	Homo sapiens	27-30
12714182-1	2003	Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene (12q22-q24) resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe) and production of the phenylketonuria (PKU) disease.	Phenylalanine	193-206	phenylalanine hydroxylase	Homo sapiens	73-76
12714182-1	2003	Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene (12q22-q24) resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe) and production of the phenylketonuria (PKU) disease.	Phenylalanine	193-206	phenylalanine hydroxylase	Homo sapiens	73-76
12733906-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent, nonheme iron enzyme that catalyzes the hydroxylation of L-Phe to L-Tyr in the rate-limiting step of phenylalanine catabolism.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	0-25
12714182-1	2003	Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene (12q22-q24) resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe) and production of the phenylketonuria (PKU) disease.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	27-30
12733906-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent, nonheme iron enzyme that catalyzes the hydroxylation of L-Phe to L-Tyr in the rate-limiting step of phenylalanine catabolism.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	27-30
12714182-1	2003	Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene (12q22-q24) resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe) and production of the phenylketonuria (PKU) disease.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	73-76
12733906-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent, nonheme iron enzyme that catalyzes the hydroxylation of L-Phe to L-Tyr in the rate-limiting step of phenylalanine catabolism.	Iron	76-80	phenylalanine hydroxylase	Homo sapiens	0-25
12714182-1	2003	Phenylalanine hydroxylase (PAH) deficiency is caused by mutations in the PAH gene (12q22-q24) resulting in a primary deficiency of the PAH enzyme activity, intolerance to the dietary intake of phenylalanine (Phe) and production of the phenylketonuria (PKU) disease.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	73-76
12733906-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent, nonheme iron enzyme that catalyzes the hydroxylation of L-Phe to L-Tyr in the rate-limiting step of phenylalanine catabolism.	Iron	76-80	phenylalanine hydroxylase	Homo sapiens	27-30
12733906-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent, nonheme iron enzyme that catalyzes the hydroxylation of L-Phe to L-Tyr in the rate-limiting step of phenylalanine catabolism.	Phenylalanine	124-129	phenylalanine hydroxylase	Homo sapiens	0-25
12714182-6	2003	In the next step, the presence of 18 common mutations of the PAH gene in 26 of the patients with classical PKU (serum Phe above 20mg/dl) was investigated, using the polymerase chain reaction restriction fragment length polymorphism (PCR-RFLP).	Phenylalanine	118-121	phenylalanine hydroxylase	Homo sapiens	61-64
12733906-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent, nonheme iron enzyme that catalyzes the hydroxylation of L-Phe to L-Tyr in the rate-limiting step of phenylalanine catabolism.	Phenylalanine	124-129	phenylalanine hydroxylase	Homo sapiens	27-30
12554741-2	2003	Recombinant human phenylalanine hydroxylase (hPAH) expressed in Escherichia coli for 24 h at 28 degrees C has been found by two-dimensional electrophoresis to exist as a mixture of four to five molecular forms as a result of nonenzymatic deamidation of labile Asn residues.	Asparagine	260-263	phenylalanine hydroxylase	Homo sapiens	18-43
12733906-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent, nonheme iron enzyme that catalyzes the hydroxylation of L-Phe to L-Tyr in the rate-limiting step of phenylalanine catabolism.	Tyrosine	133-138	phenylalanine hydroxylase	Homo sapiens	0-25
12733906-1	2003	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent, nonheme iron enzyme that catalyzes the hydroxylation of L-Phe to L-Tyr in the rate-limiting step of phenylalanine catabolism.	Tyrosine	133-138	phenylalanine hydroxylase	Homo sapiens	27-30
12733906-8	2003	These results provide insight into the PAH reaction and disease mechanism at a molecular level, indicating that the first step of the mechanism is formation of a peroxy-pterin species, which subsequently reacts with the Fe(II) site if the pterin is properly oriented for formation of an Fe-OO-pterin bridge and an open coordination position is available on the Fe(II).	peroxy-pterin	162-175	phenylalanine hydroxylase	Homo sapiens	39-42
12733906-8	2003	These results provide insight into the PAH reaction and disease mechanism at a molecular level, indicating that the first step of the mechanism is formation of a peroxy-pterin species, which subsequently reacts with the Fe(II) site if the pterin is properly oriented for formation of an Fe-OO-pterin bridge and an open coordination position is available on the Fe(II).	ammonium ferrous sulfate	220-226	phenylalanine hydroxylase	Homo sapiens	39-42
12733906-8	2003	These results provide insight into the PAH reaction and disease mechanism at a molecular level, indicating that the first step of the mechanism is formation of a peroxy-pterin species, which subsequently reacts with the Fe(II) site if the pterin is properly oriented for formation of an Fe-OO-pterin bridge and an open coordination position is available on the Fe(II).	Pterins	169-175	phenylalanine hydroxylase	Homo sapiens	39-42
12733906-8	2003	These results provide insight into the PAH reaction and disease mechanism at a molecular level, indicating that the first step of the mechanism is formation of a peroxy-pterin species, which subsequently reacts with the Fe(II) site if the pterin is properly oriented for formation of an Fe-OO-pterin bridge and an open coordination position is available on the Fe(II).	fe-oo-pterin	287-299	phenylalanine hydroxylase	Homo sapiens	39-42
12733906-8	2003	These results provide insight into the PAH reaction and disease mechanism at a molecular level, indicating that the first step of the mechanism is formation of a peroxy-pterin species, which subsequently reacts with the Fe(II) site if the pterin is properly oriented for formation of an Fe-OO-pterin bridge and an open coordination position is available on the Fe(II).	ammonium ferrous sulfate	361-367	phenylalanine hydroxylase	Homo sapiens	39-42
12554741-2	2003	Recombinant human phenylalanine hydroxylase (hPAH) expressed in Escherichia coli for 24 h at 28 degrees C has been found by two-dimensional electrophoresis to exist as a mixture of four to five molecular forms as a result of nonenzymatic deamidation of labile Asn residues.	Asparagine	260-263	phenylalanine hydroxylase	Homo sapiens	45-49
12554741-11	2003	Moreover, deamidation of Asn(32) in the wt-hPAH (24 h expression at 28 degrees C) and the Asn(32) --> Asp mutation both increase the initial rate of phosphorylation of Ser(16) by cAMP-dependent protein kinase (p < 0.005).	Asparagine	25-28	phenylalanine hydroxylase	Homo sapiens	43-47
12554741-11	2003	Moreover, deamidation of Asn(32) in the wt-hPAH (24 h expression at 28 degrees C) and the Asn(32) --> Asp mutation both increase the initial rate of phosphorylation of Ser(16) by cAMP-dependent protein kinase (p < 0.005).	Serine	171-174	phenylalanine hydroxylase	Homo sapiens	43-47
12655545-8	2003	The intracellular steady-state levels of the mutant PAH enzyme are therefore reduced, leading to an overall decrease in phenylalanine hydroxylation within cells and thus to hyperphenylalaninemia.	Phenylalanine	120-133	phenylalanine hydroxylase	Homo sapiens	52-55
12644360-1	2003	BACKGROUND: Reports relating phenylalanine kinetics and metabolism to psychiatric disorders led us to undertake the comprehensive screening of the phenylalanine hydroxylase (PAH) coding region and functional testing of discovered mutations in a sample of psychiatric patients and healthy control subjects.	Phenylalanine	29-42	phenylalanine hydroxylase	Homo sapiens	174-177
12644360-6	2003	The four schizophrenic patients heterozygous for the novel K274E mutation showed significantly decreased phenylalanine kinetics, reduced conversion to tyrosine, and increased synthesis of the PAH cofactor tetrahydrobiopterin compared with schizophrenic subjects without the mutation.	sapropterin	205-224	phenylalanine hydroxylase	Homo sapiens	192-195
12603326-0	2003	Deamidation of labile asparagine residues in the autoregulatory sequence of human phenylalanine hydroxylase.	Asparagine	22-32	phenylalanine hydroxylase	Homo sapiens	82-107
12603326-1	2003	Two dimensional electrophoresis has revealed a microheterogeneity in the recombinant human phenylalanine hydroxylase (hPAH) protomer, that is the result of spontaneous nonenzymatic deamidations of labile asparagine (Asn) residues [Solstad, T. and Flatmark, T. (2000) Eur.	Asparagine	204-214	phenylalanine hydroxylase	Homo sapiens	91-116
12603326-1	2003	Two dimensional electrophoresis has revealed a microheterogeneity in the recombinant human phenylalanine hydroxylase (hPAH) protomer, that is the result of spontaneous nonenzymatic deamidations of labile asparagine (Asn) residues [Solstad, T. and Flatmark, T. (2000) Eur.	Asparagine	216-219	phenylalanine hydroxylase	Homo sapiens	91-116
12603331-0	2003	Studies on the regulatory properties of the pterin cofactor and dopamine bound at the active site of human phenylalanine hydroxylase.	Pterins	44-50	phenylalanine hydroxylase	Homo sapiens	107-132
12603331-0	2003	Studies on the regulatory properties of the pterin cofactor and dopamine bound at the active site of human phenylalanine hydroxylase.	Dopamine	64-72	phenylalanine hydroxylase	Homo sapiens	107-132
12603331-1	2003	The catalytic activity of phenylalanine hydroxylase (PAH, phenylalanine 4-monooxygenase EC 1.14.16.1) is regulated by three main mechanisms, i.e. substrate (l-phenylalanine, L-Phe) activation, pterin cofactor inhibition and phosphorylation of a single serine (Ser16) residue.	Phenylalanine	157-172	phenylalanine hydroxylase	Homo sapiens	26-51
12603331-1	2003	The catalytic activity of phenylalanine hydroxylase (PAH, phenylalanine 4-monooxygenase EC 1.14.16.1) is regulated by three main mechanisms, i.e. substrate (l-phenylalanine, L-Phe) activation, pterin cofactor inhibition and phosphorylation of a single serine (Ser16) residue.	Phenylalanine	174-179	phenylalanine hydroxylase	Homo sapiens	26-51
12603331-1	2003	The catalytic activity of phenylalanine hydroxylase (PAH, phenylalanine 4-monooxygenase EC 1.14.16.1) is regulated by three main mechanisms, i.e. substrate (l-phenylalanine, L-Phe) activation, pterin cofactor inhibition and phosphorylation of a single serine (Ser16) residue.	Pterins	193-199	phenylalanine hydroxylase	Homo sapiens	26-51
12603331-1	2003	The catalytic activity of phenylalanine hydroxylase (PAH, phenylalanine 4-monooxygenase EC 1.14.16.1) is regulated by three main mechanisms, i.e. substrate (l-phenylalanine, L-Phe) activation, pterin cofactor inhibition and phosphorylation of a single serine (Ser16) residue.	Serine	252-258	phenylalanine hydroxylase	Homo sapiens	26-51
12588145-1	2003	The complex [(PAH)(4)Cu(II)(4)Cu(I)(2)Br(10)] (1) (PAH = picolinamide hydrazone) containing a Cu(II)(4)Cu(I)(2) hexanuclear cluster, with two well-separated Cu(II)(2) dinuclear centers, results from a redox reaction involving a hydrolytically unstable ligand, salicilyl picolinamide hydrazone, and CuBr(2) in aqueous acetonitrile.	cu(ii)	21-27	phenylalanine hydroxylase	Homo sapiens	14-17
12588145-1	2003	The complex [(PAH)(4)Cu(II)(4)Cu(I)(2)Br(10)] (1) (PAH = picolinamide hydrazone) containing a Cu(II)(4)Cu(I)(2) hexanuclear cluster, with two well-separated Cu(II)(2) dinuclear centers, results from a redox reaction involving a hydrolytically unstable ligand, salicilyl picolinamide hydrazone, and CuBr(2) in aqueous acetonitrile.	Copper	21-23	phenylalanine hydroxylase	Homo sapiens	14-17
12588145-1	2003	The complex [(PAH)(4)Cu(II)(4)Cu(I)(2)Br(10)] (1) (PAH = picolinamide hydrazone) containing a Cu(II)(4)Cu(I)(2) hexanuclear cluster, with two well-separated Cu(II)(2) dinuclear centers, results from a redox reaction involving a hydrolytically unstable ligand, salicilyl picolinamide hydrazone, and CuBr(2) in aqueous acetonitrile.	Copper	21-24	phenylalanine hydroxylase	Homo sapiens	14-17
12588145-1	2003	The complex [(PAH)(4)Cu(II)(4)Cu(I)(2)Br(10)] (1) (PAH = picolinamide hydrazone) containing a Cu(II)(4)Cu(I)(2) hexanuclear cluster, with two well-separated Cu(II)(2) dinuclear centers, results from a redox reaction involving a hydrolytically unstable ligand, salicilyl picolinamide hydrazone, and CuBr(2) in aqueous acetonitrile.	cu(ii)	94-100	phenylalanine hydroxylase	Homo sapiens	14-17
12379147-1	2003	The optical biosensor technique, based on the surface plasmon resonance (SPR) phenomenon, was used for real-time measurements of the slow conformational transition (isomerization) which occurs in human phenylalanine hydroxylase (hPAH) on the binding/dissociation of L-phenylalanine (L-Phe).	Phenylalanine	266-281	phenylalanine hydroxylase	Homo sapiens	202-227
12379147-1	2003	The optical biosensor technique, based on the surface plasmon resonance (SPR) phenomenon, was used for real-time measurements of the slow conformational transition (isomerization) which occurs in human phenylalanine hydroxylase (hPAH) on the binding/dissociation of L-phenylalanine (L-Phe).	Phenylalanine	266-281	phenylalanine hydroxylase	Homo sapiens	229-233
12379147-1	2003	The optical biosensor technique, based on the surface plasmon resonance (SPR) phenomenon, was used for real-time measurements of the slow conformational transition (isomerization) which occurs in human phenylalanine hydroxylase (hPAH) on the binding/dissociation of L-phenylalanine (L-Phe).	Phenylalanine	283-288	phenylalanine hydroxylase	Homo sapiens	202-227
12379147-1	2003	The optical biosensor technique, based on the surface plasmon resonance (SPR) phenomenon, was used for real-time measurements of the slow conformational transition (isomerization) which occurs in human phenylalanine hydroxylase (hPAH) on the binding/dissociation of L-phenylalanine (L-Phe).	Phenylalanine	283-288	phenylalanine hydroxylase	Homo sapiens	229-233
12379147-7	2003	The binding isotherm for tetrameric and dimeric wt-hPAH revealed a [S](0.5)-value of 98+/-7 microM (h =1.0) and 158+/-11 microM, respectively, i.e. for the tetramer it is slightly lower than the value (145+/-5 microM) obtained for the co-operative binding (h =1.6+/-0.4) of L-Phe as measured by the change in intrinsic tryptophan fluorescence.	Phenylalanine	274-279	phenylalanine hydroxylase	Homo sapiens	51-55
12379147-7	2003	The binding isotherm for tetrameric and dimeric wt-hPAH revealed a [S](0.5)-value of 98+/-7 microM (h =1.0) and 158+/-11 microM, respectively, i.e. for the tetramer it is slightly lower than the value (145+/-5 microM) obtained for the co-operative binding (h =1.6+/-0.4) of L-Phe as measured by the change in intrinsic tryptophan fluorescence.	Tryptophan	319-329	phenylalanine hydroxylase	Homo sapiens	51-55
12379147-11	2003	The substrate analogue 3-(2-thienyl)-L-alanine revealed an SPR response comparable with that of L-Phe on binding to wild-type hPAH.	2-thienylalanine	23-46	phenylalanine hydroxylase	Homo sapiens	126-130
12379147-11	2003	The substrate analogue 3-(2-thienyl)-L-alanine revealed an SPR response comparable with that of L-Phe on binding to wild-type hPAH.	Phenylalanine	96-101	phenylalanine hydroxylase	Homo sapiens	126-130
12728980-4	2003	In the last two decades, one highly conserved group of PAH-catabolic genes from Pseudomonas species, called the nah-like genes, has been well investigated, and much has been found, including the structure-function relationships and the evolutionary trails of the catabolic enzymes.	sodium bisulfide	112-115	phenylalanine hydroxylase	Homo sapiens	55-58
12728980-5	2003	However, recently, PAH-catabolic genes, which are evolutionarily different from the nah-like genes, have been characterized from both Gram-negative bacteria other than Pseudomonas species and Gram-positive bacteria, and the information about these genes is expanding.	sodium bisulfide	84-87	phenylalanine hydroxylase	Homo sapiens	19-22
12696880-0	2003	Posttranslational hydroxylation of human phenylalanine hydroxylase is a novel example of enzyme self-repair within the second coordination sphere of catalytic iron.	Iron	159-163	phenylalanine hydroxylase	Homo sapiens	41-66
12696880-1	2003	Phenylalanine hydroxylase, a mononuclear non-heme iron enzyme, catalyzes the hydroxylation of phenylalanine to tyrosine in the presence of oxygen and reduced pterin cofactor.	Iron	50-54	phenylalanine hydroxylase	Homo sapiens	0-25
12696880-1	2003	Phenylalanine hydroxylase, a mononuclear non-heme iron enzyme, catalyzes the hydroxylation of phenylalanine to tyrosine in the presence of oxygen and reduced pterin cofactor.	Phenylalanine	94-107	phenylalanine hydroxylase	Homo sapiens	0-25
12696880-1	2003	Phenylalanine hydroxylase, a mononuclear non-heme iron enzyme, catalyzes the hydroxylation of phenylalanine to tyrosine in the presence of oxygen and reduced pterin cofactor.	Tyrosine	111-119	phenylalanine hydroxylase	Homo sapiens	0-25
12696880-1	2003	Phenylalanine hydroxylase, a mononuclear non-heme iron enzyme, catalyzes the hydroxylation of phenylalanine to tyrosine in the presence of oxygen and reduced pterin cofactor.	Oxygen	139-145	phenylalanine hydroxylase	Homo sapiens	0-25
12696880-1	2003	Phenylalanine hydroxylase, a mononuclear non-heme iron enzyme, catalyzes the hydroxylation of phenylalanine to tyrosine in the presence of oxygen and reduced pterin cofactor.	Pterins	158-164	phenylalanine hydroxylase	Homo sapiens	0-25
12696880-3	2003	One such interaction involves Tyr325 in human phenylalanine hydroxylase (hPAH), which forms a hydrogen-bonding network with an aqua ligand on iron and the pterin cofactor.	Hydrogen	94-102	phenylalanine hydroxylase	Homo sapiens	46-71
12696880-3	2003	One such interaction involves Tyr325 in human phenylalanine hydroxylase (hPAH), which forms a hydrogen-bonding network with an aqua ligand on iron and the pterin cofactor.	Hydrogen	94-102	phenylalanine hydroxylase	Homo sapiens	73-77
12696880-3	2003	One such interaction involves Tyr325 in human phenylalanine hydroxylase (hPAH), which forms a hydrogen-bonding network with an aqua ligand on iron and the pterin cofactor.	Iron	142-146	phenylalanine hydroxylase	Homo sapiens	46-71
12696880-3	2003	One such interaction involves Tyr325 in human phenylalanine hydroxylase (hPAH), which forms a hydrogen-bonding network with an aqua ligand on iron and the pterin cofactor.	Iron	142-146	phenylalanine hydroxylase	Homo sapiens	73-77
12653545-11	2003	The same conformational changes appear to be involved in the activation of PAH induced by L-Phe.	Phenylalanine	90-95	phenylalanine hydroxylase	Homo sapiens	75-78
12586143-2	2003	The aim of this investigation was to trace back the alterations of the formation and the distribution behavior of PAH and PCDD/PCDF to the presence of CuO or a mixture of metal oxides (CdO, CuO, Fe(2)O(3), PbO, MoO(3), ZnO).	cupric oxide	151-154	phenylalanine hydroxylase	Homo sapiens	114-117
12586143-2	2003	The aim of this investigation was to trace back the alterations of the formation and the distribution behavior of PAH and PCDD/PCDF to the presence of CuO or a mixture of metal oxides (CdO, CuO, Fe(2)O(3), PbO, MoO(3), ZnO).	metal oxides	171-183	phenylalanine hydroxylase	Homo sapiens	114-117
12586143-2	2003	The aim of this investigation was to trace back the alterations of the formation and the distribution behavior of PAH and PCDD/PCDF to the presence of CuO or a mixture of metal oxides (CdO, CuO, Fe(2)O(3), PbO, MoO(3), ZnO).	cupric oxide	190-193	phenylalanine hydroxylase	Homo sapiens	114-117
12586143-2	2003	The aim of this investigation was to trace back the alterations of the formation and the distribution behavior of PAH and PCDD/PCDF to the presence of CuO or a mixture of metal oxides (CdO, CuO, Fe(2)O(3), PbO, MoO(3), ZnO).	fe(2)o	195-201	phenylalanine hydroxylase	Homo sapiens	114-117
12586143-2	2003	The aim of this investigation was to trace back the alterations of the formation and the distribution behavior of PAH and PCDD/PCDF to the presence of CuO or a mixture of metal oxides (CdO, CuO, Fe(2)O(3), PbO, MoO(3), ZnO).	pbo	206-209	phenylalanine hydroxylase	Homo sapiens	114-117
12586143-2	2003	The aim of this investigation was to trace back the alterations of the formation and the distribution behavior of PAH and PCDD/PCDF to the presence of CuO or a mixture of metal oxides (CdO, CuO, Fe(2)O(3), PbO, MoO(3), ZnO).	moo	211-214	phenylalanine hydroxylase	Homo sapiens	114-117
12586143-2	2003	The aim of this investigation was to trace back the alterations of the formation and the distribution behavior of PAH and PCDD/PCDF to the presence of CuO or a mixture of metal oxides (CdO, CuO, Fe(2)O(3), PbO, MoO(3), ZnO).	Zinc Oxide	219-222	phenylalanine hydroxylase	Homo sapiens	114-117
12586143-3	2003	The total amount of the 16 PAH target compounds was reduced by the factor of 5-9 when the mixture of metal oxides was present rather than merely CuO.	metal oxides	101-113	phenylalanine hydroxylase	Homo sapiens	27-30
12631267-3	2003	Based on the crystal structures 5pah for PAH and 2toh for TH (Protein Data Bank), we have used molecular docking to model the binding of 6(R)-l-erythro-5,6,7,8-tetrahydrobiopterin (BH4) and the substrates phenylalanine and tyrosine to the catalytic domains of PAH and TH.	sapropterin	137-179	phenylalanine hydroxylase	Homo sapiens	41-44
12631267-3	2003	Based on the crystal structures 5pah for PAH and 2toh for TH (Protein Data Bank), we have used molecular docking to model the binding of 6(R)-l-erythro-5,6,7,8-tetrahydrobiopterin (BH4) and the substrates phenylalanine and tyrosine to the catalytic domains of PAH and TH.	sapropterin	137-179	phenylalanine hydroxylase	Homo sapiens	260-263
12631267-6	2003	Despite favorable energy scores, tyrosine in a position trans to PAH residue His290 or TH residue His336 interferes with the access of the essential cofactor dioxygen to the catalytic center, thereby blocking the enzymatic reaction.	Tyrosine	33-41	phenylalanine hydroxylase	Homo sapiens	65-68
12631267-6	2003	Despite favorable energy scores, tyrosine in a position trans to PAH residue His290 or TH residue His336 interferes with the access of the essential cofactor dioxygen to the catalytic center, thereby blocking the enzymatic reaction.	Oxygen	158-166	phenylalanine hydroxylase	Homo sapiens	65-68
12631267-8	2003	Two alternative conformations, rotated 180 degrees around an imaginary iron-catecholamine axis, were found for DA and l-DOPA in PAH and for DA in TH.	Iron	71-75	phenylalanine hydroxylase	Homo sapiens	128-131
12631267-8	2003	Two alternative conformations, rotated 180 degrees around an imaginary iron-catecholamine axis, were found for DA and l-DOPA in PAH and for DA in TH.	Catecholamines	76-89	phenylalanine hydroxylase	Homo sapiens	128-131
12631267-8	2003	Two alternative conformations, rotated 180 degrees around an imaginary iron-catecholamine axis, were found for DA and l-DOPA in PAH and for DA in TH.	Levodopa	118-124	phenylalanine hydroxylase	Homo sapiens	128-131
12659094-0	2003	Tetrahydrobiopterin-responsive hyperphenylalaninaemia due to homozygous mutations in the phenylalanine hydroxylase gene.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	89-114
12542580-2	2003	Subjects from the same family who share the same mutations in the phenylalanine hydroxylase (PAH) gene are expected to display similar disease courses, and therefore, when blood phenylalanine (Phe) levels, genotype and dietary treatment are all similar, differences in patient outcomes require additional explanations.	Phenylalanine	66-79	phenylalanine hydroxylase	Homo sapiens	93-96
12542580-2	2003	Subjects from the same family who share the same mutations in the phenylalanine hydroxylase (PAH) gene are expected to display similar disease courses, and therefore, when blood phenylalanine (Phe) levels, genotype and dietary treatment are all similar, differences in patient outcomes require additional explanations.	Phenylalanine	193-196	phenylalanine hydroxylase	Homo sapiens	66-91
12521113-7	2003	Further analysis showed that the distribution coefficient (KD) increased with the particular organic carbon content of sediments, consistent with the PAH partition theory.	Carbon	101-107	phenylalanine hydroxylase	Homo sapiens	150-153
12618080-6	2003	These observations suggest that residual PAH activity (in vitro) is a prerequisite for BH(4)-responsiveness.	sapropterin	87-92	phenylalanine hydroxylase	Homo sapiens	41-44
12618080-9	2003	BH(4)-responsive PAH-deficient patients have only been reported since 1999.	sapropterin	0-5	phenylalanine hydroxylase	Homo sapiens	17-20
12521113-8	2003	The organic carbon normalised distribution coefficient (K(oc)) also increased with the compounds" octanol/water partition coefficient (K(ow)), confirming the potential applicability of the linear free energy relationships in the modelling and prediction of PAH behaviour in marine environments.	Carbon	12-18	phenylalanine hydroxylase	Homo sapiens	257-260
12521113-8	2003	The organic carbon normalised distribution coefficient (K(oc)) also increased with the compounds" octanol/water partition coefficient (K(ow)), confirming the potential applicability of the linear free energy relationships in the modelling and prediction of PAH behaviour in marine environments.	Octanols	98-105	phenylalanine hydroxylase	Homo sapiens	257-260
12521113-8	2003	The organic carbon normalised distribution coefficient (K(oc)) also increased with the compounds" octanol/water partition coefficient (K(ow)), confirming the potential applicability of the linear free energy relationships in the modelling and prediction of PAH behaviour in marine environments.	Water	106-111	phenylalanine hydroxylase	Homo sapiens	257-260
12542289-5	2003	Increasing concentrations of 1-methylphenanthrene relative to phenanthrene were found in the urban air close to the city center, indicating that traffic probably contributed to the higher PAH concentrations detected.	1-methylphenanthrene	29-49	phenylalanine hydroxylase	Homo sapiens	188-191
12542289-5	2003	Increasing concentrations of 1-methylphenanthrene relative to phenanthrene were found in the urban air close to the city center, indicating that traffic probably contributed to the higher PAH concentrations detected.	phenanthrene	37-49	phenylalanine hydroxylase	Homo sapiens	188-191
12542289-7	2003	The PAH compounds sampled with SPMDs were mainly associated with gaseous PAHs, while both gas phase and particle-bound PAHs were detected in the plant samples.	Polycyclic Aromatic Hydrocarbons	73-77	phenylalanine hydroxylase	Homo sapiens	4-7
12409276-0	2002	Two novel genetic lesions and a common BH4-responsive mutation of the PAH gene in Italian patients with hyperphenylalaninemia.	sapropterin	39-42	phenylalanine hydroxylase	Homo sapiens	70-73
12971421-3	2003	The phenylalanine hydroxylase mutation H170D/IVS1nt5G>T was found to be responsive to tetrahydrobiopterin with significant decrease in blood phenylalanine concentration and increase in tyrosine blood content.	sapropterin	89-108	phenylalanine hydroxylase	Homo sapiens	4-29
12971421-3	2003	The phenylalanine hydroxylase mutation H170D/IVS1nt5G>T was found to be responsive to tetrahydrobiopterin with significant decrease in blood phenylalanine concentration and increase in tyrosine blood content.	Tyrosine	188-196	phenylalanine hydroxylase	Homo sapiens	4-29
12414107-1	2002	Sepiapterin reductase (SPR) is the enzyme that catalyzes the final step of the synthesis of tetrahydrobiopterin (BH4), the cofactor for phenylalanine hydroxylase, tyrosine hydroxylase (TH), tryptophan hydroxylase, and nitric oxide synthase (NOS).	sapropterin	92-111	phenylalanine hydroxylase	Homo sapiens	136-161
12443929-7	2002	The regions of two genes have been sequenced: D1 dopamine receptor gene (subfamily of the G-protein coupled receptor L-DOPA genes) and the intron 12 of the gene for phenylalanine hydroxylase (PAH) responsible for phenylketonuria or hyperphenylalaninemia.	Levodopa	117-123	phenylalanine hydroxylase	Homo sapiens	165-190
12443929-7	2002	The regions of two genes have been sequenced: D1 dopamine receptor gene (subfamily of the G-protein coupled receptor L-DOPA genes) and the intron 12 of the gene for phenylalanine hydroxylase (PAH) responsible for phenylketonuria or hyperphenylalaninemia.	Levodopa	117-123	phenylalanine hydroxylase	Homo sapiens	192-195
12728980-2	2003	The decontamination of a PAH-polluted environment is of importance because some PAHs are toxic, mutagenic, and carcinogenic and therefore are health hazards.	Polycyclic Aromatic Hydrocarbons	80-84	phenylalanine hydroxylase	Homo sapiens	25-28
12110506-1	2002	Evaluation of renal hemodynamics requires estimation of effective renal plasma flow, which is commonly measured by the renal clearance of p-aminohippuric acid (PAH).	p-Aminohippuric Acid	138-158	phenylalanine hydroxylase	Homo sapiens	160-163
12414107-1	2002	Sepiapterin reductase (SPR) is the enzyme that catalyzes the final step of the synthesis of tetrahydrobiopterin (BH4), the cofactor for phenylalanine hydroxylase, tyrosine hydroxylase (TH), tryptophan hydroxylase, and nitric oxide synthase (NOS).	sapropterin	113-116	phenylalanine hydroxylase	Homo sapiens	136-161
12185072-0	2002	Phosphorylation and mutations of Ser(16) in human phenylalanine hydroxylase.	Serine	33-36	phenylalanine hydroxylase	Homo sapiens	50-75
12185072-2	2002	Phosphorylation of phenylalanine hydroxylase (PAH) at Ser(16) by cyclic AMP-dependent protein kinase is a post-translational modification that increases its basal activity and facilitates its activation by the substrate l-Phe.	Serine	54-57	phenylalanine hydroxylase	Homo sapiens	19-44
12185072-2	2002	Phosphorylation of phenylalanine hydroxylase (PAH) at Ser(16) by cyclic AMP-dependent protein kinase is a post-translational modification that increases its basal activity and facilitates its activation by the substrate l-Phe.	Serine	54-57	phenylalanine hydroxylase	Homo sapiens	46-49
12185072-2	2002	Phosphorylation of phenylalanine hydroxylase (PAH) at Ser(16) by cyclic AMP-dependent protein kinase is a post-translational modification that increases its basal activity and facilitates its activation by the substrate l-Phe.	Phenylalanine	220-225	phenylalanine hydroxylase	Homo sapiens	19-44
12185072-2	2002	Phosphorylation of phenylalanine hydroxylase (PAH) at Ser(16) by cyclic AMP-dependent protein kinase is a post-translational modification that increases its basal activity and facilitates its activation by the substrate l-Phe.	Phenylalanine	220-225	phenylalanine hydroxylase	Homo sapiens	46-49
12185072-6	2002	The modeled reorientation of the N-terminal tail residues (Met(1)-Leu(15)) on phosphorylation is in agreement with the observed conformational change and increased accessibility of the substrate to the active site, as indicated by circular dichroism spectroscopy and the enzyme kinetic data for the full-length phosphorylated and nonphosphorylated human PAH.	Leucine	66-69	phenylalanine hydroxylase	Homo sapiens	354-357
12185072-7	2002	To further validate the model we have prepared and characterized mutants substituting Ser(16) with a negatively charged residue and found that S16E largely mimics the effects of phosphorylation of human PAH.	Serine	86-89	phenylalanine hydroxylase	Homo sapiens	203-206
12269833-2	2002	PAH trans-dihydrodiol proximate carcinogens are oxidized by aldo-keto reductases (AKRs) to their corresponding reactive and redox-active o-quinones which may have the properties of initiators and promoters.	trans-dihydrodiol	4-21	phenylalanine hydroxylase	Homo sapiens	0-3
12269833-2	2002	PAH trans-dihydrodiol proximate carcinogens are oxidized by aldo-keto reductases (AKRs) to their corresponding reactive and redox-active o-quinones which may have the properties of initiators and promoters.	o-quinones	137-147	phenylalanine hydroxylase	Homo sapiens	0-3
12229918-1	2002	A fluorometric screening method was used to estimate total polycyclic aromatic hydrocarbon (t-PAH) concentrations in sediments collected from the St. Louis River Area of Concern (AOC) in northeastern Minnesota.	Polycyclic Aromatic Hydrocarbons	59-90	phenylalanine hydroxylase	Homo sapiens	94-97
12210276-1	2002	Phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine, shares physical, structural and catalytic properties with tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) that catalyze the rate-limiting steps in the biosynthesis of the neurotransmitters dopamine, noradrenaline, and serotonin.	Norepinephrine	304-317	phenylalanine hydroxylase	Homo sapiens	0-25
12210276-1	2002	Phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine, shares physical, structural and catalytic properties with tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) that catalyze the rate-limiting steps in the biosynthesis of the neurotransmitters dopamine, noradrenaline, and serotonin.	Norepinephrine	304-317	phenylalanine hydroxylase	Homo sapiens	27-30
12210276-1	2002	Phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine, shares physical, structural and catalytic properties with tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) that catalyze the rate-limiting steps in the biosynthesis of the neurotransmitters dopamine, noradrenaline, and serotonin.	Serotonin	323-332	phenylalanine hydroxylase	Homo sapiens	0-25
12210276-1	2002	Phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine, shares physical, structural and catalytic properties with tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) that catalyze the rate-limiting steps in the biosynthesis of the neurotransmitters dopamine, noradrenaline, and serotonin.	Serotonin	323-332	phenylalanine hydroxylase	Homo sapiens	27-30
12210276-3	2002	A mutation in the functionally critical tetrahydrobiopterin cofactor binding domain of the PAH gene had been identified in African-American patients with the diagnosis of schizophrenia, and biochemical analyses suggested that this mutation has physiological consequences related to amine neurotransmitter function.	sapropterin	40-59	phenylalanine hydroxylase	Homo sapiens	91-94
12210276-3	2002	A mutation in the functionally critical tetrahydrobiopterin cofactor binding domain of the PAH gene had been identified in African-American patients with the diagnosis of schizophrenia, and biochemical analyses suggested that this mutation has physiological consequences related to amine neurotransmitter function.	Amines	282-287	phenylalanine hydroxylase	Homo sapiens	91-94
12110506-3	2002	We describe a rapid, precise, and accurate microplate-based assay of PAH using p-dimethylaminocinnamaldehyde, which produces a red color on reaction with PAH, and compare it with a reference HPLC method.	4-dimethylaminocinnamaldehyde	79-108	phenylalanine hydroxylase	Homo sapiens	69-72
12110506-3	2002	We describe a rapid, precise, and accurate microplate-based assay of PAH using p-dimethylaminocinnamaldehyde, which produces a red color on reaction with PAH, and compare it with a reference HPLC method.	4-dimethylaminocinnamaldehyde	79-108	phenylalanine hydroxylase	Homo sapiens	154-157
12142458-1	2002	Phenylalanine hydroxylase (PAH) is activated by its substrate phenylalanine, and through phosphorylation by cAMP-dependent protein kinase at Ser16 in the N-terminal autoregulatory sequence of the enzyme.	Phenylalanine	62-75	phenylalanine hydroxylase	Homo sapiens	0-25
12142458-1	2002	Phenylalanine hydroxylase (PAH) is activated by its substrate phenylalanine, and through phosphorylation by cAMP-dependent protein kinase at Ser16 in the N-terminal autoregulatory sequence of the enzyme.	Phenylalanine	62-75	phenylalanine hydroxylase	Homo sapiens	27-30
12142458-8	2002	Our results support the model whereby upon phenylalanine binding, the mobile N-terminal 18 residues of PAH associate with the folded core of the molecule; phosphorylation may facilitate this interaction.	Phenylalanine	43-56	phenylalanine hydroxylase	Homo sapiens	103-106
12096915-4	2002	The enzyme phenylalanine hydroxylase (PheOH) catalyzes the hydroxylation of l-phenylalanine into l-tyrosine utilizing the cofactors (6R)-l-erythro-5,6,7,8 tetrahydrobiopterin (BH(4)) and molecular oxygen.	Phenylalanine	76-91	phenylalanine hydroxylase	Homo sapiens	11-36
12126628-0	2002	Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its implications for the mechanism of catalysis and substrate activation.	sapropterin	105-124	phenylalanine hydroxylase	Homo sapiens	74-99
12126628-0	2002	Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its implications for the mechanism of catalysis and substrate activation.	2-thienylalanine	129-152	phenylalanine hydroxylase	Homo sapiens	74-99
12126628-1	2002	Phenylalanine hydroxylase catalyzes the stereospecific hydroxylation of L-phenylalanine, the committed step in the degradation of this amino acid.	Phenylalanine	72-87	phenylalanine hydroxylase	Homo sapiens	0-25
12096915-4	2002	The enzyme phenylalanine hydroxylase (PheOH) catalyzes the hydroxylation of l-phenylalanine into l-tyrosine utilizing the cofactors (6R)-l-erythro-5,6,7,8 tetrahydrobiopterin (BH(4)) and molecular oxygen.	Tyrosine	97-107	phenylalanine hydroxylase	Homo sapiens	11-36
12096915-4	2002	The enzyme phenylalanine hydroxylase (PheOH) catalyzes the hydroxylation of l-phenylalanine into l-tyrosine utilizing the cofactors (6R)-l-erythro-5,6,7,8 tetrahydrobiopterin (BH(4)) and molecular oxygen.	sapropterin	133-174	phenylalanine hydroxylase	Homo sapiens	11-36
12096915-4	2002	The enzyme phenylalanine hydroxylase (PheOH) catalyzes the hydroxylation of l-phenylalanine into l-tyrosine utilizing the cofactors (6R)-l-erythro-5,6,7,8 tetrahydrobiopterin (BH(4)) and molecular oxygen.	Oxygen	197-203	phenylalanine hydroxylase	Homo sapiens	11-36
12137049-0	2002	Structural characterisation of humic acid-bound PAH residues in soil by 13C-CPMAS-NMR-spectroscopy: evidence of covalent bonds.	Humic Substances	31-41	phenylalanine hydroxylase	Homo sapiens	48-51
12137049-0	2002	Structural characterisation of humic acid-bound PAH residues in soil by 13C-CPMAS-NMR-spectroscopy: evidence of covalent bonds.	13c	72-75	phenylalanine hydroxylase	Homo sapiens	48-51
12137049-4	2002	Based on these results a ratio of 13C-activity(PAH)/13C-activity(soil) approximately 1.5/1.0 in the test material was suggested.	13c	34-37	phenylalanine hydroxylase	Homo sapiens	47-50
12137049-5	2002	The chemical transformation of a PAH and its bound residue formation in a soil system detected by changes of chemical shifts in the 13C-NMR spectrum was proven for the first time.	13c	132-135	phenylalanine hydroxylase	Homo sapiens	33-36
12056888-0	2002	L-phenylalanine binding and domain organization in human phenylalanine hydroxylase: a differential scanning calorimetry study.	Phenylalanine	0-15	phenylalanine hydroxylase	Homo sapiens	57-82
12174822-1	2002	The effect of tetrahydrobiopterin (BH(4)) administration was studied in three infants with BH(4) responsive phenylalanine hydroxylase (PAH) deficiency by correlating different BH(4) doses with plasma phenylalanine levels under defined protein intake.	sapropterin	14-33	phenylalanine hydroxylase	Homo sapiens	108-133
12056888-1	2002	Human phenylalanine hydroxylase (hPAH) is a tetrameric enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine; a dysfunction of this enzyme causes phenylketonuria.	Phenylalanine	98-113	phenylalanine hydroxylase	Homo sapiens	6-31
12056888-1	2002	Human phenylalanine hydroxylase (hPAH) is a tetrameric enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine; a dysfunction of this enzyme causes phenylketonuria.	Phenylalanine	98-113	phenylalanine hydroxylase	Homo sapiens	33-37
12056888-1	2002	Human phenylalanine hydroxylase (hPAH) is a tetrameric enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine; a dysfunction of this enzyme causes phenylketonuria.	Phenylalanine	115-120	phenylalanine hydroxylase	Homo sapiens	6-31
12056888-1	2002	Human phenylalanine hydroxylase (hPAH) is a tetrameric enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine; a dysfunction of this enzyme causes phenylketonuria.	Phenylalanine	115-120	phenylalanine hydroxylase	Homo sapiens	33-37
12056888-1	2002	Human phenylalanine hydroxylase (hPAH) is a tetrameric enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine; a dysfunction of this enzyme causes phenylketonuria.	Tyrosine	125-135	phenylalanine hydroxylase	Homo sapiens	6-31
12056888-1	2002	Human phenylalanine hydroxylase (hPAH) is a tetrameric enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine; a dysfunction of this enzyme causes phenylketonuria.	Tyrosine	125-135	phenylalanine hydroxylase	Homo sapiens	33-37
12056888-3	2002	Two partially overlapping transitions are seen in differential scanning calorimetry (DSC) thermograms for wild-type hPAH in 0.1 M Na-Hepes buffer, 0.1 M NaCl, pH 7.0.	na-hepes	130-138	phenylalanine hydroxylase	Homo sapiens	116-120
12056888-8	2002	Application of this approach to the L-Phe effect on the DSC thermograms for hPAH suggests that (i) there are no binding sites for L-Phe in the regulatory domains; therefore, contrary to the common belief, the activation of PAH by L-Phe seems to be the result of its homotropic cooperative binding to the active sites.	Phenylalanine	36-41	phenylalanine hydroxylase	Homo sapiens	76-80
12056888-8	2002	Application of this approach to the L-Phe effect on the DSC thermograms for hPAH suggests that (i) there are no binding sites for L-Phe in the regulatory domains; therefore, contrary to the common belief, the activation of PAH by L-Phe seems to be the result of its homotropic cooperative binding to the active sites.	Phenylalanine	36-41	phenylalanine hydroxylase	Homo sapiens	77-80
11999982-2	2002	We report two new patients with tetrahydrobiopterin (BH4)-responsive phenylketonuria and compare their phenylalanine hydroxylase (PAH) genotypes (A395P/ IVS12+g>a and R261Q/165T, respectively) to those of previous cases from the literature.	sapropterin	32-51	phenylalanine hydroxylase	Homo sapiens	130-133
11944680-0	2002	Catalysis of PAH biodegradation by humic acid shown in synchrotron infrared studies.	Humic Substances	35-45	phenylalanine hydroxylase	Homo sapiens	13-16
11944680-2	2002	By utilizing an infrared spectromicroscope and a very bright, nondestructive synchrotron photon source, we monitored in situ and, over time, the influence of HA on the progression of degradation of pyrene (a model PAH) by a bacterial colony on a magnetite surface.	pyrene	198-204	phenylalanine hydroxylase	Homo sapiens	214-217
11944680-3	2002	Our results indicate that HA dramatically shortens the onset time for PAH biodegradation from 168 to 2 h. In the absence of HA, it takes the bacteria about 168 h to produce sufficient glycolipids to solubilize pyrene and make it bioavailable for biodegradation.	Glycolipids	184-195	phenylalanine hydroxylase	Homo sapiens	70-73
11944680-3	2002	Our results indicate that HA dramatically shortens the onset time for PAH biodegradation from 168 to 2 h. In the absence of HA, it takes the bacteria about 168 h to produce sufficient glycolipids to solubilize pyrene and make it bioavailable for biodegradation.	pyrene	210-216	phenylalanine hydroxylase	Homo sapiens	70-73
11944795-5	2002	The profiles of PAH/BaP at the measurement sites showed that the main source of PAHs in spring and summer was traffic while a substantial amount of autumn and winter PAHs, besides traffic, came from heating.	Polycyclic Aromatic Hydrocarbons	80-84	phenylalanine hydroxylase	Homo sapiens	16-19
11935335-1	2002	The liver-specific phenylalanine hydroxylase catalyzes the conversion of phenylalanine to tyrosine.	Tyrosine	90-98	phenylalanine hydroxylase	Homo sapiens	19-44
11914042-2	2002	The mutations on the phenylalanine hydroxylase gene indicated that she might be responsive to tetrahydrobiopterin therapy.	sapropterin	94-113	phenylalanine hydroxylase	Homo sapiens	21-46
11999982-4	2002	Interestingly, many of the PAH gene mutations detected in BH4-responsive patients have been associated with an inconsistent phenotype in the past.	sapropterin	58-61	phenylalanine hydroxylase	Homo sapiens	27-30
12210276-1	2002	Phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine, shares physical, structural and catalytic properties with tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) that catalyze the rate-limiting steps in the biosynthesis of the neurotransmitters dopamine, noradrenaline, and serotonin.	Phenylalanine	67-80	phenylalanine hydroxylase	Homo sapiens	0-25
12210276-1	2002	Phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine, shares physical, structural and catalytic properties with tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) that catalyze the rate-limiting steps in the biosynthesis of the neurotransmitters dopamine, noradrenaline, and serotonin.	Phenylalanine	67-80	phenylalanine hydroxylase	Homo sapiens	27-30
12210276-1	2002	Phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine, shares physical, structural and catalytic properties with tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) that catalyze the rate-limiting steps in the biosynthesis of the neurotransmitters dopamine, noradrenaline, and serotonin.	Tyrosine	84-92	phenylalanine hydroxylase	Homo sapiens	0-25
12210276-1	2002	Phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine, shares physical, structural and catalytic properties with tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) that catalyze the rate-limiting steps in the biosynthesis of the neurotransmitters dopamine, noradrenaline, and serotonin.	Tyrosine	84-92	phenylalanine hydroxylase	Homo sapiens	27-30
12210276-1	2002	Phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine, shares physical, structural and catalytic properties with tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) that catalyze the rate-limiting steps in the biosynthesis of the neurotransmitters dopamine, noradrenaline, and serotonin.	Dopamine	294-302	phenylalanine hydroxylase	Homo sapiens	0-25
12210276-1	2002	Phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine, shares physical, structural and catalytic properties with tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) that catalyze the rate-limiting steps in the biosynthesis of the neurotransmitters dopamine, noradrenaline, and serotonin.	Dopamine	294-302	phenylalanine hydroxylase	Homo sapiens	27-30
12009881-1	2002	Previous studies of ferrous wild-type phenylalanine hydroxylase, [Fe(2+)]PAH(T)[], have shown the active site to be a six-coordinate distorted octahedral site.	ammonium ferrous sulfate	66-72	phenylalanine hydroxylase	Homo sapiens	38-63
12009881-1	2002	Previous studies of ferrous wild-type phenylalanine hydroxylase, [Fe(2+)]PAH(T)[], have shown the active site to be a six-coordinate distorted octahedral site.	p-Aminohippuric Acid	73-76	phenylalanine hydroxylase	Homo sapiens	38-63
12083705-0	2002	Assessment of PAH contamination in estuarine sediments using the equilibrium partitioning-toxic unit approach.	estuarine	35-44	phenylalanine hydroxylase	Homo sapiens	14-17
12018402-2	2002	Exposure to PAH and benzene was assessed by means of urinary measurements of 1-hydroxypyrene and t,t-muconic acid, respectively.	1-hydroxypyrene	77-92	phenylalanine hydroxylase	Homo sapiens	12-15
12018402-2	2002	Exposure to PAH and benzene was assessed by means of urinary measurements of 1-hydroxypyrene and t,t-muconic acid, respectively.	t,t-muconic acid	97-113	phenylalanine hydroxylase	Homo sapiens	12-15
12018402-11	2002	There is clear evidence that fire fighting activities are associated with exposure to PAH above environmental background, as assessed by 1-hydroxypyrene measurements, despite the use of protective equipment.	1-hydroxypyrene	137-152	phenylalanine hydroxylase	Homo sapiens	86-89
11999982-2	2002	We report two new patients with tetrahydrobiopterin (BH4)-responsive phenylketonuria and compare their phenylalanine hydroxylase (PAH) genotypes (A395P/ IVS12+g>a and R261Q/165T, respectively) to those of previous cases from the literature.	sapropterin	32-51	phenylalanine hydroxylase	Homo sapiens	103-128
11791850-7	2001	The equilibrium PAH concentrations in the leach water from bitumens stay well below the surface water limits that exist in several EEC-countries and are also more than an order of magnitude lower than the current EEC limits for potable water.	Water	48-53	phenylalanine hydroxylase	Homo sapiens	16-19
11723206-2	2001	An extensive evaluation for the usual causes of these difficulties was unrevealing, but her serum phenylalanine concentration was markedly elevated and genetic analysis demonstrated mutations in the phenylalanine hydroxylase gene consistent with classic phenylketonuria.	Phenylalanine	98-111	phenylalanine hydroxylase	Homo sapiens	199-224
12200907-1	2002	UNLABELLED: The aim of this study was to determine whether any relationship exists between the severity of mutation of the phenylalanine hydroxylase (PAH) gene and the plasma concentrations of phenylalanine (Phe) and tyrosine (Tyr) under fasting and semifasting conditions among heterozygotes in a matched case-control study.	Phenylalanine	123-136	phenylalanine hydroxylase	Homo sapiens	150-153
12200907-1	2002	UNLABELLED: The aim of this study was to determine whether any relationship exists between the severity of mutation of the phenylalanine hydroxylase (PAH) gene and the plasma concentrations of phenylalanine (Phe) and tyrosine (Tyr) under fasting and semifasting conditions among heterozygotes in a matched case-control study.	Phenylalanine	208-211	phenylalanine hydroxylase	Homo sapiens	123-148
12200907-1	2002	UNLABELLED: The aim of this study was to determine whether any relationship exists between the severity of mutation of the phenylalanine hydroxylase (PAH) gene and the plasma concentrations of phenylalanine (Phe) and tyrosine (Tyr) under fasting and semifasting conditions among heterozygotes in a matched case-control study.	Phenylalanine	208-211	phenylalanine hydroxylase	Homo sapiens	150-153
12200907-1	2002	UNLABELLED: The aim of this study was to determine whether any relationship exists between the severity of mutation of the phenylalanine hydroxylase (PAH) gene and the plasma concentrations of phenylalanine (Phe) and tyrosine (Tyr) under fasting and semifasting conditions among heterozygotes in a matched case-control study.	Tyrosine	217-225	phenylalanine hydroxylase	Homo sapiens	123-148
12200907-1	2002	UNLABELLED: The aim of this study was to determine whether any relationship exists between the severity of mutation of the phenylalanine hydroxylase (PAH) gene and the plasma concentrations of phenylalanine (Phe) and tyrosine (Tyr) under fasting and semifasting conditions among heterozygotes in a matched case-control study.	Tyrosine	217-225	phenylalanine hydroxylase	Homo sapiens	150-153
12200907-1	2002	UNLABELLED: The aim of this study was to determine whether any relationship exists between the severity of mutation of the phenylalanine hydroxylase (PAH) gene and the plasma concentrations of phenylalanine (Phe) and tyrosine (Tyr) under fasting and semifasting conditions among heterozygotes in a matched case-control study.	Tyrosine	227-230	phenylalanine hydroxylase	Homo sapiens	150-153
11939197-0	2002	Quantification of monohydroxy-PAH metabolites in urine by solid-phase extraction with isotope dilution-GC-MS. For measurement of biomarkers from polycyclic aromatic hydrocarbon (PAH) exposure, an analytical method is described quantifying hydroxylated PAH (OH-PAH) in urine samples.	Polycyclic Aromatic Hydrocarbons	145-176	phenylalanine hydroxylase	Homo sapiens	30-33
11939197-0	2002	Quantification of monohydroxy-PAH metabolites in urine by solid-phase extraction with isotope dilution-GC-MS. For measurement of biomarkers from polycyclic aromatic hydrocarbon (PAH) exposure, an analytical method is described quantifying hydroxylated PAH (OH-PAH) in urine samples.	Polycyclic Aromatic Hydrocarbons	145-176	phenylalanine hydroxylase	Homo sapiens	178-181
11939197-0	2002	Quantification of monohydroxy-PAH metabolites in urine by solid-phase extraction with isotope dilution-GC-MS. For measurement of biomarkers from polycyclic aromatic hydrocarbon (PAH) exposure, an analytical method is described quantifying hydroxylated PAH (OH-PAH) in urine samples.	Polycyclic Aromatic Hydrocarbons	145-176	phenylalanine hydroxylase	Homo sapiens	178-181
11807932-2	2002	The potency of PAH mixtures often is calculated using relative potency values (BAP equivalency factors).	Benzo(a)pyrene	79-82	phenylalanine hydroxylase	Homo sapiens	15-18
11807932-5	2002	Moreover, when the PAH composition of the mixture has been analysed, prediction of the potency of PAH mixtures by BAP equivalency factors could be compared with the observed PAH potency.	Benzo(a)pyrene	114-117	phenylalanine hydroxylase	Homo sapiens	19-22
11807932-5	2002	Moreover, when the PAH composition of the mixture has been analysed, prediction of the potency of PAH mixtures by BAP equivalency factors could be compared with the observed PAH potency.	Benzo(a)pyrene	114-117	phenylalanine hydroxylase	Homo sapiens	98-101
11807932-5	2002	Moreover, when the PAH composition of the mixture has been analysed, prediction of the potency of PAH mixtures by BAP equivalency factors could be compared with the observed PAH potency.	Benzo(a)pyrene	114-117	phenylalanine hydroxylase	Homo sapiens	98-101
11807932-7	2002	Evaluation of several studies with various PAH mixtures revealed that the potency ratio between pure BAP and the PAH mixture in the same assay is highly dependent on the exposure pathway and the target organ, therefore potency estimates for PAH mixtures should be derived separately for oral, dermal and inhalative exposure using data from studies with the relevant pathway.	Benzo(a)pyrene	101-104	phenylalanine hydroxylase	Homo sapiens	43-46
11807932-7	2002	Evaluation of several studies with various PAH mixtures revealed that the potency ratio between pure BAP and the PAH mixture in the same assay is highly dependent on the exposure pathway and the target organ, therefore potency estimates for PAH mixtures should be derived separately for oral, dermal and inhalative exposure using data from studies with the relevant pathway.	Benzo(a)pyrene	101-104	phenylalanine hydroxylase	Homo sapiens	113-116
11807932-7	2002	Evaluation of several studies with various PAH mixtures revealed that the potency ratio between pure BAP and the PAH mixture in the same assay is highly dependent on the exposure pathway and the target organ, therefore potency estimates for PAH mixtures should be derived separately for oral, dermal and inhalative exposure using data from studies with the relevant pathway.	Benzo(a)pyrene	101-104	phenylalanine hydroxylase	Homo sapiens	113-116
11807932-9	2002	By using incidence data for all exposure-related tumours, a slope factor for humans of 11.5 (human excess risk per oral lifetime exposure with 1 mg BAP kg(-1)day(-1) in a PAH mixture) was obtained.	Benzo(a)pyrene	148-151	phenylalanine hydroxylase	Homo sapiens	171-174
11807932-10	2002	Our analysis led to the conclusion that the contribution of BAP to the carcinogenic potency of the mixture depends on the exposure pathway and type of cancer observed but is relatively constant for various PAH mixtures from industrial sources.	Benzo(a)pyrene	60-63	phenylalanine hydroxylase	Homo sapiens	206-209
11823989-1	2002	Recent evidence provided by the in vivo measure of the activity of phenylalanine hydroxylase in humans indicates that the kidney plays a role greater than previously presumed in phenylalanine conversion to tyrosine, an amino acid which has been considered nonessential so far.	Tyrosine	206-214	phenylalanine hydroxylase	Homo sapiens	67-92
11859869-1	2002	Hyperphenylalaninemia result from a block in the conversion of phenylalanine into tyrosine due to a defect in either the enzyme phenylalanine hydroxylase (98% of subjects) or in the metabolism of the cofactor tetrahydrobiopterin.	Phenylalanine	5-18	phenylalanine hydroxylase	Homo sapiens	128-153
11859869-1	2002	Hyperphenylalaninemia result from a block in the conversion of phenylalanine into tyrosine due to a defect in either the enzyme phenylalanine hydroxylase (98% of subjects) or in the metabolism of the cofactor tetrahydrobiopterin.	Tyrosine	82-90	phenylalanine hydroxylase	Homo sapiens	128-153
11747434-6	2001	The resulting ternary TPH-BH2-L-Trp structure is very similar to that previously determined by the same methods for the complex of phenylalanine hydroxylase (PAH) with BH2 and L-Phe [Teigen, K., et al.	bh2	26-29	phenylalanine hydroxylase	Homo sapiens	131-156
11747434-6	2001	The resulting ternary TPH-BH2-L-Trp structure is very similar to that previously determined by the same methods for the complex of phenylalanine hydroxylase (PAH) with BH2 and L-Phe [Teigen, K., et al.	bh2	26-29	phenylalanine hydroxylase	Homo sapiens	158-161
11747434-6	2001	The resulting ternary TPH-BH2-L-Trp structure is very similar to that previously determined by the same methods for the complex of phenylalanine hydroxylase (PAH) with BH2 and L-Phe [Teigen, K., et al.	Tryptophan	30-35	phenylalanine hydroxylase	Homo sapiens	131-156
11747434-6	2001	The resulting ternary TPH-BH2-L-Trp structure is very similar to that previously determined by the same methods for the complex of phenylalanine hydroxylase (PAH) with BH2 and L-Phe [Teigen, K., et al.	Tryptophan	30-35	phenylalanine hydroxylase	Homo sapiens	158-161
11747434-6	2001	The resulting ternary TPH-BH2-L-Trp structure is very similar to that previously determined by the same methods for the complex of phenylalanine hydroxylase (PAH) with BH2 and L-Phe [Teigen, K., et al.	bh2	168-171	phenylalanine hydroxylase	Homo sapiens	131-156
11747434-6	2001	The resulting ternary TPH-BH2-L-Trp structure is very similar to that previously determined by the same methods for the complex of phenylalanine hydroxylase (PAH) with BH2 and L-Phe [Teigen, K., et al.	bh2	168-171	phenylalanine hydroxylase	Homo sapiens	158-161
11747434-6	2001	The resulting ternary TPH-BH2-L-Trp structure is very similar to that previously determined by the same methods for the complex of phenylalanine hydroxylase (PAH) with BH2 and L-Phe [Teigen, K., et al.	Phenylalanine	176-181	phenylalanine hydroxylase	Homo sapiens	131-156
11747434-6	2001	The resulting ternary TPH-BH2-L-Trp structure is very similar to that previously determined by the same methods for the complex of phenylalanine hydroxylase (PAH) with BH2 and L-Phe [Teigen, K., et al.	Phenylalanine	176-181	phenylalanine hydroxylase	Homo sapiens	158-161
11747434-12	2001	The different conformation of the dihydroxypropyl chain of BH2 in PAH and TPH seems to be related to the presence of nonconserved residues, i.e., Tyr235 and Pro238 in TPH, at the cofactor binding site.	bh2	59-62	phenylalanine hydroxylase	Homo sapiens	66-69
11747434-13	2001	Moreover, Phe313, which seems to interact with the substrate through ring stacking, corresponds to a Trp residue in both tyrosine hydroxylase and PAH (Trp326) and appears to be an important residue for influencing the substrate specificity in this family of enzymes.	Tryptophan	101-104	phenylalanine hydroxylase	Homo sapiens	146-149
11747434-14	2001	We show that the W326F mutation in PAH increases the relative preference for L-Trp as the substrate, while the F313W mutation in TPH increases the preference for L-Phe, possibly by a conserved active site volume effect.	Tryptophan	77-82	phenylalanine hydroxylase	Homo sapiens	35-38
11791850-7	2001	The equilibrium PAH concentrations in the leach water from bitumens stay well below the surface water limits that exist in several EEC-countries and are also more than an order of magnitude lower than the current EEC limits for potable water.	Water	96-101	phenylalanine hydroxylase	Homo sapiens	16-19
11791850-7	2001	The equilibrium PAH concentrations in the leach water from bitumens stay well below the surface water limits that exist in several EEC-countries and are also more than an order of magnitude lower than the current EEC limits for potable water.	Water	96-101	phenylalanine hydroxylase	Homo sapiens	16-19
11694255-1	2001	BACKGROUND: Hyperphenylalaninemia (HPA) may be caused by either a deficiency in phenylalanine-4-hydroxylase or in tetrahydrobiopterin (BH4), the essential cofactor required for the hydroxylation of aromatic amino acids.	Amino Acids, Aromatic	198-218	phenylalanine hydroxylase	Homo sapiens	80-107
11573942-4	2001	Glucocorticoid receptor and HNF1, bound to their cognate sites, cooperatively increase the glucocorticoid response of the PAH gene, this response being synergistically enhanced by cAMP after long-term treatment.	Cyclic AMP	180-184	phenylalanine hydroxylase	Homo sapiens	122-125
11718561-0	2001	High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin.	sapropterin	158-177	phenylalanine hydroxylase	Homo sapiens	68-93
11718561-1	2001	The crystal structures of the catalytic domain (DeltaN1-102/DeltaC428-452) of human phenylalanine hydroxylase (hPheOH) in its catalytically competent Fe(II) form and binary complex with the reduced pterin cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) have been determined to 1.7 and 1.5 A, respectively.	ammonium ferrous sulfate	150-156	phenylalanine hydroxylase	Homo sapiens	84-109
11718561-1	2001	The crystal structures of the catalytic domain (DeltaN1-102/DeltaC428-452) of human phenylalanine hydroxylase (hPheOH) in its catalytically competent Fe(II) form and binary complex with the reduced pterin cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) have been determined to 1.7 and 1.5 A, respectively.	Pterins	198-204	phenylalanine hydroxylase	Homo sapiens	84-109
11718561-1	2001	The crystal structures of the catalytic domain (DeltaN1-102/DeltaC428-452) of human phenylalanine hydroxylase (hPheOH) in its catalytically competent Fe(II) form and binary complex with the reduced pterin cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) have been determined to 1.7 and 1.5 A, respectively.	(r)-l-erythro-5,6,7,8-tetrahydrobiopterin	215-256	phenylalanine hydroxylase	Homo sapiens	84-109
11718561-1	2001	The crystal structures of the catalytic domain (DeltaN1-102/DeltaC428-452) of human phenylalanine hydroxylase (hPheOH) in its catalytically competent Fe(II) form and binary complex with the reduced pterin cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) have been determined to 1.7 and 1.5 A, respectively.	sapropterin	258-261	phenylalanine hydroxylase	Homo sapiens	84-109
11718561-0	2001	High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin.	ammonium ferrous sulfate	122-128	phenylalanine hydroxylase	Homo sapiens	68-93
11675021-1	2001	We have uncovered a fundamental difference in the regulation of the rodent and the human phenylalanine hydroxylase (PAH) genes: expression of human PAH is independent of glucocorticoids and/or cAMP in contrast to the mouse gene which is not only highly inducible but dependent upon hormones for expression.	Cyclic AMP	193-197	phenylalanine hydroxylase	Homo sapiens	89-114
11675021-1	2001	We have uncovered a fundamental difference in the regulation of the rodent and the human phenylalanine hydroxylase (PAH) genes: expression of human PAH is independent of glucocorticoids and/or cAMP in contrast to the mouse gene which is not only highly inducible but dependent upon hormones for expression.	Cyclic AMP	193-197	phenylalanine hydroxylase	Homo sapiens	116-119
11513424-3	2001	The software allows the determination of PAH emissions as a function of the fuel composition parameters (aromatic content, cetane index, gross heat power, nitrogen and sulphur content) and operation conditions (torque and engine speed).	n-hexadecane	123-129	phenylalanine hydroxylase	Homo sapiens	41-44
11549037-1	2001	The addition of composted PAH-contaminated soil to PAH-contaminated soil spiked with 14C-labeled pyrene resulted in rapid mineralization of pyrene (more than 57% after 21 days compared with 3.4% in un-amended soil).	Carbon-14	85-88	phenylalanine hydroxylase	Homo sapiens	26-29
11549037-1	2001	The addition of composted PAH-contaminated soil to PAH-contaminated soil spiked with 14C-labeled pyrene resulted in rapid mineralization of pyrene (more than 57% after 21 days compared with 3.4% in un-amended soil).	Carbon-14	85-88	phenylalanine hydroxylase	Homo sapiens	51-54
11549037-1	2001	The addition of composted PAH-contaminated soil to PAH-contaminated soil spiked with 14C-labeled pyrene resulted in rapid mineralization of pyrene (more than 57% after 21 days compared with 3.4% in un-amended soil).	pyrene	97-103	phenylalanine hydroxylase	Homo sapiens	26-29
11549037-1	2001	The addition of composted PAH-contaminated soil to PAH-contaminated soil spiked with 14C-labeled pyrene resulted in rapid mineralization of pyrene (more than 57% after 21 days compared with 3.4% in un-amended soil).	pyrene	97-103	phenylalanine hydroxylase	Homo sapiens	51-54
11549037-1	2001	The addition of composted PAH-contaminated soil to PAH-contaminated soil spiked with 14C-labeled pyrene resulted in rapid mineralization of pyrene (more than 57% after 21 days compared with 3.4% in un-amended soil).	pyrene	140-146	phenylalanine hydroxylase	Homo sapiens	26-29
11549037-1	2001	The addition of composted PAH-contaminated soil to PAH-contaminated soil spiked with 14C-labeled pyrene resulted in rapid mineralization of pyrene (more than 57% after 21 days compared with 3.4% in un-amended soil).	pyrene	140-146	phenylalanine hydroxylase	Homo sapiens	51-54
11549037-4	2001	The amendment of PAH-contaminated soil with materials containing humic acids or humic acid extracts is suggested as a method of bioremediation.	Humic Substances	65-76	phenylalanine hydroxylase	Homo sapiens	17-20
11549037-4	2001	The amendment of PAH-contaminated soil with materials containing humic acids or humic acid extracts is suggested as a method of bioremediation.	Humic Substances	65-75	phenylalanine hydroxylase	Homo sapiens	17-20
11513424-3	2001	The software allows the determination of PAH emissions as a function of the fuel composition parameters (aromatic content, cetane index, gross heat power, nitrogen and sulphur content) and operation conditions (torque and engine speed).	Nitrogen	155-163	phenylalanine hydroxylase	Homo sapiens	41-44
11444803-1	2001	In the present study the optical biosensor technique, based on the surface plasmon resonance (SPR) phenomenon, was used for real-time measurements of the reversible binding of the pterin cofactor (6R)-l-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) and l-phenylalanine (l-Phe) to human phenylalanine hydroxylase (hPAH).	Pterins	180-186	phenylalanine hydroxylase	Homo sapiens	284-309
11444803-2	2001	When BH(4) (241 Da) was injected over the sensor chip with immobilized tetrameric wt-hPAH a positive DeltaRU response was observed with a square-wave type of sensorgram and a saturable response (about 25 RU/(pmol subunit/mm(2)) with a [S](0.5) value of 5.6 +/- 0.8 microM for the pterin cofactor.	Pterins	280-286	phenylalanine hydroxylase	Homo sapiens	85-89
11444803-1	2001	In the present study the optical biosensor technique, based on the surface plasmon resonance (SPR) phenomenon, was used for real-time measurements of the reversible binding of the pterin cofactor (6R)-l-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) and l-phenylalanine (l-Phe) to human phenylalanine hydroxylase (hPAH).	Pterins	180-186	phenylalanine hydroxylase	Homo sapiens	311-315
11444803-1	2001	In the present study the optical biosensor technique, based on the surface plasmon resonance (SPR) phenomenon, was used for real-time measurements of the reversible binding of the pterin cofactor (6R)-l-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) and l-phenylalanine (l-Phe) to human phenylalanine hydroxylase (hPAH).	sapropterin	197-238	phenylalanine hydroxylase	Homo sapiens	284-309
11444803-1	2001	In the present study the optical biosensor technique, based on the surface plasmon resonance (SPR) phenomenon, was used for real-time measurements of the reversible binding of the pterin cofactor (6R)-l-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) and l-phenylalanine (l-Phe) to human phenylalanine hydroxylase (hPAH).	sapropterin	197-238	phenylalanine hydroxylase	Homo sapiens	311-315
11408366-0	2001	Polycyclic aromatic hydrocarbon/metal mixtures: effect on PAH induction of CYP1A1 in human HEPG2 cells.	Polycyclic Aromatic Hydrocarbons	0-31	phenylalanine hydroxylase	Homo sapiens	58-61
11472242-3	2001	TPH belongs to the family of the aromatic amino acid hydroxylases, including phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH), which all have a strict requirement for dioxygen, non-heme iron (II) and tetrahydrobiopterin (BH4).	Oxygen	180-188	phenylalanine hydroxylase	Homo sapiens	77-102
11472242-3	2001	TPH belongs to the family of the aromatic amino acid hydroxylases, including phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH), which all have a strict requirement for dioxygen, non-heme iron (II) and tetrahydrobiopterin (BH4).	Oxygen	180-188	phenylalanine hydroxylase	Homo sapiens	104-107
11472242-3	2001	TPH belongs to the family of the aromatic amino acid hydroxylases, including phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH), which all have a strict requirement for dioxygen, non-heme iron (II) and tetrahydrobiopterin (BH4).	Iron	199-203	phenylalanine hydroxylase	Homo sapiens	77-102
11472242-3	2001	TPH belongs to the family of the aromatic amino acid hydroxylases, including phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH), which all have a strict requirement for dioxygen, non-heme iron (II) and tetrahydrobiopterin (BH4).	Iron	199-203	phenylalanine hydroxylase	Homo sapiens	104-107
11408366-0	2001	Polycyclic aromatic hydrocarbon/metal mixtures: effect on PAH induction of CYP1A1 in human HEPG2 cells.	Metals	32-37	phenylalanine hydroxylase	Homo sapiens	58-61
11472242-3	2001	TPH belongs to the family of the aromatic amino acid hydroxylases, including phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH), which all have a strict requirement for dioxygen, non-heme iron (II) and tetrahydrobiopterin (BH4).	sapropterin	213-232	phenylalanine hydroxylase	Homo sapiens	77-102
11408366-1	2001	Environmental polycyclic aromatic hydrocarbons (PAHs) and metals coexist, and such mixtures could affect the carcinogenicity of PAHs, possibly by modification of PAH induction of the PAH-bioactivating CYP1A.	Polycyclic Aromatic Hydrocarbons	14-46	phenylalanine hydroxylase	Homo sapiens	48-51
11472242-3	2001	TPH belongs to the family of the aromatic amino acid hydroxylases, including phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH), which all have a strict requirement for dioxygen, non-heme iron (II) and tetrahydrobiopterin (BH4).	sapropterin	213-232	phenylalanine hydroxylase	Homo sapiens	104-107
11472242-3	2001	TPH belongs to the family of the aromatic amino acid hydroxylases, including phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH), which all have a strict requirement for dioxygen, non-heme iron (II) and tetrahydrobiopterin (BH4).	sapropterin	234-237	phenylalanine hydroxylase	Homo sapiens	77-102
11472242-3	2001	TPH belongs to the family of the aromatic amino acid hydroxylases, including phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH), which all have a strict requirement for dioxygen, non-heme iron (II) and tetrahydrobiopterin (BH4).	sapropterin	234-237	phenylalanine hydroxylase	Homo sapiens	104-107
11408366-1	2001	Environmental polycyclic aromatic hydrocarbons (PAHs) and metals coexist, and such mixtures could affect the carcinogenicity of PAHs, possibly by modification of PAH induction of the PAH-bioactivating CYP1A.	Polycyclic Aromatic Hydrocarbons	14-46	phenylalanine hydroxylase	Homo sapiens	128-131
11472242-4	2001	During the last three years there has been a formidable increase in the amount of structural information about PAH and TH, which has provided new insights into the active site structure, the binding of substrates, inhibitors and pterins, as well as on the effect of disease-causing mutations in these hydroxylases.	Pterins	229-236	phenylalanine hydroxylase	Homo sapiens	111-114
11408366-1	2001	Environmental polycyclic aromatic hydrocarbons (PAHs) and metals coexist, and such mixtures could affect the carcinogenicity of PAHs, possibly by modification of PAH induction of the PAH-bioactivating CYP1A.	Polycyclic Aromatic Hydrocarbons	48-52	phenylalanine hydroxylase	Homo sapiens	128-131
11408366-1	2001	Environmental polycyclic aromatic hydrocarbons (PAHs) and metals coexist, and such mixtures could affect the carcinogenicity of PAHs, possibly by modification of PAH induction of the PAH-bioactivating CYP1A.	Polycyclic Aromatic Hydrocarbons	128-132	phenylalanine hydroxylase	Homo sapiens	48-51
11408366-2	2001	The effect on PAH-mediated CYP1A induction of arsenic, lead, mercury, or cadmium (ranked as the most hazardous environmental metals by the Environmental Protection Agency and the Agency for Toxic Substances and Disease Registry) has thus been investigated.	Arsenic	46-53	phenylalanine hydroxylase	Homo sapiens	14-17
11408366-2	2001	The effect on PAH-mediated CYP1A induction of arsenic, lead, mercury, or cadmium (ranked as the most hazardous environmental metals by the Environmental Protection Agency and the Agency for Toxic Substances and Disease Registry) has thus been investigated.	Mercury	61-68	phenylalanine hydroxylase	Homo sapiens	14-17
11408366-2	2001	The effect on PAH-mediated CYP1A induction of arsenic, lead, mercury, or cadmium (ranked as the most hazardous environmental metals by the Environmental Protection Agency and the Agency for Toxic Substances and Disease Registry) has thus been investigated.	Cadmium	73-80	phenylalanine hydroxylase	Homo sapiens	14-17
11386853-0	2001	Glycerol increases the yield and activity of human phenylalanine hydroxylase mutant enzymes produced in a prokaryotic expression system.	Glycerol	0-8	phenylalanine hydroxylase	Homo sapiens	51-76
11488391-5	2001	The CO concentration correlated well with the total PAH (R2 > .89), and thus can be used as a surrogate indicator for PAH emission.	Carbon Monoxide	4-6	phenylalanine hydroxylase	Homo sapiens	52-55
11488391-5	2001	The CO concentration correlated well with the total PAH (R2 > .89), and thus can be used as a surrogate indicator for PAH emission.	Carbon Monoxide	4-6	phenylalanine hydroxylase	Homo sapiens	121-124
11301319-0	2001	The effect of substrate, dihydrobiopterin, and dopamine on the EPR spectroscopic properties and the midpoint potential of the catalytic iron in recombinant human phenylalanine hydroxylase.	7,8-dihydrobiopterin	25-41	phenylalanine hydroxylase	Homo sapiens	162-187
11301319-0	2001	The effect of substrate, dihydrobiopterin, and dopamine on the EPR spectroscopic properties and the midpoint potential of the catalytic iron in recombinant human phenylalanine hydroxylase.	Dopamine	47-55	phenylalanine hydroxylase	Homo sapiens	162-187
11301319-0	2001	The effect of substrate, dihydrobiopterin, and dopamine on the EPR spectroscopic properties and the midpoint potential of the catalytic iron in recombinant human phenylalanine hydroxylase.	Iron	136-140	phenylalanine hydroxylase	Homo sapiens	162-187
11301319-1	2001	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	0-25
11301319-1	2001	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	27-30
11301319-1	2001	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr.	Heme	73-77	phenylalanine hydroxylase	Homo sapiens	0-25
11301319-1	2001	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr.	Heme	73-77	phenylalanine hydroxylase	Homo sapiens	27-30
11301319-1	2001	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr.	Iron	78-82	phenylalanine hydroxylase	Homo sapiens	0-25
11301319-1	2001	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr.	Iron	78-82	phenylalanine hydroxylase	Homo sapiens	27-30
11301319-1	2001	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr.	Phenylalanine	118-123	phenylalanine hydroxylase	Homo sapiens	0-25
11301319-1	2001	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr.	Phenylalanine	118-123	phenylalanine hydroxylase	Homo sapiens	27-30
11301319-1	2001	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr.	Tyrosine	127-132	phenylalanine hydroxylase	Homo sapiens	0-25
11301319-1	2001	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr.	Tyrosine	127-132	phenylalanine hydroxylase	Homo sapiens	27-30
11301319-2	2001	The paramagnetic ferric iron at the active site of recombinant human PAH (hPAH) and its midpoint potential at pH 7.25 (E(m)(Fe(III)/Fe(II))) were studied by EPR spectroscopy.	ferric sulfate	17-28	phenylalanine hydroxylase	Homo sapiens	69-72
11301319-2	2001	The paramagnetic ferric iron at the active site of recombinant human PAH (hPAH) and its midpoint potential at pH 7.25 (E(m)(Fe(III)/Fe(II))) were studied by EPR spectroscopy.	hydralazine 4-anisaldehyde hydrazone	74-78	phenylalanine hydroxylase	Homo sapiens	69-72
11301319-2	2001	The paramagnetic ferric iron at the active site of recombinant human PAH (hPAH) and its midpoint potential at pH 7.25 (E(m)(Fe(III)/Fe(II))) were studied by EPR spectroscopy.	ferric sulfate	124-131	phenylalanine hydroxylase	Homo sapiens	69-72
11326337-4	2001	Database searches were used to identify regions in the N-terminal domain of PAH with homology to the regulatory domain of prephenate dehydratase (PDH), the rate-limiting enzyme in the bacterial phenylalanine biosynthesis pathway.	Phenylalanine	194-207	phenylalanine hydroxylase	Homo sapiens	76-79
11326337-5	2001	Naturally occurring N-terminal PAH mutations are distributed in a nonrandom pattern and cluster within residues 46-48 (GAL) and 65-69 (IESRP), two motifs highly conserved in PDH.	cyclohexenoesculetin-beta-galactoside	119-122	phenylalanine hydroxylase	Homo sapiens	31-34
11326337-6	2001	To examine whether N-terminal PAH mutations affect the ability of PAH to bind phenylalanine at the regulatory domain, wild-type and five mutant (G46S, A47V, T63P/H64N, I65T, and R68S) forms of the N-terminal domain (residues 2-120) of human PAH were expressed as fusion proteins in Escherichia coli.	Phenylalanine	78-91	phenylalanine hydroxylase	Homo sapiens	66-69
11326337-6	2001	To examine whether N-terminal PAH mutations affect the ability of PAH to bind phenylalanine at the regulatory domain, wild-type and five mutant (G46S, A47V, T63P/H64N, I65T, and R68S) forms of the N-terminal domain (residues 2-120) of human PAH were expressed as fusion proteins in Escherichia coli.	Phenylalanine	78-91	phenylalanine hydroxylase	Homo sapiens	66-69
11326337-8	2001	Our data suggest that impairment of phenylalanine-mediated activation of PAH may be an important disease-causing mechanism of some N-terminal PAH mutations, which may explain some well-documented genotype-phenotype discrepancies in PAH deficiency.	Phenylalanine	36-49	phenylalanine hydroxylase	Homo sapiens	73-76
11326337-8	2001	Our data suggest that impairment of phenylalanine-mediated activation of PAH may be an important disease-causing mechanism of some N-terminal PAH mutations, which may explain some well-documented genotype-phenotype discrepancies in PAH deficiency.	Phenylalanine	36-49	phenylalanine hydroxylase	Homo sapiens	142-145
11386853-4	2001	Based on these observations, the effect of glycerol as a stabilizer agent of recombinant mutant forms of human phenylalanine hydroxylase enzymes (hPAH) produced in a prokaryotic expression system was investigated.	Glycerol	43-51	phenylalanine hydroxylase	Homo sapiens	111-136
11386853-4	2001	Based on these observations, the effect of glycerol as a stabilizer agent of recombinant mutant forms of human phenylalanine hydroxylase enzymes (hPAH) produced in a prokaryotic expression system was investigated.	Glycerol	43-51	phenylalanine hydroxylase	Homo sapiens	146-150
11386853-5	2001	The wild-type and two mutant forms of the hPAH protein (R270K and V388M) were expressed in the presence of glycerol in the culture medium.	Glycerol	107-115	phenylalanine hydroxylase	Homo sapiens	42-46
11386853-7	2001	The results obtained demonstrate that glycerol not only improved the yield of the soluble hPAH proteins (2- to 3-fold depending on the mutant enzyme) produced but also increased the specific activity of the purified recombinant enzymes.	Glycerol	38-46	phenylalanine hydroxylase	Homo sapiens	90-94
11274478-1	2001	GTP cyclohydrolase I feedback regulatory protein (GFRP) mediates feedback inhibition of GTP cyclohydrolase I activity by 6R-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4), which is an essential cofactor for key enzymes producing catecholamines, serotonin, and nitric oxide as well as phenylalanine hydroxylase.	sapropterin	121-161	phenylalanine hydroxylase	Homo sapiens	281-306
11337875-7	2001	Overall, these studies show that the addition of high affinity sorbents effectively reduces pore-water PAH concentrations and bioavailability and suggests that sorbent addition may serve as an option for in situ remediation of some contaminated sediments.	Water	97-102	phenylalanine hydroxylase	Homo sapiens	103-106
11382545-0	2001	Dietary supplements of mixtures of indispensable amino acids lacking threonine, phenylalanine or histidine increase the activity of hepatic threonine dehydrogenase, phenylalanine hydroxylase or histidase, respectively, and prevent growth depressions in chicks caused by dietary excesses of threonine, phenylalanine, or histidine* Experiments were carried out to determine whether the addition of a mixture of indispensable amino acids (IAA) lacking in threonine, phenylalanine or histidine, respectively, to a nutritionally complete diet would increase the hepatic activities of the rate-limiting enzymes for catabolism of threonine, phenylalanine or histidine and prevent the adverse effects of the amino acid on growth when the dietary level of the amino acid is excessive.	Threonine	69-78	phenylalanine hydroxylase	Homo sapiens	165-190
11382545-0	2001	Dietary supplements of mixtures of indispensable amino acids lacking threonine, phenylalanine or histidine increase the activity of hepatic threonine dehydrogenase, phenylalanine hydroxylase or histidase, respectively, and prevent growth depressions in chicks caused by dietary excesses of threonine, phenylalanine, or histidine* Experiments were carried out to determine whether the addition of a mixture of indispensable amino acids (IAA) lacking in threonine, phenylalanine or histidine, respectively, to a nutritionally complete diet would increase the hepatic activities of the rate-limiting enzymes for catabolism of threonine, phenylalanine or histidine and prevent the adverse effects of the amino acid on growth when the dietary level of the amino acid is excessive.	Phenylalanine	80-93	phenylalanine hydroxylase	Homo sapiens	165-190
11382545-0	2001	Dietary supplements of mixtures of indispensable amino acids lacking threonine, phenylalanine or histidine increase the activity of hepatic threonine dehydrogenase, phenylalanine hydroxylase or histidase, respectively, and prevent growth depressions in chicks caused by dietary excesses of threonine, phenylalanine, or histidine* Experiments were carried out to determine whether the addition of a mixture of indispensable amino acids (IAA) lacking in threonine, phenylalanine or histidine, respectively, to a nutritionally complete diet would increase the hepatic activities of the rate-limiting enzymes for catabolism of threonine, phenylalanine or histidine and prevent the adverse effects of the amino acid on growth when the dietary level of the amino acid is excessive.	Histidine	97-106	phenylalanine hydroxylase	Homo sapiens	165-190
11382545-6	2001	Chicks that received the amino acids in diets that also contained the IAA supplement had better growth and feed consumption, lower plasma concentrations of threonine, phenylalanine or histidine, higher plasma concentrations of other indispensable amino acids, and higher activities of threonine dehydrogenase, phenylalanine hydroxylase, and histidase than chicks receiving excess amino acids in the absence of IAA supplements.	Amino Acids, Essential	70-73	phenylalanine hydroxylase	Homo sapiens	310-335
11405341-5	2001	Recently, there have been several reports of PKU patients showing a normalization of their L-Phe concentrations upon oral administration of the natural cofactor to PAH, (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4).	Phenylalanine	91-96	phenylalanine hydroxylase	Homo sapiens	164-167
11405341-5	2001	Recently, there have been several reports of PKU patients showing a normalization of their L-Phe concentrations upon oral administration of the natural cofactor to PAH, (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4).	sapropterin	169-211	phenylalanine hydroxylase	Homo sapiens	164-167
11405341-5	2001	Recently, there have been several reports of PKU patients showing a normalization of their L-Phe concentrations upon oral administration of the natural cofactor to PAH, (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4).	sapropterin	213-216	phenylalanine hydroxylase	Homo sapiens	164-167
11405341-6	2001	In an attempt to correlate the clinical responsiveness to BH4 administration with PKU genotype, we propose specific structural consequences for this subset of PAH mutations.	sapropterin	58-61	phenylalanine hydroxylase	Homo sapiens	159-162
11405341-7	2001	Based on the location and proximity of this subset of mutations to the cofactor-binding site in the three-dimensional structure of PAH, a hypothesis for BH4 responsiveness in PKU patients is presented.	sapropterin	153-156	phenylalanine hydroxylase	Homo sapiens	131-134
11405341-8	2001	It is believed that some of these mutations result in expressed mutant enzymes that are Km variants (with a lower binding affinity for BH4) of the standard PAH enzyme phenotype.	sapropterin	135-138	phenylalanine hydroxylase	Homo sapiens	156-159
11405341-9	2001	Oral administration of excess BH4 thus makes it possible for these mutant enzymes to suppress their low binding affinity for BH4, enabling this subset of PAH mutations to perform the L-Phe hydroxylation reaction.	sapropterin	30-33	phenylalanine hydroxylase	Homo sapiens	154-157
11405341-9	2001	Oral administration of excess BH4 thus makes it possible for these mutant enzymes to suppress their low binding affinity for BH4, enabling this subset of PAH mutations to perform the L-Phe hydroxylation reaction.	sapropterin	125-128	phenylalanine hydroxylase	Homo sapiens	154-157
11405341-9	2001	Oral administration of excess BH4 thus makes it possible for these mutant enzymes to suppress their low binding affinity for BH4, enabling this subset of PAH mutations to perform the L-Phe hydroxylation reaction.	Phenylalanine	183-188	phenylalanine hydroxylase	Homo sapiens	154-157
11405341-10	2001	Most of the BH4-responsive PAH mutations map to the catalytic domain of PAH in either of two categories.	sapropterin	12-15	phenylalanine hydroxylase	Homo sapiens	27-30
11405341-10	2001	Most of the BH4-responsive PAH mutations map to the catalytic domain of PAH in either of two categories.	sapropterin	12-15	phenylalanine hydroxylase	Homo sapiens	72-75
11405341-12	2001	Based on the series of known mutations that have been found to be responsive to BH4, we propose that other subsets of PAH mutations will have a high likelihood of being responsive to oral BH4 administration.	sapropterin	80-83	phenylalanine hydroxylase	Homo sapiens	118-121
11405341-12	2001	Based on the series of known mutations that have been found to be responsive to BH4, we propose that other subsets of PAH mutations will have a high likelihood of being responsive to oral BH4 administration.	sapropterin	188-191	phenylalanine hydroxylase	Homo sapiens	118-121
11328945-8	2001	Phenylalanine hydroxylase mutations in the mothers and offspring did not have an independent relationship to congenital heart disease but were related through the basal maternal phenylalanine levels.	Phenylalanine	178-191	phenylalanine hydroxylase	Homo sapiens	0-25
11279601-0	2001	Lung carcinogenesis: resveratrol modulates the expression of genes involved in the metabolism of PAH in human bronchial epithelial cells.	Resveratrol	21-32	phenylalanine hydroxylase	Homo sapiens	97-100
11274478-1	2001	GTP cyclohydrolase I feedback regulatory protein (GFRP) mediates feedback inhibition of GTP cyclohydrolase I activity by 6R-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4), which is an essential cofactor for key enzymes producing catecholamines, serotonin, and nitric oxide as well as phenylalanine hydroxylase.	sapropterin	163-166	phenylalanine hydroxylase	Homo sapiens	281-306
11274478-1	2001	GTP cyclohydrolase I feedback regulatory protein (GFRP) mediates feedback inhibition of GTP cyclohydrolase I activity by 6R-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4), which is an essential cofactor for key enzymes producing catecholamines, serotonin, and nitric oxide as well as phenylalanine hydroxylase.	Catecholamines	226-240	phenylalanine hydroxylase	Homo sapiens	281-306
11274478-1	2001	GTP cyclohydrolase I feedback regulatory protein (GFRP) mediates feedback inhibition of GTP cyclohydrolase I activity by 6R-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4), which is an essential cofactor for key enzymes producing catecholamines, serotonin, and nitric oxide as well as phenylalanine hydroxylase.	Serotonin	242-251	phenylalanine hydroxylase	Homo sapiens	281-306
11274478-1	2001	GTP cyclohydrolase I feedback regulatory protein (GFRP) mediates feedback inhibition of GTP cyclohydrolase I activity by 6R-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4), which is an essential cofactor for key enzymes producing catecholamines, serotonin, and nitric oxide as well as phenylalanine hydroxylase.	Nitric Oxide	257-269	phenylalanine hydroxylase	Homo sapiens	281-306
11161839-1	2001	Phenylalanine hydroxylase (PAH) is a homotetrameric enzyme that catalyzes the conversion of phenylalanine to tyrosine, the rate-limiting step of phenylalanine disposal in humans.	Phenylalanine	92-105	phenylalanine hydroxylase	Homo sapiens	0-25
11161839-1	2001	Phenylalanine hydroxylase (PAH) is a homotetrameric enzyme that catalyzes the conversion of phenylalanine to tyrosine, the rate-limiting step of phenylalanine disposal in humans.	Phenylalanine	92-105	phenylalanine hydroxylase	Homo sapiens	27-30
11161839-1	2001	Phenylalanine hydroxylase (PAH) is a homotetrameric enzyme that catalyzes the conversion of phenylalanine to tyrosine, the rate-limiting step of phenylalanine disposal in humans.	Tyrosine	109-117	phenylalanine hydroxylase	Homo sapiens	0-25
11161839-1	2001	Phenylalanine hydroxylase (PAH) is a homotetrameric enzyme that catalyzes the conversion of phenylalanine to tyrosine, the rate-limiting step of phenylalanine disposal in humans.	Tyrosine	109-117	phenylalanine hydroxylase	Homo sapiens	27-30
11161839-1	2001	Phenylalanine hydroxylase (PAH) is a homotetrameric enzyme that catalyzes the conversion of phenylalanine to tyrosine, the rate-limiting step of phenylalanine disposal in humans.	Phenylalanine	145-158	phenylalanine hydroxylase	Homo sapiens	0-25
11161839-1	2001	Phenylalanine hydroxylase (PAH) is a homotetrameric enzyme that catalyzes the conversion of phenylalanine to tyrosine, the rate-limiting step of phenylalanine disposal in humans.	Phenylalanine	145-158	phenylalanine hydroxylase	Homo sapiens	27-30
11161839-2	2001	Primary dysfunction of PAH caused by mutations in the PAH gene results in hyperphenylalaninemia, which may impair cognitive development unless corrected by dietary restriction of phenylalanine.	Phenylalanine	79-92	phenylalanine hydroxylase	Homo sapiens	23-26
11161839-2	2001	Primary dysfunction of PAH caused by mutations in the PAH gene results in hyperphenylalaninemia, which may impair cognitive development unless corrected by dietary restriction of phenylalanine.	Phenylalanine	79-92	phenylalanine hydroxylase	Homo sapiens	54-57
11349272-6	2001	An exception occurs when the PAH is generated simultaneously with the aerosol and unusually high solubilities are observed, indicative of adsorption to active carbon surfaces.	Carbon	159-165	phenylalanine hydroxylase	Homo sapiens	29-32
11171986-5	2001	Replacing serine-29 of rat PAH with cysteine from the same site of human PAH increased the activity by more than 4-fold.	Serine	10-16	phenylalanine hydroxylase	Homo sapiens	73-76
11171986-5	2001	Replacing serine-29 of rat PAH with cysteine from the same site of human PAH increased the activity by more than 4-fold.	Cysteine	36-44	phenylalanine hydroxylase	Homo sapiens	73-76
11163771-1	2001	Phenylalanine hydroxylase (PAH) is activated by its substrate phenylalanine and inhibited by its cofactor tetrahydrobiopterin (BH(4)).	Phenylalanine	62-75	phenylalanine hydroxylase	Homo sapiens	0-25
11163771-1	2001	Phenylalanine hydroxylase (PAH) is activated by its substrate phenylalanine and inhibited by its cofactor tetrahydrobiopterin (BH(4)).	Phenylalanine	62-75	phenylalanine hydroxylase	Homo sapiens	27-30
11163771-1	2001	Phenylalanine hydroxylase (PAH) is activated by its substrate phenylalanine and inhibited by its cofactor tetrahydrobiopterin (BH(4)).	sapropterin	106-125	phenylalanine hydroxylase	Homo sapiens	0-25
11163771-1	2001	Phenylalanine hydroxylase (PAH) is activated by its substrate phenylalanine and inhibited by its cofactor tetrahydrobiopterin (BH(4)).	sapropterin	106-125	phenylalanine hydroxylase	Homo sapiens	27-30
11163771-4	2001	Our data support the model where the N-terminal sequence of PAH acts as an intrasteric autoregulatory sequence, responsible for transmitting the effect of phenylalanine activation to the active site.	Phenylalanine	155-168	phenylalanine hydroxylase	Homo sapiens	60-63
11428133-1	2001	The proximity of a busy highway (90,000 vehicles/day) increased the amount of polycyclic aromatic hydrocarbons (PAHs) in soil at the depth of 5-15 cm from 106 ng/g as a grassland background to 3095 ng/g dry soil at the highway verge (a sum of 10 PAH species).	Polycyclic Aromatic Hydrocarbons	78-110	phenylalanine hydroxylase	Homo sapiens	112-115
11214902-1	2001	An A-->T substitution in cDNA nucleotide 1197 (c.1197A/T) of the human phenylalanine hydroxylase (PAH) gene has been regarded as a silent mutation, because both the wild-type (GUA) and the mutant (GUU) alleles encode a valine residue at codon 399 (V399 V).	Valine	222-228	phenylalanine hydroxylase	Homo sapiens	101-104
11175307-0	2000	Development of a skin-based metabolic sink for phenylalanine by overexpression of phenylalanine hydroxylase and GTP cyclohydrolase in primary human keratinocytes.	Phenylalanine	47-60	phenylalanine hydroxylase	Homo sapiens	82-107
11206195-6	2001	In addition, the initial uptake rate of [3H]PAH from the basolateral side was decreased by both PAH and probenecid, but not by genistein.	Probenecid	104-114	phenylalanine hydroxylase	Homo sapiens	44-47
11206195-7	2001	Therefore, it is suggested that the transport of PAH in Caco-2 cells is regulated by several transporters: a genistein-sensitive transporter on the apical membrane and probenecid-sensitive transporters on both the basolateral and apical membranes.	Probenecid	168-178	phenylalanine hydroxylase	Homo sapiens	49-52
11257884-7	2001	PAH biodegradation ceased when nitrate was depleted and resumed when the enrichment was fed nitrate, demonstrating that PAH biodegradation was dependent upon nitrate reduction.	Nitrates	31-38	phenylalanine hydroxylase	Homo sapiens	0-3
11257884-7	2001	PAH biodegradation ceased when nitrate was depleted and resumed when the enrichment was fed nitrate, demonstrating that PAH biodegradation was dependent upon nitrate reduction.	Nitrates	31-38	phenylalanine hydroxylase	Homo sapiens	120-123
11257884-7	2001	PAH biodegradation ceased when nitrate was depleted and resumed when the enrichment was fed nitrate, demonstrating that PAH biodegradation was dependent upon nitrate reduction.	Nitrates	92-99	phenylalanine hydroxylase	Homo sapiens	0-3
11257884-7	2001	PAH biodegradation ceased when nitrate was depleted and resumed when the enrichment was fed nitrate, demonstrating that PAH biodegradation was dependent upon nitrate reduction.	Nitrates	92-99	phenylalanine hydroxylase	Homo sapiens	120-123
11257884-7	2001	PAH biodegradation ceased when nitrate was depleted and resumed when the enrichment was fed nitrate, demonstrating that PAH biodegradation was dependent upon nitrate reduction.	Nitrates	92-99	phenylalanine hydroxylase	Homo sapiens	0-3
11257884-7	2001	PAH biodegradation ceased when nitrate was depleted and resumed when the enrichment was fed nitrate, demonstrating that PAH biodegradation was dependent upon nitrate reduction.	Nitrates	92-99	phenylalanine hydroxylase	Homo sapiens	120-123
11257884-10	2001	PAH carbon was incorporated into cell mass and mineralized after complete biodegradation of the PAHs, with 78-102% recoveries of radiolabel for naphthalene and phenanthrene, respectively.	Carbon	4-10	phenylalanine hydroxylase	Homo sapiens	0-3
11257884-10	2001	PAH carbon was incorporated into cell mass and mineralized after complete biodegradation of the PAHs, with 78-102% recoveries of radiolabel for naphthalene and phenanthrene, respectively.	Polycyclic Aromatic Hydrocarbons	96-100	phenylalanine hydroxylase	Homo sapiens	0-3
11257884-10	2001	PAH carbon was incorporated into cell mass and mineralized after complete biodegradation of the PAHs, with 78-102% recoveries of radiolabel for naphthalene and phenanthrene, respectively.	naphthalene	144-155	phenylalanine hydroxylase	Homo sapiens	0-3
11257884-10	2001	PAH carbon was incorporated into cell mass and mineralized after complete biodegradation of the PAHs, with 78-102% recoveries of radiolabel for naphthalene and phenanthrene, respectively.	phenanthrene	160-172	phenylalanine hydroxylase	Homo sapiens	0-3
11257884-11	2001	PAH carbon incorporation into biomass also varied considerably.	Carbon	4-10	phenylalanine hydroxylase	Homo sapiens	0-3
11257884-13	2001	PAH degradation was approximately stoichiometric with the amount of nitrate consumed.	Nitrates	68-75	phenylalanine hydroxylase	Homo sapiens	0-3
11257884-14	2001	Headspace analysis showed production of N2O, suggesting the enrichment coupled the biodegradation of PAH to denitrification.	Nitrous Oxide	40-43	phenylalanine hydroxylase	Homo sapiens	101-104
11206195-1	2001	The intestinal transport of an organic anion, p-aminohippuric acid (PAH), was studied in Caco-2 cell monolayers and rat intestinal tissue mounted in Ussing chambers.	p-Aminohippuric Acid	46-66	phenylalanine hydroxylase	Homo sapiens	68-71
11206195-5	2001	Addition of probenecid and genistein at the basolateral side decreased the secretory transport of [3H]PAH; the accumulation was not changed by probenecid, but was increased by genistein.	Probenecid	12-22	phenylalanine hydroxylase	Homo sapiens	102-105
11206195-5	2001	Addition of probenecid and genistein at the basolateral side decreased the secretory transport of [3H]PAH; the accumulation was not changed by probenecid, but was increased by genistein.	Genistein	27-36	phenylalanine hydroxylase	Homo sapiens	102-105
11206195-5	2001	Addition of probenecid and genistein at the basolateral side decreased the secretory transport of [3H]PAH; the accumulation was not changed by probenecid, but was increased by genistein.	Tritium	99-101	phenylalanine hydroxylase	Homo sapiens	102-105
11206195-5	2001	Addition of probenecid and genistein at the basolateral side decreased the secretory transport of [3H]PAH; the accumulation was not changed by probenecid, but was increased by genistein.	Genistein	176-185	phenylalanine hydroxylase	Homo sapiens	102-105
11206195-6	2001	In addition, the initial uptake rate of [3H]PAH from the basolateral side was decreased by both PAH and probenecid, but not by genistein.	Tritium	41-43	phenylalanine hydroxylase	Homo sapiens	44-47
11206195-6	2001	In addition, the initial uptake rate of [3H]PAH from the basolateral side was decreased by both PAH and probenecid, but not by genistein.	Tritium	41-43	phenylalanine hydroxylase	Homo sapiens	96-99
11057619-3	2000	The results of this study revealed that adding 3% and 5% (fuel vol%) Fluorene in the diesel fuel increases the amount of total-PAH emission by 2.6 and 5.7 times, respectively and increases the amount of Fluorene emission by 52.9 and 152 times, respectively, than no additives.	fluorene	69-77	phenylalanine hydroxylase	Homo sapiens	127-130
11057619-5	2000	To regulate the content of poly-aromatic content in diesel fuel, in contrast to the total aromatic content, will be more suitable for the management of PAH emission.	poly-aromatic	27-40	phenylalanine hydroxylase	Homo sapiens	152-155
11144026-4	2000	Part of the polycyclic aromatic hydrocarbons PAH and alkyl PAH was also degraded.	Polycyclic Aromatic Hydrocarbons	12-44	phenylalanine hydroxylase	Homo sapiens	45-48
11144026-4	2000	Part of the polycyclic aromatic hydrocarbons PAH and alkyl PAH was also degraded.	Polycyclic Aromatic Hydrocarbons	12-44	phenylalanine hydroxylase	Homo sapiens	59-62
10980574-1	2000	Phenylalanine hydroxylase (PAH) is the enzyme that converts phenylalanine to tyrosine as a rate-limiting step in phenylalanine catabolism and protein and neurotransmitter biosynthesis.	Phenylalanine	60-73	phenylalanine hydroxylase	Homo sapiens	0-25
10875932-8	2000	In conclusion, serine 349, located in the three-dimensional structure lining the active site and involved in the structural maintenance of the iron binding site, is essential for the structural stability and assembly and also for the catalytic properties of the PAH enzyme, whereas the L348V and V388M mutations affect the folding properties and stability of the protein.	Serine	15-21	phenylalanine hydroxylase	Homo sapiens	262-265
10875932-8	2000	In conclusion, serine 349, located in the three-dimensional structure lining the active site and involved in the structural maintenance of the iron binding site, is essential for the structural stability and assembly and also for the catalytic properties of the PAH enzyme, whereas the L348V and V388M mutations affect the folding properties and stability of the protein.	Iron	143-147	phenylalanine hydroxylase	Homo sapiens	262-265
11012685-0	2000	Microheterogeneity of recombinant human phenylalanine hydroxylase as a result of nonenzymatic deamidations of labile amide containing amino acids.	Amides	117-122	phenylalanine hydroxylase	Homo sapiens	40-65
10980574-1	2000	Phenylalanine hydroxylase (PAH) is the enzyme that converts phenylalanine to tyrosine as a rate-limiting step in phenylalanine catabolism and protein and neurotransmitter biosynthesis.	Tyrosine	77-85	phenylalanine hydroxylase	Homo sapiens	0-25
10980574-1	2000	Phenylalanine hydroxylase (PAH) is the enzyme that converts phenylalanine to tyrosine as a rate-limiting step in phenylalanine catabolism and protein and neurotransmitter biosynthesis.	Phenylalanine	113-126	phenylalanine hydroxylase	Homo sapiens	0-25
10933781-1	2000	The catalytic domains of the pterin-dependent enzymes phenylalanine hydroxylase and tyrosine hydroxylase are homologous, yet differ in their substrate specificities.	Pterins	29-35	phenylalanine hydroxylase	Homo sapiens	54-79
10964764-0	2000	Studies of ochratoxin A-induced inhibition of phenylalanine hydroxylase and its reversal by phenylalanine.	ochratoxin A	11-23	phenylalanine hydroxylase	Homo sapiens	46-71
10964764-4	2000	We have examined the effects of low doses of ochratoxin A on the activity of phenylalanine hydroxylase in kidney and in liver of experimental animals.	ochratoxin A	45-57	phenylalanine hydroxylase	Homo sapiens	77-102
10964764-5	2000	Daily administration of ochratoxin A (50 microg/kg body wt, for 10 and 35 days, respectively) caused a significant reduction in the phenylalanine hydroxylase activity.	ochratoxin A	24-36	phenylalanine hydroxylase	Homo sapiens	132-157
10964764-9	2000	Simultaneous application of ochratoxin A with phenylalanine could reduce inhibition of phenylalanine hydroxylase, in particular in liver.	ochratoxin A	28-40	phenylalanine hydroxylase	Homo sapiens	87-112
10964764-9	2000	Simultaneous application of ochratoxin A with phenylalanine could reduce inhibition of phenylalanine hydroxylase, in particular in liver.	Phenylalanine	46-59	phenylalanine hydroxylase	Homo sapiens	87-112
10933781-3	2000	Analysis of the effects of the mutations on the isolated catalytic domain of phenylalanine hydroxylase identified three residues that contribute to the ability to hydroxylate tyrosine, His264, Tyr277, and Val379.	Tyrosine	175-183	phenylalanine hydroxylase	Homo sapiens	77-102
10933781-5	2000	The steady-state kinetic parameters of the mutated enzymes showed that the identity of the residue in tyrosine hydroxylase at the position corresponding to position 379 of phenylalanine hydroxylase is critical for dihydroxyphenylalanine formation.	Dihydroxyphenylalanine	214-236	phenylalanine hydroxylase	Homo sapiens	172-197
10933781-7	2000	However, mutation of the corresponding valine 379 of phenylalanine hydroxylase to aspartate was not sufficient to allow phenylalanine hydroxylase to form dihydroxyphenylalanine at rates comparable to that of tyrosine hydroxylase.	Aspartic Acid	82-91	phenylalanine hydroxylase	Homo sapiens	53-78
10907879-2	2000	The addition of a cyclopenta ring also decreases the resolution of vibrational fine structure in the cases where the fine structure is particularly intense in the spectrum of the unsubstituted PAH.	cyclopenta	18-28	phenylalanine hydroxylase	Homo sapiens	193-196
10924272-1	2000	Hyperphenylalaninemia, which can cause neurological disorders and mental retardation, results from a mutation in phenylalanine hydroxylase or an enzyme required for biosynthesis or regeneration of its cofactor, tetrahydrobiopterin.	sapropterin	211-230	phenylalanine hydroxylase	Homo sapiens	113-138
10900078-1	2000	Tryptophan hydroxylase (TPH), the rate-limiting enzyme in the biosynthesis of the neurotransmitter serotonin (5-HT) belongs to the aromatic amino acid hydroxylase superfamily, which includes phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH).	Serotonin	99-108	phenylalanine hydroxylase	Homo sapiens	191-216
10855726-0	2000	Biological degradation of selected hydrocarbons in an old PAH/creosote contaminated soil from a gas work site.	Hydrocarbons	35-47	phenylalanine hydroxylase	Homo sapiens	58-61
10866613-1	2000	A new synthetic approach to polycyclic aromatic compounds is described that entails in the key steps double Suzuki coupling of PAH bisboronic acid derivatives with o-bromoaryl aldehydes to furnish aryl dialdehydes that are converted to larger polycyclic aromatic ring systems by either (a) conversion to diolefins by Wittig reaction followed by photocyclization or (b) reductive cyclization with triflic acid and 1,3-propanediol.	o-bromoaryl aldehydes	164-185	phenylalanine hydroxylase	Homo sapiens	127-130
10866613-1	2000	A new synthetic approach to polycyclic aromatic compounds is described that entails in the key steps double Suzuki coupling of PAH bisboronic acid derivatives with o-bromoaryl aldehydes to furnish aryl dialdehydes that are converted to larger polycyclic aromatic ring systems by either (a) conversion to diolefins by Wittig reaction followed by photocyclization or (b) reductive cyclization with triflic acid and 1,3-propanediol.	aryl dialdehydes	197-213	phenylalanine hydroxylase	Homo sapiens	127-130
10866613-1	2000	A new synthetic approach to polycyclic aromatic compounds is described that entails in the key steps double Suzuki coupling of PAH bisboronic acid derivatives with o-bromoaryl aldehydes to furnish aryl dialdehydes that are converted to larger polycyclic aromatic ring systems by either (a) conversion to diolefins by Wittig reaction followed by photocyclization or (b) reductive cyclization with triflic acid and 1,3-propanediol.	Alkadienes	304-313	phenylalanine hydroxylase	Homo sapiens	127-130
10866613-1	2000	A new synthetic approach to polycyclic aromatic compounds is described that entails in the key steps double Suzuki coupling of PAH bisboronic acid derivatives with o-bromoaryl aldehydes to furnish aryl dialdehydes that are converted to larger polycyclic aromatic ring systems by either (a) conversion to diolefins by Wittig reaction followed by photocyclization or (b) reductive cyclization with triflic acid and 1,3-propanediol.	trifluoromethanesulfonic acid	396-408	phenylalanine hydroxylase	Homo sapiens	127-130
10866613-1	2000	A new synthetic approach to polycyclic aromatic compounds is described that entails in the key steps double Suzuki coupling of PAH bisboronic acid derivatives with o-bromoaryl aldehydes to furnish aryl dialdehydes that are converted to larger polycyclic aromatic ring systems by either (a) conversion to diolefins by Wittig reaction followed by photocyclization or (b) reductive cyclization with triflic acid and 1,3-propanediol.	1,3-propanediol	413-428	phenylalanine hydroxylase	Homo sapiens	127-130
10855726-0	2000	Biological degradation of selected hydrocarbons in an old PAH/creosote contaminated soil from a gas work site.	Creosote	62-70	phenylalanine hydroxylase	Homo sapiens	58-61
11587443-0	2000	Nutrient-limited biodegradation of PAH in various soil strata at a creosote contaminated site.	Creosote	67-75	phenylalanine hydroxylase	Homo sapiens	35-38
10779621-6	2000	Strains degrading naphthalene, a simple PAH, did exist in the soil inocula used, but could be isolated only when enrichments were performed using pure naphthalene as the sole carbon source.	naphthalene	18-29	phenylalanine hydroxylase	Homo sapiens	40-43
10779621-6	2000	Strains degrading naphthalene, a simple PAH, did exist in the soil inocula used, but could be isolated only when enrichments were performed using pure naphthalene as the sole carbon source.	naphthalene	151-162	phenylalanine hydroxylase	Homo sapiens	40-43
10779621-6	2000	Strains degrading naphthalene, a simple PAH, did exist in the soil inocula used, but could be isolated only when enrichments were performed using pure naphthalene as the sole carbon source.	Carbon	175-181	phenylalanine hydroxylase	Homo sapiens	40-43
10767173-8	2000	The Pah enzyme activities of the various models correlate inversely with the corresponding phenylalanine levels in plasma and brain and the delay in plasma clearance response following a phenylalanine challenge.	Phenylalanine	91-104	phenylalanine hydroxylase	Homo sapiens	4-7
10767173-8	2000	The Pah enzyme activities of the various models correlate inversely with the corresponding phenylalanine levels in plasma and brain and the delay in plasma clearance response following a phenylalanine challenge.	Phenylalanine	187-200	phenylalanine hydroxylase	Homo sapiens	4-7
10767175-5	2000	The recombinant V388M mutant form exhibited a reduced specific activity equivalent to 30% of the wild-type hPAH enzyme when assayed using the synthetic cofactor (6-methyltetrahydropterin).	6-methyltetrahydropterin	162-186	phenylalanine hydroxylase	Homo sapiens	107-111
10767175-7	2000	The enzyme kinetic studies of the V388M mutant protein revealed that this enzyme was a kinetic variant form of hPAH with a reduced affinity for l-phenylalanine and for the natural cofactor ((6R)-tetrahydrobiopterin).	Phenylalanine	144-159	phenylalanine hydroxylase	Homo sapiens	111-115
10767175-7	2000	The enzyme kinetic studies of the V388M mutant protein revealed that this enzyme was a kinetic variant form of hPAH with a reduced affinity for l-phenylalanine and for the natural cofactor ((6R)-tetrahydrobiopterin).	sapropterin	190-214	phenylalanine hydroxylase	Homo sapiens	111-115
10698483-3	2000	This study investigates the relationship between PAH-DNA adduct levels (in maternal and newborn WBCs) and two polymorphisms: (a) an MspI RFLP in the 3" noncoding region of cytochrome P4501A1 (CYP1A1); and (b) an A-->G transition in nucleotide 313 of glutathione S-transferase P1 (GSTP1), resulting in an ile105val substitution.	ile105val	307-316	phenylalanine hydroxylase	Homo sapiens	49-52
10698483-5	2000	GSTP1 catalyzes the detoxification of PAH; the val allele has greater catalytic efficiency toward PAH diol epoxides.	Valine	47-50	phenylalanine hydroxylase	Homo sapiens	38-41
10698483-5	2000	GSTP1 catalyzes the detoxification of PAH; the val allele has greater catalytic efficiency toward PAH diol epoxides.	Valine	47-50	phenylalanine hydroxylase	Homo sapiens	98-101
11587443-11	2000	Our data illustrate the need for a better understanding of the role of nutrients in the degradation of high molecular weight hydrocarbons for the successful application of bioremediation at PAH contaminated sites.	Hydrocarbons	125-137	phenylalanine hydroxylase	Homo sapiens	190-193
10610798-0	1999	The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: implications for the catalytic mechanism.	Phenylalanine	43-56	phenylalanine hydroxylase	Homo sapiens	81-106
23886023-1	2000	1-Hydroxypyrene (1-OHP) urinary excretion has been studied in subjects exposed to polycyclic aromatic hydrocarbons (PAH) from different sources (urban air pollution, cigarette smoking, food contamination or occupational exposure).	1-hydroxypyrene	0-15	phenylalanine hydroxylase	Homo sapiens	116-119
23886023-1	2000	1-Hydroxypyrene (1-OHP) urinary excretion has been studied in subjects exposed to polycyclic aromatic hydrocarbons (PAH) from different sources (urban air pollution, cigarette smoking, food contamination or occupational exposure).	Polycyclic Aromatic Hydrocarbons	82-114	phenylalanine hydroxylase	Homo sapiens	116-119
10607731-13	2000	Higher levels of BPDE-DNA adducts in individuals with the combined CYP1A1(1/*2 or *2A/*2A)-GSTM1*0/*0 genotype suggest that these genotype combinations are at increased risk for contracting lung cancer when exposed to PAH.	7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide	17-21	phenylalanine hydroxylase	Homo sapiens	218-221
10610798-0	1999	The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: implications for the catalytic mechanism.	Pterins	61-67	phenylalanine hydroxylase	Homo sapiens	81-106
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	0-25
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	sapropterin	37-56	phenylalanine hydroxylase	Homo sapiens	27-30
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	Heme	65-69	phenylalanine hydroxylase	Homo sapiens	0-25
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	Heme	65-69	phenylalanine hydroxylase	Homo sapiens	27-30
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	Iron	70-74	phenylalanine hydroxylase	Homo sapiens	0-25
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	Iron	70-74	phenylalanine hydroxylase	Homo sapiens	27-30
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	Phenylalanine	110-115	phenylalanine hydroxylase	Homo sapiens	0-25
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	Phenylalanine	110-115	phenylalanine hydroxylase	Homo sapiens	27-30
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	Tyrosine	119-124	phenylalanine hydroxylase	Homo sapiens	0-25
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	Tyrosine	119-124	phenylalanine hydroxylase	Homo sapiens	27-30
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	Oxygen	141-147	phenylalanine hydroxylase	Homo sapiens	0-25
10610798-1	1999	Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate.	Oxygen	141-147	phenylalanine hydroxylase	Homo sapiens	27-30
10610798-3	1999	The conformation and distances to the catalytic iron of both L-Phe and the cofactor analogue L-erythro-7,8-dihydrobiopterin (BH2) simultaneously bound to recombinant human PAH have been estimated by (1)H NMR.	Iron	48-52	phenylalanine hydroxylase	Homo sapiens	172-175
10610798-3	1999	The conformation and distances to the catalytic iron of both L-Phe and the cofactor analogue L-erythro-7,8-dihydrobiopterin (BH2) simultaneously bound to recombinant human PAH have been estimated by (1)H NMR.	Phenylalanine	61-66	phenylalanine hydroxylase	Homo sapiens	172-175
10610798-3	1999	The conformation and distances to the catalytic iron of both L-Phe and the cofactor analogue L-erythro-7,8-dihydrobiopterin (BH2) simultaneously bound to recombinant human PAH have been estimated by (1)H NMR.	7,8-dihydrobiopterin	93-123	phenylalanine hydroxylase	Homo sapiens	172-175
10610798-3	1999	The conformation and distances to the catalytic iron of both L-Phe and the cofactor analogue L-erythro-7,8-dihydrobiopterin (BH2) simultaneously bound to recombinant human PAH have been estimated by (1)H NMR.	bh2	125-128	phenylalanine hydroxylase	Homo sapiens	172-175
10610798-6	1999	The mode of coordination of Glu330 to the iron moiety seems to determine the amino acid substrate specificity in PAH and in the homologous enzyme tyrosine hydroxylase.	Iron	42-46	phenylalanine hydroxylase	Homo sapiens	113-116
10816664-7	1999	In both melanocytes and keratinocytes 6BH4 controls the L-tyrosine supply via phenylalanine hydroxylase (PAH).	6bh4	38-42	phenylalanine hydroxylase	Homo sapiens	78-103
10643998-1	1999	It has been recognised that the active transport of L-phenylalanine and its autocrine turnover to L-tyrosine via phenylalanine hydroxylase in the cytosol of epidermal melanocytes provides the majority of the L-tyrosine pool for melanogenesis.	Phenylalanine	52-67	phenylalanine hydroxylase	Homo sapiens	113-138
10643998-1	1999	It has been recognised that the active transport of L-phenylalanine and its autocrine turnover to L-tyrosine via phenylalanine hydroxylase in the cytosol of epidermal melanocytes provides the majority of the L-tyrosine pool for melanogenesis.	Tyrosine	98-108	phenylalanine hydroxylase	Homo sapiens	113-138
10643998-1	1999	It has been recognised that the active transport of L-phenylalanine and its autocrine turnover to L-tyrosine via phenylalanine hydroxylase in the cytosol of epidermal melanocytes provides the majority of the L-tyrosine pool for melanogenesis.	Tyrosine	208-218	phenylalanine hydroxylase	Homo sapiens	113-138
10643998-2	1999	In this context, it has been shown that the cofactor 6(R)-L-erythro 5,6,7,8 tetrahydrobiopterin (6BH4) is produced de novo, recycled and regulated in both epidermal melanocytes and keratinocytes to control tyrosine hydroxylase, phenylalanine hydroxylase and tyrosinase activity.	sapropterin	53-95	phenylalanine hydroxylase	Homo sapiens	228-253
10643998-2	1999	In this context, it has been shown that the cofactor 6(R)-L-erythro 5,6,7,8 tetrahydrobiopterin (6BH4) is produced de novo, recycled and regulated in both epidermal melanocytes and keratinocytes to control tyrosine hydroxylase, phenylalanine hydroxylase and tyrosinase activity.	6bh4	97-101	phenylalanine hydroxylase	Homo sapiens	228-253
10559199-0	1999	Urea-induced denaturation of human phenylalanine hydroxylase.	Urea	0-4	phenylalanine hydroxylase	Homo sapiens	35-60
10559199-3	1999	At pH 7.50, purified human phenylalanine hydroxylase is transiently activated in the presence of 0-4 M urea but slowly inactivated at higher denaturant concentrations.	Urea	103-107	phenylalanine hydroxylase	Homo sapiens	27-52
10502602-3	1999	PAH samples from the stack flue gas (gas and particle phases) of these 25 boilers were collected by using a PAH stack sampling system.	flue	27-31	phenylalanine hydroxylase	Homo sapiens	0-3
10502602-9	1999	Nap was the most predominant PAH occurring in the stack flue gas.	N-(4-aminophenethyl)spiroperidol	0-3	phenylalanine hydroxylase	Homo sapiens	29-32
10502602-9	1999	Nap was the most predominant PAH occurring in the stack flue gas.	flue	56-60	phenylalanine hydroxylase	Homo sapiens	29-32
11543061-3	1999	These features disappear with increasing distance from the central source, and they show striking similarities to recent laboratory data of PAH cations, providing the first identification of emission features arising specifically from ionized PAHs in the interstellar medium.	Polycyclic Aromatic Hydrocarbons	243-247	phenylalanine hydroxylase	Homo sapiens	140-143
10462491-2	1999	In addition, a significantly more efficient autocrine turnover of L-phenylalanine to L-tyrosine via intracellular phenylalanine hydroxylase was demonstrated in melanocytes.	Phenylalanine	66-81	phenylalanine hydroxylase	Homo sapiens	114-139
10462491-2	1999	In addition, a significantly more efficient autocrine turnover of L-phenylalanine to L-tyrosine via intracellular phenylalanine hydroxylase was demonstrated in melanocytes.	Tyrosine	85-95	phenylalanine hydroxylase	Homo sapiens	114-139
10462491-5	1999	The transport of extracellular L-phenylalanine and its intracellular metabolism to L-tyrosine via intracellular phenylalanine hydroxylase are coupled to calcium uptake/efflux, whereas L-tyrosine uptake is calcium independent.	Phenylalanine	31-46	phenylalanine hydroxylase	Homo sapiens	112-137
10462491-5	1999	The transport of extracellular L-phenylalanine and its intracellular metabolism to L-tyrosine via intracellular phenylalanine hydroxylase are coupled to calcium uptake/efflux, whereas L-tyrosine uptake is calcium independent.	Tyrosine	83-93	phenylalanine hydroxylase	Homo sapiens	112-137
10462491-5	1999	The transport of extracellular L-phenylalanine and its intracellular metabolism to L-tyrosine via intracellular phenylalanine hydroxylase are coupled to calcium uptake/efflux, whereas L-tyrosine uptake is calcium independent.	Calcium	153-160	phenylalanine hydroxylase	Homo sapiens	112-137
10462491-5	1999	The transport of extracellular L-phenylalanine and its intracellular metabolism to L-tyrosine via intracellular phenylalanine hydroxylase are coupled to calcium uptake/efflux, whereas L-tyrosine uptake is calcium independent.	Calcium	205-212	phenylalanine hydroxylase	Homo sapiens	112-137
10444341-1	1999	Phenylalanine hydroxylase (PAH) is the key enzyme in phenylalanine metabolism.	Phenylalanine	53-66	phenylalanine hydroxylase	Homo sapiens	0-25
10444341-1	1999	Phenylalanine hydroxylase (PAH) is the key enzyme in phenylalanine metabolism.	Phenylalanine	53-66	phenylalanine hydroxylase	Homo sapiens	27-30
10444341-9	1999	Human kidney PAH may play a significant role in phenylalanine homeostasis of the organism, as impaired phenylalanine hydroxylation has been observed in renal failure and differences in the regulation of the kidney versus the liver enzyme have been indicated.	Phenylalanine	48-61	phenylalanine hydroxylase	Homo sapiens	13-16
10491778-0	1999	Influence of GSTM1 genotypes on anti-BPDE-DNA adduct levels in mononuclear white blood cells of humans exposed to PAH.	7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide	37-41	phenylalanine hydroxylase	Homo sapiens	114-117
10491778-3	1999	PAH exposure was assessed in each group by means of the urinary excretion of 1-pyrenol (mean group levels 1.2, 0.7, 0.3, and 0.1 mumol/mol creatinine in coke-oven workers, chimney sweeps, aluminum-anode plant workers, and control subjects, respectively).	1-hydroxypyrene	77-86	phenylalanine hydroxylase	Homo sapiens	0-3
10491778-9	1999	In coke-oven workers, chimney sweeps, and aluminum workers, respectively, the multiplicative effect of the null genotype with occupational PAH exposure gives risks of 162 (= 27.2 x 5.94), 10 (= 1.70 x 5.94), and 3 (= 0.50 x 5.94) times higher probability (risk) of high BPDE-DNA adduct formation than that of non-exposed subjects with the active GSTM1 genotype.	Aluminum	42-50	phenylalanine hydroxylase	Homo sapiens	139-142
10491778-9	1999	In coke-oven workers, chimney sweeps, and aluminum workers, respectively, the multiplicative effect of the null genotype with occupational PAH exposure gives risks of 162 (= 27.2 x 5.94), 10 (= 1.70 x 5.94), and 3 (= 0.50 x 5.94) times higher probability (risk) of high BPDE-DNA adduct formation than that of non-exposed subjects with the active GSTM1 genotype.	7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide	270-274	phenylalanine hydroxylase	Homo sapiens	139-142
10491778-10	1999	CONCLUSION: Our results indicate a greater risk of anti-BPDE-DNA adduct formation resulting from occupational high-level PAH-exposure in GSTM1 null (GSTM1 *0/*0) workers.	7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide	56-60	phenylalanine hydroxylase	Homo sapiens	121-124
10331871-1	1999	Phenylalanine hydroxylase converts phenylalanine to tyrosine, a rate-limiting step in phenylalanine catabolism and protein and neurotransmitter biosynthesis.	Phenylalanine	35-48	phenylalanine hydroxylase	Homo sapiens	0-25
10331871-1	1999	Phenylalanine hydroxylase converts phenylalanine to tyrosine, a rate-limiting step in phenylalanine catabolism and protein and neurotransmitter biosynthesis.	Tyrosine	52-60	phenylalanine hydroxylase	Homo sapiens	0-25
10191121-2	1999	We previously reported that the yeast Saccharomyces cerevisiae contains a homolog to Cln3p, designated Btn1p, and that the human Cln3p complemented the pH-dependent resistance to D-(-)-threo-2-amino-1-[p-nitrophenyl]-1, 3-propanediol in btn1-Delta yeast mutants.	d-(-)-threo-2-amino-1-[p-nitrophenyl]-1, 3-propanediol	179-233	phenylalanine hydroxylase	Homo sapiens	152-154
10218078-13	1999	Inhaled nitric oxide has also been used to treat PAH in newborns and other forms of acute and chronic PAH.	Nitric Oxide	8-20	phenylalanine hydroxylase	Homo sapiens	49-52
10218078-13	1999	Inhaled nitric oxide has also been used to treat PAH in newborns and other forms of acute and chronic PAH.	Nitric Oxide	8-20	phenylalanine hydroxylase	Homo sapiens	102-105
10037716-0	1999	The accessibility of iron at the active site of recombinant human phenylalanine hydroxylase to water as studied by 1H NMR paramagnetic relaxation.	Iron	21-25	phenylalanine hydroxylase	Homo sapiens	66-91
10037716-0	1999	The accessibility of iron at the active site of recombinant human phenylalanine hydroxylase to water as studied by 1H NMR paramagnetic relaxation.	Water	95-100	phenylalanine hydroxylase	Homo sapiens	66-91
10037716-0	1999	The accessibility of iron at the active site of recombinant human phenylalanine hydroxylase to water as studied by 1H NMR paramagnetic relaxation.	Hydrogen	115-117	phenylalanine hydroxylase	Homo sapiens	66-91
10037716-2	1999	The high-spin (S = 5/2) Fe(III) ion at the active site of recombinant human phenylalanine hydroxylase (PAH) has a paramagnetic effect on the longitudinal relaxation rate of water protons.	ferric sulfate	24-31	phenylalanine hydroxylase	Homo sapiens	76-101
10037716-2	1999	The high-spin (S = 5/2) Fe(III) ion at the active site of recombinant human phenylalanine hydroxylase (PAH) has a paramagnetic effect on the longitudinal relaxation rate of water protons.	ferric sulfate	24-31	phenylalanine hydroxylase	Homo sapiens	103-106
10037716-2	1999	The high-spin (S = 5/2) Fe(III) ion at the active site of recombinant human phenylalanine hydroxylase (PAH) has a paramagnetic effect on the longitudinal relaxation rate of water protons.	Water	173-178	phenylalanine hydroxylase	Homo sapiens	76-101
10037716-2	1999	The high-spin (S = 5/2) Fe(III) ion at the active site of recombinant human phenylalanine hydroxylase (PAH) has a paramagnetic effect on the longitudinal relaxation rate of water protons.	Water	173-178	phenylalanine hydroxylase	Homo sapiens	103-106
10037716-7	1999	Thus, the recombinant human PAH appears to have a more solvent-accessible catalytic iron than the rat enzyme, in which the water coordinated to the metal is slowly exchanging with the solvent.	Iron	84-88	phenylalanine hydroxylase	Homo sapiens	28-31
10037716-7	1999	Thus, the recombinant human PAH appears to have a more solvent-accessible catalytic iron than the rat enzyme, in which the water coordinated to the metal is slowly exchanging with the solvent.	Water	123-128	phenylalanine hydroxylase	Homo sapiens	28-31
10037716-7	1999	Thus, the recombinant human PAH appears to have a more solvent-accessible catalytic iron than the rat enzyme, in which the water coordinated to the metal is slowly exchanging with the solvent.	Metals	148-153	phenylalanine hydroxylase	Homo sapiens	28-31
10037716-9	1999	In the presence of saturating (5 mM) concentrations of the substrate L-Phe, the paramagnetic molar relaxivity for human PAH decreased to 0.72 (+/- 0.05) x 10(3) s-1 M-1 with no significant change in the Ea.	Phenylalanine	69-74	phenylalanine hydroxylase	Homo sapiens	120-123
10511262-0	1999	Urinary 1-hydroxypyrene and other PAH metabolites as biomarkers of exposure to environmental PAH in air particulate matter.	1-hydroxypyrene	8-23	phenylalanine hydroxylase	Homo sapiens	93-96
10511262-2	1999	PAH metabolites in human urine can be used as biomarkers of internal dose to assess recent exposure to PAHs.	Polycyclic Aromatic Hydrocarbons	103-107	phenylalanine hydroxylase	Homo sapiens	0-3
10511262-3	1999	The most widely used urinary PAH metabolites are 1-hydroxypyrene (1-OHP) or 1-hydroxypyrene-O-glucuronide (1-OHP-gluc), the major form of 1-OHP in human urine, because of their relatively high concentration and prevalence in urine and their relative ease of measurement.	1-hydroxypyrene	49-64	phenylalanine hydroxylase	Homo sapiens	29-32
10511262-3	1999	The most widely used urinary PAH metabolites are 1-hydroxypyrene (1-OHP) or 1-hydroxypyrene-O-glucuronide (1-OHP-gluc), the major form of 1-OHP in human urine, because of their relatively high concentration and prevalence in urine and their relative ease of measurement.	Oxaliplatin	66-71	phenylalanine hydroxylase	Homo sapiens	29-32
10511262-3	1999	The most widely used urinary PAH metabolites are 1-hydroxypyrene (1-OHP) or 1-hydroxypyrene-O-glucuronide (1-OHP-gluc), the major form of 1-OHP in human urine, because of their relatively high concentration and prevalence in urine and their relative ease of measurement.	1-hydroxypyrene-o-glucuronide	76-105	phenylalanine hydroxylase	Homo sapiens	29-32
10511262-3	1999	The most widely used urinary PAH metabolites are 1-hydroxypyrene (1-OHP) or 1-hydroxypyrene-O-glucuronide (1-OHP-gluc), the major form of 1-OHP in human urine, because of their relatively high concentration and prevalence in urine and their relative ease of measurement.	Oxaliplatin	107-112	phenylalanine hydroxylase	Homo sapiens	29-32
10511262-3	1999	The most widely used urinary PAH metabolites are 1-hydroxypyrene (1-OHP) or 1-hydroxypyrene-O-glucuronide (1-OHP-gluc), the major form of 1-OHP in human urine, because of their relatively high concentration and prevalence in urine and their relative ease of measurement.	Oxaliplatin	107-112	phenylalanine hydroxylase	Homo sapiens	29-32
10356314-9	1999	The result of treatment with the phenylalanine-restricted diet was that these individuals could participate in society and were able to arrest the neurodegenerative course characteristic of persons with mutations classified as severe in the phenylalanine hydroxylase gene.	Phenylalanine	33-46	phenylalanine hydroxylase	Homo sapiens	241-266
10356315-2	1999	For this reason, various indexes that measure plasma concentrations of phenylalanine (Phe) and tyrosine (Tyr), as an expression of Phe metabolizing capacity, have been used for the detection of carriers for mutations in the PAH gene.	Phenylalanine	71-84	phenylalanine hydroxylase	Homo sapiens	224-227
10356315-2	1999	For this reason, various indexes that measure plasma concentrations of phenylalanine (Phe) and tyrosine (Tyr), as an expression of Phe metabolizing capacity, have been used for the detection of carriers for mutations in the PAH gene.	Phenylalanine	86-89	phenylalanine hydroxylase	Homo sapiens	224-227
10356315-2	1999	For this reason, various indexes that measure plasma concentrations of phenylalanine (Phe) and tyrosine (Tyr), as an expression of Phe metabolizing capacity, have been used for the detection of carriers for mutations in the PAH gene.	Tyrosine	95-103	phenylalanine hydroxylase	Homo sapiens	224-227
10356315-2	1999	For this reason, various indexes that measure plasma concentrations of phenylalanine (Phe) and tyrosine (Tyr), as an expression of Phe metabolizing capacity, have been used for the detection of carriers for mutations in the PAH gene.	Tyrosine	105-108	phenylalanine hydroxylase	Homo sapiens	224-227
10356315-2	1999	For this reason, various indexes that measure plasma concentrations of phenylalanine (Phe) and tyrosine (Tyr), as an expression of Phe metabolizing capacity, have been used for the detection of carriers for mutations in the PAH gene.	Phenylalanine	131-134	phenylalanine hydroxylase	Homo sapiens	224-227
10356315-7	1999	The results found show a relationship between the severity of PKU/HPA mutations in the PAH gene and their biochemical phenotype (Phe/Tyr, Phe2/Tyr) as an expression of the residual enzymatic activity.	Phenylalanine	129-132	phenylalanine hydroxylase	Homo sapiens	87-90
10356315-7	1999	The results found show a relationship between the severity of PKU/HPA mutations in the PAH gene and their biochemical phenotype (Phe/Tyr, Phe2/Tyr) as an expression of the residual enzymatic activity.	Tyrosine	133-136	phenylalanine hydroxylase	Homo sapiens	87-90
10356315-7	1999	The results found show a relationship between the severity of PKU/HPA mutations in the PAH gene and their biochemical phenotype (Phe/Tyr, Phe2/Tyr) as an expression of the residual enzymatic activity.	Tyrosine	143-146	phenylalanine hydroxylase	Homo sapiens	87-90
11543340-6	1999	This refines the Ionization Potential estimates which are between 10 and 13 eV, hence reminiscent of PAH or fullerene cations for those DIBs.	N,N-Diisopropylbenzothiazole-2-sulfenamide	136-140	phenylalanine hydroxylase	Homo sapiens	101-104
9894540-0	1999	Exposure to PAH and fluoride in aluminum reduction plants in Norway: historical estimation of exposure using process parameters and industrial hygiene measurements.	Aluminum	32-40	phenylalanine hydroxylase	Homo sapiens	12-15
10321973-3	1999	BH4 is a cofactor for three pteridine-requiring monooxygenases that hydroxylate aromatic L-amino acids, i.e., tyrosine hydroxylase (TH), tryptophan hydroxylase (TPH), and phenylalanine hydroxylase (PAH), as well as for nitric oxide synthase (NOS).	sapropterin	0-3	phenylalanine hydroxylase	Homo sapiens	171-196
10321973-3	1999	BH4 is a cofactor for three pteridine-requiring monooxygenases that hydroxylate aromatic L-amino acids, i.e., tyrosine hydroxylase (TH), tryptophan hydroxylase (TPH), and phenylalanine hydroxylase (PAH), as well as for nitric oxide synthase (NOS).	sapropterin	0-3	phenylalanine hydroxylase	Homo sapiens	198-201
10321973-3	1999	BH4 is a cofactor for three pteridine-requiring monooxygenases that hydroxylate aromatic L-amino acids, i.e., tyrosine hydroxylase (TH), tryptophan hydroxylase (TPH), and phenylalanine hydroxylase (PAH), as well as for nitric oxide synthase (NOS).	aromatic l-amino acids	80-102	phenylalanine hydroxylase	Homo sapiens	171-196
10321973-3	1999	BH4 is a cofactor for three pteridine-requiring monooxygenases that hydroxylate aromatic L-amino acids, i.e., tyrosine hydroxylase (TH), tryptophan hydroxylase (TPH), and phenylalanine hydroxylase (PAH), as well as for nitric oxide synthase (NOS).	aromatic l-amino acids	80-102	phenylalanine hydroxylase	Homo sapiens	198-201
23902352-4	1999	Significantly different ratios for the regiospecific oxidation of phenanthrene were found for smokers when compared with non-smokers (1,2-oxidation vs 3,4-oxidation was 1.45 in the case of smokers, but 2.34 in the case of non-smokers) indicating a cigarette smoke - but not PAH - caused induction of CYP 1A2 in smokers.	phenanthrene	66-78	phenylalanine hydroxylase	Homo sapiens	274-277
10872454-1	1999	Phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase constitute a small family of monooxygenases that utilize tetrahydropterins as substrates.	tetrahydropterin	133-150	phenylalanine hydroxylase	Homo sapiens	0-75
10872454-7	1999	In addition, phenylalanine hydroxylase is allosterically regulated by its substrates, phenylalanine and tetrahydrobiopterin.	sapropterin	104-123	phenylalanine hydroxylase	Homo sapiens	13-38
23902352-5	1999	As a consequence of the degree of PAH exposure the ratio dihydrodiols/phenols depends on the total amount of metabolites excreted.	trans-1,2-dihydro-1,2-naphthalenediol	57-69	phenylalanine hydroxylase	Homo sapiens	34-37
23902352-5	1999	As a consequence of the degree of PAH exposure the ratio dihydrodiols/phenols depends on the total amount of metabolites excreted.	Phenols	70-77	phenylalanine hydroxylase	Homo sapiens	34-37
10693064-4	1999	PAH mutations were identified by extraction of genomic DNA from leucocytes (whole blood in EDTA), PAH exon amplification was determined by polymerase chain reaction, restriction enzyme analysis was carried out for some recognised mutations, and DNA sequence analysis for the other mutations.	Edetic Acid	91-95	phenylalanine hydroxylase	Homo sapiens	0-3
9860305-9	1998	Simple linear regression analysis showed a correlation between pretreatment phenylalanine concentrations and predicted PAH activity in 29 Japanese PKU patients (y=31.9-1.03x, r=0.59, P<0.0001).	Phenylalanine	76-89	phenylalanine hydroxylase	Homo sapiens	119-122
10089284-1	1998	Background: 6-Pyruvoyl-tetrahydrobiopterin synthase (PTPS) is required for biosynthesis of tetrahydrobiopterin, the cofactor of various enzymes including the hepatic phenylalanine hydroxylase.	sapropterin	23-42	phenylalanine hydroxylase	Homo sapiens	166-191
11717935-1	1998	OBJECTIVE: To establish a sensitive, accurate and reliable method for analysis of short tandem repeat (STR) markers for gene diagnosis, capillary electrophoresis (CE) was used for analysis of a polymorphic tetranucleotide (TCTA)n in intron 3 of the phenylalanine hydroxylase (PAH) gene.	tetranucleotide	206-221	phenylalanine hydroxylase	Homo sapiens	249-274
11717935-1	1998	OBJECTIVE: To establish a sensitive, accurate and reliable method for analysis of short tandem repeat (STR) markers for gene diagnosis, capillary electrophoresis (CE) was used for analysis of a polymorphic tetranucleotide (TCTA)n in intron 3 of the phenylalanine hydroxylase (PAH) gene.	tetranucleotide	206-221	phenylalanine hydroxylase	Homo sapiens	276-279
9819237-1	1998	The aromatic amino acid hydroxylases tyrosine and phenylalanine hydroxylase both contain non-heme iron, utilize oxygen and tetrahydrobiopterin, and are tetramers of identical subunits.	Heme	93-97	phenylalanine hydroxylase	Homo sapiens	50-75
9819237-1	1998	The aromatic amino acid hydroxylases tyrosine and phenylalanine hydroxylase both contain non-heme iron, utilize oxygen and tetrahydrobiopterin, and are tetramers of identical subunits.	Iron	98-102	phenylalanine hydroxylase	Homo sapiens	50-75
9819237-1	1998	The aromatic amino acid hydroxylases tyrosine and phenylalanine hydroxylase both contain non-heme iron, utilize oxygen and tetrahydrobiopterin, and are tetramers of identical subunits.	Oxygen	112-118	phenylalanine hydroxylase	Homo sapiens	50-75
9819237-1	1998	The aromatic amino acid hydroxylases tyrosine and phenylalanine hydroxylase both contain non-heme iron, utilize oxygen and tetrahydrobiopterin, and are tetramers of identical subunits.	sapropterin	123-142	phenylalanine hydroxylase	Homo sapiens	50-75
9819237-3	1998	The hydroxyl oxygens of tyrosine 371 in tyrosine hydroxylase and of tyrosine 325 of phenylalanine hydroxylase are 5 and 4.5 A, respectively, away from the active site iron in the enzymes.	Oxygen	13-20	phenylalanine hydroxylase	Homo sapiens	84-109
9819237-3	1998	The hydroxyl oxygens of tyrosine 371 in tyrosine hydroxylase and of tyrosine 325 of phenylalanine hydroxylase are 5 and 4.5 A, respectively, away from the active site iron in the enzymes.	Iron	167-171	phenylalanine hydroxylase	Homo sapiens	84-109
9804920-1	1998	Bitumen samples and fumes consist essentially of polycyclic hydrocarbons (PAH) and their derivatives, some of which are known to be carcinogenic or co-carcinogenic in animals.	Hydrocarbons, Cyclic	49-72	phenylalanine hydroxylase	Homo sapiens	74-77
9804920-5	1998	Urinary 1-hydroxypyrene (1-OHP) excretion was used as a biomarker of occupational exposure to PAH.	1-hydroxypyrene	8-23	phenylalanine hydroxylase	Homo sapiens	94-97
9804920-5	1998	Urinary 1-hydroxypyrene (1-OHP) excretion was used as a biomarker of occupational exposure to PAH.	Oxaliplatin	25-30	phenylalanine hydroxylase	Homo sapiens	94-97
9843368-0	1998	Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution.	catechol	93-101	phenylalanine hydroxylase	Homo sapiens	39-64
9843368-2	1998	Here we present the crystal structure of the dimeric catalytic domain (residues 117-424) of human phenylalanine hydroxylase (hPheOH), cocrystallized with various potent and well-known catechol inhibitors and refined at a resolution of 2.0 A.	catechol	184-192	phenylalanine hydroxylase	Homo sapiens	98-123
9792411-1	1998	Phenylalanine hydroxylase (PAH) catalyzes the conversion of phenylalanine to tyrosine; its activity is the major determinant of phenylalanine disposal.	Phenylalanine	60-73	phenylalanine hydroxylase	Homo sapiens	0-25
9675155-2	1998	It is a pterin 4alpha-carbinolamine dehydratase that is involved in the regeneration of the cofactor tetrahydrobiopterin during the phenylalanine hydroxylase- catalyzed hydroxylation of phenylalanine.	sapropterin	101-120	phenylalanine hydroxylase	Homo sapiens	132-157
9642259-1	1998	Phenylalanine hydroxylase (PheOH) catalyzes the conversion of L-phenylalanine to L-tyrosine, the rate-limiting step in the oxidative degradation of phenylalanine.	Phenylalanine	62-77	phenylalanine hydroxylase	Homo sapiens	0-25
9642259-1	1998	Phenylalanine hydroxylase (PheOH) catalyzes the conversion of L-phenylalanine to L-tyrosine, the rate-limiting step in the oxidative degradation of phenylalanine.	Tyrosine	81-91	phenylalanine hydroxylase	Homo sapiens	0-25
9642259-1	1998	Phenylalanine hydroxylase (PheOH) catalyzes the conversion of L-phenylalanine to L-tyrosine, the rate-limiting step in the oxidative degradation of phenylalanine.	Phenylalanine	64-77	phenylalanine hydroxylase	Homo sapiens	0-25
9637722-2	1998	In phenylketonuria (PKU), the enzyme phenylalanine hydroxylase is deficient, resulting in a decreased conversion of phenylalanine (Phe) into tyrosine (Tyr).	Phenylalanine	131-134	phenylalanine hydroxylase	Homo sapiens	37-62
9637722-2	1998	In phenylketonuria (PKU), the enzyme phenylalanine hydroxylase is deficient, resulting in a decreased conversion of phenylalanine (Phe) into tyrosine (Tyr).	Tyrosine	141-149	phenylalanine hydroxylase	Homo sapiens	37-62
9637722-2	1998	In phenylketonuria (PKU), the enzyme phenylalanine hydroxylase is deficient, resulting in a decreased conversion of phenylalanine (Phe) into tyrosine (Tyr).	Tyrosine	151-154	phenylalanine hydroxylase	Homo sapiens	37-62
9686365-0	1998	Phenylalanine and tyrosine metabolism in phenylketonuria heterozygotes: influence of different phenylalanine hydroxylase mutations.	Phenylalanine	0-13	phenylalanine hydroxylase	Homo sapiens	95-120
9700593-1	1998	The wide variation in phenylalanine hydroxylating capacity observed among patients with phenylketonuria (PKU) is primarily due to allelic heterogeneity at the phenylalanine hydroxylase (PAH) locus.	Phenylalanine	22-35	phenylalanine hydroxylase	Homo sapiens	159-184
9700593-1	1998	The wide variation in phenylalanine hydroxylating capacity observed among patients with phenylketonuria (PKU) is primarily due to allelic heterogeneity at the phenylalanine hydroxylase (PAH) locus.	Phenylalanine	22-35	phenylalanine hydroxylase	Homo sapiens	186-189
9700593-2	1998	In this study, we examined phenylalanine metabolism after an oral phenylalanine load in 148 carriers of known PAH gene mutations.	Phenylalanine	27-40	phenylalanine hydroxylase	Homo sapiens	110-113
9700593-3	1998	As a group, heterozygotes formed less tyrosine than normozygotes (p < 0.001), and there was a tendency that carriers of a severe PAH mutation formed less tyrosine than carriers of a mild mutation.	Tyrosine	157-165	phenylalanine hydroxylase	Homo sapiens	132-135
9717460-4	1998	The ternary complex PAH-AHR-ARNT acts as a transcription factor and binds aromatic hydrocarbon responsive element to increase the expression of CYP1A1 gene.	aromatic	74-82	phenylalanine hydroxylase	Homo sapiens	20-23
9717460-4	1998	The ternary complex PAH-AHR-ARNT acts as a transcription factor and binds aromatic hydrocarbon responsive element to increase the expression of CYP1A1 gene.	Hydrocarbons	83-94	phenylalanine hydroxylase	Homo sapiens	20-23
9574457-1	1998	PAH (N-(4-aminobenzoyl)-glycin) clearance measurements have been used for 50 years in clinical research for the determination of renal plasma flow.	n-(4-aminobenzoyl)-glycin	5-30	phenylalanine hydroxylase	Homo sapiens	0-3
9574457-10	1998	The fraction of PAH excreted by the kidney CLR/CLS calculated from HPLC data (n = 143) is, as expected, always < 1 (mean = 0.73 +/- 0.11), whereas the colorimetric method gives a mean extraction ratio of 0.87 +/- 0.13 implying unphysio-logical values (> 1) in some cases.	Chlorine	47-50	phenylalanine hydroxylase	Homo sapiens	16-19
9465044-0	1998	Identification of hepatic nuclear factor 1 binding sites in the 5" flanking region of the human phenylalanine hydroxylase gene: implication of a dual function of phenylalanine hydroxylase stimulator in the phenylalanine hydroxylation system.	Phenylalanine	96-109	phenylalanine hydroxylase	Homo sapiens	162-187
9465044-8	1998	This study suggests a possible dual function of PHS in vivo in the human phenylalanine hydroxylation system: it is involved in the regeneration of the cofactor tetrahydrobiopterin and can also enhance the expression of the human PAH gene.	Phenylalanine	73-86	phenylalanine hydroxylase	Homo sapiens	229-232
9480820-3	1998	The latter event leads to an accumulation of the nonenzymatic isomer (7R) L-erythro 5,6,7,8 tetrahydrobiopterin (7BH4) inhibiting phenylalanine hydroxylase (PAH) with an apparent Ki = 10(-6) M. One consequence of decreased epidermal PAH activities would be a build-up of L-phenylalanine.	sapropterin	84-111	phenylalanine hydroxylase	Homo sapiens	130-155
9480820-3	1998	The latter event leads to an accumulation of the nonenzymatic isomer (7R) L-erythro 5,6,7,8 tetrahydrobiopterin (7BH4) inhibiting phenylalanine hydroxylase (PAH) with an apparent Ki = 10(-6) M. One consequence of decreased epidermal PAH activities would be a build-up of L-phenylalanine.	2-amino-4-hydroxy-7-(dihydroxypropyl)-5,6,7,8-tetrahydrobiopterin	113-117	phenylalanine hydroxylase	Homo sapiens	130-155
9480820-3	1998	The latter event leads to an accumulation of the nonenzymatic isomer (7R) L-erythro 5,6,7,8 tetrahydrobiopterin (7BH4) inhibiting phenylalanine hydroxylase (PAH) with an apparent Ki = 10(-6) M. One consequence of decreased epidermal PAH activities would be a build-up of L-phenylalanine.	Phenylalanine	271-286	phenylalanine hydroxylase	Homo sapiens	130-155
9488590-3	1998	The geometric mean of benzo(a)pyrene air measurements (an index compound of PAH levels) was 70 times higher in traffic police officers (3.67 ng/m3) than in referents (0.05 ng/m3).	Benzo(a)pyrene	22-36	phenylalanine hydroxylase	Homo sapiens	76-79
9488590-4	1998	The urinary concentration of 1-OH-P was clearly associated with cigarette smoking and, to a lesser extent, with exposure to ETS and particulate PAH pollution.	Oxaliplatin	29-35	phenylalanine hydroxylase	Homo sapiens	144-147
9824245-1	1998	A sensitive and specific high-performance liquid chromatographic assay was developed for the simultaneous determination of p-aminohippuric acid (PAH), acetyl-p-aminohippuric acid (aPAH), and iothalamate in human plasma and urine.	p-Aminohippuric Acid	123-143	phenylalanine hydroxylase	Homo sapiens	145-148
9532730-1	1998	PAH emission from the powered engines fueled by a 95 leadfree gasoline (95-LFG), a 92 leadfree gasoline (92-LFG) and a Premium leaded gasoline (PLG) with two gasoline additives (SA and SB) were collected using a PAH sampling system with a particulate interception device.	Antimony	185-187	phenylalanine hydroxylase	Homo sapiens	0-3
9577752-8	1998	Conventional and CRM asphalt worker airborne exposures to the PAH carcinogen marker, BaP, were very low with concentrations comparable to ambient air in many cities.	benzylaminopurine	85-88	phenylalanine hydroxylase	Homo sapiens	62-65
9490012-5	1998	Our results also demonstrate that the conformational events involved in the activation of hPAH by its substrate (L-Phe) are mainly related to changes in the tertiary/quaternary structure.	Phenylalanine	113-118	phenylalanine hydroxylase	Homo sapiens	90-94
9498680-3	1998	The suitability of the method for profile analysis of PAH metabolites is shown by analysing a smokers urine after enzymatic cleavage (and additionally after spiking with the target analytes) and spiked water.	Water	202-207	phenylalanine hydroxylase	Homo sapiens	54-57
9792411-1	1998	Phenylalanine hydroxylase (PAH) catalyzes the conversion of phenylalanine to tyrosine; its activity is the major determinant of phenylalanine disposal.	Phenylalanine	60-73	phenylalanine hydroxylase	Homo sapiens	27-30
9792411-1	1998	Phenylalanine hydroxylase (PAH) catalyzes the conversion of phenylalanine to tyrosine; its activity is the major determinant of phenylalanine disposal.	Tyrosine	77-85	phenylalanine hydroxylase	Homo sapiens	0-25
9792411-1	1998	Phenylalanine hydroxylase (PAH) catalyzes the conversion of phenylalanine to tyrosine; its activity is the major determinant of phenylalanine disposal.	Tyrosine	77-85	phenylalanine hydroxylase	Homo sapiens	27-30
9792411-1	1998	Phenylalanine hydroxylase (PAH) catalyzes the conversion of phenylalanine to tyrosine; its activity is the major determinant of phenylalanine disposal.	Phenylalanine	128-141	phenylalanine hydroxylase	Homo sapiens	0-25
9792411-1	1998	Phenylalanine hydroxylase (PAH) catalyzes the conversion of phenylalanine to tyrosine; its activity is the major determinant of phenylalanine disposal.	Phenylalanine	128-141	phenylalanine hydroxylase	Homo sapiens	27-30
27414767-6	1997	Cytochrome P-450 enzymes can hydroxylate salicylate to produce 2,5-DHBA, and it is likely that phenylalanine hydroxylase produces most of the p-tyrosine detected in hepatic tissues.	Tyrosine	142-152	phenylalanine hydroxylase	Homo sapiens	95-120
9305947-6	1997	All three proteins containing the catalytic domain of phenylalanine hydroxylase were unable to hydroxylate tyrosine.	Tyrosine	107-115	phenylalanine hydroxylase	Homo sapiens	54-79
9305947-7	1997	Only wild-type phenylalanine hydroxylase required pretreatment with phenylalanine for full activity with tetrahydrobiopterin as substrate.	sapropterin	105-124	phenylalanine hydroxylase	Homo sapiens	15-40
9200859-3	1997	The objective of this study was to examine the applicability of urinary 1-OH-pyrene as a biological monitoring index for human low-level PAH exposure, such as the PAH exposure experienced while working in the street.	1-oh-pyrene	72-83	phenylalanine hydroxylase	Homo sapiens	137-140
9200859-3	1997	The objective of this study was to examine the applicability of urinary 1-OH-pyrene as a biological monitoring index for human low-level PAH exposure, such as the PAH exposure experienced while working in the street.	1-oh-pyrene	72-83	phenylalanine hydroxylase	Homo sapiens	163-166
9200859-12	1997	A positive correlation between total PAH levels and the pyrene levels was observed.	pyrene	56-62	phenylalanine hydroxylase	Homo sapiens	37-40
9109411-1	1997	A recombinant truncated form (delta1-102/delta428-452) of the non-heme iron-dependent metalloenzyme human phenylalanine hydroxylase (hPAH, phenylalanine 4-monooxygenase; EC 1.14.16.1) was expressed in E. coli, purified to homogeneity as a homodimer (70 kDa) and crystallized using the hanging drop vapour diffusion method.	Iron	71-75	phenylalanine hydroxylase	Homo sapiens	106-131
9109411-1	1997	A recombinant truncated form (delta1-102/delta428-452) of the non-heme iron-dependent metalloenzyme human phenylalanine hydroxylase (hPAH, phenylalanine 4-monooxygenase; EC 1.14.16.1) was expressed in E. coli, purified to homogeneity as a homodimer (70 kDa) and crystallized using the hanging drop vapour diffusion method.	Iron	71-75	phenylalanine hydroxylase	Homo sapiens	139-168
9380432-0	1997	Analysis of phenylalanine hydroxylase genotypes and hyperphenylalaninemia phenotypes using L-[1-13C]phenylalanine oxidation rates in vivo: a pilot study.	l-[1-13c]phenylalanine	91-113	phenylalanine hydroxylase	Homo sapiens	12-37
9380432-8	1997	The findings indicate that the in vivo metrical trait (phenylalanine oxidation rate) is not a simple equivalent of phenylalanine hydroxylation activity (unit of protein phenotype) and, as expected, is an emergent property under the control of more than the PAH locus.	Phenylalanine	55-68	phenylalanine hydroxylase	Homo sapiens	257-260
9341091-3	1997	Studies with naphthalene indicated that PAH oxidation was sulfate dependent.	naphthalene	13-24	phenylalanine hydroxylase	Homo sapiens	40-43
9204951-3	1997	This essential cofactor controls the production of L-tyrosine from L-phenylalanine via phenylalanine hydroxylase (PAH).	Tyrosine	51-61	phenylalanine hydroxylase	Homo sapiens	87-112
9204951-3	1997	This essential cofactor controls the production of L-tyrosine from L-phenylalanine via phenylalanine hydroxylase (PAH).	Phenylalanine	67-82	phenylalanine hydroxylase	Homo sapiens	87-112
9290252-4	1997	Decreased mineralization of [14C]-phenanthrene and [14C]-pyrene was usually due to either preferential use of the supplement as carbon source and/or stimulation of non-PAH degrading microorganisms.	[14c]-phenanthrene	28-46	phenylalanine hydroxylase	Homo sapiens	168-171
9290252-4	1997	Decreased mineralization of [14C]-phenanthrene and [14C]-pyrene was usually due to either preferential use of the supplement as carbon source and/or stimulation of non-PAH degrading microorganisms.	[14c]-pyrene	51-63	phenylalanine hydroxylase	Homo sapiens	168-171
15093403-5	1997	In addition, a smaller particle has a higher specific surface area and therefore may contain more organic carbon, which allows for more PAH adsorption.	Carbon	106-112	phenylalanine hydroxylase	Homo sapiens	136-139
9022714-9	1996	The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH.	Phenylalanine	145-150	phenylalanine hydroxylase	Homo sapiens	36-40
9222757-1	1997	6-Pyruvoyl-tetrahydrobiopterin synthase (PTPS) is involved in tetrahydrobiopterin (BH4) biosynthesis, the cofactor for various enzymes including the hepatic phenylalanine hydroxylase.	sapropterin	11-30	phenylalanine hydroxylase	Homo sapiens	157-182
9222757-1	1997	6-Pyruvoyl-tetrahydrobiopterin synthase (PTPS) is involved in tetrahydrobiopterin (BH4) biosynthesis, the cofactor for various enzymes including the hepatic phenylalanine hydroxylase.	sapropterin	83-86	phenylalanine hydroxylase	Homo sapiens	157-182
9022714-4	1996	The deletion mutants lacking the carboxy-terminal 24 amino acids hPAH (Ser2-Gln428) and hPAH(Gly103-Gln428) formed catalytically active dimers, and incubation with L-Phe did not promote the formation of tetramers, a characteristic property of dimeric wt-hPAH.	Phenylalanine	164-169	phenylalanine hydroxylase	Homo sapiens	65-69
9022714-9	1996	The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH.	Phenylalanine	145-150	phenylalanine hydroxylase	Homo sapiens	60-64
9022714-4	1996	The deletion mutants lacking the carboxy-terminal 24 amino acids hPAH (Ser2-Gln428) and hPAH(Gly103-Gln428) formed catalytically active dimers, and incubation with L-Phe did not promote the formation of tetramers, a characteristic property of dimeric wt-hPAH.	Phenylalanine	164-169	phenylalanine hydroxylase	Homo sapiens	88-92
9022714-9	1996	The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH.	Phenylalanine	145-150	phenylalanine hydroxylase	Homo sapiens	60-64
9022714-4	1996	The deletion mutants lacking the carboxy-terminal 24 amino acids hPAH (Ser2-Gln428) and hPAH(Gly103-Gln428) formed catalytically active dimers, and incubation with L-Phe did not promote the formation of tetramers, a characteristic property of dimeric wt-hPAH.	Phenylalanine	164-169	phenylalanine hydroxylase	Homo sapiens	88-92
9022714-9	1996	The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH.	Tryptophan	176-186	phenylalanine hydroxylase	Homo sapiens	36-40
9022714-6	1996	The deletion mutants hPAH(Asp112-Lys452), hPAH(Ser2-Gln428) and hPAH(Gly103-Gln428) were all activated by prior incubation with L-Phe, but did not reveal any positive cooperativity of substrate binding (h = 1.0).	Phenylalanine	128-133	phenylalanine hydroxylase	Homo sapiens	21-25
9022714-6	1996	The deletion mutants hPAH(Asp112-Lys452), hPAH(Ser2-Gln428) and hPAH(Gly103-Gln428) were all activated by prior incubation with L-Phe, but did not reveal any positive cooperativity of substrate binding (h = 1.0).	Phenylalanine	128-133	phenylalanine hydroxylase	Homo sapiens	42-46
9022714-9	1996	The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH.	Tryptophan	176-186	phenylalanine hydroxylase	Homo sapiens	60-64
9022714-6	1996	The deletion mutants hPAH(Asp112-Lys452), hPAH(Ser2-Gln428) and hPAH(Gly103-Gln428) were all activated by prior incubation with L-Phe, but did not reveal any positive cooperativity of substrate binding (h = 1.0).	Phenylalanine	128-133	phenylalanine hydroxylase	Homo sapiens	42-46
9022714-9	1996	The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH.	Tryptophan	176-186	phenylalanine hydroxylase	Homo sapiens	60-64
9022714-9	1996	The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH.	Phenylalanine	241-246	phenylalanine hydroxylase	Homo sapiens	36-40
9022714-9	1996	The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH.	Phenylalanine	241-246	phenylalanine hydroxylase	Homo sapiens	60-64
9022714-9	1996	The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH.	Phenylalanine	241-246	phenylalanine hydroxylase	Homo sapiens	60-64
9022714-10	1996	Moreover, prior incubation of the enzyme forms with lysophosphatidylcholine, a commonly used activator of the PAH, only increased the activity of those forms containing the wt-hPAH amino-terminal sequence.	Lysophosphatidylcholines	52-75	phenylalanine hydroxylase	Homo sapiens	110-113
9022714-10	1996	Moreover, prior incubation of the enzyme forms with lysophosphatidylcholine, a commonly used activator of the PAH, only increased the activity of those forms containing the wt-hPAH amino-terminal sequence.	Lysophosphatidylcholines	52-75	phenylalanine hydroxylase	Homo sapiens	176-180
9022714-11	1996	Our results are compatible with a model in which incubation of wt-hPAH with L-Phe induces both a conformational change (with cooperativity in the tetrameric enzyme) which relieves the inhibition imposed by the amino-terminal domain to the high-affinity binding of L-Phe, and an additional activation, as observed for the truncated forms lacking the amino-terminal.	Phenylalanine	76-81	phenylalanine hydroxylase	Homo sapiens	66-70
9022714-11	1996	Our results are compatible with a model in which incubation of wt-hPAH with L-Phe induces both a conformational change (with cooperativity in the tetrameric enzyme) which relieves the inhibition imposed by the amino-terminal domain to the high-affinity binding of L-Phe, and an additional activation, as observed for the truncated forms lacking the amino-terminal.	Phenylalanine	264-269	phenylalanine hydroxylase	Homo sapiens	66-70
8921003-1	1996	Mammalian phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine to L-tyrosine in the presence of dioxygen and tetrahydrobiopterin; it is a highly regulated enzyme.	Phenylalanine	70-85	phenylalanine hydroxylase	Homo sapiens	10-35
8828600-4	1996	This paper gives a summary of the effect of each type of mutation on PAH activity and illustrates how the combination of mutations (the genotype) is associated with the Phe tolerance (the metabolic phenotype).	Phenylalanine	169-172	phenylalanine hydroxylase	Homo sapiens	69-72
8921003-1	1996	Mammalian phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine to L-tyrosine in the presence of dioxygen and tetrahydrobiopterin; it is a highly regulated enzyme.	Phenylalanine	70-85	phenylalanine hydroxylase	Homo sapiens	37-40
8921003-1	1996	Mammalian phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine to L-tyrosine in the presence of dioxygen and tetrahydrobiopterin; it is a highly regulated enzyme.	Tyrosine	89-99	phenylalanine hydroxylase	Homo sapiens	10-35
8921003-1	1996	Mammalian phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine to L-tyrosine in the presence of dioxygen and tetrahydrobiopterin; it is a highly regulated enzyme.	Tyrosine	89-99	phenylalanine hydroxylase	Homo sapiens	37-40
8921003-1	1996	Mammalian phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine to L-tyrosine in the presence of dioxygen and tetrahydrobiopterin; it is a highly regulated enzyme.	Oxygen	119-127	phenylalanine hydroxylase	Homo sapiens	10-35
8921003-1	1996	Mammalian phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine to L-tyrosine in the presence of dioxygen and tetrahydrobiopterin; it is a highly regulated enzyme.	Oxygen	119-127	phenylalanine hydroxylase	Homo sapiens	37-40
8921003-1	1996	Mammalian phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine to L-tyrosine in the presence of dioxygen and tetrahydrobiopterin; it is a highly regulated enzyme.	sapropterin	132-151	phenylalanine hydroxylase	Homo sapiens	10-35
8921003-1	1996	Mammalian phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine to L-tyrosine in the presence of dioxygen and tetrahydrobiopterin; it is a highly regulated enzyme.	sapropterin	132-151	phenylalanine hydroxylase	Homo sapiens	37-40
8933030-5	1996	Studies are presented that demonstrate that high ambient levels of benzo[a]pyrene are associated with high levels of DNA adducts in human blood cell DNA and that the same DNA adduct levels drop when the ambient PAH levels decrease significantly.	Benzo(a)pyrene	67-81	phenylalanine hydroxylase	Homo sapiens	211-214
8906465-1	1996	Tetrahydrobiopterin is a cofactor in hydroxylation reactions, including phenylalanine 4-monooxygenase, tyrosine 3-monooxygenase, tryptophan 5-monooxygenase, alkyl glycol ether monooxygenase and nitric oxide synthase.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	72-101
8682503-5	1996	Since BH4 deficiency could not be excluded in any of these patients, the latter results may be explained by the occurrence of mutations affecting the genes controlling the synthesis and recycling of tetrahydrobiopterin: the cofactor of PAH.	sapropterin	199-218	phenylalanine hydroxylase	Homo sapiens	236-239
9275410-2	1996	METHODS: The single strand conformation polymorphism (SSCP) combined with silver staining technique were used to screen the mutations in the four exons of phenylalanine hydroxylase (PAH) gene.	Silver	74-80	phenylalanine hydroxylase	Homo sapiens	155-180
9275410-2	1996	METHODS: The single strand conformation polymorphism (SSCP) combined with silver staining technique were used to screen the mutations in the four exons of phenylalanine hydroxylase (PAH) gene.	Silver	74-80	phenylalanine hydroxylase	Homo sapiens	182-185
8694494-2	1996	The aim of this study was to evaluate the suitability of urinary 1-hydroxypyrene to characterize respiratory exposure to PAH, which is most relevant for assessing individual health risks.	1-hydroxypyrene	65-80	phenylalanine hydroxylase	Homo sapiens	121-124
8694494-9	1996	The results presented in this investigation indicate that biological monitoring of the pyrene metabolite 1-hydroxypyrene is a useful indicator of a general PAH exposure, but cannot replace personal air sampling for assessing the lung cancer risk of individuals.	pyrene	87-93	phenylalanine hydroxylase	Homo sapiens	156-159
8694494-9	1996	The results presented in this investigation indicate that biological monitoring of the pyrene metabolite 1-hydroxypyrene is a useful indicator of a general PAH exposure, but cannot replace personal air sampling for assessing the lung cancer risk of individuals.	1-hydroxypyrene	105-120	phenylalanine hydroxylase	Homo sapiens	156-159
16535261-2	1996	Sulfate reduction was necessary for PAH oxidation.	Sulfates	0-7	phenylalanine hydroxylase	Homo sapiens	36-39
8632937-9	1996	Strong correlations were observed between the level of PAH activity predicted from the genotype, when known from previous in vitro expression studies of the mutant proteins, and pretreatment serum PHE levels (r = .841) or clinical severity (Kendall rank-order correlation coefficient, .936).	Phenylalanine	197-200	phenylalanine hydroxylase	Homo sapiens	55-58
16535261-3	1996	These results suggest that the self-purification capacity of PAH-contaminated sulfate-reducing environments may be greater than previously recognized.	Sulfates	78-85	phenylalanine hydroxylase	Homo sapiens	61-64
21619081-7	1996	For the five biphasic solvent systems studied, linear relationships were found between the partition coefficients and the sp(3) and sp(2) hybridized carbon atom number for the alkylbenzene and PAH series, respectively.	sp(3)	122-127	phenylalanine hydroxylase	Homo sapiens	193-196
21619081-7	1996	For the five biphasic solvent systems studied, linear relationships were found between the partition coefficients and the sp(3) and sp(2) hybridized carbon atom number for the alkylbenzene and PAH series, respectively.	sp(2)	132-137	phenylalanine hydroxylase	Homo sapiens	193-196
21619081-7	1996	For the five biphasic solvent systems studied, linear relationships were found between the partition coefficients and the sp(3) and sp(2) hybridized carbon atom number for the alkylbenzene and PAH series, respectively.	Carbon	149-155	phenylalanine hydroxylase	Homo sapiens	193-196
8570624-7	1996	The hPAH-AR mice will serve as a valuable model for studying the sex- and age-invariant expression of liver-specific genes, particularly those involved in the activation of environmental hepatocarcinogens such as the aromatic hydrocarbons.	Hydrocarbons	226-238	phenylalanine hydroxylase	Homo sapiens	4-8
8967723-3	1996	Exposure to aromatic amines in dyestuff manufacture, in the rubber and textile industry, occupations entailing exposure to paints and solvents, leather dust, inks, some metals, PAH, combustion products and diesel exhausts have been identified as risk factors from epidemiological studies.	aromatic amines	12-27	phenylalanine hydroxylase	Homo sapiens	177-180
8573072-3	1996	The fusion protein and human phenylalanine hydroxylase were both phosphorylated at Ser-16 with a stoichiometry of 1 mol of Pi/mol of subunit.	Serine	83-86	phenylalanine hydroxylase	Homo sapiens	29-54
8573072-4	1996	The rate of phosphorylation of human phenylalanine hydroxylase was inhibited about 40% by the cofactor tetrahydrobiopterin, and this inhibition was completely prevented by the simultaneous presence of L-phenylalanine (i.e. at turnover conditions).	sapropterin	103-122	phenylalanine hydroxylase	Homo sapiens	37-62
8573072-4	1996	The rate of phosphorylation of human phenylalanine hydroxylase was inhibited about 40% by the cofactor tetrahydrobiopterin, and this inhibition was completely prevented by the simultaneous presence of L-phenylalanine (i.e. at turnover conditions).	Phenylalanine	201-216	phenylalanine hydroxylase	Homo sapiens	37-62
8573072-6	1996	Pre-incubation with L-Phe increased the specific activity of phenylalanine hydroxylase 2- to 4-fold, L-Phe acting with positive cooperativity.	Phenylalanine	20-25	phenylalanine hydroxylase	Homo sapiens	61-86
8573072-6	1996	Pre-incubation with L-Phe increased the specific activity of phenylalanine hydroxylase 2- to 4-fold, L-Phe acting with positive cooperativity.	Phenylalanine	101-106	phenylalanine hydroxylase	Homo sapiens	61-86
8573072-8	1996	When the target sequence of the restriction protease factor Xa (Ile-Glu-Gly-Arg) was used as the linker between maltose-binding protein and human phenylalanine hydroxylase, cleavage of the fusion protein gave a mixture of full-length hydroxylase and a truncated form of the enzyme lacking the 13 N-terminal residues.	Isoleucine	64-68	phenylalanine hydroxylase	Homo sapiens	146-171
8573072-8	1996	When the target sequence of the restriction protease factor Xa (Ile-Glu-Gly-Arg) was used as the linker between maltose-binding protein and human phenylalanine hydroxylase, cleavage of the fusion protein gave a mixture of full-length hydroxylase and a truncated form of the enzyme lacking the 13 N-terminal residues.	Glu-Gly-Arg	68-79	phenylalanine hydroxylase	Homo sapiens	146-171
8573072-8	1996	When the target sequence of the restriction protease factor Xa (Ile-Glu-Gly-Arg) was used as the linker between maltose-binding protein and human phenylalanine hydroxylase, cleavage of the fusion protein gave a mixture of full-length hydroxylase and a truncated form of the enzyme lacking the 13 N-terminal residues.	Maltose	112-119	phenylalanine hydroxylase	Homo sapiens	146-171
15048450-2	1996	This sensor has been used for the simultaneous determination of PAH mixtures (pyrene, benzo(e)pyrene and benzo(ghi)perylene).	pyrene	78-84	phenylalanine hydroxylase	Homo sapiens	64-67
15048450-2	1996	This sensor has been used for the simultaneous determination of PAH mixtures (pyrene, benzo(e)pyrene and benzo(ghi)perylene).	benzo(e)pyrene	86-100	phenylalanine hydroxylase	Homo sapiens	64-67
15048450-2	1996	This sensor has been used for the simultaneous determination of PAH mixtures (pyrene, benzo(e)pyrene and benzo(ghi)perylene).	1,12-benzoperylene	105-123	phenylalanine hydroxylase	Homo sapiens	64-67
21619230-10	1996	Good agreement was obtained between a 45-min SPME and methylene chloride extraction for the determination of PAH concentrations in creosote-contaminated water, demonstrating that SPME is a useful technique for the rapid determination of hydrocarbons in complex water matrices.	Methylene Chloride	54-72	phenylalanine hydroxylase	Homo sapiens	109-112
8946176-1	1996	Phenylalanine hydroxylase (PAH) is the enzyme which converts phenylalanine into tyrosine.	Phenylalanine	61-74	phenylalanine hydroxylase	Homo sapiens	0-25
21619230-10	1996	Good agreement was obtained between a 45-min SPME and methylene chloride extraction for the determination of PAH concentrations in creosote-contaminated water, demonstrating that SPME is a useful technique for the rapid determination of hydrocarbons in complex water matrices.	Creosote	131-139	phenylalanine hydroxylase	Homo sapiens	109-112
21619230-10	1996	Good agreement was obtained between a 45-min SPME and methylene chloride extraction for the determination of PAH concentrations in creosote-contaminated water, demonstrating that SPME is a useful technique for the rapid determination of hydrocarbons in complex water matrices.	Water	153-158	phenylalanine hydroxylase	Homo sapiens	109-112
21619230-10	1996	Good agreement was obtained between a 45-min SPME and methylene chloride extraction for the determination of PAH concentrations in creosote-contaminated water, demonstrating that SPME is a useful technique for the rapid determination of hydrocarbons in complex water matrices.	Hydrocarbons	237-249	phenylalanine hydroxylase	Homo sapiens	109-112
8946176-1	1996	Phenylalanine hydroxylase (PAH) is the enzyme which converts phenylalanine into tyrosine.	Phenylalanine	61-74	phenylalanine hydroxylase	Homo sapiens	27-30
8946176-1	1996	Phenylalanine hydroxylase (PAH) is the enzyme which converts phenylalanine into tyrosine.	Tyrosine	80-88	phenylalanine hydroxylase	Homo sapiens	0-25
8946176-1	1996	Phenylalanine hydroxylase (PAH) is the enzyme which converts phenylalanine into tyrosine.	Tyrosine	80-88	phenylalanine hydroxylase	Homo sapiens	27-30
8892014-4	1996	We report two siblings of different sex and identical genotype at the PAH locus who demonstrate a difference in phenylalanine disposal.	Phenylalanine	112-125	phenylalanine hydroxylase	Homo sapiens	70-73
8834591-2	1996	A number of industrial processes such as coke production, coal tar processing, production of electric energy and certain rubber goods as well as metallurgy, especially aluminium metallurgy with its anodes made of coal tar pitch are the major sources of PAH emission.	Aluminum	168-177	phenylalanine hydroxylase	Homo sapiens	253-256
8834591-3	1996	An attempt was made to determine PAH concentrations at selected workposts at an aluminium production plant.	Aluminum	80-89	phenylalanine hydroxylase	Homo sapiens	33-36
8950848-1	1996	An A/C polymorphism was identified at nucleotide-11 from the acceptor site of IVS3 of the phenylalanine hydroxylase gene.	nucleotide-11	38-51	phenylalanine hydroxylase	Homo sapiens	90-115
7547912-0	1995	Tryptophan fluorescence of human phenylalanine hydroxylase produced in Escherichia coli.	Tryptophan	0-10	phenylalanine hydroxylase	Homo sapiens	33-58
33867678-6	1995	To date, lifetime probes for analyte recognition (binding) have been identified for Ca 2+, Mg 2 +, K + and pH.	Magnesium	91-93	phenylalanine hydroxylase	Homo sapiens	107-109
7547912-8	1995	After incubation with phenylalanine, the quantum yield of wild-type hPAH increases by 15%, and the emission maximum is shifted from 336.5 to 347 nm.	Phenylalanine	22-35	phenylalanine hydroxylase	Homo sapiens	68-72
7547912-1	1995	Human phenylalanine hydroxylase (hPAH) contains three tryptophan residues (W120, W187, and W326).	Tryptophan	54-64	phenylalanine hydroxylase	Homo sapiens	6-31
7547912-1	1995	Human phenylalanine hydroxylase (hPAH) contains three tryptophan residues (W120, W187, and W326).	Tryptophan	54-64	phenylalanine hydroxylase	Homo sapiens	33-37
7547912-7	1995	On the basis of measurements of mutants containing only one tryptophan, it was calculated that W120, W187, and W326 account for approximately 61, 13, and 26% of the total tryptophan fluorescence of hPAH, respectively, while the positions of the emission maxima (335.5-336.5 nm) and the widths at half-height (55-60 nm) of the emission spectra of the individual tryptophans were rather similar.	Tryptophan	60-70	phenylalanine hydroxylase	Homo sapiens	198-202
7547912-7	1995	On the basis of measurements of mutants containing only one tryptophan, it was calculated that W120, W187, and W326 account for approximately 61, 13, and 26% of the total tryptophan fluorescence of hPAH, respectively, while the positions of the emission maxima (335.5-336.5 nm) and the widths at half-height (55-60 nm) of the emission spectra of the individual tryptophans were rather similar.	Tryptophan	171-181	phenylalanine hydroxylase	Homo sapiens	198-202
7547912-7	1995	On the basis of measurements of mutants containing only one tryptophan, it was calculated that W120, W187, and W326 account for approximately 61, 13, and 26% of the total tryptophan fluorescence of hPAH, respectively, while the positions of the emission maxima (335.5-336.5 nm) and the widths at half-height (55-60 nm) of the emission spectra of the individual tryptophans were rather similar.	Tryptophan	361-372	phenylalanine hydroxylase	Homo sapiens	198-202
11540308-10	1995	The synthesis of laboratory analogs of meteoritic hydrocarbons through plasma hydrogenation of PAH species is underway, as is chemical analysis of those analogs.	Hydrocarbons	50-62	phenylalanine hydroxylase	Homo sapiens	95-98
7657610-5	1995	The 3" region of the phenylalanine hydroxylase intron 10 has two unusual characteristic features: multiple potential branch sites and a series of four guanosine residues, which interrupt the polypyrimidine tract at positions -8 to -11 from the 3" splice site.	Guanosine	151-160	phenylalanine hydroxylase	Homo sapiens	21-46
7657610-5	1995	The 3" region of the phenylalanine hydroxylase intron 10 has two unusual characteristic features: multiple potential branch sites and a series of four guanosine residues, which interrupt the polypyrimidine tract at positions -8 to -11 from the 3" splice site.	polypyrimidine	191-205	phenylalanine hydroxylase	Homo sapiens	21-46
7762520-0	1995	Phenylalanine hydroxylase activity in preterm infants: is tyrosine a conditionally essential amino acid?	tyrosine a	58-68	phenylalanine hydroxylase	Homo sapiens	0-25
7762520-0	1995	Phenylalanine hydroxylase activity in preterm infants: is tyrosine a conditionally essential amino acid?	Amino Acids, Essential	83-103	phenylalanine hydroxylase	Homo sapiens	0-25
7762520-1	1995	To assess the production of the nonessential amino acid tyrosine in preterm infants, we estimated the activity of phenylalanine hydroxylase (PAH) in three groups of infants by measuring the conversion of phenylalanine to tyrosine, using a model based on a primed constant 200-min intravenous infusion of [2H5]phenylalanine.	Tyrosine	56-64	phenylalanine hydroxylase	Homo sapiens	114-139
7762520-1	1995	To assess the production of the nonessential amino acid tyrosine in preterm infants, we estimated the activity of phenylalanine hydroxylase (PAH) in three groups of infants by measuring the conversion of phenylalanine to tyrosine, using a model based on a primed constant 200-min intravenous infusion of [2H5]phenylalanine.	Tyrosine	56-64	phenylalanine hydroxylase	Homo sapiens	141-144
7762520-1	1995	To assess the production of the nonessential amino acid tyrosine in preterm infants, we estimated the activity of phenylalanine hydroxylase (PAH) in three groups of infants by measuring the conversion of phenylalanine to tyrosine, using a model based on a primed constant 200-min intravenous infusion of [2H5]phenylalanine.	Phenylalanine	114-127	phenylalanine hydroxylase	Homo sapiens	141-144
7762520-1	1995	To assess the production of the nonessential amino acid tyrosine in preterm infants, we estimated the activity of phenylalanine hydroxylase (PAH) in three groups of infants by measuring the conversion of phenylalanine to tyrosine, using a model based on a primed constant 200-min intravenous infusion of [2H5]phenylalanine.	Tyrosine	221-229	phenylalanine hydroxylase	Homo sapiens	114-139
7762520-1	1995	To assess the production of the nonessential amino acid tyrosine in preterm infants, we estimated the activity of phenylalanine hydroxylase (PAH) in three groups of infants by measuring the conversion of phenylalanine to tyrosine, using a model based on a primed constant 200-min intravenous infusion of [2H5]phenylalanine.	Tyrosine	221-229	phenylalanine hydroxylase	Homo sapiens	141-144
7762520-1	1995	To assess the production of the nonessential amino acid tyrosine in preterm infants, we estimated the activity of phenylalanine hydroxylase (PAH) in three groups of infants by measuring the conversion of phenylalanine to tyrosine, using a model based on a primed constant 200-min intravenous infusion of [2H5]phenylalanine.	[2h5]phenylalanine	304-322	phenylalanine hydroxylase	Homo sapiens	114-139
7762520-1	1995	To assess the production of the nonessential amino acid tyrosine in preterm infants, we estimated the activity of phenylalanine hydroxylase (PAH) in three groups of infants by measuring the conversion of phenylalanine to tyrosine, using a model based on a primed constant 200-min intravenous infusion of [2H5]phenylalanine.	[2h5]phenylalanine	304-322	phenylalanine hydroxylase	Homo sapiens	141-144
7762520-9	1995	Provision of phenylalanine in the context of parenteral amino acid nutrition solution accelerated PAH conversion of phenylalanine to tyrosine, suggesting that the enzyme system is capable of responding normally to provision of substrate.	Phenylalanine	13-26	phenylalanine hydroxylase	Homo sapiens	98-101
7762520-9	1995	Provision of phenylalanine in the context of parenteral amino acid nutrition solution accelerated PAH conversion of phenylalanine to tyrosine, suggesting that the enzyme system is capable of responding normally to provision of substrate.	Phenylalanine	116-129	phenylalanine hydroxylase	Homo sapiens	98-101
7762520-9	1995	Provision of phenylalanine in the context of parenteral amino acid nutrition solution accelerated PAH conversion of phenylalanine to tyrosine, suggesting that the enzyme system is capable of responding normally to provision of substrate.	Tyrosine	133-141	phenylalanine hydroxylase	Homo sapiens	98-101
7887915-6	1995	By contrast, when expressed as a fusion protein in the pMAL system, hPAH was resistant to cleavage by host cell proteases and was conveniently purified by affinity chromatography on an amylose resin.	Amylose	185-192	phenylalanine hydroxylase	Homo sapiens	68-72
7887915-8	1995	After cleavage by restriction protease, factor Xa or enterokinase, hPAH was separated from uncleaved fusion protein, MBP and restriction proteases by hydroxylapatite or ion-exchange (DEAE) chromatography.	Durapatite	150-165	phenylalanine hydroxylase	Homo sapiens	67-71
7887915-8	1995	After cleavage by restriction protease, factor Xa or enterokinase, hPAH was separated from uncleaved fusion protein, MBP and restriction proteases by hydroxylapatite or ion-exchange (DEAE) chromatography.	2-diethylaminoethanol	183-187	phenylalanine hydroxylase	Homo sapiens	67-71
7716499-0	1995	The elimination of 1-hydroxypyrene in the urine of the general population and workers with different occupational exposures to PAH.	1-hydroxypyrene	19-34	phenylalanine hydroxylase	Homo sapiens	127-130
7550799-3	1995	Measurement of PAH metabolites in human urine provides a means of assessing individual internal dose of PAHs.	Polycyclic Aromatic Hydrocarbons	104-108	phenylalanine hydroxylase	Homo sapiens	15-18
7550799-7	1995	Urinary 1-OHPG was measured by synchronous fluorescence spectroscopy after immunoaffinity chromatography specific for PAH metabolites.	1-ohpg	8-14	phenylalanine hydroxylase	Homo sapiens	118-121
7550799-13	1995	CONCLUSIONS: These results indicate that 1-OHPG is a common urinary metabolite in people with recent occupational exposure to PAHs and is associated with both job category and estimated stratum of PAH exposure.	1-ohpg	41-47	phenylalanine hydroxylase	Homo sapiens	126-129
7600314-1	1995	There is a polymorphic tetranucleotide short tandem repeats (STR) sequence in the intron 3 of the phenylalanine hydroxylase (PAH) gene.	tetranucleotide	23-38	phenylalanine hydroxylase	Homo sapiens	98-123
7600314-1	1995	There is a polymorphic tetranucleotide short tandem repeats (STR) sequence in the intron 3 of the phenylalanine hydroxylase (PAH) gene.	tetranucleotide	23-38	phenylalanine hydroxylase	Homo sapiens	125-128
7766948-4	1994	In contrast, infusion of a recombinant adenoviral vector expressing the human PAH cDNA into the portal circulation of PAH-deficient mice restores 10-80% of normal hepatic PAH activity and completely normalizes serum phenylalanine levels.	Phenylalanine	216-229	phenylalanine hydroxylase	Homo sapiens	78-81
7766948-4	1994	In contrast, infusion of a recombinant adenoviral vector expressing the human PAH cDNA into the portal circulation of PAH-deficient mice restores 10-80% of normal hepatic PAH activity and completely normalizes serum phenylalanine levels.	Phenylalanine	216-229	phenylalanine hydroxylase	Homo sapiens	118-121
8001258-2	1994	These molecules are polycyclic aromatic hydrocarbons (PAHs) that have, respectively, two hindered bay regions and two fjord regions; the former PAH is a known carcinogen.	Polycyclic Aromatic Hydrocarbons	20-52	phenylalanine hydroxylase	Homo sapiens	54-57
8502995-1	1993	Guanosine triphosphate (GTP) cyclohydrolase I, the rate-limiting enzyme in the biosynthesis of tetrahydrobiopterin (BH4), is subject to feedback inhibition by BH4, a cofactor for phenylalanine hydroxylase.	sapropterin	116-119	phenylalanine hydroxylase	Homo sapiens	179-204
7978233-5	1994	Both D- and L-phenylalanine are attacked by OH., although only the latter is a substrate for the enzyme phenylalanine hydroxylase.	d- and l-phenylalanine	5-27	phenylalanine hydroxylase	Homo sapiens	104-129
8048786-4	1994	Biological monitoring was undertaken to measure the effect of the extra hygienic measures on the urinary 1-hydroxypyrene excretion, which is a measure of the internal PAH exposure.	1-hydroxypyrene	105-120	phenylalanine hydroxylase	Homo sapiens	167-170
8204666-6	1994	In the epidermis and in cultured melanocytes, 7-BH4 is a potent competitive inhibitor of phenylalanine hydroxylase (Ki = 10(-6) M) and its accumulation in the epidermis of patients with vitiligo blocks the supply of L-tyrosine from L-phenylalanine.	2-amino-4-hydroxy-7-(dihydroxypropyl)-5,6,7,8-tetrahydrobiopterin	46-51	phenylalanine hydroxylase	Homo sapiens	89-114
7514214-9	1994	The first group was treated pre- and postnatally with Phe and alpha-methylphenylalanine (a phenylalanine hydroxylase inhibitor).	alpha-methylphenylalanine	62-87	phenylalanine hydroxylase	Homo sapiens	91-116
8188266-1	1994	Tetrahydrobiopterin (BH4) is the redox cofactor for the aromatic amino acid hydroxylases such as phenylalanine hydroxylase.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	97-122
8188266-1	1994	Tetrahydrobiopterin (BH4) is the redox cofactor for the aromatic amino acid hydroxylases such as phenylalanine hydroxylase.	sapropterin	21-24	phenylalanine hydroxylase	Homo sapiens	97-122
8296774-1	1994	The relation between aluminum, fluorine, calcium, and pH in drinking water and the risk for cognitive impairment was studied using data collected in 1988-1989 in a population-based survey of 3,777 French men and women aged 65 years and older (the Paquid study).	Water	69-74	phenylalanine hydroxylase	Homo sapiens	54-56
8352282-2	1993	They are most often caused by mutations in the phenylalanine hydroxylase gene and, less frequently but with usually more serious consequences, in genes necessary for the synthesis and regeneration of the cofactor, tetrahydrobiopterin.	sapropterin	214-233	phenylalanine hydroxylase	Homo sapiens	47-72
8352282-4	1993	Phenylalanine hydroxylase catalyzes a coupled reaction in which phenylalanine is converted to tyrosine and in which tetrahydrobiopterin is converted to the unstable carbinolamine, 4a-hydroxytetrahydrobiopterin.	Phenylalanine	64-77	phenylalanine hydroxylase	Homo sapiens	0-25
8352282-4	1993	Phenylalanine hydroxylase catalyzes a coupled reaction in which phenylalanine is converted to tyrosine and in which tetrahydrobiopterin is converted to the unstable carbinolamine, 4a-hydroxytetrahydrobiopterin.	Tyrosine	94-102	phenylalanine hydroxylase	Homo sapiens	0-25
8352282-4	1993	Phenylalanine hydroxylase catalyzes a coupled reaction in which phenylalanine is converted to tyrosine and in which tetrahydrobiopterin is converted to the unstable carbinolamine, 4a-hydroxytetrahydrobiopterin.	sapropterin	116-135	phenylalanine hydroxylase	Homo sapiens	0-25
8352282-4	1993	Phenylalanine hydroxylase catalyzes a coupled reaction in which phenylalanine is converted to tyrosine and in which tetrahydrobiopterin is converted to the unstable carbinolamine, 4a-hydroxytetrahydrobiopterin.	Aminomethanol	165-178	phenylalanine hydroxylase	Homo sapiens	0-25
8352282-4	1993	Phenylalanine hydroxylase catalyzes a coupled reaction in which phenylalanine is converted to tyrosine and in which tetrahydrobiopterin is converted to the unstable carbinolamine, 4a-hydroxytetrahydrobiopterin.	4a-hydroxytetrahydrobiopterin	180-209	phenylalanine hydroxylase	Homo sapiens	0-25
8379619-11	1993	Significant concentrations of PAH up to 269 micrograms PAH m-3 (4 micrograms BaP m-3) occurred during ignition of the cupola furnace.	benzylaminopurine	77-80	phenylalanine hydroxylase	Homo sapiens	30-33
8379619-11	1993	Significant concentrations of PAH up to 269 micrograms PAH m-3 (4 micrograms BaP m-3) occurred during ignition of the cupola furnace.	benzylaminopurine	77-80	phenylalanine hydroxylase	Homo sapiens	55-58
7687023-3	1993	On the basis of PAH levels in the work environment and hydroxypyrene concentrations in the urine, the workers from the graphite electrode producing plant were the most exposed.	Graphite	119-127	phenylalanine hydroxylase	Homo sapiens	16-19
7844888-3	1994	Direct sequencing was conducted on the regions of the exon 7 and 12 in the phenylalanine hydroxylase (PAH) gene amplified by the polymerase chain reaction, using solid-phase technology involving the biotin streptavidin system.	Biotin	199-205	phenylalanine hydroxylase	Homo sapiens	75-100
7844888-3	1994	Direct sequencing was conducted on the regions of the exon 7 and 12 in the phenylalanine hydroxylase (PAH) gene amplified by the polymerase chain reaction, using solid-phase technology involving the biotin streptavidin system.	Biotin	199-205	phenylalanine hydroxylase	Homo sapiens	102-105
8178819-1	1994	A variant type of hyperphenylalaninemia is caused by a deficiency of tetrahydrobiopterin (BH4), the obligatory cofactor for phenylalanine hydroxylase.	sapropterin	69-88	phenylalanine hydroxylase	Homo sapiens	124-149
8178819-1	1994	A variant type of hyperphenylalaninemia is caused by a deficiency of tetrahydrobiopterin (BH4), the obligatory cofactor for phenylalanine hydroxylase.	sapropterin	90-93	phenylalanine hydroxylase	Homo sapiens	124-149
8132651-1	1994	Human phenylalanine hydroxylase (PAH) is specifically expressed in the liver to convert L-phenylalanine to L-tyrosine.	Phenylalanine	88-103	phenylalanine hydroxylase	Homo sapiens	6-31
8132651-1	1994	Human phenylalanine hydroxylase (PAH) is specifically expressed in the liver to convert L-phenylalanine to L-tyrosine.	Phenylalanine	88-103	phenylalanine hydroxylase	Homo sapiens	33-36
8132651-1	1994	Human phenylalanine hydroxylase (PAH) is specifically expressed in the liver to convert L-phenylalanine to L-tyrosine.	Tyrosine	107-117	phenylalanine hydroxylase	Homo sapiens	6-31
8132651-1	1994	Human phenylalanine hydroxylase (PAH) is specifically expressed in the liver to convert L-phenylalanine to L-tyrosine.	Tyrosine	107-117	phenylalanine hydroxylase	Homo sapiens	33-36
8128228-4	1994	This by-product is a potent competitive inhibitor in the phenylalanine hydroxylase reaction with an inhibition constant of 10(-6) M. Thus, 6-BH4 seems to control melanin biosynthesis in the human epidermis, whereas 7-BH4 may initiate depigmentation in patients with vitiligo.	6-bh4	139-144	phenylalanine hydroxylase	Homo sapiens	57-82
8128228-4	1994	This by-product is a potent competitive inhibitor in the phenylalanine hydroxylase reaction with an inhibition constant of 10(-6) M. Thus, 6-BH4 seems to control melanin biosynthesis in the human epidermis, whereas 7-BH4 may initiate depigmentation in patients with vitiligo.	Melanins	162-169	phenylalanine hydroxylase	Homo sapiens	57-82
8128228-4	1994	This by-product is a potent competitive inhibitor in the phenylalanine hydroxylase reaction with an inhibition constant of 10(-6) M. Thus, 6-BH4 seems to control melanin biosynthesis in the human epidermis, whereas 7-BH4 may initiate depigmentation in patients with vitiligo.	2-amino-4-hydroxy-7-(dihydroxypropyl)-5,6,7,8-tetrahydrobiopterin	215-220	phenylalanine hydroxylase	Homo sapiens	57-82
8108417-4	1994	The P. aeruginosa PhhA appears to contain iron and is pterin dependent.	Iron	42-46	phenylalanine hydroxylase	Homo sapiens	18-22
8108417-4	1994	The P. aeruginosa PhhA appears to contain iron and is pterin dependent.	Pterins	54-60	phenylalanine hydroxylase	Homo sapiens	18-22
8108417-7	1994	Expression of PhhA from its native promoter required phhB.	phhb	53-57	phenylalanine hydroxylase	Homo sapiens	14-18
7967476-1	1994	We examined whether the degree of residual activity from the mutant phenylalanine hydroxylase (PAH) allele affected phenylalanine metabolism in heterozygotes for phenylketonuria (PKU) or non-PKU hyperphenylalaninaemia (HPA).	Phenylalanine	68-81	phenylalanine hydroxylase	Homo sapiens	95-98
7967476-7	1994	Differences in the activities from the carried mutant PAH allele on phenylalanine metabolism in heterozygotes are, however, small compared to the activity from the normal PAH allele and are easily obscured by other factors leading to inter- or intra-individual variation in phenylalanine metabolism.	Phenylalanine	68-81	phenylalanine hydroxylase	Homo sapiens	54-57
7967476-7	1994	Differences in the activities from the carried mutant PAH allele on phenylalanine metabolism in heterozygotes are, however, small compared to the activity from the normal PAH allele and are easily obscured by other factors leading to inter- or intra-individual variation in phenylalanine metabolism.	Phenylalanine	68-81	phenylalanine hydroxylase	Homo sapiens	171-174
7967476-7	1994	Differences in the activities from the carried mutant PAH allele on phenylalanine metabolism in heterozygotes are, however, small compared to the activity from the normal PAH allele and are easily obscured by other factors leading to inter- or intra-individual variation in phenylalanine metabolism.	Phenylalanine	274-287	phenylalanine hydroxylase	Homo sapiens	54-57
7967476-7	1994	Differences in the activities from the carried mutant PAH allele on phenylalanine metabolism in heterozygotes are, however, small compared to the activity from the normal PAH allele and are easily obscured by other factors leading to inter- or intra-individual variation in phenylalanine metabolism.	Phenylalanine	274-287	phenylalanine hydroxylase	Homo sapiens	171-174
8305846-3	1993	There is a partially overlapping substrate specificity between the PAH, dicarboxylate, and sulfate transport systems but also between the PAH and organic cation transport system.	malonic acid	72-85	phenylalanine hydroxylase	Homo sapiens	138-141
8305846-3	1993	There is a partially overlapping substrate specificity between the PAH, dicarboxylate, and sulfate transport systems but also between the PAH and organic cation transport system.	Sulfates	91-98	phenylalanine hydroxylase	Homo sapiens	67-70
8305846-3	1993	There is a partially overlapping substrate specificity between the PAH, dicarboxylate, and sulfate transport systems but also between the PAH and organic cation transport system.	Sulfates	91-98	phenylalanine hydroxylase	Homo sapiens	138-141
8502995-1	1993	Guanosine triphosphate (GTP) cyclohydrolase I, the rate-limiting enzyme in the biosynthesis of tetrahydrobiopterin (BH4), is subject to feedback inhibition by BH4, a cofactor for phenylalanine hydroxylase.	sapropterin	95-114	phenylalanine hydroxylase	Homo sapiens	179-204
8502995-1	1993	Guanosine triphosphate (GTP) cyclohydrolase I, the rate-limiting enzyme in the biosynthesis of tetrahydrobiopterin (BH4), is subject to feedback inhibition by BH4, a cofactor for phenylalanine hydroxylase.	sapropterin	159-162	phenylalanine hydroxylase	Homo sapiens	179-204
8098196-1	1993	The lysine residues at positions 194 and 198 in phenylalanine hydroxylase have been shown to react with a photoaffinity label which is an analog of phenyltetrahydropterin (Gibbs, B. S., and Benkovic, S. J.	Lysine	4-10	phenylalanine hydroxylase	Homo sapiens	48-73
8098196-1	1993	The lysine residues at positions 194 and 198 in phenylalanine hydroxylase have been shown to react with a photoaffinity label which is an analog of phenyltetrahydropterin (Gibbs, B. S., and Benkovic, S. J.	phenyltetrahydropterin	148-170	phenylalanine hydroxylase	Homo sapiens	48-73
8098196-3	1993	The related enzyme tyrosine hydroxylase has a lysine at position 241 which, given the 75% identity between its C-terminal 330 amino acids and those of phenylalanine hydroxylase, corresponds to lysine194 of phenylalanine hydroxylase.	Lysine	46-52	phenylalanine hydroxylase	Homo sapiens	151-176
8098196-3	1993	The related enzyme tyrosine hydroxylase has a lysine at position 241 which, given the 75% identity between its C-terminal 330 amino acids and those of phenylalanine hydroxylase, corresponds to lysine194 of phenylalanine hydroxylase.	Lysine	46-52	phenylalanine hydroxylase	Homo sapiens	206-231
8444221-8	1993	There was a strong relationship between the average in vitro PAH activity of the two mutant enzymes and both the phenylalanine tolerance and the neonatal pretreatment serum phenylalanine concentration.	Phenylalanine	113-126	phenylalanine hydroxylase	Homo sapiens	61-64
8319640-0	1993	Association of PAH-DNA adducts in peripheral white blood cells with dietary exposure to polyaromatic hydrocarbons.	polyaromatic hydrocarbons	88-113	phenylalanine hydroxylase	Homo sapiens	15-18
8319640-1	1993	Previous investigations suggest that dietary sources of polycyclic aromatic hydrocarbons (PAHs) contribute to the PAH-DNA adduct load in peripheral white blood cells (WBCs).	Polycyclic Aromatic Hydrocarbons	56-88	phenylalanine hydroxylase	Homo sapiens	90-93
8319662-5	1993	We analyzed WBC DNA from coke-oven workers and from workers in an aluminum production plant and demonstrated the presence of PAH-DNA adducts.	Aluminum	66-74	phenylalanine hydroxylase	Homo sapiens	125-128
8319662-9	1993	The more sensitive 32P-postlabeling assay showed the presence of PAH-DNA adducts in 91% of the aluminum workers.	Phosphorus-32	19-22	phenylalanine hydroxylase	Homo sapiens	65-68
8319662-9	1993	The more sensitive 32P-postlabeling assay showed the presence of PAH-DNA adducts in 91% of the aluminum workers.	Aluminum	95-103	phenylalanine hydroxylase	Homo sapiens	65-68
8444221-8	1993	There was a strong relationship between the average in vitro PAH activity of the two mutant enzymes and both the phenylalanine tolerance and the neonatal pretreatment serum phenylalanine concentration.	Phenylalanine	173-186	phenylalanine hydroxylase	Homo sapiens	61-64
8425536-0	1993	The cooperative binding of phenylalanine to phenylalanine 4-monooxygenase studied by 1H-NMR paramagnetic relaxation.	Hydrogen	85-87	phenylalanine hydroxylase	Homo sapiens	44-73
8425536-2	1993	The effect of the paramagnetic high-spin Fe(III) ion in phenylalanine 4-monooxygenase (phenylalanine hydroxylase, EC 1.14.16.1) on the water proton longitudinal relaxation rate has been used to study the environment of the iron center.	ferric sulfate	41-48	phenylalanine hydroxylase	Homo sapiens	56-85
8425536-2	1993	The effect of the paramagnetic high-spin Fe(III) ion in phenylalanine 4-monooxygenase (phenylalanine hydroxylase, EC 1.14.16.1) on the water proton longitudinal relaxation rate has been used to study the environment of the iron center.	ferric sulfate	41-48	phenylalanine hydroxylase	Homo sapiens	87-112
8425536-2	1993	The effect of the paramagnetic high-spin Fe(III) ion in phenylalanine 4-monooxygenase (phenylalanine hydroxylase, EC 1.14.16.1) on the water proton longitudinal relaxation rate has been used to study the environment of the iron center.	Water	135-140	phenylalanine hydroxylase	Homo sapiens	56-85
8425536-2	1993	The effect of the paramagnetic high-spin Fe(III) ion in phenylalanine 4-monooxygenase (phenylalanine hydroxylase, EC 1.14.16.1) on the water proton longitudinal relaxation rate has been used to study the environment of the iron center.	Water	135-140	phenylalanine hydroxylase	Homo sapiens	87-112
8425536-2	1993	The effect of the paramagnetic high-spin Fe(III) ion in phenylalanine 4-monooxygenase (phenylalanine hydroxylase, EC 1.14.16.1) on the water proton longitudinal relaxation rate has been used to study the environment of the iron center.	Iron	207-211	phenylalanine hydroxylase	Homo sapiens	56-85
8425536-2	1993	The effect of the paramagnetic high-spin Fe(III) ion in phenylalanine 4-monooxygenase (phenylalanine hydroxylase, EC 1.14.16.1) on the water proton longitudinal relaxation rate has been used to study the environment of the iron center.	Iron	207-211	phenylalanine hydroxylase	Homo sapiens	87-112
1564251-2	1992	To see if this might be linked to exposure to polycyclic aromatic hydrocarbons (PAHs) contained in refinery streams, a review of animal data on the relationship between PAH exposure, UV light and melanoma induction has been carried out and compared with human data.	Polycyclic Aromatic Hydrocarbons	46-78	phenylalanine hydroxylase	Homo sapiens	80-83
1359535-7	1992	Thus, our results suggest that the observed hyperphenylalaninemia in patients who excrete 7-BH4 in their urine may arise directly from the inhibition of phenylalanine hydroxylase by low levels of this pterin.	2-amino-4-hydroxy-7-(dihydroxypropyl)-5,6,7,8-tetrahydrobiopterin	90-95	phenylalanine hydroxylase	Homo sapiens	153-178
1359535-7	1992	Thus, our results suggest that the observed hyperphenylalaninemia in patients who excrete 7-BH4 in their urine may arise directly from the inhibition of phenylalanine hydroxylase by low levels of this pterin.	Pterins	201-207	phenylalanine hydroxylase	Homo sapiens	153-178
1338705-1	1992	The known mutant alleles of human phenylalanine hydroxylase gene were analyzed in 25 phenylketonuria (PKU) families from North China by polymerase chain reaction combined with allele-specific oligonucleotide dot hybridization techniques.	Oligonucleotides	192-207	phenylalanine hydroxylase	Homo sapiens	34-59
1328385-2	1992	An agonist-activated phospholipase D/phosphatidic acid phosphohydrolase (PAH) pathway was recently demonstrated in human neutrophils, and evidence suggests that phosphatidic acid (PA) and/or diradylglycerol (DG) generated from this pathway participates in activation of the O2(-)-generating respiratory burst.	Phosphatidic Acids	37-54	phenylalanine hydroxylase	Homo sapiens	73-76
1328385-2	1992	An agonist-activated phospholipase D/phosphatidic acid phosphohydrolase (PAH) pathway was recently demonstrated in human neutrophils, and evidence suggests that phosphatidic acid (PA) and/or diradylglycerol (DG) generated from this pathway participates in activation of the O2(-)-generating respiratory burst.	Phosphatidic Acids	73-75	phenylalanine hydroxylase	Homo sapiens	35-71
1328385-2	1992	An agonist-activated phospholipase D/phosphatidic acid phosphohydrolase (PAH) pathway was recently demonstrated in human neutrophils, and evidence suggests that phosphatidic acid (PA) and/or diradylglycerol (DG) generated from this pathway participates in activation of the O2(-)-generating respiratory burst.	diarachidonyl diglyceride	191-206	phenylalanine hydroxylase	Homo sapiens	35-71
1328385-2	1992	An agonist-activated phospholipase D/phosphatidic acid phosphohydrolase (PAH) pathway was recently demonstrated in human neutrophils, and evidence suggests that phosphatidic acid (PA) and/or diradylglycerol (DG) generated from this pathway participates in activation of the O2(-)-generating respiratory burst.	diarachidonyl diglyceride	191-206	phenylalanine hydroxylase	Homo sapiens	73-76
1328385-2	1992	An agonist-activated phospholipase D/phosphatidic acid phosphohydrolase (PAH) pathway was recently demonstrated in human neutrophils, and evidence suggests that phosphatidic acid (PA) and/or diradylglycerol (DG) generated from this pathway participates in activation of the O2(-)-generating respiratory burst.	Superoxides	274-276	phenylalanine hydroxylase	Homo sapiens	35-71
1328385-2	1992	An agonist-activated phospholipase D/phosphatidic acid phosphohydrolase (PAH) pathway was recently demonstrated in human neutrophils, and evidence suggests that phosphatidic acid (PA) and/or diradylglycerol (DG) generated from this pathway participates in activation of the O2(-)-generating respiratory burst.	Superoxides	274-276	phenylalanine hydroxylase	Homo sapiens	73-76
1328385-7	1992	In many cases, inhibition of [3H]-DG generation corresponded to an increase in [3H]-PA, implicating PAH as the locus of inhibition.	Tritium	30-33	phenylalanine hydroxylase	Homo sapiens	100-103
1328385-7	1992	In many cases, inhibition of [3H]-DG generation corresponded to an increase in [3H]-PA, implicating PAH as the locus of inhibition.	3h]-pa	80-86	phenylalanine hydroxylase	Homo sapiens	100-103
1288453-11	1992	A mutation which changed the affinity of PAH for phenylalanine was associated with mild hyperphenylalaninemia.	Phenylalanine	49-62	phenylalanine hydroxylase	Homo sapiens	41-44
1326329-1	1992	Human phenylalanine hydroxylase (PAH) is expressed in a liver-specific manner and catalyzes the enzymatic conversion of phenylalanine to tyrosine.	Phenylalanine	6-19	phenylalanine hydroxylase	Homo sapiens	33-36
1326329-1	1992	Human phenylalanine hydroxylase (PAH) is expressed in a liver-specific manner and catalyzes the enzymatic conversion of phenylalanine to tyrosine.	Tyrosine	137-145	phenylalanine hydroxylase	Homo sapiens	6-31
1326329-1	1992	Human phenylalanine hydroxylase (PAH) is expressed in a liver-specific manner and catalyzes the enzymatic conversion of phenylalanine to tyrosine.	Tyrosine	137-145	phenylalanine hydroxylase	Homo sapiens	33-36
1477371-3	1992	Its molecular weight was similar to that of major chymotryptic peptide of human liver PH.	Peptides	63-70	phenylalanine hydroxylase	Homo sapiens	86-88
1358789-6	1992	Three children had inherited a G-to-A transition at codon 415 in exon 12 of the PAH gene, resulting in the substitution of asparagine for aspartate, whereas one child possessed an A-to-G transition at codon 306 in exon 9, causing the replacement of an isoleucine by a valine in the enzyme.	Asparagine	123-133	phenylalanine hydroxylase	Homo sapiens	80-83
1358789-6	1992	Three children had inherited a G-to-A transition at codon 415 in exon 12 of the PAH gene, resulting in the substitution of asparagine for aspartate, whereas one child possessed an A-to-G transition at codon 306 in exon 9, causing the replacement of an isoleucine by a valine in the enzyme.	Aspartic Acid	138-147	phenylalanine hydroxylase	Homo sapiens	80-83
1358789-6	1992	Three children had inherited a G-to-A transition at codon 415 in exon 12 of the PAH gene, resulting in the substitution of asparagine for aspartate, whereas one child possessed an A-to-G transition at codon 306 in exon 9, causing the replacement of an isoleucine by a valine in the enzyme.	Isoleucine	252-262	phenylalanine hydroxylase	Homo sapiens	80-83
1358789-6	1992	Three children had inherited a G-to-A transition at codon 415 in exon 12 of the PAH gene, resulting in the substitution of asparagine for aspartate, whereas one child possessed an A-to-G transition at codon 306 in exon 9, causing the replacement of an isoleucine by a valine in the enzyme.	Valine	268-274	phenylalanine hydroxylase	Homo sapiens	80-83
1484144-1	1992	Phenylalanine hydroxylase (EC 1.14.16.1) antigen and activity have been identified among proteins extracted with a buffer containing 0.4% Triton X-100 from adult human liver bioptate fraction, which was sedimented at 105,000 x g (n = 4).	Octoxynol	138-150	phenylalanine hydroxylase	Homo sapiens	0-25
1355046-3	1992	It has been shown that the 7-substituted isomers of biopterin and neopterin derive from L-tetrahydrobiopterin and D-tetrahydroneopterin and are formed during hydroxylation of phenylalanine to tyrosine with rat liver dehydratase-free phenylalanine hydroxylase.	Biopterin	52-61	phenylalanine hydroxylase	Homo sapiens	233-258
1355046-3	1992	It has been shown that the 7-substituted isomers of biopterin and neopterin derive from L-tetrahydrobiopterin and D-tetrahydroneopterin and are formed during hydroxylation of phenylalanine to tyrosine with rat liver dehydratase-free phenylalanine hydroxylase.	Neopterin	66-75	phenylalanine hydroxylase	Homo sapiens	233-258
1355046-3	1992	It has been shown that the 7-substituted isomers of biopterin and neopterin derive from L-tetrahydrobiopterin and D-tetrahydroneopterin and are formed during hydroxylation of phenylalanine to tyrosine with rat liver dehydratase-free phenylalanine hydroxylase.	Phenylalanine	175-188	phenylalanine hydroxylase	Homo sapiens	233-258
1355046-6	1992	Tetrahydroneopterin and 6-hydroxymethyltetrahydropterin also are converted to their corresponding 7-substituted isomers and serve as cofactors in the phenylalanine hydroxylase reaction.	tetrahydroneopterin	0-19	phenylalanine hydroxylase	Homo sapiens	150-175
1355046-6	1992	Tetrahydroneopterin and 6-hydroxymethyltetrahydropterin also are converted to their corresponding 7-substituted isomers and serve as cofactors in the phenylalanine hydroxylase reaction.	6-(hydroxymethyl)tetrahydropterin	24-55	phenylalanine hydroxylase	Homo sapiens	150-175
1355046-9	1992	7-Tetrahydrobiopterin is both a substrate (cofactor) and a competitive inhibitor with 6-tetrahydrobiopterin (Ki approximately 8 microM) in the phenylalanine hydroxylase reaction.	7-tetrahydrobiopterin	0-21	phenylalanine hydroxylase	Homo sapiens	143-168
1355046-9	1992	7-Tetrahydrobiopterin is both a substrate (cofactor) and a competitive inhibitor with 6-tetrahydrobiopterin (Ki approximately 8 microM) in the phenylalanine hydroxylase reaction.	6-tetrahydrobiopterin	86-107	phenylalanine hydroxylase	Homo sapiens	143-168
1588012-5	1992	The dose of BH4 needed to normalize liver phenylalanine hydroxylase is one eighth to one fourth that required for normal neurotransmitter metabolism in the central nervous system.	sapropterin	12-15	phenylalanine hydroxylase	Homo sapiens	42-67
8272161-7	1993	A prolonged interaction of active oxygen species with chemical carcinogens (N-nitroso- or diazonium compounds, PAH) can exhibit a significant promoting effect on the development of intestinal type of gastric cancer from its precancerous conditions, above all after partial gastrectomy.	Oxygen	34-40	phenylalanine hydroxylase	Homo sapiens	111-114
1307495-1	1992	The known mutant alleles of the human phenylalanine hydroxylase (PAN) gene were analyzed in 25 phenylketonuria (PKU) families from North China by using polymerase chain reaction and allele-specific oligonucleotide dot blot hybridization techniques.	Oligonucleotides	198-213	phenylalanine hydroxylase	Homo sapiens	38-63
1307495-1	1992	The known mutant alleles of the human phenylalanine hydroxylase (PAN) gene were analyzed in 25 phenylketonuria (PKU) families from North China by using polymerase chain reaction and allele-specific oligonucleotide dot blot hybridization techniques.	Oligonucleotides	198-213	phenylalanine hydroxylase	Homo sapiens	65-68
1458831-7	1992	With the natural cofactor H4Bip, no activation of the enzyme with Phe was necessary (in contrast to mammalian phenylalanine hydroxylase), and this tetrahydropteridine inhibits phenylalanine hydroxylase activity when the enzyme is exposed to it before phenylalanine addition.	h4bip	26-31	phenylalanine hydroxylase	Homo sapiens	110-135
1458831-7	1992	With the natural cofactor H4Bip, no activation of the enzyme with Phe was necessary (in contrast to mammalian phenylalanine hydroxylase), and this tetrahydropteridine inhibits phenylalanine hydroxylase activity when the enzyme is exposed to it before phenylalanine addition.	h4bip	26-31	phenylalanine hydroxylase	Homo sapiens	176-201
1458831-7	1992	With the natural cofactor H4Bip, no activation of the enzyme with Phe was necessary (in contrast to mammalian phenylalanine hydroxylase), and this tetrahydropteridine inhibits phenylalanine hydroxylase activity when the enzyme is exposed to it before phenylalanine addition.	5,6,7,8-tetrahydropteridine	147-166	phenylalanine hydroxylase	Homo sapiens	110-135
1458831-7	1992	With the natural cofactor H4Bip, no activation of the enzyme with Phe was necessary (in contrast to mammalian phenylalanine hydroxylase), and this tetrahydropteridine inhibits phenylalanine hydroxylase activity when the enzyme is exposed to it before phenylalanine addition.	5,6,7,8-tetrahydropteridine	147-166	phenylalanine hydroxylase	Homo sapiens	176-201
1388263-8	1992	Ki,NMeN and Ki,PAH of cimetidine (pKa 6.98) and buspirone (pKa 7.2) which interact with both transport systems, did not vary between perfusate pH 6.0 and 8.0.	Cimetidine	22-32	phenylalanine hydroxylase	Homo sapiens	15-18
2062852-1	1991	A monoclonal anti-idiotype antibody, NS7, previously shown to mimic the binding of the pterin cofactor of phenylalanine hydroxylase (phenylalanine 4-monooxygenase, EC 1.14.16.1) has been used to localize the cofactor binding site within the phenylalanine hydroxylase catalytic domain to a 27-amino-acid sequence that is highly conserved among the three aromatic amino acid hydroxylases.	Pterins	87-93	phenylalanine hydroxylase	Homo sapiens	106-131
1959929-5	1991	The regions that have been found to be linked to TSC in different families map to the positions of three enzymes, phenylalanine hydroxylase (12q22-24), tyrosinase (11q14-22), and dopamine-beta-hydroxylase (9q34), all of which are involved in the conversion of phenylalanine to catecholamine neurotransmitters or melanin.	Catecholamines	277-290	phenylalanine hydroxylase	Homo sapiens	114-139
1959929-5	1991	The regions that have been found to be linked to TSC in different families map to the positions of three enzymes, phenylalanine hydroxylase (12q22-24), tyrosinase (11q14-22), and dopamine-beta-hydroxylase (9q34), all of which are involved in the conversion of phenylalanine to catecholamine neurotransmitters or melanin.	Melanins	312-319	phenylalanine hydroxylase	Homo sapiens	114-139
1867197-1	1991	Hyperphenylalaninemia (HPA) results from defective hydroxylation of phenylalanine in the liver, in most cases because of defective phenylalanine hydroxylase.	Phenylalanine	5-18	phenylalanine hydroxylase	Homo sapiens	131-156
1809305-1	1991	In order to investigate the organic compound fraction of the Naples aerosol a chromatographic method was used for the separation and analysis of the polycyclic aromatic (PAH).	polycyclic aromatic	149-168	phenylalanine hydroxylase	Homo sapiens	170-173
1709636-3	1991	We report here a 3-base pair in-frame deletion of the PAH gene (delta 194) in a mild variant, with markedly reduced affinity of the enzyme for phenylalanine (Km = 160 nM), and we provide functional evidence for responsibility of the deletion in the mutant phenotype.	Phenylalanine	143-156	phenylalanine hydroxylase	Homo sapiens	54-57
1350519-5	1992	Exon 3 (Arg111----stop) and exon 6 (Tyr204----Cys204) mutations of the PAH gene were studied using the polymerase chain reaction (PCR) and allele specific oligonucleotide probe hybridization in 42 PKU families from North China.	Oligonucleotides	155-170	phenylalanine hydroxylase	Homo sapiens	71-74
1301201-3	1992	Here we report (1) identification of another mutation, on a haplotype 9 chromosome, which converts codon 65 from isoleucine (ATT) to threonine (ACT), (2) expression analysis of the I65T mutation in COS cells demonstrating 75% loss of both immunoreactive protein and enzyme activity, and (3) expression analysis of the most prevalent PKU allele (M1V) in eastern Quebec, showing nondetectable levels of PAH protein and activity, a finding compatible with a mutation in the translation initiation codon.	Isoleucine	113-123	phenylalanine hydroxylase	Homo sapiens	401-404
1301201-3	1992	Here we report (1) identification of another mutation, on a haplotype 9 chromosome, which converts codon 65 from isoleucine (ATT) to threonine (ACT), (2) expression analysis of the I65T mutation in COS cells demonstrating 75% loss of both immunoreactive protein and enzyme activity, and (3) expression analysis of the most prevalent PKU allele (M1V) in eastern Quebec, showing nondetectable levels of PAH protein and activity, a finding compatible with a mutation in the translation initiation codon.	Threonine	133-142	phenylalanine hydroxylase	Homo sapiens	401-404
1301201-3	1992	Here we report (1) identification of another mutation, on a haplotype 9 chromosome, which converts codon 65 from isoleucine (ATT) to threonine (ACT), (2) expression analysis of the I65T mutation in COS cells demonstrating 75% loss of both immunoreactive protein and enzyme activity, and (3) expression analysis of the most prevalent PKU allele (M1V) in eastern Quebec, showing nondetectable levels of PAH protein and activity, a finding compatible with a mutation in the translation initiation codon.	carbonyl sulfide	198-201	phenylalanine hydroxylase	Homo sapiens	401-404
1301927-1	1992	The frequency and distribution of eight mutations (R111X, IVS4nt-1, Y204C, R243Q, IVS7nt-2, W326X, Y356X, and R413P) in the phenylalanine hydroxylase gene of Orientals in Japan and Korea were examined by allele-specific oligonucleotide hybridization.	Oligonucleotides	220-235	phenylalanine hydroxylase	Homo sapiens	124-149
1371594-2	1992	Nitro-PAH were found to be the most significant mutagens formed from the reactions of naphthalene and fluorene.	naphthalene	86-97	phenylalanine hydroxylase	Homo sapiens	6-9
1371594-2	1992	Nitro-PAH were found to be the most significant mutagens formed from the reactions of naphthalene and fluorene.	fluorene	102-110	phenylalanine hydroxylase	Homo sapiens	6-9
1371594-3	1992	The mutagram (bar graph of mutagenic activity versus HPLC fraction) of the phenanthrene reaction products closely resembled that of an ambient air particulate extract with the most mutagenic activity being in a fraction more polar than that in which the nitro-PAH elute.	phenanthrene	75-87	phenylalanine hydroxylase	Homo sapiens	260-263
1959225-7	1991	A deficiency of the cofactor tetrahydrobiopterin (BH4), which is required for phenylalanine hydroxylase activity, leads to hyperphenylalaninemia.	sapropterin	29-48	phenylalanine hydroxylase	Homo sapiens	78-103
1959225-7	1991	A deficiency of the cofactor tetrahydrobiopterin (BH4), which is required for phenylalanine hydroxylase activity, leads to hyperphenylalaninemia.	sapropterin	50-53	phenylalanine hydroxylase	Homo sapiens	78-103
1683521-3	1991	Sequence analysis on the mutant PAH gene of this haplotype 2 patient, who was born to first-cousin parents, disclosed it to be a C-to-T transition in exon 7.	Carbon	129-130	phenylalanine hydroxylase	Homo sapiens	32-35
1944771-0	1991	Studies on the partially uncoupled oxidation of tetrahydropterins by phenylalanine hydroxylase.	tetrahydropterin	48-65	phenylalanine hydroxylase	Homo sapiens	69-94
1944771-1	1991	The uncoupled portion of the partially uncoupled oxidation of tetrahydropterins by phenylalanine hydroxylase can be described by the same model as we have recently derived for the fully uncoupled reaction (Davis, M.D.	tetrahydropterin	62-79	phenylalanine hydroxylase	Homo sapiens	83-108
1944771-5	1991	Although essentially no hydrogen peroxide is formed during the fully coupled oxidation of tetrahydrobiopterin or 6-methyltetrahydropterin by phenylalanine hydroxylase when phenylalanine is the amino acid substrate, significant amounts of hydrogen peroxide are formed during the partially uncoupled oxidation of 6-methyltetrahydropterin when para-fluorophenylalanine or para-chlorophenylalanine are used in place of phenylalanine.	sapropterin	90-109	phenylalanine hydroxylase	Homo sapiens	141-166
1944771-5	1991	Although essentially no hydrogen peroxide is formed during the fully coupled oxidation of tetrahydrobiopterin or 6-methyltetrahydropterin by phenylalanine hydroxylase when phenylalanine is the amino acid substrate, significant amounts of hydrogen peroxide are formed during the partially uncoupled oxidation of 6-methyltetrahydropterin when para-fluorophenylalanine or para-chlorophenylalanine are used in place of phenylalanine.	6-methyltetrahydropterin	113-137	phenylalanine hydroxylase	Homo sapiens	141-166
1944771-5	1991	Although essentially no hydrogen peroxide is formed during the fully coupled oxidation of tetrahydrobiopterin or 6-methyltetrahydropterin by phenylalanine hydroxylase when phenylalanine is the amino acid substrate, significant amounts of hydrogen peroxide are formed during the partially uncoupled oxidation of 6-methyltetrahydropterin when para-fluorophenylalanine or para-chlorophenylalanine are used in place of phenylalanine.	Hydrogen Peroxide	238-255	phenylalanine hydroxylase	Homo sapiens	141-166
1944771-5	1991	Although essentially no hydrogen peroxide is formed during the fully coupled oxidation of tetrahydrobiopterin or 6-methyltetrahydropterin by phenylalanine hydroxylase when phenylalanine is the amino acid substrate, significant amounts of hydrogen peroxide are formed during the partially uncoupled oxidation of 6-methyltetrahydropterin when para-fluorophenylalanine or para-chlorophenylalanine are used in place of phenylalanine.	6-methyltetrahydropterin	311-335	phenylalanine hydroxylase	Homo sapiens	141-166
1944771-5	1991	Although essentially no hydrogen peroxide is formed during the fully coupled oxidation of tetrahydrobiopterin or 6-methyltetrahydropterin by phenylalanine hydroxylase when phenylalanine is the amino acid substrate, significant amounts of hydrogen peroxide are formed during the partially uncoupled oxidation of 6-methyltetrahydropterin when para-fluorophenylalanine or para-chlorophenylalanine are used in place of phenylalanine.	p-Fluorophenylalanine	341-365	phenylalanine hydroxylase	Homo sapiens	141-166
1944771-5	1991	Although essentially no hydrogen peroxide is formed during the fully coupled oxidation of tetrahydrobiopterin or 6-methyltetrahydropterin by phenylalanine hydroxylase when phenylalanine is the amino acid substrate, significant amounts of hydrogen peroxide are formed during the partially uncoupled oxidation of 6-methyltetrahydropterin when para-fluorophenylalanine or para-chlorophenylalanine are used in place of phenylalanine.	Fenclonine	369-393	phenylalanine hydroxylase	Homo sapiens	141-166
1944771-5	1991	Although essentially no hydrogen peroxide is formed during the fully coupled oxidation of tetrahydrobiopterin or 6-methyltetrahydropterin by phenylalanine hydroxylase when phenylalanine is the amino acid substrate, significant amounts of hydrogen peroxide are formed during the partially uncoupled oxidation of 6-methyltetrahydropterin when para-fluorophenylalanine or para-chlorophenylalanine are used in place of phenylalanine.	Phenylalanine	172-185	phenylalanine hydroxylase	Homo sapiens	141-166
1944771-7	1991	The 4a-carbinolamine tetrahydropterin intermediate has been observed during the fully uncoupled tyrosine-dependent oxidations of tetrahydropterin and 6-methyltetrahydropterin by lysolecithin-activated phenylalanine hydroxylase, suggesting that this species is also a common intermediate for uncoupled oxidations by this enzyme.	4a-Carbinolamine tetrahydropterin	4-37	phenylalanine hydroxylase	Homo sapiens	201-226
1944771-7	1991	The 4a-carbinolamine tetrahydropterin intermediate has been observed during the fully uncoupled tyrosine-dependent oxidations of tetrahydropterin and 6-methyltetrahydropterin by lysolecithin-activated phenylalanine hydroxylase, suggesting that this species is also a common intermediate for uncoupled oxidations by this enzyme.	Tyrosine	96-104	phenylalanine hydroxylase	Homo sapiens	201-226
1944771-7	1991	The 4a-carbinolamine tetrahydropterin intermediate has been observed during the fully uncoupled tyrosine-dependent oxidations of tetrahydropterin and 6-methyltetrahydropterin by lysolecithin-activated phenylalanine hydroxylase, suggesting that this species is also a common intermediate for uncoupled oxidations by this enzyme.	tetrahydropterin	21-37	phenylalanine hydroxylase	Homo sapiens	201-226
1944771-7	1991	The 4a-carbinolamine tetrahydropterin intermediate has been observed during the fully uncoupled tyrosine-dependent oxidations of tetrahydropterin and 6-methyltetrahydropterin by lysolecithin-activated phenylalanine hydroxylase, suggesting that this species is also a common intermediate for uncoupled oxidations by this enzyme.	6-methyltetrahydropterin	150-174	phenylalanine hydroxylase	Homo sapiens	201-226
2014036-9	1991	The predicted level of phenylalanine hydroxylase activity correlated strongly with the pretreatment serum level of phenylalanine (r = 0.91, P less than 0.001 in the Danish patients and r = 0.74, P less than 0.001 in the German patients), phenylalanine tolerance in the Danish patients (r = 0.84, P less than 0.001), and the serum phenylalanine level measured after standardized oral protein loading in the German patients (r = 0.84, P less than 0.001).	Phenylalanine	115-128	phenylalanine hydroxylase	Homo sapiens	23-48
2014036-9	1991	The predicted level of phenylalanine hydroxylase activity correlated strongly with the pretreatment serum level of phenylalanine (r = 0.91, P less than 0.001 in the Danish patients and r = 0.74, P less than 0.001 in the German patients), phenylalanine tolerance in the Danish patients (r = 0.84, P less than 0.001), and the serum phenylalanine level measured after standardized oral protein loading in the German patients (r = 0.84, P less than 0.001).	Phenylalanine	115-128	phenylalanine hydroxylase	Homo sapiens	23-48
2062852-1	1991	A monoclonal anti-idiotype antibody, NS7, previously shown to mimic the binding of the pterin cofactor of phenylalanine hydroxylase (phenylalanine 4-monooxygenase, EC 1.14.16.1) has been used to localize the cofactor binding site within the phenylalanine hydroxylase catalytic domain to a 27-amino-acid sequence that is highly conserved among the three aromatic amino acid hydroxylases.	Pterins	87-93	phenylalanine hydroxylase	Homo sapiens	133-162
2062852-1	1991	A monoclonal anti-idiotype antibody, NS7, previously shown to mimic the binding of the pterin cofactor of phenylalanine hydroxylase (phenylalanine 4-monooxygenase, EC 1.14.16.1) has been used to localize the cofactor binding site within the phenylalanine hydroxylase catalytic domain to a 27-amino-acid sequence that is highly conserved among the three aromatic amino acid hydroxylases.	Pterins	87-93	phenylalanine hydroxylase	Homo sapiens	241-266
2062852-2	1991	The binding of NS7 to a synthetic peptide corresponding to the phenylalanine hydroxylase sequence from residue 263 to residue 289 was blocked by the competitive inhibitor of phenylalanine hydroxylase enzyme activity, 7,8-dihydro-6,7-dimethylpterin.	quinonoid-2-amino-4-hydroxy-6,7-dimethyldihydropteridine	217-247	phenylalanine hydroxylase	Homo sapiens	63-88
2062852-2	1991	The binding of NS7 to a synthetic peptide corresponding to the phenylalanine hydroxylase sequence from residue 263 to residue 289 was blocked by the competitive inhibitor of phenylalanine hydroxylase enzyme activity, 7,8-dihydro-6,7-dimethylpterin.	quinonoid-2-amino-4-hydroxy-6,7-dimethyldihydropteridine	217-247	phenylalanine hydroxylase	Homo sapiens	174-199
2062852-3	1991	In addition this peptide competed with native phenylalanine hydroxylase for binding to 6,7-dimethyl-5,6,7,8-tetrahydropterin conjugated to a polyglutamate carrier.	2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine	87-124	phenylalanine hydroxylase	Homo sapiens	46-71
2062852-3	1991	In addition this peptide competed with native phenylalanine hydroxylase for binding to 6,7-dimethyl-5,6,7,8-tetrahydropterin conjugated to a polyglutamate carrier.	Polyglutamic Acid	141-154	phenylalanine hydroxylase	Homo sapiens	46-71
2044609-2	1991	An A-to-G transition at the second base of codon 414 results in the substitution of Cys for Tyr in the mutant PAH protein.	Cysteine	84-87	phenylalanine hydroxylase	Homo sapiens	110-113
2069475-1	1991	The occurrence of increased levels of blood phenylalanine after therapeutic administration of folate analogues has been occasionally reported and attributed to the inhibition of dihydropteridine reductase, an enzyme maintaining the cofactor of phenylalanine hydroxylase in its active tetrahydrogenated form (tetrahydrobiopterin).	Phenylalanine	44-57	phenylalanine hydroxylase	Homo sapiens	244-269
2069475-1	1991	The occurrence of increased levels of blood phenylalanine after therapeutic administration of folate analogues has been occasionally reported and attributed to the inhibition of dihydropteridine reductase, an enzyme maintaining the cofactor of phenylalanine hydroxylase in its active tetrahydrogenated form (tetrahydrobiopterin).	Folic Acid	94-100	phenylalanine hydroxylase	Homo sapiens	244-269
2006152-1	1991	A missense mutation has been identified in the human phenylalanine hydroxylase [PAH; phenylalanine 4-monooxygenase; L-phenylalanine, tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating), EC 1.14.16.1] gene in a Chinese patient with classic phenylketonuria (PKU).	p-Aminohippuric Acid	80-83	phenylalanine hydroxylase	Homo sapiens	53-78
2006152-1	1991	A missense mutation has been identified in the human phenylalanine hydroxylase [PAH; phenylalanine 4-monooxygenase; L-phenylalanine, tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating), EC 1.14.16.1] gene in a Chinese patient with classic phenylketonuria (PKU).	p-Aminohippuric Acid	80-83	phenylalanine hydroxylase	Homo sapiens	85-114
2044609-2	1991	An A-to-G transition at the second base of codon 414 results in the substitution of Cys for Tyr in the mutant PAH protein.	Tyrosine	92-95	phenylalanine hydroxylase	Homo sapiens	110-113
15092109-5	1991	The losses of PAH compounds in these field experiments can be related, in part, to their physico-chemical properties, notably the octanol: water partition coefficient.	Octanols	130-137	phenylalanine hydroxylase	Homo sapiens	14-17
2069475-1	1991	The occurrence of increased levels of blood phenylalanine after therapeutic administration of folate analogues has been occasionally reported and attributed to the inhibition of dihydropteridine reductase, an enzyme maintaining the cofactor of phenylalanine hydroxylase in its active tetrahydrogenated form (tetrahydrobiopterin).	sapropterin	308-327	phenylalanine hydroxylase	Homo sapiens	244-269
1653727-0	1991	The modulation of phenylalanine hydroxylase activity by okadaic acid.	Okadaic Acid	56-68	phenylalanine hydroxylase	Homo sapiens	18-43
15092109-5	1991	The losses of PAH compounds in these field experiments can be related, in part, to their physico-chemical properties, notably the octanol: water partition coefficient.	Water	139-144	phenylalanine hydroxylase	Homo sapiens	14-17
1672294-2	1991	Both mutations occurred in exon 7 of the PAH gene, resulting in the substitution of Trp for Arg at amino acid 252 (R252W) and of Leu for Pro (P281L) at amino acid 281 of the protein.	Leucine	129-132	phenylalanine hydroxylase	Homo sapiens	41-44
1672294-2	1991	Both mutations occurred in exon 7 of the PAH gene, resulting in the substitution of Trp for Arg at amino acid 252 (R252W) and of Leu for Pro (P281L) at amino acid 281 of the protein.	Proline	137-140	phenylalanine hydroxylase	Homo sapiens	41-44
2244891-6	1990	Our results also suggest that tetrahydroneopterin can be a cofactor for the phenylalanine hydroxylase system in vivo.	tetrahydroneopterin	30-49	phenylalanine hydroxylase	Homo sapiens	76-101
1997387-0	1991	PAH 399 GTA (Val)----GTT(Val), a new silent mutation found in the Chinese.	Valine	13-16	phenylalanine hydroxylase	Homo sapiens	0-3
1997387-0	1991	PAH 399 GTA (Val)----GTT(Val), a new silent mutation found in the Chinese.	Valine	25-28	phenylalanine hydroxylase	Homo sapiens	0-3
1671881-2	1991	The abolition of an invariant BamHI site located in the coding sequence of the PAH gene (exon 7) led to the recognition of two new point mutations at codon 272 and 273 (272gly----stop and 273ser----phe, respectively).	Phenylalanine	198-201	phenylalanine hydroxylase	Homo sapiens	79-82
2073747-3	1990	The activity of purified PAH was inhibited by p-Cl-phenylalanine (p-Cl-Phe), 3-J-tyrosine (3-J-Tyr) and 6-F-tryptophane (6-F-Trp) by 73%, 26% and 10%, respectively.	p-cl-phenylalanine	46-64	phenylalanine hydroxylase	Homo sapiens	25-28
2073747-3	1990	The activity of purified PAH was inhibited by p-Cl-phenylalanine (p-Cl-Phe), 3-J-tyrosine (3-J-Tyr) and 6-F-tryptophane (6-F-Trp) by 73%, 26% and 10%, respectively.	p-cl-phe	66-74	phenylalanine hydroxylase	Homo sapiens	25-28
2073747-3	1990	The activity of purified PAH was inhibited by p-Cl-phenylalanine (p-Cl-Phe), 3-J-tyrosine (3-J-Tyr) and 6-F-tryptophane (6-F-Trp) by 73%, 26% and 10%, respectively.	3-j-tyrosine	77-89	phenylalanine hydroxylase	Homo sapiens	25-28
2073747-3	1990	The activity of purified PAH was inhibited by p-Cl-phenylalanine (p-Cl-Phe), 3-J-tyrosine (3-J-Tyr) and 6-F-tryptophane (6-F-Trp) by 73%, 26% and 10%, respectively.	3-j-tyr	91-98	phenylalanine hydroxylase	Homo sapiens	25-28
2073747-3	1990	The activity of purified PAH was inhibited by p-Cl-phenylalanine (p-Cl-Phe), 3-J-tyrosine (3-J-Tyr) and 6-F-tryptophane (6-F-Trp) by 73%, 26% and 10%, respectively.	6-f-tryptophane	104-119	phenylalanine hydroxylase	Homo sapiens	25-28
2073747-3	1990	The activity of purified PAH was inhibited by p-Cl-phenylalanine (p-Cl-Phe), 3-J-tyrosine (3-J-Tyr) and 6-F-tryptophane (6-F-Trp) by 73%, 26% and 10%, respectively.	6-f-trp	121-128	phenylalanine hydroxylase	Homo sapiens	25-28
2220810-4	1990	Haplotypes at the PAH locus were determined for 19 individuals with moderately elevated plasma phenylalanine and normal urinary neopterin/biopterin ratios.	Phenylalanine	95-108	phenylalanine hydroxylase	Homo sapiens	18-21
2213015-3	1990	Phosphate-activated glutaminase and glutamic acid decarboxylase were correlated with tissue pH and lactate, and also were reduced by in vitro acidification, suggesting that the low activities of these enzymes in agonal controls were related to decreased pH consequent upon lactate accumulation.	Glutamic Acid	36-49	phenylalanine hydroxylase	Homo sapiens	92-94
2213015-3	1990	Phosphate-activated glutaminase and glutamic acid decarboxylase were correlated with tissue pH and lactate, and also were reduced by in vitro acidification, suggesting that the low activities of these enzymes in agonal controls were related to decreased pH consequent upon lactate accumulation.	Glutamic Acid	36-49	phenylalanine hydroxylase	Homo sapiens	254-256
2213015-3	1990	Phosphate-activated glutaminase and glutamic acid decarboxylase were correlated with tissue pH and lactate, and also were reduced by in vitro acidification, suggesting that the low activities of these enzymes in agonal controls were related to decreased pH consequent upon lactate accumulation.	Lactic Acid	273-280	phenylalanine hydroxylase	Homo sapiens	92-94
2220810-4	1990	Haplotypes at the PAH locus were determined for 19 individuals with moderately elevated plasma phenylalanine and normal urinary neopterin/biopterin ratios.	Neopterin	128-137	phenylalanine hydroxylase	Homo sapiens	18-21
2220810-4	1990	Haplotypes at the PAH locus were determined for 19 individuals with moderately elevated plasma phenylalanine and normal urinary neopterin/biopterin ratios.	Biopterin	138-147	phenylalanine hydroxylase	Homo sapiens	18-21
2220810-7	1990	Elevated plasma phenylalanine was seen to genetically segregate with specific PAH alleles in each family.	Phenylalanine	16-29	phenylalanine hydroxylase	Homo sapiens	78-81
2220810-9	1990	At theta = 0 this gives a probability of linkage between the PAH locus and the locus for moderate phenylalanine elevations that is approximately 3,600:1.	Phenylalanine	98-111	phenylalanine hydroxylase	Homo sapiens	61-64
2121612-2	1990	The strong hybridization signals observed in genomic blots when D. melanogaster DNA was probed with 32P-labeled human pah cDNA, indicated the existence of a high degree of sequence similarity between the pah genes of both species.	Phosphorus-32	100-103	phenylalanine hydroxylase	Homo sapiens	118-121
2121612-2	1990	The strong hybridization signals observed in genomic blots when D. melanogaster DNA was probed with 32P-labeled human pah cDNA, indicated the existence of a high degree of sequence similarity between the pah genes of both species.	Phosphorus-32	100-103	phenylalanine hydroxylase	Homo sapiens	204-207
33819046-1	2021	Phenylketonuria (PKU) is a disease of the catabolism of phenylalanine (Phe), caused by an impaired function of the enzyme phenylalanine hydroxylase.	Phenylalanine	56-69	phenylalanine hydroxylase	Homo sapiens	122-147
2303485-8	1990	However, compared with the normal cofactor, tetrahydrobiopterin, the Km values of tetrahydro-7-biopterin for phenylalanine hydroxylase and dihydropteridine reductase are 20 and 5 times higher, respectively.	sapropterin	44-63	phenylalanine hydroxylase	Homo sapiens	109-134
2303485-8	1990	However, compared with the normal cofactor, tetrahydrobiopterin, the Km values of tetrahydro-7-biopterin for phenylalanine hydroxylase and dihydropteridine reductase are 20 and 5 times higher, respectively.	7-(1,2-dihydroxypropyl)-5,6,7,8-tetrahydrobiopterin	82-104	phenylalanine hydroxylase	Homo sapiens	109-134
1971144-5	1990	Furthermore, since the site of mutation involves a CpG dinucleotide, they may represent hot spots for mutation in the human PAH locus.	cytidylyl-3'-5'-guanosine	51-67	phenylalanine hydroxylase	Homo sapiens	124-127
1975096-0	1990	Prenatal detection of an Arg----Ter mutation at codon 111 of the PAH gene using DNA amplification.	Arginine	25-28	phenylalanine hydroxylase	Homo sapiens	65-68
1975096-6	1990	The results indicated that the fetal DNA carried a PAH 111 Arg----Ter mutant gene inherited from his father.	Arginine	59-62	phenylalanine hydroxylase	Homo sapiens	51-54
33819046-1	2021	Phenylketonuria (PKU) is a disease of the catabolism of phenylalanine (Phe), caused by an impaired function of the enzyme phenylalanine hydroxylase.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	122-147
33818088-0	2021	Halochromic Polymer Nanosensors for Simple Visual Detection of Local pH in Coatings.	Polymers	12-19	phenylalanine hydroxylase	Homo sapiens	69-71
33764067-0	2021	Transformation of Hexagonal Birnessite upon Reaction with Thallium(I): Effects of Birnessite Crystallinity, pH, and Thallium Concentration.	birnessite	28-38	phenylalanine hydroxylase	Homo sapiens	108-110
33764067-4	2021	Instead, both birnessites transformed into a 2 x 2 tunneled phase with dehydrated Tl(I) in its tunnels at pH 4, but only partially at pH 6, and at pH 8.0 they remained layered.	birnessite	14-25	phenylalanine hydroxylase	Homo sapiens	106-108
33764067-4	2021	Instead, both birnessites transformed into a 2 x 2 tunneled phase with dehydrated Tl(I) in its tunnels at pH 4, but only partially at pH 6, and at pH 8.0 they remained layered.	birnessite	14-25	phenylalanine hydroxylase	Homo sapiens	134-136
33764067-4	2021	Instead, both birnessites transformed into a 2 x 2 tunneled phase with dehydrated Tl(I) in its tunnels at pH 4, but only partially at pH 6, and at pH 8.0 they remained layered.	birnessite	14-25	phenylalanine hydroxylase	Homo sapiens	134-136
33940423-7	2021	It is found that pH plays a significant role in the reaction, and ammonium sulfate has significant impacts on the enhancement of aqueous phase sulfate production through regulating the pH of solution.	Ammonium Sulfate	66-82	phenylalanine hydroxylase	Homo sapiens	185-187
33940423-7	2021	It is found that pH plays a significant role in the reaction, and ammonium sulfate has significant impacts on the enhancement of aqueous phase sulfate production through regulating the pH of solution.	Sulfates	75-82	phenylalanine hydroxylase	Homo sapiens	185-187
33761262-2	2021	For phospholipid bilayers, the large range of pH- and ionic strength-dependent surface charge densities adopted by titanium dioxide and other oxidic surfaces leads to a rich landscape of phenomena that provides exquisite control of membrane interactions with such substrates.	phospholipid bilayers	4-25	phenylalanine hydroxylase	Homo sapiens	46-48
33761262-2	2021	For phospholipid bilayers, the large range of pH- and ionic strength-dependent surface charge densities adopted by titanium dioxide and other oxidic surfaces leads to a rich landscape of phenomena that provides exquisite control of membrane interactions with such substrates.	titanium dioxide	115-131	phenylalanine hydroxylase	Homo sapiens	46-48
33823042-6	2021	We observed reduced fronto-temporal functional connectivity in patients with PE compared to patients without PE between the right pMTG and the right and left IFG of the PH-network.	pmtg	130-134	phenylalanine hydroxylase	Homo sapiens	169-171
33790391-9	2021	Finally, we compare our results with those of a FLEWS constructed directly from water level data and find that FLEWS via PH creates fewer false alarms than the conventional technique.	Water	80-85	phenylalanine hydroxylase	Homo sapiens	121-123
33823348-4	2021	The Langmuir maximum adsorption capacity of the adsorbent at a pH of 5.0 and a temperature of 30  C is 1057.3 mg/g (mercuric nitrate) and 773.29 mg/g (mercuric chloride), respectively.	Mercury(II) nitrate	116-132	phenylalanine hydroxylase	Homo sapiens	63-65
33823348-7	2021	The chemical species of Hg-containing ions at different pH and temperatures was studied.	Mercury	24-26	phenylalanine hydroxylase	Homo sapiens	56-58
33800986-3	2021	Regarding the physicochemical parameters, only ash content, pH and L* values were affected by NaCl replacement.	Sodium Chloride	94-98	phenylalanine hydroxylase	Homo sapiens	60-62
33808760-4	2021	Here, we report that 3-hydroxyquinolin-2(1H)-one derivatives can act as protectors of hPAH enzyme activity.	3-hydroxyquinolin-2(1h)-	21-45	phenylalanine hydroxylase	Homo sapiens	86-90
33798520-3	2021	The adsorption of toluene and ethylbenzene on the MSW-BC was mildly dependent on the pH, and the peak adsorption ability (44-47 mug/g) was recorded at a baseline pH of ~8 in mono and dual contaminant system.	Toluene	18-25	phenylalanine hydroxylase	Homo sapiens	85-87
33798520-3	2021	The adsorption of toluene and ethylbenzene on the MSW-BC was mildly dependent on the pH, and the peak adsorption ability (44-47 mug/g) was recorded at a baseline pH of ~8 in mono and dual contaminant system.	Toluene	18-25	phenylalanine hydroxylase	Homo sapiens	162-164
33798520-3	2021	The adsorption of toluene and ethylbenzene on the MSW-BC was mildly dependent on the pH, and the peak adsorption ability (44-47 mug/g) was recorded at a baseline pH of ~8 in mono and dual contaminant system.	ethylbenzene	30-42	phenylalanine hydroxylase	Homo sapiens	85-87
33798520-3	2021	The adsorption of toluene and ethylbenzene on the MSW-BC was mildly dependent on the pH, and the peak adsorption ability (44-47 mug/g) was recorded at a baseline pH of ~8 in mono and dual contaminant system.	ethylbenzene	30-42	phenylalanine hydroxylase	Homo sapiens	162-164
33808830-0	2021	Monovalent Salt and pH-Induced Gelation of Oxidised Cellulose Nanofibrils and Starch Networks: Combining Rheology and Small-Angle X-ray Scattering.	Starch	78-84	phenylalanine hydroxylase	Homo sapiens	20-22
33808830-1	2021	Water quality parameters such as salt content and various pH environments can alter the stability of gels as well as their rheological properties.	Water	0-5	phenylalanine hydroxylase	Homo sapiens	58-60
33808830-5	2021	However, at lower pH (4.0), the stiffness and viscosity of the OCNF and OCNF:starch gels appeared to increase due to proton-induced fibrillar interactions.	Starch	77-83	phenylalanine hydroxylase	Homo sapiens	18-20
33802968-0	2021	Highly Sensitive Magnesium-Doped ZnO Nanorod pH Sensors Based on Electrolyte-Insulator-Semiconductor (EIS) Sensors.	Magnesium	17-26	phenylalanine hydroxylase	Homo sapiens	45-47
33802968-0	2021	Highly Sensitive Magnesium-Doped ZnO Nanorod pH Sensors Based on Electrolyte-Insulator-Semiconductor (EIS) Sensors.	Zinc Oxide	33-36	phenylalanine hydroxylase	Homo sapiens	45-47
33802968-3	2021	The results indicated that the ZnO nanorods doped with 3% Mg had a high hydrogen ion sensitivity (83.77 mV/pH), linearity (96.06%), hysteresis (3 mV), and drift (0.218 mV/h) due to the improved crystalline quality and the surface hydroxyl group role of ZnO.	Zinc Oxide	31-34	phenylalanine hydroxylase	Homo sapiens	107-109
33802968-3	2021	The results indicated that the ZnO nanorods doped with 3% Mg had a high hydrogen ion sensitivity (83.77 mV/pH), linearity (96.06%), hysteresis (3 mV), and drift (0.218 mV/h) due to the improved crystalline quality and the surface hydroxyl group role of ZnO.	Magnesium	58-60	phenylalanine hydroxylase	Homo sapiens	107-109
33778252-4	2021	The sensor array is composed of pH indicators and aniline dyes from classical spot tests, which enabled molecular recognition of a variety of aldehydes, ketones, and carboxylic acids as demonstrated by hierarchical clustering and principal component analyses.	Aldehydes	142-151	phenylalanine hydroxylase	Homo sapiens	32-34
33778252-4	2021	The sensor array is composed of pH indicators and aniline dyes from classical spot tests, which enabled molecular recognition of a variety of aldehydes, ketones, and carboxylic acids as demonstrated by hierarchical clustering and principal component analyses.	Ketones	153-160	phenylalanine hydroxylase	Homo sapiens	32-34
33778252-4	2021	The sensor array is composed of pH indicators and aniline dyes from classical spot tests, which enabled molecular recognition of a variety of aldehydes, ketones, and carboxylic acids as demonstrated by hierarchical clustering and principal component analyses.	Carboxylic Acids	166-182	phenylalanine hydroxylase	Homo sapiens	32-34
33031611-0	2021	Reversible silylium transfer between P-H and Si-H donors.	silylium	11-19	phenylalanine hydroxylase	Homo sapiens	37-40
33031611-3	2021	The resulting Et3Si+ ion remains associated with the Mo complex, stabilized by eta1-P-H donation, yet undergoes rapid exchange with an eta1-Si-H adduct of free silane in solution.	et3si	14-19	phenylalanine hydroxylase	Homo sapiens	84-87
33031611-3	2021	The resulting Et3Si+ ion remains associated with the Mo complex, stabilized by eta1-P-H donation, yet undergoes rapid exchange with an eta1-Si-H adduct of free silane in solution.	Silicon	17-19	phenylalanine hydroxylase	Homo sapiens	84-87
33032220-1	2021	It has not been well understood that the influences of pH and accompanying anions on the toxicity of selenate (Se(VI)).	Selenic Acid	101-109	phenylalanine hydroxylase	Homo sapiens	55-57
33032220-2	2021	The influences of pH and major anions on Se(VI) toxicity to wheat root elongation were determined and modeled based on the biotic ligand model (BLM) and free ion activity model (FIAM) concepts.	se(vi)	41-47	phenylalanine hydroxylase	Homo sapiens	18-20
33032220-4	2021	The EC50{SeO42-} values increased from 133 to 203 muM while the EC50{HSeO4-} values sharply decreased from 210 to 0.102 nM with the pH increasing from 4.5 to 8.0.	hseo4	69-74	phenylalanine hydroxylase	Homo sapiens	132-134
33032220-5	2021	The effect of pH on Se(VI) toxicity could be explained by the changes of Se(VI) species in different pH solutions as SeO42- and HSeO4-were differently toxic to wheat root elongation.	seo42	117-122	phenylalanine hydroxylase	Homo sapiens	14-16
33032220-5	2021	The effect of pH on Se(VI) toxicity could be explained by the changes of Se(VI) species in different pH solutions as SeO42- and HSeO4-were differently toxic to wheat root elongation.	seo42	117-122	phenylalanine hydroxylase	Homo sapiens	101-103
33032220-5	2021	The effect of pH on Se(VI) toxicity could be explained by the changes of Se(VI) species in different pH solutions as SeO42- and HSeO4-were differently toxic to wheat root elongation.	hseo4	128-133	phenylalanine hydroxylase	Homo sapiens	14-16
33032220-5	2021	The effect of pH on Se(VI) toxicity could be explained by the changes of Se(VI) species in different pH solutions as SeO42- and HSeO4-were differently toxic to wheat root elongation.	hseo4	128-133	phenylalanine hydroxylase	Homo sapiens	101-103
33237230-10	2020	The pH values for calcium hydroxide paste were higher than bioceramic paste at 1, 24, and 72 h (p<0.05).	Calcium Hydroxide	18-35	phenylalanine hydroxylase	Homo sapiens	4-6
33237230-15	2020	The new calcium silicate-based canal dressing presented alkaline pH, high calcium release, and acceptable radiopacity.	calcium silicate	8-24	phenylalanine hydroxylase	Homo sapiens	65-67
33237230-15	2020	The new calcium silicate-based canal dressing presented alkaline pH, high calcium release, and acceptable radiopacity.	Calcium	8-15	phenylalanine hydroxylase	Homo sapiens	65-67
32322939-5	2020	PH was defined as hypoparathormonemia (<=12 pg/mL) or the need for calcium/vitamin D supplementation to achieve normal calcium levels for more than 12 months.	Calcium	67-74	phenylalanine hydroxylase	Homo sapiens	0-2
32322939-5	2020	PH was defined as hypoparathormonemia (<=12 pg/mL) or the need for calcium/vitamin D supplementation to achieve normal calcium levels for more than 12 months.	Vitamin D	75-84	phenylalanine hydroxylase	Homo sapiens	0-2
32322939-5	2020	PH was defined as hypoparathormonemia (<=12 pg/mL) or the need for calcium/vitamin D supplementation to achieve normal calcium levels for more than 12 months.	Calcium	119-126	phenylalanine hydroxylase	Homo sapiens	0-2
34979171-7	2022	The correlation analysis between the soil properties and rate constants of the model showed that the pH, clay, and amorphous Fe/Al oxides might be the key factors controlling the aging and reduction processes of Cr(VI), and the OM and CEC might greatly affect the aging process of Cr(III).	Chromium	212-214	phenylalanine hydroxylase	Homo sapiens	101-103
34979171-7	2022	The correlation analysis between the soil properties and rate constants of the model showed that the pH, clay, and amorphous Fe/Al oxides might be the key factors controlling the aging and reduction processes of Cr(VI), and the OM and CEC might greatly affect the aging process of Cr(III).	Chromium	281-283	phenylalanine hydroxylase	Homo sapiens	101-103
34810009-10	2022	The impacts of environmental factors such as pH and co-existing ions on As(III)/As(V) removal, have been discussed.	Arsenic	72-74	phenylalanine hydroxylase	Homo sapiens	45-47
34847429-0	2022	Construction of synergistic pH/H2O2-responsive prodrug for prolonging blood circulation and accelerating cellular internalization.	Hydrogen Peroxide	31-35	phenylalanine hydroxylase	Homo sapiens	28-30
34847429-2	2022	The shielding group (5"-DFUR) was found to be effective in prolonging circulation at physiological pH 7.4 and improving accumulation in the acidic microenvironment of the tumor.	doxifluridine	21-28	phenylalanine hydroxylase	Homo sapiens	99-101
34958905-3	2022	VFA production at pH 10 increased up to 30300 mgCOD/L (yield of 630 mg COD/gVSfed) but reduced over time to  10000 mgCOD/L.	Fatty Acids, Volatile	0-3	phenylalanine hydroxylase	Homo sapiens	18-20
34958905-4	2022	Lowering pH to 9 led to the restoration of VFA production with a maximum of 32000 mg COD/L (676 mg COD/g VSfed) due to changes in microbial structure.	Fatty Acids, Volatile	43-46	phenylalanine hydroxylase	Homo sapiens	9-11
34958905-5	2022	VFA was composed mainly of acetic acid, but propionic acid increased at pH 9.	propionic acid	44-58	phenylalanine hydroxylase	Homo sapiens	72-74
34894599-0	2022	Electrografted anthraquinone to monitor pH at the biofilm-anode interface in a wastewater microbial fuel cell.	Anthraquinones	15-28	phenylalanine hydroxylase	Homo sapiens	40-42
34894599-1	2022	Electrografted anthraquinone on graphite was used as a probe to monitor the pH change at the biofilm-electrode interface at the anode of a microbial fuel cell inoculated with wastewater.	Anthraquinones	15-28	phenylalanine hydroxylase	Homo sapiens	76-78
34894599-1	2022	Electrografted anthraquinone on graphite was used as a probe to monitor the pH change at the biofilm-electrode interface at the anode of a microbial fuel cell inoculated with wastewater.	Graphite	32-40	phenylalanine hydroxylase	Homo sapiens	76-78
34894599-2	2022	The grafting procedure was optimized so that the pH-dependent electrochemical response of the grafted quinone did not overlay with that of the electroactive biofilm.	quinone	102-109	phenylalanine hydroxylase	Homo sapiens	49-51
34894599-3	2022	The variation of the formal potential of the grafted quinone as a function of pH was linear over the pH range 1-10 with a slope of - 64 mV.	quinone	53-60	phenylalanine hydroxylase	Homo sapiens	78-80
34894599-3	2022	The variation of the formal potential of the grafted quinone as a function of pH was linear over the pH range 1-10 with a slope of - 64 mV.	quinone	53-60	phenylalanine hydroxylase	Homo sapiens	101-103
34546526-1	2022	The orthodontic kinetic release of metal ions was studied in order to have a conclusive in vivo data for variation of metal ion concentrations with time (month) at normal oral temperature 37 C, which affects the saliva quality and quantity, pH, and chemical and physical characteristics of food and liquid.	Metals	118-123	phenylalanine hydroxylase	Homo sapiens	241-243
34546526-3	2022	The kinetic release experiment of the metal ion concentrations (nickel, chromium, titanium, iron, and copper) in the saliva uptakes follows a pseudo-second-order kinetic model; the release rate of metal ions was in series Fe2+ > Ti2+ > Ni2+ > Cu2+ > Cr3+, and the highest saliva pH and flow rate were detected after 1 month for fixed orthodontics appliance was (7.16 +- 0.55) and (0.88 +- 0.55) respectively.	Metals	38-43	phenylalanine hydroxylase	Homo sapiens	279-281
34546526-3	2022	The kinetic release experiment of the metal ion concentrations (nickel, chromium, titanium, iron, and copper) in the saliva uptakes follows a pseudo-second-order kinetic model; the release rate of metal ions was in series Fe2+ > Ti2+ > Ni2+ > Cu2+ > Cr3+, and the highest saliva pH and flow rate were detected after 1 month for fixed orthodontics appliance was (7.16 +- 0.55) and (0.88 +- 0.55) respectively.	Copper	102-108	phenylalanine hydroxylase	Homo sapiens	279-281
34546526-3	2022	The kinetic release experiment of the metal ion concentrations (nickel, chromium, titanium, iron, and copper) in the saliva uptakes follows a pseudo-second-order kinetic model; the release rate of metal ions was in series Fe2+ > Ti2+ > Ni2+ > Cu2+ > Cr3+, and the highest saliva pH and flow rate were detected after 1 month for fixed orthodontics appliance was (7.16 +- 0.55) and (0.88 +- 0.55) respectively.	Metals	197-202	phenylalanine hydroxylase	Homo sapiens	279-281
34904389-1	2022	AIMS: The relationship between insulin resistance (IR) and glucose intolerance with pulmonary hypertension (PH) has been suggested in recent investigations.	Glucose	59-66	phenylalanine hydroxylase	Homo sapiens	108-110
34461510-5	2022	A favourable reduction of pH and a betterment of parameters related to colour were detected in wines from iron deficient subzones.	Iron	106-110	phenylalanine hydroxylase	Homo sapiens	26-28
34656000-1	2022	Previous studies have noted lower L* (lightness) values for both dark-cutting beef and normal-pH beef enhanced with lactate.	Lactic Acid	116-123	phenylalanine hydroxylase	Homo sapiens	94-96
34555612-1	2022	The recovery of metal(loid)s from municipal solid waste (MSW) samples <10 years old and >10 years old was investigated using a series of pH-dependence leaching batch tests ranging between pH 2 and 10.	Metalloids	16-28	phenylalanine hydroxylase	Homo sapiens	188-190
34555612-3	2022	The Visual MINTEQ geochemical software was then used to model the metal(loid)s release in the presence of different HA concentrations ranging from 28 mg/L to 100 mg/L, which can be found in landfill sites and pH ranging from 2 to 10.	Metals	66-71	phenylalanine hydroxylase	Homo sapiens	209-211
34633489-3	2022	Holmium laser fragmentation of calcium oxalate stones produces calcium carbonate solubility of which is dependent on pH, citrate, and phosphate.	Holmium	0-7	phenylalanine hydroxylase	Homo sapiens	117-119
34633489-3	2022	Holmium laser fragmentation of calcium oxalate stones produces calcium carbonate solubility of which is dependent on pH, citrate, and phosphate.	Calcium Oxalate	31-46	phenylalanine hydroxylase	Homo sapiens	117-119
34633489-3	2022	Holmium laser fragmentation of calcium oxalate stones produces calcium carbonate solubility of which is dependent on pH, citrate, and phosphate.	Calcium Carbonate	63-80	phenylalanine hydroxylase	Homo sapiens	117-119
34757181-7	2022	The dissolution rate decreases when: 1) citrate is consumed by the reaction with the released Al cations; 2) the pH increases during a reaction in poorly buffered solutions; 3) the dissolution products are accumulated; 4) fibers are not fully wetted with the fluid.	Citric Acid	40-47	phenylalanine hydroxylase	Homo sapiens	113-115
34757181-7	2022	The dissolution rate decreases when: 1) citrate is consumed by the reaction with the released Al cations; 2) the pH increases during a reaction in poorly buffered solutions; 3) the dissolution products are accumulated; 4) fibers are not fully wetted with the fluid.	Aluminum	94-96	phenylalanine hydroxylase	Homo sapiens	113-115
34964593-6	2022	We applied SLEEQ to evaluate the endosomal escape behavior of two pH-responsive nanoparticles: the first with a poly(2-diisopropylamino ethyl methacrylate) (PDPAEMA) core and the second with 1:1 ratio of poly(2-diethylamino ethyl methacrylate) (PDEAEMA) and PDPAEMA.	poly(2-(diisopropylamino)ethyl methacrylate)	112-155	phenylalanine hydroxylase	Homo sapiens	66-68
34964593-6	2022	We applied SLEEQ to evaluate the endosomal escape behavior of two pH-responsive nanoparticles: the first with a poly(2-diisopropylamino ethyl methacrylate) (PDPAEMA) core and the second with 1:1 ratio of poly(2-diethylamino ethyl methacrylate) (PDEAEMA) and PDPAEMA.	poly(2-(diisopropylamino)ethyl methacrylate)	157-164	phenylalanine hydroxylase	Homo sapiens	66-68
34793937-6	2022	Decreased lamotrigine solubility with increasing pH (from 1.37+-0.09 (pH=1) to 0.22+-0.03 mg/mL (pH=7)) was obtained.	Lamotrigine	10-21	phenylalanine hydroxylase	Homo sapiens	49-51
34793937-6	2022	Decreased lamotrigine solubility with increasing pH (from 1.37+-0.09 (pH=1) to 0.22+-0.03 mg/mL (pH=7)) was obtained.	Lamotrigine	10-21	phenylalanine hydroxylase	Homo sapiens	70-72
34793937-6	2022	Decreased lamotrigine solubility with increasing pH (from 1.37+-0.09 (pH=1) to 0.22+-0.03 mg/mL (pH=7)) was obtained.	Lamotrigine	10-21	phenylalanine hydroxylase	Homo sapiens	97-99
34425273-1	2022	HYPOTHESIS: Sodium-montmorillonite (Na-Mt) particles are geometrically anisometric that carry a pH dependent anisotropic surface charge.	sodium-montmorillonite	12-34	phenylalanine hydroxylase	Homo sapiens	96-98
34695763-0	2022	Surface evolution of aluminosilicate glass fibers during dissolution: Influence of pH, solid-to-solution ratio and organic treatment.	aluminosilicate	21-36	phenylalanine hydroxylase	Homo sapiens	83-85
34695763-9	2022	That is, dissolution is controlled by: a SiO2 rich surface layer at pH < 4.5; by adsorption of an Al and Al-Si mixed surface layer at 5 < pH < 11 and by divalent cation adsorption and formation of secondary phases (silicates, hydroxides) at pH ~ 13.	Silicon Dioxide	41-45	phenylalanine hydroxylase	Homo sapiens	68-70
34482146-3	2022	Additionally, the performance of La-SSBC was stable even at wider range of pH level, the existence of abundant active anions, and recycling experiments.	la-ssbc	33-40	phenylalanine hydroxylase	Homo sapiens	75-77
34474952-5	2022	By data optimization, we determined the most suitable conditions for electrochemical oxidation of canagliflozin, namely 50 microm cell size, 300 mM electrolyte concentration, 0.1 mL/h electrolyte flow rate, and electrolyte pH = 4.	Canagliflozin	98-111	phenylalanine hydroxylase	Homo sapiens	223-225
34979171-4	2022	The results of correlation analysis between EC10 and soil properties showed that the toxicity of Cr was affected by pH, organic matter (OM), clay, cation exchange capacity (CEC), and amorphous Fe oxides.	Chromium	97-99	phenylalanine hydroxylase	Homo sapiens	116-118
34424477-5	2022	When the pH was 7 and the rainfall intensity was 80 mL/h, the increase of leaching time contributed to the rapidly decreased amount of manganese released, and the leaching process reached equilibrium gradually.	Manganese	135-144	phenylalanine hydroxylase	Homo sapiens	9-11
34715338-3	2022	To systematically understand the existing status and lay a foundation for promoting the technology, the chemical mechanism of hydrothermal hydrolysis of algal biomass is elaborated in this paper, and the influences of temperature, residence time, total solid content, and pH, on the biomethane production of hydrolyzed algal biomass are summarized.	biomethane	283-293	phenylalanine hydroxylase	Homo sapiens	272-274
34715504-0	2022	Design of doxorubicin encapsulated pH-/thermo-responsive and cationic shell-crosslinked magnetic drug delivery system.	Doxorubicin	10-21	phenylalanine hydroxylase	Homo sapiens	35-37
34715504-9	2022	A pH (54.8% release in 48 h; pH = 5.4) and temperature (51.0% release in 48 h; 42  C)-dependent release of DOX was observed, displaying a Korsmeyer-Peppas kinetics model at low pH and Weibull model at high temperatures.	Doxorubicin	107-110	phenylalanine hydroxylase	Homo sapiens	2-4
34715504-9	2022	A pH (54.8% release in 48 h; pH = 5.4) and temperature (51.0% release in 48 h; 42  C)-dependent release of DOX was observed, displaying a Korsmeyer-Peppas kinetics model at low pH and Weibull model at high temperatures.	Doxorubicin	107-110	phenylalanine hydroxylase	Homo sapiens	29-31
34715504-9	2022	A pH (54.8% release in 48 h; pH = 5.4) and temperature (51.0% release in 48 h; 42  C)-dependent release of DOX was observed, displaying a Korsmeyer-Peppas kinetics model at low pH and Weibull model at high temperatures.	Doxorubicin	107-110	phenylalanine hydroxylase	Homo sapiens	177-179
34874161-4	2021	In an aqueous NaCl solution at pH 2, for example, the ratio of the current at "ON" state and that at "OFF" state can be about 800 and 200 for 1 and 100 mM, respectively.	nacl solution	14-27	phenylalanine hydroxylase	Homo sapiens	31-33
34952194-1	2022	Phenylalanine hydroxylase (PAH) is involved in immune defence reactions by providing the starting material, tyrosine, to synthesise catecholamines and melanin.	Tyrosine	108-116	phenylalanine hydroxylase	Homo sapiens	0-25
34952194-1	2022	Phenylalanine hydroxylase (PAH) is involved in immune defence reactions by providing the starting material, tyrosine, to synthesise catecholamines and melanin.	Tyrosine	108-116	phenylalanine hydroxylase	Homo sapiens	27-30
34952194-1	2022	Phenylalanine hydroxylase (PAH) is involved in immune defence reactions by providing the starting material, tyrosine, to synthesise catecholamines and melanin.	Catecholamines	132-146	phenylalanine hydroxylase	Homo sapiens	0-25
34952194-1	2022	Phenylalanine hydroxylase (PAH) is involved in immune defence reactions by providing the starting material, tyrosine, to synthesise catecholamines and melanin.	Catecholamines	132-146	phenylalanine hydroxylase	Homo sapiens	27-30
34952194-1	2022	Phenylalanine hydroxylase (PAH) is involved in immune defence reactions by providing the starting material, tyrosine, to synthesise catecholamines and melanin.	Melanins	151-158	phenylalanine hydroxylase	Homo sapiens	0-25
34952194-1	2022	Phenylalanine hydroxylase (PAH) is involved in immune defence reactions by providing the starting material, tyrosine, to synthesise catecholamines and melanin.	Melanins	151-158	phenylalanine hydroxylase	Homo sapiens	27-30
34952194-2	2022	PAH is an important metabolic enzyme of aromatic amino acids and the rate-limiting enzyme in the hydroxylation of amino acid phenylalanine to tyrosine.	Amino Acids, Aromatic	40-60	phenylalanine hydroxylase	Homo sapiens	0-3
34952194-2	2022	PAH is an important metabolic enzyme of aromatic amino acids and the rate-limiting enzyme in the hydroxylation of amino acid phenylalanine to tyrosine.	Phenylalanine	125-138	phenylalanine hydroxylase	Homo sapiens	0-3
34952194-2	2022	PAH is an important metabolic enzyme of aromatic amino acids and the rate-limiting enzyme in the hydroxylation of amino acid phenylalanine to tyrosine.	Tyrosine	142-150	phenylalanine hydroxylase	Homo sapiens	0-3
34755446-2	2022	This work introduces a highly efficient, regenerable membrane for the removal of PAHs from water, featuring excellent filter performance and pH-driven release, thanks to the integration of a cavitand receptor in electrospun polyacrylonitrile (PAN) fibers.	Polycyclic Aromatic Hydrocarbons	81-85	phenylalanine hydroxylase	Homo sapiens	141-143
34755446-7	2022	The regeneration of the membrane is performed by exploiting the pH-driven conformational switching of the cavitand between the vase form, where the PAHs uptake takes place, to the kite one, where the PAHs release occurs.	Polycyclic Aromatic Hydrocarbons	148-152	phenylalanine hydroxylase	Homo sapiens	64-66
34969342-2	2021	In recent years, the pH-driven method has received considerable attention due to its unique characteristics of low energy and organic solvent-free during the construction of biopolymer-based nanoencapsulation.	Biopolymers	174-184	phenylalanine hydroxylase	Homo sapiens	21-23
34898211-8	2021	We show that monomer attraction is driven mainly by molecular anisotropic dipole-dipole interactions that increase with increasing pH.	dipole-dipole	74-87	phenylalanine hydroxylase	Homo sapiens	131-133
34957700-0	2022	Amorphous/Crystalline Heterophase Ruthenium Nanosheets for pH-Universal Hydrogen Evolution.	Ruthenium	34-43	phenylalanine hydroxylase	Homo sapiens	59-61
34957700-0	2022	Amorphous/Crystalline Heterophase Ruthenium Nanosheets for pH-Universal Hydrogen Evolution.	Hydrogen	72-80	phenylalanine hydroxylase	Homo sapiens	59-61
34957700-6	2022	Accordingly, electrochemical measurements demonstrate that the amorphous/crystalline heterophase Ru exhibits improved hydrogen evolution efficiency as compared with pure amorphous Ru and pure crystalline Ru, at pH-universal conditions.	Ruthenium	97-99	phenylalanine hydroxylase	Homo sapiens	211-213
34957700-6	2022	Accordingly, electrochemical measurements demonstrate that the amorphous/crystalline heterophase Ru exhibits improved hydrogen evolution efficiency as compared with pure amorphous Ru and pure crystalline Ru, at pH-universal conditions.	Hydrogen	118-126	phenylalanine hydroxylase	Homo sapiens	211-213
34957700-6	2022	Accordingly, electrochemical measurements demonstrate that the amorphous/crystalline heterophase Ru exhibits improved hydrogen evolution efficiency as compared with pure amorphous Ru and pure crystalline Ru, at pH-universal conditions.	Ruthenium	204-206	phenylalanine hydroxylase	Homo sapiens	211-213
34186408-1	2021	Catalytic reduction by alcohols over clay minerals works efficiently under a wide range of pH and represents an emerging approach to control Cr(VI) contamination.	Alcohols	23-31	phenylalanine hydroxylase	Homo sapiens	91-93
34426347-3	2021	This review attempts to summarize and discuss the state of the art in the treatment of soils contaminated with recalcitrant organic contaminants by using ozone, emphasizing the influence of operating conditions, such as the content and age of soil organic matter, grain size, moisture content, pH, and ozone dose.	Ozone	154-159	phenylalanine hydroxylase	Homo sapiens	294-296
34874591-3	2021	SAXS experiments have shown that lipoplexes based on the ionizable lipid 2-dioleyloxy-N,N-dimethyl-3-aminopropane (DODMA), under a certain range of conditions, have a lamellar structure, where lipid bilayers are separated by mRNA-rich layers, with an overall periodicity or spacing between 6.5 and 8.0 nm and a complex pH-dependence.	lipid 2-dioleyloxy-n,n-dimethyl-3-aminopropane	67-113	phenylalanine hydroxylase	Homo sapiens	319-321
34874591-3	2021	SAXS experiments have shown that lipoplexes based on the ionizable lipid 2-dioleyloxy-N,N-dimethyl-3-aminopropane (DODMA), under a certain range of conditions, have a lamellar structure, where lipid bilayers are separated by mRNA-rich layers, with an overall periodicity or spacing between 6.5 and 8.0 nm and a complex pH-dependence.	DODMA	115-120	phenylalanine hydroxylase	Homo sapiens	319-321
34874591-3	2021	SAXS experiments have shown that lipoplexes based on the ionizable lipid 2-dioleyloxy-N,N-dimethyl-3-aminopropane (DODMA), under a certain range of conditions, have a lamellar structure, where lipid bilayers are separated by mRNA-rich layers, with an overall periodicity or spacing between 6.5 and 8.0 nm and a complex pH-dependence.	Lipid Bilayers	193-207	phenylalanine hydroxylase	Homo sapiens	319-321
34874591-7	2021	We observe also that at high pH levels DODMA lipids undergo a gradual shift towards the hydrophobic part of the bilayer.	DODMA	39-44	phenylalanine hydroxylase	Homo sapiens	29-31
34605141-0	2021	Interfacial Super-Assembly of Ordered Mesoporous Carbon-Silica/AAO Hybrid Membrane with Enhanced Permselectivity for Temperature- and pH-Regulated Smart Ion Transport.	mesoporous	38-48	phenylalanine hydroxylase	Homo sapiens	134-136
34605141-0	2021	Interfacial Super-Assembly of Ordered Mesoporous Carbon-Silica/AAO Hybrid Membrane with Enhanced Permselectivity for Temperature- and pH-Regulated Smart Ion Transport.	Carbon	49-55	phenylalanine hydroxylase	Homo sapiens	134-136
34605141-0	2021	Interfacial Super-Assembly of Ordered Mesoporous Carbon-Silica/AAO Hybrid Membrane with Enhanced Permselectivity for Temperature- and pH-Regulated Smart Ion Transport.	Silicon Dioxide	56-62	phenylalanine hydroxylase	Homo sapiens	134-136
34605141-0	2021	Interfacial Super-Assembly of Ordered Mesoporous Carbon-Silica/AAO Hybrid Membrane with Enhanced Permselectivity for Temperature- and pH-Regulated Smart Ion Transport.	4,6-DIDEOXY-4-{[4-[(4-O-HEXOPYRANOSYLHEXOPYRANOSYL)OXY]-5,6-DIHYDROXY-3-(HYDROXYMETHYL)CYCLOHEX-2-EN-1-YL]AMINO}HEXOPYRANOSYL-(1->4)HEXOPYRANOSYL-(1->4)HEXOPYRANOSE	63-66	phenylalanine hydroxylase	Homo sapiens	134-136
34605141-4	2021	Here, we fabricate a new mesoporous carbon-silica/anodized aluminum (MCS/AAO) nanofluidic device with enhanced permselectivity for temperature- and pH-regulated energy generation.	mesoporous	25-35	phenylalanine hydroxylase	Homo sapiens	148-150
34605141-4	2021	Here, we fabricate a new mesoporous carbon-silica/anodized aluminum (MCS/AAO) nanofluidic device with enhanced permselectivity for temperature- and pH-regulated energy generation.	Carbon	36-42	phenylalanine hydroxylase	Homo sapiens	148-150
34605141-4	2021	Here, we fabricate a new mesoporous carbon-silica/anodized aluminum (MCS/AAO) nanofluidic device with enhanced permselectivity for temperature- and pH-regulated energy generation.	Aluminum	59-67	phenylalanine hydroxylase	Homo sapiens	148-150
34569192-0	2021	Construction of pH-Dependent Nanozymes with Oxygen Vacancies as the High-Efficient Reactive Oxygen Species Scavenger for Oral-Administrated Anti-Inflammatory Therapy.	Oxygen	44-50	phenylalanine hydroxylase	Homo sapiens	16-18
34569192-0	2021	Construction of pH-Dependent Nanozymes with Oxygen Vacancies as the High-Efficient Reactive Oxygen Species Scavenger for Oral-Administrated Anti-Inflammatory Therapy.	Reactive Oxygen Species	83-106	phenylalanine hydroxylase	Homo sapiens	16-18
34569192-4	2021	As expected, the obtained NiCo2 O4 @PVP exhibits pH-dependent multiple mimic enzymatic activities.	nico2 o4	26-34	phenylalanine hydroxylase	Homo sapiens	49-51
34265724-0	2021	Building the bridge between U(VI) and Ca-bentonite - Influence of concentration, ionic strength, pH, clay composition and competing ions.	u(vi)	28-33	phenylalanine hydroxylase	Homo sapiens	97-99
34265724-0	2021	Building the bridge between U(VI) and Ca-bentonite - Influence of concentration, ionic strength, pH, clay composition and competing ions.	ca-bentonite	38-50	phenylalanine hydroxylase	Homo sapiens	97-99
34265724-8	2021	The retention is reversible especially with decreasing pH (<10.5) as the aquo complex Ca2UO2(CO3)3(aq) is formed.	ca2uo2(co3)3	86-98	phenylalanine hydroxylase	Homo sapiens	55-57
34174648-0	2021	Development of pH-driven zein/tea saponin composite nanoparticles for encapsulation and oral delivery of curcumin.	Saponins	34-41	phenylalanine hydroxylase	Homo sapiens	15-17
34174648-0	2021	Development of pH-driven zein/tea saponin composite nanoparticles for encapsulation and oral delivery of curcumin.	Curcumin	105-113	phenylalanine hydroxylase	Homo sapiens	15-17
34910721-0	2021	Effects of low pH on the coral reef cryptic invertebrate communities near CO2 vents in Papua New Guinea.	Carbon Dioxide	74-77	phenylalanine hydroxylase	Homo sapiens	15-17
34705314-0	2021	Tuning Ruthenium Carbene Complexes for Selective P-H activation via Metal-Ligand Cooperation.	ruthenium carbene	7-24	phenylalanine hydroxylase	Homo sapiens	49-52
34705314-0	2021	Tuning Ruthenium Carbene Complexes for Selective P-H activation via Metal-Ligand Cooperation.	Metals	68-73	phenylalanine hydroxylase	Homo sapiens	49-52
34705314-1	2021	The use of iminophosphoryl-tethered ruthenium carbene complexes for activation of secondary phosphine P-H bonds is reported.	ruthenium carbene	36-53	phenylalanine hydroxylase	Homo sapiens	102-105
34705314-1	2021	The use of iminophosphoryl-tethered ruthenium carbene complexes for activation of secondary phosphine P-H bonds is reported.	phosphine	92-101	phenylalanine hydroxylase	Homo sapiens	102-105
34705314-3	2021	Hence, the electron-rich silyl-substituted complex undergoes cyclometallation or shift of the imine moiety after cooperative activation of the P-H bond across the M=C linkage, depending on the electronics of the applied phosphine.	Imines	94-99	phenylalanine hydroxylase	Homo sapiens	143-146
34705314-3	2021	Hence, the electron-rich silyl-substituted complex undergoes cyclometallation or shift of the imine moiety after cooperative activation of the P-H bond across the M=C linkage, depending on the electronics of the applied phosphine.	Carbon	165-166	phenylalanine hydroxylase	Homo sapiens	143-146
34705314-3	2021	Hence, the electron-rich silyl-substituted complex undergoes cyclometallation or shift of the imine moiety after cooperative activation of the P-H bond across the M=C linkage, depending on the electronics of the applied phosphine.	phosphine	220-229	phenylalanine hydroxylase	Homo sapiens	143-146
34705314-5	2021	Consistently, replacement of the trimethylsilyl (TMS) group by the electron-withdrawing 4-nitrophenyl substituent allowed for the selective cooperative P-H activation to form stable activation products.	Trimethylsilyl radical	33-47	phenylalanine hydroxylase	Homo sapiens	152-155
34705314-5	2021	Consistently, replacement of the trimethylsilyl (TMS) group by the electron-withdrawing 4-nitrophenyl substituent allowed for the selective cooperative P-H activation to form stable activation products.	tms	49-52	phenylalanine hydroxylase	Homo sapiens	152-155
34890630-0	2022	Studies on the pH-dependent solubility of various grades of calcium phosphate-based pharmaceutical excipients.	calcium phosphate	60-77	phenylalanine hydroxylase	Homo sapiens	15-17
34890630-4	2022	The study has shown that the solubility of calcium phosphates as well as their dissolution rate decreases significantly with increasing pH of dissolution fluids.	Calcium Phosphates	43-61	phenylalanine hydroxylase	Homo sapiens	136-138
34217932-3	2021	This work evaluates the role of different extraction methods (agitation, sonication at sediment pH, and sonication at alkaline pH) on the characteristics (mass, size, shape and composition) of water-mobilizable colloids from sediment of Champsanglard dam reservoir (France).	Water	193-198	phenylalanine hydroxylase	Homo sapiens	96-98
34217932-3	2021	This work evaluates the role of different extraction methods (agitation, sonication at sediment pH, and sonication at alkaline pH) on the characteristics (mass, size, shape and composition) of water-mobilizable colloids from sediment of Champsanglard dam reservoir (France).	Water	193-198	phenylalanine hydroxylase	Homo sapiens	127-129
34217932-8	2021	Concerning phosphorus, competition with hydroxide ions for sorption site or dissolution of phosphate minerals in alkaline pH caused release of dissolved P to solution and decrease of P content in recovered colloids.	Phosphates	91-100	phenylalanine hydroxylase	Homo sapiens	122-124
34217932-8	2021	Concerning phosphorus, competition with hydroxide ions for sorption site or dissolution of phosphate minerals in alkaline pH caused release of dissolved P to solution and decrease of P content in recovered colloids.	Phosphorus	153-154	phenylalanine hydroxylase	Homo sapiens	122-124
34217932-8	2021	Concerning phosphorus, competition with hydroxide ions for sorption site or dissolution of phosphate minerals in alkaline pH caused release of dissolved P to solution and decrease of P content in recovered colloids.	Phosphorus	183-184	phenylalanine hydroxylase	Homo sapiens	122-124
34174648-7	2021	Besides, the encapsulation changed the crystalline state of curcumin to amorphous, and the pH-driven mechanism was probably related to hydrogen bonding, hydrophobic and electrostatic interactions.	Curcumin	60-68	phenylalanine hydroxylase	Homo sapiens	91-93
34174648-7	2021	Besides, the encapsulation changed the crystalline state of curcumin to amorphous, and the pH-driven mechanism was probably related to hydrogen bonding, hydrophobic and electrostatic interactions.	Hydrogen	135-143	phenylalanine hydroxylase	Homo sapiens	91-93
34186408-1	2021	Catalytic reduction by alcohols over clay minerals works efficiently under a wide range of pH and represents an emerging approach to control Cr(VI) contamination.	Chromium	141-143	phenylalanine hydroxylase	Homo sapiens	91-93
34217948-0	2021	Effects of surface oxidation on the pH-dependent surface charge of oxidized aluminum gallium nitride.	aluminum gallium nitride	76-100	phenylalanine hydroxylase	Homo sapiens	36-38
34217948-7	2021	The surface is negatively charged at pH 10 and pH 12, and sufficiently charged to attract cooperative adsorption of CTAB aggregates at pH 12.	Cetrimonium	116-120	phenylalanine hydroxylase	Homo sapiens	37-39
34217948-7	2021	The surface is negatively charged at pH 10 and pH 12, and sufficiently charged to attract cooperative adsorption of CTAB aggregates at pH 12.	Cetrimonium	116-120	phenylalanine hydroxylase	Homo sapiens	47-49
34217948-7	2021	The surface is negatively charged at pH 10 and pH 12, and sufficiently charged to attract cooperative adsorption of CTAB aggregates at pH 12.	Cetrimonium	116-120	phenylalanine hydroxylase	Homo sapiens	135-137
34217948-10	2021	This suggests that the (oxidized-AlGaN)/GaN surface has a higher surface hydroxyl group density than unoxidized AlGaN, which explains the higher sensitivity for pH sensors based on (oxidized-AlGaN)/GaN structures.	poly(dG-dA)n.poly(dC-dT)n	40-43	phenylalanine hydroxylase	Homo sapiens	161-163
34217948-10	2021	This suggests that the (oxidized-AlGaN)/GaN surface has a higher surface hydroxyl group density than unoxidized AlGaN, which explains the higher sensitivity for pH sensors based on (oxidized-AlGaN)/GaN structures.	aluminum gallium nitride	112-117	phenylalanine hydroxylase	Homo sapiens	161-163
34928835-5	2021	The kinetics study revealed that equilibrium was reached after 120 min for both metals, and maximal adsorbed quantities of cadmium (76 mg/g) and iron (55 mg/g ) were obtained at pH = 10 and 8 respectively.	Cadmium	123-130	phenylalanine hydroxylase	Homo sapiens	178-180
34755756-4	2021	Body pH, temperature, and interaction of immune cells also cause metal ion leaching and lose host cell interaction and effective mineralization for better durability.	Metals	65-70	phenylalanine hydroxylase	Homo sapiens	5-7
34857271-0	2021	Mg-Fe layered double hydroxides modified titanium enhanced the adhesion of human gingival fibroblasts through regulation of local pH level.	Magnesium	0-2	phenylalanine hydroxylase	Homo sapiens	130-132
34857271-0	2021	Mg-Fe layered double hydroxides modified titanium enhanced the adhesion of human gingival fibroblasts through regulation of local pH level.	Iron	3-5	phenylalanine hydroxylase	Homo sapiens	130-132
34857271-0	2021	Mg-Fe layered double hydroxides modified titanium enhanced the adhesion of human gingival fibroblasts through regulation of local pH level.	Hydroxides	21-31	phenylalanine hydroxylase	Homo sapiens	130-132
34928835-5	2021	The kinetics study revealed that equilibrium was reached after 120 min for both metals, and maximal adsorbed quantities of cadmium (76 mg/g) and iron (55 mg/g ) were obtained at pH = 10 and 8 respectively.	Iron	145-149	phenylalanine hydroxylase	Homo sapiens	178-180
34928845-6	2021	The maximum removal efficiencies of fluoride, iron and manganese were optimized via Response surface methodology considering the independent factors in the range of MO@AA dosage (5-9 g/L), pH (4-6) and contact time (4-12 h).	Fluorides	36-44	phenylalanine hydroxylase	Homo sapiens	189-191
34928845-6	2021	The maximum removal efficiencies of fluoride, iron and manganese were optimized via Response surface methodology considering the independent factors in the range of MO@AA dosage (5-9 g/L), pH (4-6) and contact time (4-12 h).	Manganese	55-64	phenylalanine hydroxylase	Homo sapiens	189-191
34837989-1	2021	BACKGROUND: Primary hyperoxaluria (PH) is a rare inherited autosomal recessive disease caused by disturbed glyoxylate metabolism.	glyoxylic acid	107-117	phenylalanine hydroxylase	Homo sapiens	35-37
34947551-0	2021	Development and Characterization of pH-Dependent Cellulose Acetate Phthalate Nanofibers by Electrospinning Technique.	acetylcellulose	49-66	phenylalanine hydroxylase	Homo sapiens	36-38
34947551-2	2021	Cellulose acetate phthalate (CAP) was selected as a pH-sensitive and antimicrobial polymer.	cellulose acetate phthalate	0-27	phenylalanine hydroxylase	Homo sapiens	52-54
34947551-2	2021	Cellulose acetate phthalate (CAP) was selected as a pH-sensitive and antimicrobial polymer.	cellulose acetate phthalate	29-32	phenylalanine hydroxylase	Homo sapiens	52-54
34632666-0	2021	Light- and pH-regulated Water-soluble Pseudorotaxanes Comprising a Cucurbit(7)uril and a Flavylium-based Axle.	Water	24-29	phenylalanine hydroxylase	Homo sapiens	11-13
34632666-0	2021	Light- and pH-regulated Water-soluble Pseudorotaxanes Comprising a Cucurbit(7)uril and a Flavylium-based Axle.	Rotaxanes	38-53	phenylalanine hydroxylase	Homo sapiens	11-13
34632666-0	2021	Light- and pH-regulated Water-soluble Pseudorotaxanes Comprising a Cucurbit(7)uril and a Flavylium-based Axle.	uril	78-82	phenylalanine hydroxylase	Homo sapiens	11-13
34632666-0	2021	Light- and pH-regulated Water-soluble Pseudorotaxanes Comprising a Cucurbit(7)uril and a Flavylium-based Axle.	Anthocyanins	89-98	phenylalanine hydroxylase	Homo sapiens	11-13
34632666-2	2021	Association results in (2) and (3)pseudorotaxanes, which are both pH and photosensitive.	Rotaxanes	34-49	phenylalanine hydroxylase	Homo sapiens	66-68
34775754-7	2021	We adjusted the base-pairing of 5-formyluracil during the PCR amplification by changing the pH.	5-formyluracil	32-46	phenylalanine hydroxylase	Homo sapiens	92-94
34888034-3	2021	Furthermore, using 2-(18F)fluoro-2-deoxy-D-glucose positron emission tomography, we dichotomized PH patients into metabolic phenotypes of high and low right ventricle (RV) glucose uptake and followed them longitudinally.	Glucose	43-50	phenylalanine hydroxylase	Homo sapiens	97-99
34888034-3	2021	Furthermore, using 2-(18F)fluoro-2-deoxy-D-glucose positron emission tomography, we dichotomized PH patients into metabolic phenotypes of high and low right ventricle (RV) glucose uptake and followed them longitudinally.	Glucose	172-179	phenylalanine hydroxylase	Homo sapiens	97-99
34888034-4	2021	In support of metabolic alterations in PH and its progression, the high RV glucose group had higher RV systolic pressure (p < 0.001), worse RV function as measured by RV fractional area change and peak global longitudinal strain (both p < 0.05) and may be associated with poorer outcomes (33% death or transplantation in the high glucose RV uptake group compared to 7% in the low RV glucose uptake group at five years follow-up, log-ranked p = 0.07).	Glucose	75-82	phenylalanine hydroxylase	Homo sapiens	39-41
34888034-4	2021	In support of metabolic alterations in PH and its progression, the high RV glucose group had higher RV systolic pressure (p < 0.001), worse RV function as measured by RV fractional area change and peak global longitudinal strain (both p < 0.05) and may be associated with poorer outcomes (33% death or transplantation in the high glucose RV uptake group compared to 7% in the low RV glucose uptake group at five years follow-up, log-ranked p = 0.07).	Glucose	330-337	phenylalanine hydroxylase	Homo sapiens	39-41
34819582-3	2021	A potentially one-time rAAV-based delivery of PAH gene into liver to convert Phe into tyrosine (Tyr), a normal way of Phe metabolism, has now also entered the clinic.	Phenylalanine	77-80	phenylalanine hydroxylase	Homo sapiens	46-49
34819582-3	2021	A potentially one-time rAAV-based delivery of PAH gene into liver to convert Phe into tyrosine (Tyr), a normal way of Phe metabolism, has now also entered the clinic.	Tyrosine	86-94	phenylalanine hydroxylase	Homo sapiens	46-49
34819582-3	2021	A potentially one-time rAAV-based delivery of PAH gene into liver to convert Phe into tyrosine (Tyr), a normal way of Phe metabolism, has now also entered the clinic.	Tyrosine	96-99	phenylalanine hydroxylase	Homo sapiens	46-49
34819582-3	2021	A potentially one-time rAAV-based delivery of PAH gene into liver to convert Phe into tyrosine (Tyr), a normal way of Phe metabolism, has now also entered the clinic.	Phenylalanine	118-121	phenylalanine hydroxylase	Homo sapiens	46-49
34853626-4	2021	In equimolar calcium and oxalate ion concentrations with different buffer solutions, dramatically slower kinetics is observed at pH 6.0 compared to pHs 3.6 and 8.6.	Calcium	13-20	phenylalanine hydroxylase	Homo sapiens	129-131
34853626-4	2021	In equimolar calcium and oxalate ion concentrations with different buffer solutions, dramatically slower kinetics is observed at pH 6.0 compared to pHs 3.6 and 8.6.	Oxalates	25-32	phenylalanine hydroxylase	Homo sapiens	129-131
34900593-1	2021	Phenylketonuria (PKU) is an inborn error of metabolism caused by variants in the phenylalanine hydroxylase (PAH) gene and it is characterized by excessively high levels of phenylalanine in body fluids.	Phenylalanine	172-185	phenylalanine hydroxylase	Homo sapiens	81-106
34478209-0	2021	Reversible pH-Controlled Catenation of a Benzobisimidazole-based Tetranuclear Rectangle.	benzobisimidazole	41-58	phenylalanine hydroxylase	Homo sapiens	11-13
34792766-5	2022	A higher initial hydrogen peroxide dose can trigger the increase of pH, leading to increased consumption of hydrogen peroxide.	Hydrogen Peroxide	17-34	phenylalanine hydroxylase	Homo sapiens	68-70
34792766-5	2022	A higher initial hydrogen peroxide dose can trigger the increase of pH, leading to increased consumption of hydrogen peroxide.	Hydrogen Peroxide	108-125	phenylalanine hydroxylase	Homo sapiens	68-70
34699177-1	2021	The tunable nature of phosphoramidate linkers enables broad applicability as pH-triggered controlled-release platforms, particularly in the context of antibody- and small-molecule-drug conjugates (ADCs and SMDCs), where there remains a need for new linker technology.	phosphoramidic acid	22-37	phenylalanine hydroxylase	Homo sapiens	77-79
34800464-7	2022	The small variation of water chemistry (EC, DO and pH), nitrate concentration and dual nitrate isotope values in deep wells during sampling period suggested that newly supplied nitrogen in deep groundwater during rainfall events also comes from deep groundwater.	Nitrogen	177-185	phenylalanine hydroxylase	Homo sapiens	51-53
34784942-2	2021	PAH impairment causes phenylalanine accumulation in the blood and brain, with a broad spectrum of pathophysiological and neurological consequences for patients.	Phenylalanine	22-35	phenylalanine hydroxylase	Homo sapiens	0-3
34784942-1	2021	BACKGROUND: Phenylketonuria (PKU) is a rare inherited metabolic disorder caused by defects in the phenylalanine-hydroxylase gene (PAH), the enzyme catalyzing the conversion of phenylalanine to tyrosine.	Phenylalanine	176-189	phenylalanine hydroxylase	Homo sapiens	98-123
34784942-1	2021	BACKGROUND: Phenylketonuria (PKU) is a rare inherited metabolic disorder caused by defects in the phenylalanine-hydroxylase gene (PAH), the enzyme catalyzing the conversion of phenylalanine to tyrosine.	Phenylalanine	176-189	phenylalanine hydroxylase	Homo sapiens	130-133
34784942-1	2021	BACKGROUND: Phenylketonuria (PKU) is a rare inherited metabolic disorder caused by defects in the phenylalanine-hydroxylase gene (PAH), the enzyme catalyzing the conversion of phenylalanine to tyrosine.	Tyrosine	193-201	phenylalanine hydroxylase	Homo sapiens	98-123
34784942-1	2021	BACKGROUND: Phenylketonuria (PKU) is a rare inherited metabolic disorder caused by defects in the phenylalanine-hydroxylase gene (PAH), the enzyme catalyzing the conversion of phenylalanine to tyrosine.	Tyrosine	193-201	phenylalanine hydroxylase	Homo sapiens	130-133
34098435-0	2021	pH-Dependent complexation between beta-lactoglobulin and lycopene: Multi-spectroscopy, molecular docking and dynamic simulation study.	Lycopene	57-65	phenylalanine hydroxylase	Homo sapiens	0-2
34098435-1	2021	This study aims to investigate the effect of pH levels (pH 7.0 and pH 8.1) on binding ability of beta-lactoglobulin (beta-LG) with lycopene (LYC) and elucidate interaction mechanisms using multi-spectroscopy and molecular docking study.	Lycopene	131-139	phenylalanine hydroxylase	Homo sapiens	45-47
34098435-1	2021	This study aims to investigate the effect of pH levels (pH 7.0 and pH 8.1) on binding ability of beta-lactoglobulin (beta-LG) with lycopene (LYC) and elucidate interaction mechanisms using multi-spectroscopy and molecular docking study.	Lycopene	131-139	phenylalanine hydroxylase	Homo sapiens	56-58
34098435-1	2021	This study aims to investigate the effect of pH levels (pH 7.0 and pH 8.1) on binding ability of beta-lactoglobulin (beta-LG) with lycopene (LYC) and elucidate interaction mechanisms using multi-spectroscopy and molecular docking study.	Lycopene	131-139	phenylalanine hydroxylase	Homo sapiens	67-69
34098435-1	2021	This study aims to investigate the effect of pH levels (pH 7.0 and pH 8.1) on binding ability of beta-lactoglobulin (beta-LG) with lycopene (LYC) and elucidate interaction mechanisms using multi-spectroscopy and molecular docking study.	Lycopene	141-144	phenylalanine hydroxylase	Homo sapiens	45-47
34098435-1	2021	This study aims to investigate the effect of pH levels (pH 7.0 and pH 8.1) on binding ability of beta-lactoglobulin (beta-LG) with lycopene (LYC) and elucidate interaction mechanisms using multi-spectroscopy and molecular docking study.	Lycopene	141-144	phenylalanine hydroxylase	Homo sapiens	56-58
34098435-1	2021	This study aims to investigate the effect of pH levels (pH 7.0 and pH 8.1) on binding ability of beta-lactoglobulin (beta-LG) with lycopene (LYC) and elucidate interaction mechanisms using multi-spectroscopy and molecular docking study.	Lycopene	141-144	phenylalanine hydroxylase	Homo sapiens	67-69
34364243-5	2021	Based on the results of this study, it was observed that the effectiveness of ammonia removal depends on the pH and air flow rate.	Ammonia	78-85	phenylalanine hydroxylase	Homo sapiens	109-111
34934543-16	2021	Conclusion Venous pH and bicarbonate levels correlate strongly with arterial pH and bicarbonate levels, respectively, in patients with renal failure.	Bicarbonates	25-36	phenylalanine hydroxylase	Homo sapiens	77-79
34829063-4	2021	Compared with the control (no Ca added), both calcium salts resulted in deteriorative color and texture properties, and promoted pH decline, cooking loss, and lipid oxidation of sausages during manufacturing and storage.	Calcium	46-53	phenylalanine hydroxylase	Homo sapiens	129-131
34833916-3	2021	In these processes, acetylenes act as three-modal adjuvants (i) activating the pyridine ring towards P-nucleophiles, (ii) deprotonating the P-H bond and (iii) facilitating the nucleophilic addition of the P-centered anion to a heterocyclic moiety followed by the release of the selectively reduced acetylenes (E-alkenes).	Alkynes	20-30	phenylalanine hydroxylase	Homo sapiens	140-143
34510656-3	2021	Using a global meta-analysis based on 901 observations from 330 15 N-labelled studies, we show that GN differs significantly among ecosystem types, with the highest rates found in croplands, in association with higher pH which stimulates nitrifying bacteria activities.	Nitrogen	67-68	phenylalanine hydroxylase	Homo sapiens	218-220
34510656-5	2021	Soil GN increases significantly with soil total N, microbial biomass, and soil pH, but decreases significantly with carbon (C) to N ratio (C: N).	gossypolone	5-7	phenylalanine hydroxylase	Homo sapiens	79-81
34805129-4	2021	In particular, strategies that are tumor/bacteria targeted or activatable by the tumor/bacteria microenvironment such as enzyme/pH/reactive oxygen species (ROS) are summarized.	Reactive Oxygen Species	131-154	phenylalanine hydroxylase	Homo sapiens	128-130
34805129-4	2021	In particular, strategies that are tumor/bacteria targeted or activatable by the tumor/bacteria microenvironment such as enzyme/pH/reactive oxygen species (ROS) are summarized.	ros	156-159	phenylalanine hydroxylase	Homo sapiens	128-130
34772119-0	2021	Evaluation of the Influence of the Combination of pH, Chloride, and Sulfate on the Corrosion Behavior of Pipeline Steel in Soil Using Response Surface Methodology.	Steel	114-119	phenylalanine hydroxylase	Homo sapiens	50-52
34496281-0	2021	Tumor-targeting pH/redox dual-responsive nanosystem epigenetically reverses cancer drug resistance by co-delivering doxorubicin and GCN5 siRNA.	Doxorubicin	116-127	phenylalanine hydroxylase	Homo sapiens	16-18
34496281-5	2021	Herein, a hyaluronic acid-coated, pH/redox dual-responsive nanosystem (HPMSNs) is fabricated for co-delivering doxorubicin (DOX) and GCN5 siRNA (siGCN5).	Hyaluronic Acid	10-25	phenylalanine hydroxylase	Homo sapiens	34-36
34496281-5	2021	Herein, a hyaluronic acid-coated, pH/redox dual-responsive nanosystem (HPMSNs) is fabricated for co-delivering doxorubicin (DOX) and GCN5 siRNA (siGCN5).	Doxorubicin	111-122	phenylalanine hydroxylase	Homo sapiens	34-36
34496281-5	2021	Herein, a hyaluronic acid-coated, pH/redox dual-responsive nanosystem (HPMSNs) is fabricated for co-delivering doxorubicin (DOX) and GCN5 siRNA (siGCN5).	Doxorubicin	124-127	phenylalanine hydroxylase	Homo sapiens	34-36
34496281-6	2021	This nanosystem can effectively encapsulate DOX and siRNA preventing premature leakage and releasing these therapeutics intracellularly via its pH/redox dual responsiveness.	Doxorubicin	44-47	phenylalanine hydroxylase	Homo sapiens	144-146
34496281-11	2021	This nanosystem efficiently co-delivered DOX and siGCN5 into drug-resistant cancer cells and significantly inhibited the tumor growth through: (1) HA shell enhanced the cellular internalization of loaded DOX and siGCN5 via CD44-mediated targeting; (2) the pH/redox dual-responsive nanosystem released the cargos in response to the intracellular environment; (3) the released siGCN5 downregulated P-gp epigenetically.	Doxorubicin	41-44	phenylalanine hydroxylase	Homo sapiens	256-258
34631051-11	2021	Future comparative clinical studies are required to clearly define the subgroups of patients that should be treated preferably with constant or pH-dependent release formulations of mesalazine.	Mesalamine	181-191	phenylalanine hydroxylase	Homo sapiens	144-146
34912184-2	2021	Nitrazine strip measures pH levels while urea and creatinine are produced mainly in amniotic fluid and not in the maternal vagina.	Nitrazine	0-9	phenylalanine hydroxylase	Homo sapiens	25-27
34478209-4	2021	It incorporates a pH sensitive benzobisimidazole-based ligand that can be selectively protonated on its bisimidazole moieties.	benzobisimidazole	31-48	phenylalanine hydroxylase	Homo sapiens	18-20
34478209-4	2021	It incorporates a pH sensitive benzobisimidazole-based ligand that can be selectively protonated on its bisimidazole moieties.	2,2'-biimidazole	104-116	phenylalanine hydroxylase	Homo sapiens	18-20
34690229-0	2022	Influence of pH and ion components in the liquid phase on the setting reaction of carbonate apatite granules.	Carbonates	82-91	phenylalanine hydroxylase	Homo sapiens	13-15
34833408-5	2021	One of the earliest investigated local factors is the pH of wounds, studied in close relation to the local perfusion, oxygen tension, and lactate concentration.	Oxygen	118-124	phenylalanine hydroxylase	Homo sapiens	54-56
34833408-5	2021	One of the earliest investigated local factors is the pH of wounds, studied in close relation to the local perfusion, oxygen tension, and lactate concentration.	Lactic Acid	138-145	phenylalanine hydroxylase	Homo sapiens	54-56
34833408-13	2021	This review describes the close interconnections between the local lactate levels, metabolism, healing mechanisms, and pH.	Lactic Acid	67-74	phenylalanine hydroxylase	Homo sapiens	119-121
34762361-2	2021	PH is reduced and NO signaling is improved in chronically hypoxic piglets treated with the NO-arginine precursor, L-citrulline.	Arginine	94-102	phenylalanine hydroxylase	Homo sapiens	0-2
34762361-2	2021	PH is reduced and NO signaling is improved in chronically hypoxic piglets treated with the NO-arginine precursor, L-citrulline.	Citrulline	114-126	phenylalanine hydroxylase	Homo sapiens	0-2
34762361-13	2021	Nonetheless, treatment with folic acid, either singly or when combined with L-citrulline, increases NO production and inhibits PH in chronically hypoxic newborn piglets.	Folic Acid	28-38	phenylalanine hydroxylase	Homo sapiens	127-129
34762361-13	2021	Nonetheless, treatment with folic acid, either singly or when combined with L-citrulline, increases NO production and inhibits PH in chronically hypoxic newborn piglets.	Citrulline	76-88	phenylalanine hydroxylase	Homo sapiens	127-129
34762361-14	2021	Folic acid merits consideration as a therapy for PH in human infants with chronic heart and lung conditions that are associated with chronic hypoxia.	Folic Acid	0-10	phenylalanine hydroxylase	Homo sapiens	49-51
34850698-14	2021	An unstable pH can alter the chemical and microbiological aspects of water, resulting in a variation of other water quality parameters.	Water	69-74	phenylalanine hydroxylase	Homo sapiens	12-14
34850698-14	2021	An unstable pH can alter the chemical and microbiological aspects of water, resulting in a variation of other water quality parameters.	Water	110-115	phenylalanine hydroxylase	Homo sapiens	12-14
34705432-2	2021	Silica nanocapsules, embedded in one layer of the coating, are used as a host for a corrosion inhibitor and as a sensor, which detect changes of pH value and release inhibitors via an optical signal.	Silicon Dioxide	0-6	phenylalanine hydroxylase	Homo sapiens	145-147
34378279-0	2021	A Glucose-Powered Activatable Nanozyme Breaking pH and H2O2 Limitations for Treating Diabetic Infections.	Glucose	2-9	phenylalanine hydroxylase	Homo sapiens	48-50
34378279-5	2021	Nanozymes bind onto bacteria through aptamer recognition, and glucose oxidation tunes local pH down and supplements H 2 O 2  for  in situ  generation of  OH on bacteria surface.	Glucose	62-69	phenylalanine hydroxylase	Homo sapiens	92-94
34657950-3	2021	Herein, we review the latest research progress on the real-time diagnosis of related diseases based on perylene diimide probes in the aspects of bioimaging, detection of biomarkers and determination of the pH in living cells.	perylenediimide	103-119	phenylalanine hydroxylase	Homo sapiens	206-208
34690229-4	2022	The aim of this study was to set CO3Ap granules by mixing CO3Ap granules with acidic phosphate solutions and evaluate the influence of the pH and ion components of the solutions.	co3ap	33-38	phenylalanine hydroxylase	Homo sapiens	139-141
34690229-5	2022	When Na+ was the counter ion, the amount of precipitated dicalcium phosphate dihydrate (DCPD) was small and the setting ability disappeared with increasing pH of the solutions.	calcium phosphate, dibasic, dihydrate	57-86	phenylalanine hydroxylase	Homo sapiens	156-158
34690229-5	2022	When Na+ was the counter ion, the amount of precipitated dicalcium phosphate dihydrate (DCPD) was small and the setting ability disappeared with increasing pH of the solutions.	calcium phosphate, dibasic, dihydrate	88-92	phenylalanine hydroxylase	Homo sapiens	156-158
34624190-0	2021	Defect Engineering of Graphene to Modulate pH Response of Graphene Devices.	Graphite	22-30	phenylalanine hydroxylase	Homo sapiens	43-45
34835558-0	2021	Designing pH-Dependent Systems Based on Nanoscale Calcium Carbonate for the Delivery of an Antitumor Drug.	Calcium Carbonate	50-67	phenylalanine hydroxylase	Homo sapiens	10-12
34835558-2	2021	The biocompatibility of CaCO3 and dependence of its stability on pH make these materials promising transporters of therapeutic agents to sites with low pH such as a tumor tissue.	Calcium Carbonate	24-29	phenylalanine hydroxylase	Homo sapiens	65-67
34835558-2	2021	The biocompatibility of CaCO3 and dependence of its stability on pH make these materials promising transporters of therapeutic agents to sites with low pH such as a tumor tissue.	Calcium Carbonate	24-29	phenylalanine hydroxylase	Homo sapiens	152-154
34835558-4	2021	We also showed a prolonged pH-dependent release of DOX from a CaNP nanocarrier and effective inhibition of cancer cell growth by a CaCO3-and-DOX-based composite (CaNP7-DOX) in in vitro models.	Doxorubicin	51-54	phenylalanine hydroxylase	Homo sapiens	27-29
34835558-4	2021	We also showed a prolonged pH-dependent release of DOX from a CaNP nanocarrier and effective inhibition of cancer cell growth by a CaCO3-and-DOX-based composite (CaNP7-DOX) in in vitro models.	Calcium Carbonate	131-136	phenylalanine hydroxylase	Homo sapiens	27-29
34835558-4	2021	We also showed a prolonged pH-dependent release of DOX from a CaNP nanocarrier and effective inhibition of cancer cell growth by a CaCO3-and-DOX-based composite (CaNP7-DOX) in in vitro models.	Doxorubicin	141-144	phenylalanine hydroxylase	Homo sapiens	27-29
34835558-4	2021	We also showed a prolonged pH-dependent release of DOX from a CaNP nanocarrier and effective inhibition of cancer cell growth by a CaCO3-and-DOX-based composite (CaNP7-DOX) in in vitro models.	Doxorubicin	168-171	phenylalanine hydroxylase	Homo sapiens	27-29
34624190-9	2021	The overall pH-sensing characteristics of the graphene will be determined by the balance of these two mechanisms.	Graphite	46-54	phenylalanine hydroxylase	Homo sapiens	12-14
34609862-0	2021	Stochastic pH Oscillations in a Model of the Urea-Urease Reaction Confined to Lipid Vesicles.	Urea	45-49	phenylalanine hydroxylase	Homo sapiens	11-13
34609862-1	2021	The urea-urease clock reaction is a pH switch from acid to basic that can turn into a pH oscillator if it occurs inside a suitable open reactor.	Urea	4-8	phenylalanine hydroxylase	Homo sapiens	36-38
34609862-1	2021	The urea-urease clock reaction is a pH switch from acid to basic that can turn into a pH oscillator if it occurs inside a suitable open reactor.	Urea	4-8	phenylalanine hydroxylase	Homo sapiens	86-88
34597506-2	2021	However, the instability of prebiotic fatty acid-based membranes to temperature and pH seems to suggest that primitive cells could only host prebiotically relevant processes in a narrow range of nonfluctuating environmental conditions.	Fatty Acids	38-48	phenylalanine hydroxylase	Homo sapiens	84-86
34679958-10	2021	This study demonstrated that the soil microbial community and availability of oxygen significantly affected the changes in moisture content, pH, and bacterial composition during the decomposition process.	Oxygen	78-84	phenylalanine hydroxylase	Homo sapiens	141-143
34622409-3	2021	The change in pH level affects the chemical oxygen demand (COD)/biochemical oxygen demand (BOD) ratio and when it is less than 0.63, chemical treatments are more effective over the biological treatment methods such as upflow anaerobic sludge blankets (UASB).	Oxygen	44-50	phenylalanine hydroxylase	Homo sapiens	14-16
34622409-3	2021	The change in pH level affects the chemical oxygen demand (COD)/biochemical oxygen demand (BOD) ratio and when it is less than 0.63, chemical treatments are more effective over the biological treatment methods such as upflow anaerobic sludge blankets (UASB).	Oxygen	76-82	phenylalanine hydroxylase	Homo sapiens	14-16
34703723-0	2021	pH-driven enhancement of anti-tubercular drug loading on iron oxide nanoparticles for drug delivery in macrophages.	ferric oxide	57-67	phenylalanine hydroxylase	Homo sapiens	0-2
34614030-4	2021	The sensor array itself is composed of pH indicators and aniline dyes that enable molecular recognition of carboxylic acids, amines and carbonyl-containing compounds.	Carboxylic Acids	107-123	phenylalanine hydroxylase	Homo sapiens	39-41
34614030-4	2021	The sensor array itself is composed of pH indicators and aniline dyes that enable molecular recognition of carboxylic acids, amines and carbonyl-containing compounds.	Amines	125-131	phenylalanine hydroxylase	Homo sapiens	39-41
34488118-0	2021	Metabolizable pH/H2O2 dual-responsive conductive polymer nanoparticles for safe and precise chemo-photothermal therapy.	Hydrogen Peroxide	17-21	phenylalanine hydroxylase	Homo sapiens	14-16
34488118-0	2021	Metabolizable pH/H2O2 dual-responsive conductive polymer nanoparticles for safe and precise chemo-photothermal therapy.	Polymers	49-56	phenylalanine hydroxylase	Homo sapiens	14-16
34488118-5	2021	After further loading of doxorubicin (DOX), PAA@PPyCOOH@DOX demonstrates outstanding photothermal performance, as well as pH/H2O2 dual-responsive release of DOX in tumors with an acidic and overexpressed H2O2 microenvironment, resulting in superior chemo-photothermal therapeutic effects.	Doxorubicin	38-41	phenylalanine hydroxylase	Homo sapiens	122-124
34488118-5	2021	After further loading of doxorubicin (DOX), PAA@PPyCOOH@DOX demonstrates outstanding photothermal performance, as well as pH/H2O2 dual-responsive release of DOX in tumors with an acidic and overexpressed H2O2 microenvironment, resulting in superior chemo-photothermal therapeutic effects.	Hydrogen Peroxide	125-129	phenylalanine hydroxylase	Homo sapiens	122-124
34488118-5	2021	After further loading of doxorubicin (DOX), PAA@PPyCOOH@DOX demonstrates outstanding photothermal performance, as well as pH/H2O2 dual-responsive release of DOX in tumors with an acidic and overexpressed H2O2 microenvironment, resulting in superior chemo-photothermal therapeutic effects.	Doxorubicin	157-160	phenylalanine hydroxylase	Homo sapiens	122-124
34488118-5	2021	After further loading of doxorubicin (DOX), PAA@PPyCOOH@DOX demonstrates outstanding photothermal performance, as well as pH/H2O2 dual-responsive release of DOX in tumors with an acidic and overexpressed H2O2 microenvironment, resulting in superior chemo-photothermal therapeutic effects.	Hydrogen Peroxide	204-208	phenylalanine hydroxylase	Homo sapiens	122-124
34455167-2	2021	Our goal was to develop a mathematical model describing pH regulation in the interstitial fluid and to examine the contribution of hydroxyapatite dissolution and precipitation to pH regulation.	Durapatite	131-145	phenylalanine hydroxylase	Homo sapiens	179-181
34285103-10	2021	Survival rate was significantly lower in the Cpc-PH than the no-PH (p=0.002) and Ipc-PH (p=0.024) groups.	ipc	81-84	phenylalanine hydroxylase	Homo sapiens	85-87
34632237-4	2021	The effects of temperature, SL concentration, rotate speed, time, and pH on the oil removal rate were studied.	Oils	80-83	phenylalanine hydroxylase	Homo sapiens	70-72
34551042-0	2021	Biliverdin chiral derivatives as chiroptical switches for pH and metal cation sensing.	Biliverdine	0-10	phenylalanine hydroxylase	Homo sapiens	58-60
34551042-7	2021	We envision the use of current chiroptical spectroscopies in connection with chiral biliverdin derivatives as natural sensors or probes of the micro-environmental conditions, such as pH or the presence of metal ions.	Biliverdine	84-94	phenylalanine hydroxylase	Homo sapiens	183-185
34174665-5	2021	Soil parent materials, pH, organic matter, and clay particle size were the key factors influencing accumulation of arsenic, chromium, and nickel.	Arsenic	115-122	phenylalanine hydroxylase	Homo sapiens	23-25
34174665-5	2021	Soil parent materials, pH, organic matter, and clay particle size were the key factors influencing accumulation of arsenic, chromium, and nickel.	Nickel	138-144	phenylalanine hydroxylase	Homo sapiens	23-25
34805653-7	2021	They are based on direct pH jumps (addition of a base to the flavylium cation) and reverse pH jumps (addition of an acid to equilibrated solutions at higher pH values).	Anthocyanins	61-70	phenylalanine hydroxylase	Homo sapiens	25-27
34570460-2	2021	Intraoral/biofilm-tooth pH is the single parameter that has demonstrated accurate assessment of dental caries risk, reflecting the summative integrated outcome of the complicated interactions between three etiological factors, namely, microorganisms/biofilm, diet/carbohydrates, and tooth/saliva/host.	Carbohydrates	264-277	phenylalanine hydroxylase	Homo sapiens	24-26
34616544-9	2021	In conclusion, PAH is a rare but severe complication associated with busulfan chemotherapy in adults.	Busulfan	69-77	phenylalanine hydroxylase	Homo sapiens	15-18
34580324-8	2021	The parameters effective on the adsorption process for polyethylene composite and bee carcasses and losses in the presence of polyethylene glycol suggested that the adsorption percentage increased for this composite by decreasing the pH, increasing the contact time, and increasing the adsorbent.	Polyethylene	55-67	phenylalanine hydroxylase	Homo sapiens	234-236
34580324-8	2021	The parameters effective on the adsorption process for polyethylene composite and bee carcasses and losses in the presence of polyethylene glycol suggested that the adsorption percentage increased for this composite by decreasing the pH, increasing the contact time, and increasing the adsorbent.	Polyethylene Glycols	126-145	phenylalanine hydroxylase	Homo sapiens	234-236
34580324-9	2021	The highest percentage of adsorption was obtained when the pH was 2, the contact time was 120 min and the adsorbent value was 8 g/L and the initial concentration of chromium was 100 ppm.	Chromium	165-173	phenylalanine hydroxylase	Homo sapiens	59-61
34580324-10	2021	The most optimal removal percentage was achieved at the pH = 2, the contact time was 30 min, and the adsorbent value was 2 g/L, and the initial chromium concentration was 100 ppm.	Chromium	144-152	phenylalanine hydroxylase	Homo sapiens	56-58
34624190-0	2021	Defect Engineering of Graphene to Modulate pH Response of Graphene Devices.	Graphite	58-66	phenylalanine hydroxylase	Homo sapiens	43-45
34624190-1	2021	Graphene-based pH sensors are a robust, durable, sensitive, and scalable approach for the sensitive detection of pH in various environments.	Graphite	0-8	phenylalanine hydroxylase	Homo sapiens	15-17
34624190-1	2021	Graphene-based pH sensors are a robust, durable, sensitive, and scalable approach for the sensitive detection of pH in various environments.	Graphite	0-8	phenylalanine hydroxylase	Homo sapiens	113-115
34624190-2	2021	However, the mechanisms through which graphene responds to pH variations are not well-understood yet.	Graphite	38-46	phenylalanine hydroxylase	Homo sapiens	59-61
34624190-3	2021	This study provides a new look into the surface science of graphene-based pH sensors to address the existing gaps and inconsistencies among the literature concerning sensing response, the role of defects, and surface/solution interactions.	Graphite	59-67	phenylalanine hydroxylase	Homo sapiens	74-76
34624190-8	2021	Selective functionalization of the surface was utilized to uncover the dominant acid-base interactions of carboxyl and amine groups at low pH while hydroxyl groups control the high pH range sensitivity.	carboxyl	106-114	phenylalanine hydroxylase	Homo sapiens	139-141
34624190-8	2021	Selective functionalization of the surface was utilized to uncover the dominant acid-base interactions of carboxyl and amine groups at low pH while hydroxyl groups control the high pH range sensitivity.	carboxyl	106-114	phenylalanine hydroxylase	Homo sapiens	181-183
34624190-8	2021	Selective functionalization of the surface was utilized to uncover the dominant acid-base interactions of carboxyl and amine groups at low pH while hydroxyl groups control the high pH range sensitivity.	Amines	119-124	phenylalanine hydroxylase	Homo sapiens	139-141
34464086-0	2021	Indirect Potentiometric pH Detection of Weak Acids with Absolute Quantitation by a Theoretical Approach.	weak acids	40-50	phenylalanine hydroxylase	Homo sapiens	24-26
34547049-4	2021	In surface water sources, higher values of chloride (OR = 0.891, p<005), phosphates (OR = 0.452, p<0.05), pH (OR = 0.174, p<0.05) and zinc (OR = 0.001, p<0.05) were associated with lower odds of faecal coliform contamination.	Water	11-16	phenylalanine hydroxylase	Homo sapiens	106-108
34547049-9	2021	For ground water systems, higher values of pH (OR = 0.083, p<0.05), phosphates (OR = 0.092, p<0.05), turbidity (OR = 0.950, p<0.05) and chloride (OR = 0.860, p<0.05) were associated with lower odds of total coliform contamination.	Water	11-16	phenylalanine hydroxylase	Homo sapiens	43-45
34576212-6	2021	Moreover, experimental studies on the effects of cannabidiol (plant-derived, non-psychoactive cannabinoid) in animal PH models have shown that cannabidiol reduces right ventricular systolic pressure and excessive remodelling and decreases pulmonary vascular hypertrophy and pulmonary vascular resistance.	Cannabidiol	49-60	phenylalanine hydroxylase	Homo sapiens	117-119
34576212-6	2021	Moreover, experimental studies on the effects of cannabidiol (plant-derived, non-psychoactive cannabinoid) in animal PH models have shown that cannabidiol reduces right ventricular systolic pressure and excessive remodelling and decreases pulmonary vascular hypertrophy and pulmonary vascular resistance.	Cannabidiol	143-154	phenylalanine hydroxylase	Homo sapiens	117-119
34576212-8	2021	However, clinical trials are still needed to recommend the use of cannabinoids in the treatment of PH.	Cannabinoids	66-78	phenylalanine hydroxylase	Homo sapiens	99-101
34464086-1	2021	A fast response potentiometric flow-through pH sensor was applied for organic acid determination.	organic acid	70-82	phenylalanine hydroxylase	Homo sapiens	44-46
34464086-2	2021	The analyte response with the pH sensor was obtained by eluent pH modification following ion exclusion chromatography with HClO4 as an eluent.	Perchloric Acid	123-128	phenylalanine hydroxylase	Homo sapiens	30-32
34464086-4	2021	The baseline pH adjustment was successfully done with an ammonia permeation device without solution mixing, which may cause analyte dilution, dispersion, and mixing noise.	Ammonia	57-64	phenylalanine hydroxylase	Homo sapiens	13-15
34464086-5	2021	After pH adjustment, the pH response was universal to the equivalent of introduced analyte acids because the pH response was obtained by the titration of the permeant ammonia by the analytes.	Ammonia	167-174	phenylalanine hydroxylase	Homo sapiens	6-8
34464086-5	2021	After pH adjustment, the pH response was universal to the equivalent of introduced analyte acids because the pH response was obtained by the titration of the permeant ammonia by the analytes.	Ammonia	167-174	phenylalanine hydroxylase	Homo sapiens	25-27
34464086-5	2021	After pH adjustment, the pH response was universal to the equivalent of introduced analyte acids because the pH response was obtained by the titration of the permeant ammonia by the analytes.	Ammonia	167-174	phenylalanine hydroxylase	Homo sapiens	109-111
34579434-6	2021	We detected strong changes in soil pH as a reaction to the supply of peat moss, elemental sulfur, and sulfur-oxidizing bacteria.	Sulfur	90-96	phenylalanine hydroxylase	Homo sapiens	35-37
34579434-6	2021	We detected strong changes in soil pH as a reaction to the supply of peat moss, elemental sulfur, and sulfur-oxidizing bacteria.	Sulfur	102-108	phenylalanine hydroxylase	Homo sapiens	35-37
34403844-2	2021	The ammonia removal in the stripping process depends on the pH, temperature, and air supply, and in general, 10.5, 60  C, 5 L/min or more are recommended as near-optimal.	Ammonia	4-11	phenylalanine hydroxylase	Homo sapiens	60-62
34579434-7	2021	The pH of the soil when peat moss and elemental sulfur each were supplied was reduced.	Sulfur	48-54	phenylalanine hydroxylase	Homo sapiens	4-6
34403844-9	2021	The electric field improved the ammonia removal more as the pH, temperature, and air supply conditions were far from optimal.	Ammonia	32-39	phenylalanine hydroxylase	Homo sapiens	60-62
34579434-8	2021	In addition, the pH decreased faster when elemental sulfur and sulfur-oxidizing bacteria were supplied together than elemental sulfur alone, satisfying an acidic soil environment suitable for blueberry cultivation.	Sulfur	52-58	phenylalanine hydroxylase	Homo sapiens	17-19
34579434-8	2021	In addition, the pH decreased faster when elemental sulfur and sulfur-oxidizing bacteria were supplied together than elemental sulfur alone, satisfying an acidic soil environment suitable for blueberry cultivation.	Sulfur	63-69	phenylalanine hydroxylase	Homo sapiens	17-19
34579434-8	2021	In addition, the pH decreased faster when elemental sulfur and sulfur-oxidizing bacteria were supplied together than elemental sulfur alone, satisfying an acidic soil environment suitable for blueberry cultivation.	Sulfur	127-133	phenylalanine hydroxylase	Homo sapiens	17-19
34579434-9	2021	In this experiment, it is shown that peat moss, elemental sulfur, and sulfur-oxidizing bacteria are suitable for lowering soil pH.	Sulfur	58-64	phenylalanine hydroxylase	Homo sapiens	127-129
34579434-9	2021	In this experiment, it is shown that peat moss, elemental sulfur, and sulfur-oxidizing bacteria are suitable for lowering soil pH.	Sulfur	70-76	phenylalanine hydroxylase	Homo sapiens	127-129
34419920-9	2021	The dominant pressures linked to PAHs and PCBs were different, respectively local and large-scale pressures were linked to PAH bioavailable contamination, and only large-scale pressures were linked to PCB bioavailable contamination.	Polychlorinated Biphenyls	42-46	phenylalanine hydroxylase	Homo sapiens	123-126
34579434-10	2021	It was demonstrated that when elemental sulfur and sulfur-oxidizing bacteria were treated together, the pH decreased faster than when treated with peat moss.	Sulfur	40-46	phenylalanine hydroxylase	Homo sapiens	104-106
34568306-4	2021	While the polymer we selected was pH sensitive that the polymer hemisphere could degrade under acidic conditions, making it possible to release drugs in a specific pH environment, such as tumor tissues.	Polymers	10-17	phenylalanine hydroxylase	Homo sapiens	34-36
34553103-6	2021	A binding site at the terminus of an oligomer detects local information about changes in pH or anion concentration and transmits that information-in the form of a directionality switch in the hydrogen-bond chain-to a remote polarity-sensitive fluorophore.	Hydrogen	192-200	phenylalanine hydroxylase	Homo sapiens	89-91
34568306-4	2021	While the polymer we selected was pH sensitive that the polymer hemisphere could degrade under acidic conditions, making it possible to release drugs in a specific pH environment, such as tumor tissues.	Polymers	10-17	phenylalanine hydroxylase	Homo sapiens	164-166
34568306-4	2021	While the polymer we selected was pH sensitive that the polymer hemisphere could degrade under acidic conditions, making it possible to release drugs in a specific pH environment, such as tumor tissues.	Polymers	56-63	phenylalanine hydroxylase	Homo sapiens	34-36
34568306-4	2021	While the polymer we selected was pH sensitive that the polymer hemisphere could degrade under acidic conditions, making it possible to release drugs in a specific pH environment, such as tumor tissues.	Polymers	56-63	phenylalanine hydroxylase	Homo sapiens	164-166
34448568-0	2021	Correction to "pH/H2O2 Dual-Responsive Chiral Mesoporous Silica Nanorods Coated with a Biocompatible Active Targeting Ligand for Cancer Therapy".	Hydrogen Peroxide	18-22	phenylalanine hydroxylase	Homo sapiens	15-17
34448568-0	2021	Correction to "pH/H2O2 Dual-Responsive Chiral Mesoporous Silica Nanorods Coated with a Biocompatible Active Targeting Ligand for Cancer Therapy".	mesoporous	46-56	phenylalanine hydroxylase	Homo sapiens	15-17
34448568-0	2021	Correction to "pH/H2O2 Dual-Responsive Chiral Mesoporous Silica Nanorods Coated with a Biocompatible Active Targeting Ligand for Cancer Therapy".	Silicon Dioxide	57-63	phenylalanine hydroxylase	Homo sapiens	15-17
34503049-5	2021	This paper reviews the effects of several factors such as pH, biosorbent dosage, initial dye concentration, contact time and temperature when utilizing chitosan-based materials as biosorbent for removing of organic dyes from contaminated water.	Chitosan	152-160	phenylalanine hydroxylase	Homo sapiens	58-60
34503049-5	2021	This paper reviews the effects of several factors such as pH, biosorbent dosage, initial dye concentration, contact time and temperature when utilizing chitosan-based materials as biosorbent for removing of organic dyes from contaminated water.	Water	238-243	phenylalanine hydroxylase	Homo sapiens	58-60
34564237-1	2021	The physicochemical parameters of water, such as pH, salinity, conductivity, and total dissolved solids, can influence mosquito larval development, survival, and abundance.	Water	34-39	phenylalanine hydroxylase	Homo sapiens	49-51
34310952-0	2021	Modulation of the Sublingual Microenvironment and pH-Dependent Transport Pathways to Enhance Atropine Sulfate Permeability for the Treatment of Organophosphates Poisoning.	Atropine	93-109	phenylalanine hydroxylase	Homo sapiens	50-52
34310952-0	2021	Modulation of the Sublingual Microenvironment and pH-Dependent Transport Pathways to Enhance Atropine Sulfate Permeability for the Treatment of Organophosphates Poisoning.	Organophosphates	144-160	phenylalanine hydroxylase	Homo sapiens	50-52
34564237-8	2021	There was a statistically significant association between mosquito species occurrence and pH and salinity, and the former had a significant influence on the mosquito species collected regardless of the type of aquatic habitat, showing that the pH of the breeding site water is an important factor in driving mosquito population dynamics and species distribution.	Water	268-273	phenylalanine hydroxylase	Homo sapiens	90-92
34564237-8	2021	There was a statistically significant association between mosquito species occurrence and pH and salinity, and the former had a significant influence on the mosquito species collected regardless of the type of aquatic habitat, showing that the pH of the breeding site water is an important factor in driving mosquito population dynamics and species distribution.	Water	268-273	phenylalanine hydroxylase	Homo sapiens	244-246
34350754-3	2021	We herein report a systematic study on the synthesis and photophysics of all possible 6,8-disubstituted luminol derivatives bearing H, Ph, and/or Me substituents.	6,8-disubstituted luminol	86-111	phenylalanine hydroxylase	Homo sapiens	135-137
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	Cadmium	153-160	phenylalanine hydroxylase	Homo sapiens	72-74
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	Cobalt	162-168	phenylalanine hydroxylase	Homo sapiens	72-74
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	Strontium	170-179	phenylalanine hydroxylase	Homo sapiens	53-55
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	Strontium	170-179	phenylalanine hydroxylase	Homo sapiens	72-74
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	Cesium	185-191	phenylalanine hydroxylase	Homo sapiens	72-74
34198010-4	2021	Based on the pH-dependent reactivity of genipin, genipin-terminated 4 arm-poly(ethylene glycol) (GeniPEG) was synthesized.	genipin	40-47	phenylalanine hydroxylase	Homo sapiens	13-15
34198010-4	2021	Based on the pH-dependent reactivity of genipin, genipin-terminated 4 arm-poly(ethylene glycol) (GeniPEG) was synthesized.	genipin	49-56	phenylalanine hydroxylase	Homo sapiens	13-15
34198010-4	2021	Based on the pH-dependent reactivity of genipin, genipin-terminated 4 arm-poly(ethylene glycol) (GeniPEG) was synthesized.	Polyethylene Glycols	74-95	phenylalanine hydroxylase	Homo sapiens	13-15
34198010-4	2021	Based on the pH-dependent reactivity of genipin, genipin-terminated 4 arm-poly(ethylene glycol) (GeniPEG) was synthesized.	genipeg	97-104	phenylalanine hydroxylase	Homo sapiens	13-15
34198010-5	2021	dECM-based hydrogels were formed within a few seconds of mixing GeniPEG and dECM at an optimum pH through crosslinking of dECM and self-crosslinking between GeniPEG molecules.	genipeg	64-71	phenylalanine hydroxylase	Homo sapiens	95-97
34119163-3	2021	We developed a phosphorylated xanthan gum-Ag(I) complex (XGP-Ag) showing pH (pH = 7.1 +- 0.3) and osmolality values (311 +- 2 mOsm/kg) close to that of human tears (pH = 6.5-7.6 and 304 +- 23 mOsm/kg) thanks to the presence of phosphate moieties along the chain.	xanthan gum	30-37	phenylalanine hydroxylase	Homo sapiens	73-75
34119163-3	2021	We developed a phosphorylated xanthan gum-Ag(I) complex (XGP-Ag) showing pH (pH = 7.1 +- 0.3) and osmolality values (311 +- 2 mOsm/kg) close to that of human tears (pH = 6.5-7.6 and 304 +- 23 mOsm/kg) thanks to the presence of phosphate moieties along the chain.	xanthan gum	30-37	phenylalanine hydroxylase	Homo sapiens	77-79
34119163-3	2021	We developed a phosphorylated xanthan gum-Ag(I) complex (XGP-Ag) showing pH (pH = 7.1 +- 0.3) and osmolality values (311 +- 2 mOsm/kg) close to that of human tears (pH = 6.5-7.6 and 304 +- 23 mOsm/kg) thanks to the presence of phosphate moieties along the chain.	xanthan gum	30-37	phenylalanine hydroxylase	Homo sapiens	165-167
34347312-2	2021	The presence of catechol moiety in dopamine was exploited to form pH-responsive cross-links with ferric ions (Fe3+ ) at different pH value.	catechol	16-24	phenylalanine hydroxylase	Homo sapiens	66-68
34347312-2	2021	The presence of catechol moiety in dopamine was exploited to form pH-responsive cross-links with ferric ions (Fe3+ ) at different pH value.	catechol	16-24	phenylalanine hydroxylase	Homo sapiens	130-132
34347312-2	2021	The presence of catechol moiety in dopamine was exploited to form pH-responsive cross-links with ferric ions (Fe3+ ) at different pH value.	Dopamine	35-43	phenylalanine hydroxylase	Homo sapiens	66-68
34347312-2	2021	The presence of catechol moiety in dopamine was exploited to form pH-responsive cross-links with ferric ions (Fe3+ ) at different pH value.	Dopamine	35-43	phenylalanine hydroxylase	Homo sapiens	130-132
34347312-2	2021	The presence of catechol moiety in dopamine was exploited to form pH-responsive cross-links with ferric ions (Fe3+ ) at different pH value.	Ferric enterobactin ion	97-103	phenylalanine hydroxylase	Homo sapiens	66-68
34347312-2	2021	The presence of catechol moiety in dopamine was exploited to form pH-responsive cross-links with ferric ions (Fe3+ ) at different pH value.	Ferric enterobactin ion	97-103	phenylalanine hydroxylase	Homo sapiens	130-132
34347312-2	2021	The presence of catechol moiety in dopamine was exploited to form pH-responsive cross-links with ferric ions (Fe3+ ) at different pH value.	ferric sulfate	110-114	phenylalanine hydroxylase	Homo sapiens	66-68
34347312-2	2021	The presence of catechol moiety in dopamine was exploited to form pH-responsive cross-links with ferric ions (Fe3+ ) at different pH value.	ferric sulfate	110-114	phenylalanine hydroxylase	Homo sapiens	130-132
34403880-1	2021	Tyrosine kinase inhibitors (TKIs) such as imatinib, nilotinib, dasatinib, and ponatinib have significantly improved the life expectancy of Philadelphia chromosome-positive (Ph+) acute lymphocytic leukemia (ALL) patients; however, resistance to TKIs remains a major clinical challenge.	Imatinib Mesylate	42-50	phenylalanine hydroxylase	Homo sapiens	173-175
34403880-1	2021	Tyrosine kinase inhibitors (TKIs) such as imatinib, nilotinib, dasatinib, and ponatinib have significantly improved the life expectancy of Philadelphia chromosome-positive (Ph+) acute lymphocytic leukemia (ALL) patients; however, resistance to TKIs remains a major clinical challenge.	nilotinib	52-61	phenylalanine hydroxylase	Homo sapiens	173-175
34403880-1	2021	Tyrosine kinase inhibitors (TKIs) such as imatinib, nilotinib, dasatinib, and ponatinib have significantly improved the life expectancy of Philadelphia chromosome-positive (Ph+) acute lymphocytic leukemia (ALL) patients; however, resistance to TKIs remains a major clinical challenge.	Dasatinib	63-72	phenylalanine hydroxylase	Homo sapiens	173-175
34403880-1	2021	Tyrosine kinase inhibitors (TKIs) such as imatinib, nilotinib, dasatinib, and ponatinib have significantly improved the life expectancy of Philadelphia chromosome-positive (Ph+) acute lymphocytic leukemia (ALL) patients; however, resistance to TKIs remains a major clinical challenge.	ponatinib	78-87	phenylalanine hydroxylase	Homo sapiens	173-175
34501755-5	2021	However, chitosan owes fewer sensitive responses (turbidity and residual metal) with the change in its input factors (dosage and pH), especially in acidic conditions.	Metals	73-78	phenylalanine hydroxylase	Homo sapiens	129-131
34514252-6	2021	Based on these, it was proposed that apart from acting as structure-directing agents, pore fillers, and pH adjusters, organic amines can also function as promoters in the condensation of polysilicic acids.	organic amines	118-132	phenylalanine hydroxylase	Homo sapiens	104-106
34514252-6	2021	Based on these, it was proposed that apart from acting as structure-directing agents, pore fillers, and pH adjusters, organic amines can also function as promoters in the condensation of polysilicic acids.	polysilicic acids	187-204	phenylalanine hydroxylase	Homo sapiens	104-106
34410145-2	2021	Although several mechanisms, such as hydrogen-abstraction acetylene/vinylacetylene addition, have previously been proposed, PAH formation and growth are not yet fully understood.	Acetylene	58-67	phenylalanine hydroxylase	Homo sapiens	124-127
34410145-2	2021	Although several mechanisms, such as hydrogen-abstraction acetylene/vinylacetylene addition, have previously been proposed, PAH formation and growth are not yet fully understood.	1-BUTEN-3-YNE	68-82	phenylalanine hydroxylase	Homo sapiens	124-127
34410145-3	2021	We propose an alternate PAH growth mechanism wherein propargyl radical reacts with butadiyne to form larger radicals containing newly fused aromatic rings.	Propargyl radical	53-70	phenylalanine hydroxylase	Homo sapiens	24-27
34410145-3	2021	We propose an alternate PAH growth mechanism wherein propargyl radical reacts with butadiyne to form larger radicals containing newly fused aromatic rings.	1,3-Butadiyne	83-92	phenylalanine hydroxylase	Homo sapiens	24-27
34410145-6	2021	Our findings challenge the conventional wisdom that radical site regeneration, being central to PAH growth, requires sequential hydrogen elimination and/or abstraction.	Hydrogen	128-136	phenylalanine hydroxylase	Homo sapiens	96-99
34723270-0	2021	Cation- and pH-Dependent Hydrogen Evolution and Oxidation Reaction Kinetics.	Hydrogen	25-33	phenylalanine hydroxylase	Homo sapiens	12-14
34723270-2	2021	In this work, a series of structure-making/breaking cations in the electrolyte were investigated as spectator cations in hydrogen evolution and oxidation reactions (HER/HOR) in the pH range of 1 to 14, whose kinetics was found to be altered by up to 2 orders of magnitude by these cations.	Hydrogen	121-129	phenylalanine hydroxylase	Homo sapiens	181-183
34704413-11	2021	The 3D structural model showed that p.Arg53His mutation reduced the hydrogen bond from 2 to 1 between the 53rd and 49th amino acids of PAH.	Hydrogen	68-76	phenylalanine hydroxylase	Homo sapiens	135-138
34578480-2	2021	The demand in the application of nanomaterials can result in the release of these anthropogenic materials into soil and water that can potentially harm the environment by affecting water and soil properties (e.g., soil texture, pH, organic matter, and water content), plants, animals, and subsequently human health.	Water	120-125	phenylalanine hydroxylase	Homo sapiens	228-230
34443981-6	2021	Otherwise, the low concentration and the higher pH of GO suspension induce more lattice defects on the ZnO crystal structure.	graphene oxide	54-56	phenylalanine hydroxylase	Homo sapiens	48-50
34443981-6	2021	Otherwise, the low concentration and the higher pH of GO suspension induce more lattice defects on the ZnO crystal structure.	Zinc Oxide	103-106	phenylalanine hydroxylase	Homo sapiens	48-50
34412683-1	2021	BACKGROUND: In classical phenylketonuria (PKU) phenylalanine (Phe) accumulates due to functional impairment of the enzyme phenylalanine hydroxylase caused by pathogenic variants in the PAH gene.	Phenylalanine	47-60	phenylalanine hydroxylase	Homo sapiens	122-147
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	cb18crown6	4-14	phenylalanine hydroxylase	Homo sapiens	53-55
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	cb18crown6	4-14	phenylalanine hydroxylase	Homo sapiens	72-74
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	SBA-15	15-21	phenylalanine hydroxylase	Homo sapiens	53-55
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	SBA-15	15-21	phenylalanine hydroxylase	Homo sapiens	72-74
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	chromium hexavalent ion	43-49	phenylalanine hydroxylase	Homo sapiens	53-55
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	zn(ii)	62-68	phenylalanine hydroxylase	Homo sapiens	72-74
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	Chromium	128-136	phenylalanine hydroxylase	Homo sapiens	53-55
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	Chromium	128-136	phenylalanine hydroxylase	Homo sapiens	72-74
34501150-6	2021	The CB18crown6/SBA-15 selectively adsorbed Cr(VI) at pH 2 and Zn(II) at pH 5, respectively, from the mixed aqueous solutions of chromium, zinc, lithium, cadmium, cobalt, strontium, and cesium ions.	Lithium	144-151	phenylalanine hydroxylase	Homo sapiens	72-74
34412683-1	2021	BACKGROUND: In classical phenylketonuria (PKU) phenylalanine (Phe) accumulates due to functional impairment of the enzyme phenylalanine hydroxylase caused by pathogenic variants in the PAH gene.	Phenylalanine	47-60	phenylalanine hydroxylase	Homo sapiens	185-188
34412683-1	2021	BACKGROUND: In classical phenylketonuria (PKU) phenylalanine (Phe) accumulates due to functional impairment of the enzyme phenylalanine hydroxylase caused by pathogenic variants in the PAH gene.	Phenylalanine	62-65	phenylalanine hydroxylase	Homo sapiens	122-147
34412683-1	2021	BACKGROUND: In classical phenylketonuria (PKU) phenylalanine (Phe) accumulates due to functional impairment of the enzyme phenylalanine hydroxylase caused by pathogenic variants in the PAH gene.	Phenylalanine	62-65	phenylalanine hydroxylase	Homo sapiens	185-188
34162223-12	2021	Observations from aged mice and human samples implicated age-related decline in hepatic Phe catabolism as a key driver of elevated plasma Phe levels and showed increased myocardial PAH-mediated Phe catabolism, a novel signature of cardiac aging.	Phenylalanine	194-197	phenylalanine hydroxylase	Homo sapiens	181-184
34422455-0	2021	Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation.	histidine-based oligopeptides	12-41	phenylalanine hydroxylase	Homo sapiens	50-52
34162223-14	2021	They highlight Phe/PAH modulation as a potential therapeutic strategy for age-associated cardiac impairment.	Phenylalanine	15-18	phenylalanine hydroxylase	Homo sapiens	19-22
34231617-3	2021	In this review, we present a detailed discussion on the catalytic addition of P-H bonds from various phosphine reagents to multiple bonds of unsaturated substrates for the synthesis of organophosphorus compounds with C-P bonds promoted by various s- and p-block metal catalysts, as published in the last decade.	phosphine	101-110	phenylalanine hydroxylase	Homo sapiens	78-81
34319854-5	2021	Multiwalled carbon nanotubes catalyzed ozonation removes 85% COD and 48% TOC removal within 180 min at pH 9 and 74% COD and 36% TOC removal was observed for activated carbon catalyzed ozonation for the same experimental conditions.	Carbon	12-18	phenylalanine hydroxylase	Homo sapiens	103-105
34384471-6	2021	Thiamine was significantly more stable in pH 3 than in pH 6 solutions.	Thiamine	0-8	phenylalanine hydroxylase	Homo sapiens	42-44
34384471-6	2021	Thiamine was significantly more stable in pH 3 than in pH 6 solutions.	Thiamine	0-8	phenylalanine hydroxylase	Homo sapiens	55-57
34231617-3	2021	In this review, we present a detailed discussion on the catalytic addition of P-H bonds from various phosphine reagents to multiple bonds of unsaturated substrates for the synthesis of organophosphorus compounds with C-P bonds promoted by various s- and p-block metal catalysts, as published in the last decade.	organophosphorus	185-201	phenylalanine hydroxylase	Homo sapiens	78-81
34231617-3	2021	In this review, we present a detailed discussion on the catalytic addition of P-H bonds from various phosphine reagents to multiple bonds of unsaturated substrates for the synthesis of organophosphorus compounds with C-P bonds promoted by various s- and p-block metal catalysts, as published in the last decade.	Metals	262-267	phenylalanine hydroxylase	Homo sapiens	78-81
34244826-11	2021	rTMS appears to influence the enzyme phenylalanine hydroxylase, which plays a central role in the biosynthesis of neurotransmitter precursors tyrosine and dihydroxyphenylalanine (DOPA).	Tyrosine	142-150	phenylalanine hydroxylase	Homo sapiens	37-62
34260224-2	2021	In this study, we present a calculation method to more intuitively quantify the relationship between aerosol pH and its influencing factors, including gaseous NH3 concentration, particle properties, relative humidity, temperature, and nonvolatile cations, based on the NHx phase-partitioning equilibrium used in the E-AIM thermodynamic model.	Ammonia	159-162	phenylalanine hydroxylase	Homo sapiens	109-111
34076541-0	2021	EXPRESS: pH-Dependent Flavin Adenine Dinucleotide and Nicotinamide Adenine Dinucleotide Ultraviolet Resonance Raman (UVRR) Spectra at Intracellular Concentration.	Flavin-Adenine Dinucleotide	22-49	phenylalanine hydroxylase	Homo sapiens	9-11
34076541-0	2021	EXPRESS: pH-Dependent Flavin Adenine Dinucleotide and Nicotinamide Adenine Dinucleotide Ultraviolet Resonance Raman (UVRR) Spectra at Intracellular Concentration.	NAD	54-87	phenylalanine hydroxylase	Homo sapiens	9-11
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	4,6-dinitro-o-cresol	170-176	phenylalanine hydroxylase	Homo sapiens	34-36
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	4,6-dinitro-o-cresol	170-176	phenylalanine hydroxylase	Homo sapiens	58-60
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	4,6-dinitro-o-cresol	170-176	phenylalanine hydroxylase	Homo sapiens	68-70
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	4,6-dinitro-o-cresol	170-176	phenylalanine hydroxylase	Homo sapiens	107-109
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	Niacinamide	181-193	phenylalanine hydroxylase	Homo sapiens	34-36
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	Niacinamide	181-193	phenylalanine hydroxylase	Homo sapiens	58-60
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	Niacinamide	181-193	phenylalanine hydroxylase	Homo sapiens	68-70
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	Niacinamide	181-193	phenylalanine hydroxylase	Homo sapiens	107-109
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	Adenine	227-234	phenylalanine hydroxylase	Homo sapiens	34-36
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	Adenine	227-234	phenylalanine hydroxylase	Homo sapiens	58-60
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	Adenine	227-234	phenylalanine hydroxylase	Homo sapiens	68-70
34076541-3	2021	Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.	Adenine	227-234	phenylalanine hydroxylase	Homo sapiens	107-109
34088096-1	2021	Transport characteristics of fragmental polyethylene glycol terephthalate (PET) microplastics in porous media were elucidated via column experiments under a series combination of electrolytes, pH, and humic acid (HA) conditions.	polyethylene terephthalate glycol	40-73	phenylalanine hydroxylase	Homo sapiens	193-195
34116292-4	2021	Sewage sludge was subjected to pH-controlled fermentation process at acidic, neutral, and alkaline pH levels with the aim of increasing metal solubilization and decreasing bioavailable metal fractions through anaerobic bioleaching.	Metals	136-141	phenylalanine hydroxylase	Homo sapiens	31-33
34116292-4	2021	Sewage sludge was subjected to pH-controlled fermentation process at acidic, neutral, and alkaline pH levels with the aim of increasing metal solubilization and decreasing bioavailable metal fractions through anaerobic bioleaching.	Metals	185-190	phenylalanine hydroxylase	Homo sapiens	31-33
34409178-4	2021	A laboratory study to replicate the phenomenon at bench-scale showed that either the algaecide itself or its copper-free acidic carrier can be used to depress pH and drive a reaction converting geosmin to an odorless dehydration product, argosmin.	Copper	109-115	phenylalanine hydroxylase	Homo sapiens	159-161
34409178-4	2021	A laboratory study to replicate the phenomenon at bench-scale showed that either the algaecide itself or its copper-free acidic carrier can be used to depress pH and drive a reaction converting geosmin to an odorless dehydration product, argosmin.	geosmin	194-201	phenylalanine hydroxylase	Homo sapiens	159-161
34361737-4	2021	Indeed, the precipitation of Fe(III) at pH > 4 interferes with the recycling of Fe species and inhibits oxidation in homogeneous Fenton; in contrast, suspended ZVI as iron source is less sensitive to the increase of pH.	ferric sulfate	29-36	phenylalanine hydroxylase	Homo sapiens	40-42
34361737-4	2021	Indeed, the precipitation of Fe(III) at pH > 4 interferes with the recycling of Fe species and inhibits oxidation in homogeneous Fenton; in contrast, suspended ZVI as iron source is less sensitive to the increase of pH.	ferric sulfate	29-36	phenylalanine hydroxylase	Homo sapiens	216-218
34361737-4	2021	Indeed, the precipitation of Fe(III) at pH > 4 interferes with the recycling of Fe species and inhibits oxidation in homogeneous Fenton; in contrast, suspended ZVI as iron source is less sensitive to the increase of pH.	Iron	80-82	phenylalanine hydroxylase	Homo sapiens	40-42
34361737-4	2021	Indeed, the precipitation of Fe(III) at pH > 4 interferes with the recycling of Fe species and inhibits oxidation in homogeneous Fenton; in contrast, suspended ZVI as iron source is less sensitive to the increase of pH.	Iron	80-82	phenylalanine hydroxylase	Homo sapiens	216-218
34361737-4	2021	Indeed, the precipitation of Fe(III) at pH > 4 interferes with the recycling of Fe species and inhibits oxidation in homogeneous Fenton; in contrast, suspended ZVI as iron source is less sensitive to the increase of pH.	Iron	167-171	phenylalanine hydroxylase	Homo sapiens	216-218
34361737-7	2021	Research results have shown that ZVI-Fenton with persulfate works best at acidic pH, but it is often possible to get reasonable degradation at pH values that are not too far from neutrality.	zvi-fenton	33-43	phenylalanine hydroxylase	Homo sapiens	81-83
34361737-7	2021	Research results have shown that ZVI-Fenton with persulfate works best at acidic pH, but it is often possible to get reasonable degradation at pH values that are not too far from neutrality.	zvi-fenton	33-43	phenylalanine hydroxylase	Homo sapiens	143-145
34361737-7	2021	Research results have shown that ZVI-Fenton with persulfate works best at acidic pH, but it is often possible to get reasonable degradation at pH values that are not too far from neutrality.	Peroxydisulfate	49-59	phenylalanine hydroxylase	Homo sapiens	81-83
34264055-5	2021	Altering the energetic landscape of magnetite formation by catalyzing the pH-dependent precursor attachment, we tune magnetite nanoparticle size continuously, exceeding sizes observed in magnetotactic bacteria.	Ferrosoferric Oxide	36-45	phenylalanine hydroxylase	Homo sapiens	74-76
34264055-6	2021	This mechanistic shift we uncover here further allows for crystal morphology control by adjusting the pH-dependent interfacial interaction between liquidlike ferrihydrite and nascent magnetite nanoparticles, establishing a new strategy to control nanoparticle morphology.	ferric oxyhydroxide	158-170	phenylalanine hydroxylase	Homo sapiens	102-104
34264055-6	2021	This mechanistic shift we uncover here further allows for crystal morphology control by adjusting the pH-dependent interfacial interaction between liquidlike ferrihydrite and nascent magnetite nanoparticles, establishing a new strategy to control nanoparticle morphology.	Ferrosoferric Oxide	183-192	phenylalanine hydroxylase	Homo sapiens	102-104
34270265-0	2021	Salt- and pH-Dependent Viscosity of SDS/LAPB Solutions: Experiments and a Semiempirical Thermodynamic Model.	Sodium Dodecyl Sulfate	36-39	phenylalanine hydroxylase	Homo sapiens	10-12
34270265-1	2021	We present novel data on the composition-, pH-, and salt-dependent zero shear viscosity of the commercially important mixture of anionic sodium dodecyl sulfate (SDS) and zwitterionic lauramidopropyl betaine (LAPB).	Sodium Dodecyl Sulfate	137-159	phenylalanine hydroxylase	Homo sapiens	43-45
34270265-1	2021	We present novel data on the composition-, pH-, and salt-dependent zero shear viscosity of the commercially important mixture of anionic sodium dodecyl sulfate (SDS) and zwitterionic lauramidopropyl betaine (LAPB).	Sodium Dodecyl Sulfate	161-164	phenylalanine hydroxylase	Homo sapiens	43-45
34270265-1	2021	We present novel data on the composition-, pH-, and salt-dependent zero shear viscosity of the commercially important mixture of anionic sodium dodecyl sulfate (SDS) and zwitterionic lauramidopropyl betaine (LAPB).	Betaine	199-206	phenylalanine hydroxylase	Homo sapiens	43-45
34270265-1	2021	We present novel data on the composition-, pH-, and salt-dependent zero shear viscosity of the commercially important mixture of anionic sodium dodecyl sulfate (SDS) and zwitterionic lauramidopropyl betaine (LAPB).	lapb	208-212	phenylalanine hydroxylase	Homo sapiens	43-45
34360752-5	2021	By envisaging a biosafe cytocompatible and haemocompatible profile, this paper reports the systematic development of a delivery system based on CS and derived with HA and CDs to nanoencapsulate the model human phenylalanine hydroxylase (hPAH) through ionotropic gelation with tripolyphosphate (TPP), while maintaining protein stability and enzyme activity.	Chitosan	144-146	phenylalanine hydroxylase	Homo sapiens	210-235
34360752-5	2021	By envisaging a biosafe cytocompatible and haemocompatible profile, this paper reports the systematic development of a delivery system based on CS and derived with HA and CDs to nanoencapsulate the model human phenylalanine hydroxylase (hPAH) through ionotropic gelation with tripolyphosphate (TPP), while maintaining protein stability and enzyme activity.	Chitosan	144-146	phenylalanine hydroxylase	Homo sapiens	237-241
34360752-5	2021	By envisaging a biosafe cytocompatible and haemocompatible profile, this paper reports the systematic development of a delivery system based on CS and derived with HA and CDs to nanoencapsulate the model human phenylalanine hydroxylase (hPAH) through ionotropic gelation with tripolyphosphate (TPP), while maintaining protein stability and enzyme activity.	Cyclodextrins	171-174	phenylalanine hydroxylase	Homo sapiens	210-235
34360752-5	2021	By envisaging a biosafe cytocompatible and haemocompatible profile, this paper reports the systematic development of a delivery system based on CS and derived with HA and CDs to nanoencapsulate the model human phenylalanine hydroxylase (hPAH) through ionotropic gelation with tripolyphosphate (TPP), while maintaining protein stability and enzyme activity.	Cyclodextrins	171-174	phenylalanine hydroxylase	Homo sapiens	237-241
34360752-5	2021	By envisaging a biosafe cytocompatible and haemocompatible profile, this paper reports the systematic development of a delivery system based on CS and derived with HA and CDs to nanoencapsulate the model human phenylalanine hydroxylase (hPAH) through ionotropic gelation with tripolyphosphate (TPP), while maintaining protein stability and enzyme activity.	triphosphoric acid	276-292	phenylalanine hydroxylase	Homo sapiens	210-235
34360752-5	2021	By envisaging a biosafe cytocompatible and haemocompatible profile, this paper reports the systematic development of a delivery system based on CS and derived with HA and CDs to nanoencapsulate the model human phenylalanine hydroxylase (hPAH) through ionotropic gelation with tripolyphosphate (TPP), while maintaining protein stability and enzyme activity.	triphosphoric acid	276-292	phenylalanine hydroxylase	Homo sapiens	237-241
34360752-5	2021	By envisaging a biosafe cytocompatible and haemocompatible profile, this paper reports the systematic development of a delivery system based on CS and derived with HA and CDs to nanoencapsulate the model human phenylalanine hydroxylase (hPAH) through ionotropic gelation with tripolyphosphate (TPP), while maintaining protein stability and enzyme activity.	triphosphoric acid	294-297	phenylalanine hydroxylase	Homo sapiens	210-235
34360752-5	2021	By envisaging a biosafe cytocompatible and haemocompatible profile, this paper reports the systematic development of a delivery system based on CS and derived with HA and CDs to nanoencapsulate the model human phenylalanine hydroxylase (hPAH) through ionotropic gelation with tripolyphosphate (TPP), while maintaining protein stability and enzyme activity.	triphosphoric acid	294-297	phenylalanine hydroxylase	Homo sapiens	237-241
34360752-6	2021	By merging the combined set of biopolymers, we were able to effectively entrap hPAH within CS nanoparticles with improvements in hPAH stability and the maintenance of functional activity, while simultaneously achieving strict control of the formulation process.	Chitosan	91-93	phenylalanine hydroxylase	Homo sapiens	79-83
34360752-6	2021	By merging the combined set of biopolymers, we were able to effectively entrap hPAH within CS nanoparticles with improvements in hPAH stability and the maintenance of functional activity, while simultaneously achieving strict control of the formulation process.	Chitosan	91-93	phenylalanine hydroxylase	Homo sapiens	129-133
34310595-8	2021	Relationships between changes in urine pH due to vitamin C treatment, which reduce urine pH, and urinary soluble (P)RR excretion were investigated in 10 healthy volunteers.	Ascorbic Acid	49-58	phenylalanine hydroxylase	Homo sapiens	39-41
34310595-8	2021	Relationships between changes in urine pH due to vitamin C treatment, which reduce urine pH, and urinary soluble (P)RR excretion were investigated in 10 healthy volunteers.	Ascorbic Acid	49-58	phenylalanine hydroxylase	Homo sapiens	89-91
34310595-11	2021	Changes in urine pH and urinary soluble (P)RR excretion due to vitamin C treatment were significantly and positively correlated (rho = 0.8182, p = 0.0038).	Ascorbic Acid	63-72	phenylalanine hydroxylase	Homo sapiens	17-19
34372233-0	2021	Fabrication and Characterization of Iridium Oxide pH Microelectrodes Based on Sputter Deposition Method.	iridium oxide	36-49	phenylalanine hydroxylase	Homo sapiens	50-52
34372233-3	2021	In this paper, we present a method for preparing iridium oxide pH microelectrodes based on the sputter deposition method.	iridium oxide	49-62	phenylalanine hydroxylase	Homo sapiens	63-65
34267239-3	2021	When added through the solution, sodium carbonate was needed to dissolve folic acid and to adjust pH.	sodium carbonate	33-49	phenylalanine hydroxylase	Homo sapiens	98-100
34252095-2	2021	In the natural environment, varying pH may play an important role in the absorption and accumulation of Cd in plants, which can cause toxicity and increase the risk to humans.	Cadmium	104-106	phenylalanine hydroxylase	Homo sapiens	36-38
34371751-5	2021	The release kinetics of KTF and THCL was significantly faster when the pH of the release medium was decreased from 7.4 towards 5.5 because of the decrease in the relative amounts of oleate anions in the lens mostly populated at the polymer-pore interfaces.	Ketotifen	24-27	phenylalanine hydroxylase	Homo sapiens	71-73
34371751-5	2021	The release kinetics of KTF and THCL was significantly faster when the pH of the release medium was decreased from 7.4 towards 5.5 because of the decrease in the relative amounts of oleate anions in the lens mostly populated at the polymer-pore interfaces.	Tetracaine	32-36	phenylalanine hydroxylase	Homo sapiens	71-73
34212661-7	2021	In addition, pH exhibited a significant negative correlation with Fe and Fe nanoparticles.	Iron	66-68	phenylalanine hydroxylase	Homo sapiens	13-15
34212661-7	2021	In addition, pH exhibited a significant negative correlation with Fe and Fe nanoparticles.	Iron	73-75	phenylalanine hydroxylase	Homo sapiens	13-15
34160205-0	2021	Mesoporous Bimetallic Au@Rh Core-Shell Nanowires as Efficient Electrocatalysts for pH-Universal Hydrogen Evolution.	mesoporous	0-10	phenylalanine hydroxylase	Homo sapiens	83-85
34160205-0	2021	Mesoporous Bimetallic Au@Rh Core-Shell Nanowires as Efficient Electrocatalysts for pH-Universal Hydrogen Evolution.	Gold	22-24	phenylalanine hydroxylase	Homo sapiens	83-85
34160205-0	2021	Mesoporous Bimetallic Au@Rh Core-Shell Nanowires as Efficient Electrocatalysts for pH-Universal Hydrogen Evolution.	Hydrogen	96-104	phenylalanine hydroxylase	Homo sapiens	83-85
34160205-1	2021	Electrochemical water splitting is one hopeful strategy for hydrogen production, and designing efficient hydrogen evolution electrocatalysts under universal pH is one of the most critical topics.	Hydrogen	60-68	phenylalanine hydroxylase	Homo sapiens	157-159
34160205-1	2021	Electrochemical water splitting is one hopeful strategy for hydrogen production, and designing efficient hydrogen evolution electrocatalysts under universal pH is one of the most critical topics.	Hydrogen	105-113	phenylalanine hydroxylase	Homo sapiens	157-159
34160205-3	2021	Due to the one-dimensional structure and mesoporous core-shell structure, Au@mRh NWs possess more active sites and provide the synergistic effect, leading to the great improvement of the electrochemical activity toward the hydrogen evolution reaction under a wide range of pH.	mesoporous	41-51	phenylalanine hydroxylase	Homo sapiens	273-275
34160205-3	2021	Due to the one-dimensional structure and mesoporous core-shell structure, Au@mRh NWs possess more active sites and provide the synergistic effect, leading to the great improvement of the electrochemical activity toward the hydrogen evolution reaction under a wide range of pH.	Gold	74-76	phenylalanine hydroxylase	Homo sapiens	273-275
34160205-3	2021	Due to the one-dimensional structure and mesoporous core-shell structure, Au@mRh NWs possess more active sites and provide the synergistic effect, leading to the great improvement of the electrochemical activity toward the hydrogen evolution reaction under a wide range of pH.	Hydrogen	223-231	phenylalanine hydroxylase	Homo sapiens	273-275
34137400-2	2021	In this review, the recent progress in the study of stimuli-activated MPTAs is summarized from different stimuli, including pH, bioactive small molecules, and enzymes.	mptas	70-75	phenylalanine hydroxylase	Homo sapiens	124-126
34152251-4	2021	RO membrane system operating parameters (pH, temperature, and trans-membrane pressure) were optimized by employing response surface methodology.	ro	0-2	phenylalanine hydroxylase	Homo sapiens	41-43
34152251-5	2021	Optimized conditions for the RO process were found to be: pH (pHo): 6.12; temperature (T): 20 C and trans-membrane pressure (TMP): 45.7 bar.	ro	29-31	phenylalanine hydroxylase	Homo sapiens	58-60
34152251-5	2021	Optimized conditions for the RO process were found to be: pH (pHo): 6.12; temperature (T): 20 C and trans-membrane pressure (TMP): 45.7 bar.	ro	29-31	phenylalanine hydroxylase	Homo sapiens	62-65
34170127-0	2021	Role of pH in the Transformation of Perfluoroalkyl Carboxylic Acids by Activated Persulfate: Implications from the Determination of Absolute Electron-Transfer Rates and Chemical Computations.	perfluoroalkyl carboxylic acids	36-67	phenylalanine hydroxylase	Homo sapiens	8-10
34170127-0	2021	Role of pH in the Transformation of Perfluoroalkyl Carboxylic Acids by Activated Persulfate: Implications from the Determination of Absolute Electron-Transfer Rates and Chemical Computations.	Peroxydisulfate	81-91	phenylalanine hydroxylase	Homo sapiens	8-10
34170127-5	2021	A pronounced pH effect has been observed for thermally activated persulfate PFCA transformation.	Peroxydisulfate	65-75	phenylalanine hydroxylase	Homo sapiens	13-15
34170127-5	2021	A pronounced pH effect has been observed for thermally activated persulfate PFCA transformation.	pfca	76-80	phenylalanine hydroxylase	Homo sapiens	13-15
34170127-6	2021	To evaluate the role of pH during SET, we directly determined absolute rate constants for perfluorobutanoic acid and trifluoroacetic acid oxidation by SO4 - in the pH range of 0.5-4.0 using laser flash photolysis.	perfluorobutyric acid	90-112	phenylalanine hydroxylase	Homo sapiens	164-166
34170127-6	2021	To evaluate the role of pH during SET, we directly determined absolute rate constants for perfluorobutanoic acid and trifluoroacetic acid oxidation by SO4 - in the pH range of 0.5-4.0 using laser flash photolysis.	sulfuric acid	151-154	phenylalanine hydroxylase	Homo sapiens	164-166
34170127-7	2021	The average of the rate constants for both substrates across all pH values was 9 +- 2 x 103 M-1 s-1 (+-2sigma), implying that acid catalysis of thermal persulfate activation may be the primary culprit of the observed pH effect, instead of pH influencing the SET step.	Peroxydisulfate	152-162	phenylalanine hydroxylase	Homo sapiens	65-67
34170127-7	2021	The average of the rate constants for both substrates across all pH values was 9 +- 2 x 103 M-1 s-1 (+-2sigma), implying that acid catalysis of thermal persulfate activation may be the primary culprit of the observed pH effect, instead of pH influencing the SET step.	Peroxydisulfate	152-162	phenylalanine hydroxylase	Homo sapiens	217-219
34579434-10	2021	It was demonstrated that when elemental sulfur and sulfur-oxidizing bacteria were treated together, the pH decreased faster than when treated with peat moss.	Sulfur	51-57	phenylalanine hydroxylase	Homo sapiens	104-106
34579434-11	2021	It could be economically beneficial to farmers to use elemental sulfur and sulfur-oxidizing bacteria, which are cheaper than peat moss, to reduce the pH of the soil.	Sulfur	64-70	phenylalanine hydroxylase	Homo sapiens	150-152
34120155-0	2021	A pH/H2O2 dual triggered nanoplatform for enhanced photodynamic antibacterial efficiency.	Hydrogen Peroxide	5-9	phenylalanine hydroxylase	Homo sapiens	2-4
34209425-2	2021	The characteristics slope (58 mV), rapid and linear response for aluminum ion was displayed by the proposed sensor within the concentration range 2.5 x 10-7-1.5 x 10-1 M, the detection limit (1.6 x 10-7) M, the selectivity behavior toward some metal cations, the response time 10 s), lifetime (150 days), the effect of pH on the suggested electrode potential and the requisite analytical validations were examined.	Aluminum	65-73	phenylalanine hydroxylase	Homo sapiens	319-321
34241364-0	2021	Cisplatin uptake and release in pH sensitive zeolitic imidazole frameworks.	Cisplatin	0-9	phenylalanine hydroxylase	Homo sapiens	32-34
34241364-0	2021	Cisplatin uptake and release in pH sensitive zeolitic imidazole frameworks.	imidazole	54-63	phenylalanine hydroxylase	Homo sapiens	32-34
34241364-4	2021	We then screen a series of biocompatible, pH-sensitive zeolitic imidazolate frameworks (ZIFs) for their ability to retain cisplatin in healthy parts of the patient and release it in the vicinity of a tumor.	imidazolate	64-75	phenylalanine hydroxylase	Homo sapiens	42-44
34241364-4	2021	We then screen a series of biocompatible, pH-sensitive zeolitic imidazolate frameworks (ZIFs) for their ability to retain cisplatin in healthy parts of the patient and release it in the vicinity of a tumor.	Cisplatin	122-131	phenylalanine hydroxylase	Homo sapiens	42-44
34241364-10	2021	If it is possible to load cisplatin during crystallization, ZIF-11 would outcompete the other MOFs screened as cisplatin cannot pass through its pore windows; therefore, release rates would be purely driven by the pH triggered framework degradation.	Cisplatin	26-35	phenylalanine hydroxylase	Homo sapiens	214-216
34241364-10	2021	If it is possible to load cisplatin during crystallization, ZIF-11 would outcompete the other MOFs screened as cisplatin cannot pass through its pore windows; therefore, release rates would be purely driven by the pH triggered framework degradation.	zif-11	60-66	phenylalanine hydroxylase	Homo sapiens	214-216
34241364-10	2021	If it is possible to load cisplatin during crystallization, ZIF-11 would outcompete the other MOFs screened as cisplatin cannot pass through its pore windows; therefore, release rates would be purely driven by the pH triggered framework degradation.	Cisplatin	111-120	phenylalanine hydroxylase	Homo sapiens	214-216
34076026-1	2021	We performed Metropolis Monte Carlo simulations to investigate the impact of varying acid and base dissociation constants on the pH-dependent ionization and conformation of weak polyampholyte microgels under salt-free conditions and under explicit consideration of the chemical ionization equilibria of the acidic and basic groups and their electrostatic interaction.	Salts	208-212	phenylalanine hydroxylase	Homo sapiens	129-131
34244826-11	2021	rTMS appears to influence the enzyme phenylalanine hydroxylase, which plays a central role in the biosynthesis of neurotransmitter precursors tyrosine and dihydroxyphenylalanine (DOPA).	Dihydroxyphenylalanine	155-177	phenylalanine hydroxylase	Homo sapiens	37-62
34244826-11	2021	rTMS appears to influence the enzyme phenylalanine hydroxylase, which plays a central role in the biosynthesis of neurotransmitter precursors tyrosine and dihydroxyphenylalanine (DOPA).	Dihydroxyphenylalanine	179-183	phenylalanine hydroxylase	Homo sapiens	37-62
34235263-4	2021	This new configuration adds the potential arising from the pH difference across the membrane and enables an open circuit voltage of ~1.6 V. In contrast, the same redox molecules operating at a single pH generate ~0.9 V. Ion transport in the BPM is coupled to the water dissociation and acid-base neutralization reactions.	Water	263-268	phenylalanine hydroxylase	Homo sapiens	59-61
34145024-9	2021	Among them the PKA targets phenylalanine hydroxylase (PAH) catalyzes the conversion of phenylalanine to tyrosine.	Phenylalanine	87-100	phenylalanine hydroxylase	Homo sapiens	27-52
34207146-1	2021	Human phenylalanine hydroxylase (PAH) is a metabolic enzyme involved in the catabolism of L-Phe in liver.	Phenylalanine	90-95	phenylalanine hydroxylase	Homo sapiens	6-31
34145024-9	2021	Among them the PKA targets phenylalanine hydroxylase (PAH) catalyzes the conversion of phenylalanine to tyrosine.	Tyrosine	104-112	phenylalanine hydroxylase	Homo sapiens	27-52
34207146-1	2021	Human phenylalanine hydroxylase (PAH) is a metabolic enzyme involved in the catabolism of L-Phe in liver.	Phenylalanine	90-95	phenylalanine hydroxylase	Homo sapiens	33-36
34204699-4	2021	Alteration in H2S biogenesis has been associated with the hallmarks of PH.	Deuterium	14-17	phenylalanine hydroxylase	Homo sapiens	71-73
34207146-5	2021	We investigate here the urea and the thermal-induced denaturation of full-length PAH and of a truncated form lacking the regulatory and the tetramerization domains.	Urea	24-28	phenylalanine hydroxylase	Homo sapiens	81-84
34204699-5	2021	H2S is also involved in pulmonary vascular cell homeostasis via the regulation of hypoxia response and mitochondrial bioenergetics, which are critical phenomena affected during the development of PH.	Deuterium	0-3	phenylalanine hydroxylase	Homo sapiens	196-198
34204699-8	2021	Altogether, current findings suggest that H2S promotes protective effects against PH, and could be a relevant target for a new therapeutic strategy, using attractive H2S-releasing molecules.	Deuterium	42-45	phenylalanine hydroxylase	Homo sapiens	82-84
34204699-8	2021	Altogether, current findings suggest that H2S promotes protective effects against PH, and could be a relevant target for a new therapeutic strategy, using attractive H2S-releasing molecules.	Deuterium	166-169	phenylalanine hydroxylase	Homo sapiens	82-84
34204933-1	2021	The research on the interaction of tartrate ions with the surface of hydroskyapatite was presented, including the measurements of the kinetics of tartrate ion adsorption and tartrate ion adsorption as a function of pH.	tartaric acid	35-43	phenylalanine hydroxylase	Homo sapiens	215-217
34204933-1	2021	The research on the interaction of tartrate ions with the surface of hydroskyapatite was presented, including the measurements of the kinetics of tartrate ion adsorption and tartrate ion adsorption as a function of pH.	hydroskyapatite	69-84	phenylalanine hydroxylase	Homo sapiens	215-217
34204933-1	2021	The research on the interaction of tartrate ions with the surface of hydroskyapatite was presented, including the measurements of the kinetics of tartrate ion adsorption and tartrate ion adsorption as a function of pH.	tartaric acid	174-182	phenylalanine hydroxylase	Homo sapiens	215-217
34076793-1	2021	In most fish exhibiting external fertilization, spermatozoa become motile after release into water, triggered by differences between intracellular and extracellular conditions such as osmotic pressure, ion composition, and pH.	Water	93-98	phenylalanine hydroxylase	Homo sapiens	223-225
34540178-4	2021	Results: By increasing the amount of glutamic acid and decreasing the pH from 5.1 to 4.7, the amount of GABA production in ultra-filtration cheese significantly increased on the 15th and 30th days of production (p<=0.05), while by increasing the amount of salt the production GABA decreased on the 15th and 30th days.	gamma-Aminobutyric Acid	104-108	phenylalanine hydroxylase	Homo sapiens	70-72
34540178-5	2021	Simultaneous optimal conditions to achieve maximum GABA production in cheese on the 15th and 30th production day was respectively 167.7917 mg/kg-1 and 220.125 mg/kg-1 using 3 mg/g glutamic acid, 2% salt at pH 4.7.	gamma-Aminobutyric Acid	51-55	phenylalanine hydroxylase	Homo sapiens	206-208
34181009-7	2021	Results: At a supraphysiologic nitrite concentration (ie, 10 000 mumol/L), the mean (SD) amount of NDMA detected in 50 mL simulated gastric fluid 2 hours after adding ranitidine increased from 222 (12) ng at pH 5 to 11 822 (434) ng at pH 1.2.	Dimethylnitrosamine	99-103	phenylalanine hydroxylase	Homo sapiens	208-210
33973571-5	2021	A ratiometric fluorescent probe, fluorescein isothiocyanate-dextran (FITC-dextran) was used to facilitate a quantitative measurement of the digestive vacuole pH by flow cytometry.	fluorescein isothiocyanate dextran	33-67	phenylalanine hydroxylase	Homo sapiens	158-160
33973571-5	2021	A ratiometric fluorescent probe, fluorescein isothiocyanate-dextran (FITC-dextran) was used to facilitate a quantitative measurement of the digestive vacuole pH by flow cytometry.	fluorescein isothiocyanate dextran	69-81	phenylalanine hydroxylase	Homo sapiens	158-160
33973571-7	2021	Saponin-permeabilized parasites were analyzed to obtain the ratio of green/yellow fluorescence intensity (Rgy) plotted as a function of pH in a pH calibration curve of FITC-dextran.	Saponins	0-7	phenylalanine hydroxylase	Homo sapiens	136-138
33973571-7	2021	Saponin-permeabilized parasites were analyzed to obtain the ratio of green/yellow fluorescence intensity (Rgy) plotted as a function of pH in a pH calibration curve of FITC-dextran.	Saponins	0-7	phenylalanine hydroxylase	Homo sapiens	144-146
33973571-7	2021	Saponin-permeabilized parasites were analyzed to obtain the ratio of green/yellow fluorescence intensity (Rgy) plotted as a function of pH in a pH calibration curve of FITC-dextran.	fluorescein isothiocyanate dextran	168-180	phenylalanine hydroxylase	Homo sapiens	136-138
33973571-7	2021	Saponin-permeabilized parasites were analyzed to obtain the ratio of green/yellow fluorescence intensity (Rgy) plotted as a function of pH in a pH calibration curve of FITC-dextran.	fluorescein isothiocyanate dextran	168-180	phenylalanine hydroxylase	Homo sapiens	144-146
33973571-8	2021	Based on the pH calibration curve, the pH of the digestive vacuole of the acetone extract-treated parasites was significantly altered (pH values ranged from 6.35- 6.71) in a concentration-dependent manner compared to the untreated parasites (pH = 5.32) (p < 0.001).	Acetone	74-81	phenylalanine hydroxylase	Homo sapiens	13-15
33973571-8	2021	Based on the pH calibration curve, the pH of the digestive vacuole of the acetone extract-treated parasites was significantly altered (pH values ranged from 6.35- 6.71) in a concentration-dependent manner compared to the untreated parasites (pH = 5.32) (p < 0.001).	Acetone	74-81	phenylalanine hydroxylase	Homo sapiens	39-41
33973571-8	2021	Based on the pH calibration curve, the pH of the digestive vacuole of the acetone extract-treated parasites was significantly altered (pH values ranged from 6.35- 6.71) in a concentration-dependent manner compared to the untreated parasites (pH = 5.32) (p < 0.001).	Acetone	74-81	phenylalanine hydroxylase	Homo sapiens	135-137
33973571-8	2021	Based on the pH calibration curve, the pH of the digestive vacuole of the acetone extract-treated parasites was significantly altered (pH values ranged from 6.35- 6.71) in a concentration-dependent manner compared to the untreated parasites (pH = 5.32) (p < 0.001).	Acetone	74-81	phenylalanine hydroxylase	Homo sapiens	242-244
34181009-7	2021	Results: At a supraphysiologic nitrite concentration (ie, 10 000 mumol/L), the mean (SD) amount of NDMA detected in 50 mL simulated gastric fluid 2 hours after adding ranitidine increased from 222 (12) ng at pH 5 to 11 822 (434) ng at pH 1.2.	Dimethylnitrosamine	99-103	phenylalanine hydroxylase	Homo sapiens	235-237
34063800-6	2021	Therefore, this review aims to obtain a better understanding on the plant-mediated synthesis process of the major transition-metal and transition-metal oxide nanoparticles, and how process parameters-concentration, temperature, contact time, pH level, and calcination temperature affect their unique properties such as particle size, morphologies, and crystallinity.	Metals	125-130	phenylalanine hydroxylase	Homo sapiens	242-244
34268097-2	2021	Researchers have already established the importance of measuring basal body temperature (BBT) and the potential of hydrogen (pH).	Hydrogen	115-123	phenylalanine hydroxylase	Homo sapiens	125-127
34063800-6	2021	Therefore, this review aims to obtain a better understanding on the plant-mediated synthesis process of the major transition-metal and transition-metal oxide nanoparticles, and how process parameters-concentration, temperature, contact time, pH level, and calcination temperature affect their unique properties such as particle size, morphologies, and crystallinity.	metal oxide	146-157	phenylalanine hydroxylase	Homo sapiens	242-244
34069533-0	2021	Deciphering the Molecular Mechanism of Water Interaction with Gelatin Methacryloyl Hydrogels: Role of Ionic Strength, pH, Drug Loading and Hydrogel Network Characteristics.	Water	39-44	phenylalanine hydroxylase	Homo sapiens	118-120
34068529-8	2021	This review describes the effects of different stimuli-responsive factors, such as pH, light, temperature, and magnetic and electric fields on GO-based materials and their applications.	graphene oxide	143-145	phenylalanine hydroxylase	Homo sapiens	83-85
34064700-1	2021	Montelukast is a weak acid drug characterized by its low solubility in the range of pH 1.2 to 4.5, which may lead to dissolution-limited absorption.	montelukast	0-11	phenylalanine hydroxylase	Homo sapiens	84-86
34163836-0	2021	Time-programmable pH: decarboxylation of nitroacetic acid allows the time-controlled rising of pH to a definite value.	nitroacetic acid	41-57	phenylalanine hydroxylase	Homo sapiens	18-20
34163836-0	2021	Time-programmable pH: decarboxylation of nitroacetic acid allows the time-controlled rising of pH to a definite value.	nitroacetic acid	41-57	phenylalanine hydroxylase	Homo sapiens	95-97
34163836-1	2021	In this report it is shown that nitroacetic acid 1 (O2NCH2CO2H) can be conveniently used to control the pH of a water solution over time.	o2nch2co2h	52-62	phenylalanine hydroxylase	Homo sapiens	104-106
34163836-1	2021	In this report it is shown that nitroacetic acid 1 (O2NCH2CO2H) can be conveniently used to control the pH of a water solution over time.	Water	112-117	phenylalanine hydroxylase	Homo sapiens	104-106
34163836-4	2021	As a proof of concept, the method is applied to control over time the pH-dependent host-guest interaction between alpha-cyclodextrin and p-aminobenzoic acid.	alpha-cyclodextrin	114-132	phenylalanine hydroxylase	Homo sapiens	70-72
34163836-4	2021	As a proof of concept, the method is applied to control over time the pH-dependent host-guest interaction between alpha-cyclodextrin and p-aminobenzoic acid.	4-Aminobenzoic Acid	137-156	phenylalanine hydroxylase	Homo sapiens	70-72
34164065-6	2021	Furthermore, NAAs self-assemble into vesicles at acidic pH, signifying their ability to form protocellular membranes under acidic geothermal conditions.	naas	13-17	phenylalanine hydroxylase	Homo sapiens	56-58
34248011-2	2021	A 24 factorial design was employed to check the effect of four factors namely pH, current density, electrolysis time and electrolyte concentration set at their high (+) and low (-) levels on the antibiotics (amoxicillin, ciprofloxacin and erythromycin) degradation in water.	Water	268-273	phenylalanine hydroxylase	Homo sapiens	78-80
34386396-9	2021	Lactate correlated positively with initial plasma glucose (IPG) (P = 0.001) and APACHE-II Score (P = 0.002); correlated negatively with systolic blood pressure (P = 0.003), pH (P = 0.002) and severity of DKA (P = 0.001).	Lactic Acid	0-7	phenylalanine hydroxylase	Homo sapiens	173-175
34193668-9	2021	The ionization of the carboxylic acid groups in the bola-type amphiphilic molecule with increasing pH is disadvantageous for micelle formation.	Carboxylic Acids	22-37	phenylalanine hydroxylase	Homo sapiens	99-101
35523347-4	2022	Across the pH range, the Be sorption curve was divided into three phases, these being pH 3-6, pH 6-10, and pH > 10, within which sorption of Be with soil was 9-97%, 90-97%, and 66-90%, respectively.	Beryllium	141-143	phenylalanine hydroxylase	Homo sapiens	11-13
34505758-0	2021	Influence of non-ionic, ionic and lipophilic polymers on the pH and conductivity of model ointments, creams and gels.	Polymers	45-53	phenylalanine hydroxylase	Homo sapiens	61-63
34745572-6	2021	Cryptophane sensors designed for proteins, metal ions, nucleic acids, pH, and temperature have achieved nanomolar-to-femtomolar limits of detection via a combination of 129Xe hyperpolarization and chemical exchange saturation transfer (CEST) techniques.	cryptophane	0-11	phenylalanine hydroxylase	Homo sapiens	70-72
35429934-0	2022	Zein-whey protein isolate-carboxymethyl cellulose complex as carrier of apigenin via pH-driven method: Fabrication, characterization, stability, and in vitro release property.	Carboxymethylcellulose Sodium	26-49	phenylalanine hydroxylase	Homo sapiens	85-87
35594627-0	2022	Machine learning based urinary pH sensing using polyaniline deposited paper device and integration of smart web app interface: Theory to application.	polyaniline	48-59	phenylalanine hydroxylase	Homo sapiens	31-33
35523347-4	2022	Across the pH range, the Be sorption curve was divided into three phases, these being pH 3-6, pH 6-10, and pH > 10, within which sorption of Be with soil was 9-97%, 90-97%, and 66-90%, respectively.	Beryllium	141-143	phenylalanine hydroxylase	Homo sapiens	86-88
35594627-1	2022	The present study employs density functional theory-based first principle calculation to investigate the electron transport properties of polyaniline following exposure to acidic and alkaline pH.	polyaniline	138-149	phenylalanine hydroxylase	Homo sapiens	192-194
35523347-4	2022	Across the pH range, the Be sorption curve was divided into three phases, these being pH 3-6, pH 6-10, and pH > 10, within which sorption of Be with soil was 9-97%, 90-97%, and 66-90%, respectively.	Beryllium	141-143	phenylalanine hydroxylase	Homo sapiens	94-96
35594627-2	2022	In-situ deposited polyaniline-based paper device maintains emeraldine salt form while it is exposed to acidic pH and converts to emeraldine base when it is subjected to alkaline pH solutions.	polyaniline	18-29	phenylalanine hydroxylase	Homo sapiens	110-112
35594627-2	2022	In-situ deposited polyaniline-based paper device maintains emeraldine salt form while it is exposed to acidic pH and converts to emeraldine base when it is subjected to alkaline pH solutions.	polyaniline	18-29	phenylalanine hydroxylase	Homo sapiens	178-180
35523347-4	2022	Across the pH range, the Be sorption curve was divided into three phases, these being pH 3-6, pH 6-10, and pH > 10, within which sorption of Be with soil was 9-97%, 90-97%, and 66-90%, respectively.	Beryllium	141-143	phenylalanine hydroxylase	Homo sapiens	107-109
35523347-5	2022	Beryllium solubility was limited at pH > 7, but a sorption study with soil showed chemisorption under both acidic and alkaline pH (pH 5.5 and 8) conditions, which was confirmed by FTIR and XPS analysis.	Beryllium	0-9	phenylalanine hydroxylase	Homo sapiens	36-38
35523347-7	2022	The irreversible chemisorption mechanism was controlled by SOM at higher pH, and by metal oxyhydroxides at lower pH.	metal oxyhydroxides	84-103	phenylalanine hydroxylase	Homo sapiens	113-115
35523347-8	2022	Both organic and inorganic components synergistically influence the specific chemisorption of Be at the intermediate pH 5.5 of field soil.	Beryllium	94-96	phenylalanine hydroxylase	Homo sapiens	117-119
35466483-1	2022	Aryl trifluoromethyl diazomethanes 2-R (R = Ph, OMe, CF 3 ) are readily decomposed by the (o-carboranyl)diphosphine gold(I) complex 1 .	aryl trifluoromethyl diazomethanes 2-r	0-38	phenylalanine hydroxylase	Homo sapiens	44-46
35594627-2	2022	In-situ deposited polyaniline-based paper device maintains emeraldine salt form while it is exposed to acidic pH and converts to emeraldine base when it is subjected to alkaline pH solutions.	emeraldine base	129-144	phenylalanine hydroxylase	Homo sapiens	178-180
35183964-0	2022	pH-driven-assembled soy peptide nanoparticles as particulate emulsifier for oil-in-water Pickering emulsion and their potential for encapsulation of vitamin D3.	Oils	76-79	phenylalanine hydroxylase	Homo sapiens	0-2
35183964-0	2022	pH-driven-assembled soy peptide nanoparticles as particulate emulsifier for oil-in-water Pickering emulsion and their potential for encapsulation of vitamin D3.	Water	83-88	phenylalanine hydroxylase	Homo sapiens	0-2
35183964-0	2022	pH-driven-assembled soy peptide nanoparticles as particulate emulsifier for oil-in-water Pickering emulsion and their potential for encapsulation of vitamin D3.	Cholecalciferol	149-159	phenylalanine hydroxylase	Homo sapiens	0-2
35500463-0	2022	A wearable electrochemical sensor based on beta-CD functionalized graphene for pH and potassium ion analysis in sweat.	Graphite	66-74	phenylalanine hydroxylase	Homo sapiens	79-81
35500463-2	2022	The sensor was composed of flexible reference electrode, pH response electrode and K+ selective electrode, which were prepared through printing beta-CD functionalized graphene (beta-CD/RGO) water suspension on conductive PET substrate with microelectronic printer.	Graphite	167-175	phenylalanine hydroxylase	Homo sapiens	57-59
35500463-2	2022	The sensor was composed of flexible reference electrode, pH response electrode and K+ selective electrode, which were prepared through printing beta-CD functionalized graphene (beta-CD/RGO) water suspension on conductive PET substrate with microelectronic printer.	Water	190-195	phenylalanine hydroxylase	Homo sapiens	57-59
35466483-1	2022	Aryl trifluoromethyl diazomethanes 2-R (R = Ph, OMe, CF 3 ) are readily decomposed by the (o-carboranyl)diphosphine gold(I) complex 1 .	(o-carboranyl)diphosphine gold	90-120	phenylalanine hydroxylase	Homo sapiens	44-46
35466483-2	2022	The resulting alpha -CF 3 substituted carbene complexes 3-R have been characterized by multi-nuclear NMR spectroscopy as well as X-ray crystallography (for 3-Ph ).	carbene	38-45	phenylalanine hydroxylase	Homo sapiens	158-160
35466483-4	2022	Reactivity studies under stoichiometric and catalytic conditions substantiate typical carbene-type behavior for 3-Ph .	carbene	86-93	phenylalanine hydroxylase	Homo sapiens	114-116
35219199-0	2022	Boron-induced activation of Ru nanoparticles anchored on carbon nanotubes for the enhanced pH-independent hydrogen evolution reaction.	Boron	0-5	phenylalanine hydroxylase	Homo sapiens	91-93
35219199-0	2022	Boron-induced activation of Ru nanoparticles anchored on carbon nanotubes for the enhanced pH-independent hydrogen evolution reaction.	Ruthenium	28-30	phenylalanine hydroxylase	Homo sapiens	91-93
35219199-0	2022	Boron-induced activation of Ru nanoparticles anchored on carbon nanotubes for the enhanced pH-independent hydrogen evolution reaction.	Carbon	57-63	phenylalanine hydroxylase	Homo sapiens	91-93
35219199-0	2022	Boron-induced activation of Ru nanoparticles anchored on carbon nanotubes for the enhanced pH-independent hydrogen evolution reaction.	Hydrogen	106-114	phenylalanine hydroxylase	Homo sapiens	91-93
35594846-3	2022	Since the surface pH of cell membrane is regulated by the transport of gases such as CO2and NH3, inferring the membrane properties can be done indirectly from pH measurements.	co2and	85-91	phenylalanine hydroxylase	Homo sapiens	18-20
35500782-8	2022	The highest fluoride removal was observed at pH 4 and found to decrease with increasing pH.	Fluorides	12-20	phenylalanine hydroxylase	Homo sapiens	45-47
35500782-8	2022	The highest fluoride removal was observed at pH 4 and found to decrease with increasing pH.	Fluorides	12-20	phenylalanine hydroxylase	Homo sapiens	88-90
35594846-3	2022	Since the surface pH of cell membrane is regulated by the transport of gases such as CO2and NH3, inferring the membrane properties can be done indirectly from pH measurements.	co2and	85-91	phenylalanine hydroxylase	Homo sapiens	159-161
35608856-0	2022	Unveiling the pH-Dependent Yields of H2O2 and OH by Aqueous-Phase Ozonolysis of m-Cresol in the Atmosphere.	Hydrogen Peroxide	37-41	phenylalanine hydroxylase	Homo sapiens	14-16
35107866-0	2022	gamma-Fe2 O3 Loading Mitoxantrone and Glucose Oxidase for pH-Responsive Chemo/Chemodynamic/Photothermal Synergistic Cancer Therapy.	gamma-fe2 o3	0-12	phenylalanine hydroxylase	Homo sapiens	58-60
35107866-0	2022	gamma-Fe2 O3 Loading Mitoxantrone and Glucose Oxidase for pH-Responsive Chemo/Chemodynamic/Photothermal Synergistic Cancer Therapy.	Mitoxantrone	21-33	phenylalanine hydroxylase	Homo sapiens	58-60
35107866-6	2022	After entering cancer cells by endocytosis, MTO-GOx@gamma-Fe2 O3 NPs decompose into Fe3+ ions and release cargo because of their pH-responsive characteristic.	ferric sulfate	84-88	phenylalanine hydroxylase	Homo sapiens	129-131
35212261-9	2022	Sleep-related hypoventilation (end-tidal CO2 > 50 mmHg for > 25% total sleep time) was present in 25% of children with PH compared to 6.3% of children without PH (adjusted prevalence ratio (PR) = 2.73; 95% CI 1.18-6.35).	Carbon Dioxide	41-44	phenylalanine hydroxylase	Homo sapiens	119-121
35412020-3	2022	The parameters affecting fluorometric detection of uranium ions, such as the pH, solvent type, ligand concentration, interaction time, and interfering ions, were investigated and adjusted.	Uranium	51-58	phenylalanine hydroxylase	Homo sapiens	77-79
35532846-3	2022	Herein, by using reversible addition-fragmentation chain transfer method, an NH-based poly(hydroxyethyl methacrylate-co-N,N-dimethylaminoethyl methacrylate) and cross-linked by poly(ethylene glycol)diacrylate with pH responsiveness character was developed.	poly(hydroxyethyl methacrylate-co-n,n-dimethylaminoethyl methacrylate	86-155	phenylalanine hydroxylase	Homo sapiens	214-216
35532846-3	2022	Herein, by using reversible addition-fragmentation chain transfer method, an NH-based poly(hydroxyethyl methacrylate-co-N,N-dimethylaminoethyl methacrylate) and cross-linked by poly(ethylene glycol)diacrylate with pH responsiveness character was developed.	poly(ethylene glycol)diacrylate	177-208	phenylalanine hydroxylase	Homo sapiens	214-216
35150934-2	2022	The present study explores the severity of PH-related lesions that can be provided by a genetic particular model in accordance to the most common non-genetic PH inducers such as chronic exposure to hypoxia or single injection of monocrotaline.	Monocrotaline	229-242	phenylalanine hydroxylase	Homo sapiens	43-45
35150934-2	2022	The present study explores the severity of PH-related lesions that can be provided by a genetic particular model in accordance to the most common non-genetic PH inducers such as chronic exposure to hypoxia or single injection of monocrotaline.	Monocrotaline	229-242	phenylalanine hydroxylase	Homo sapiens	158-160
35358878-1	2022	A proper pH environment is essential for a wide variety of industries and applications especially related to water treatment.	Water	109-114	phenylalanine hydroxylase	Homo sapiens	9-11
35506537-4	2022	Taking advantage of the pH-dependent molecular rearrangement, Cy-TPA NPs under weak acidic conditions exhibit enhanced near-infrared absorption and "turn on" fluorescence and photothermal performance.	cy-tpa	62-68	phenylalanine hydroxylase	Homo sapiens	24-26
35569853-1	2022	Here, nanocomposite-decorated laser-induced graphene-based flexible hybrid sensor is newly developed for simultaneous detection of heavy metals, pesticides, and pH in freshwater.	Graphite	44-52	phenylalanine hydroxylase	Homo sapiens	161-163
35569853-7	2022	Furthermore, a polyaniline/antimony/laser-induced graphene-based pH sensor is also integrated, showing an excellent sensitivity of -72.08 mV pH-1 in the pH range (2-9).	polyaniline	15-26	phenylalanine hydroxylase	Homo sapiens	65-67
35569853-7	2022	Furthermore, a polyaniline/antimony/laser-induced graphene-based pH sensor is also integrated, showing an excellent sensitivity of -72.08 mV pH-1 in the pH range (2-9).	polyaniline	15-26	phenylalanine hydroxylase	Homo sapiens	141-143
35569853-7	2022	Furthermore, a polyaniline/antimony/laser-induced graphene-based pH sensor is also integrated, showing an excellent sensitivity of -72.08 mV pH-1 in the pH range (2-9).	polyaniline	15-26	phenylalanine hydroxylase	Homo sapiens	153-155
35569853-7	2022	Furthermore, a polyaniline/antimony/laser-induced graphene-based pH sensor is also integrated, showing an excellent sensitivity of -72.08 mV pH-1 in the pH range (2-9).	Graphite	50-58	phenylalanine hydroxylase	Homo sapiens	65-67
35569853-7	2022	Furthermore, a polyaniline/antimony/laser-induced graphene-based pH sensor is also integrated, showing an excellent sensitivity of -72.08 mV pH-1 in the pH range (2-9).	Graphite	50-58	phenylalanine hydroxylase	Homo sapiens	141-143
35569853-7	2022	Furthermore, a polyaniline/antimony/laser-induced graphene-based pH sensor is also integrated, showing an excellent sensitivity of -72.08 mV pH-1 in the pH range (2-9).	Graphite	50-58	phenylalanine hydroxylase	Homo sapiens	153-155
35535664-3	2022	It was found that a design concept with an oxygen-responsive dye in polymer nanoparticles and a pH-responsive dye in an organically modified siloxane polymer resulted in a robust pH/O2 dual optical sensor.	Oxygen	43-49	phenylalanine hydroxylase	Homo sapiens	179-181
35535664-3	2022	It was found that a design concept with an oxygen-responsive dye in polymer nanoparticles and a pH-responsive dye in an organically modified siloxane polymer resulted in a robust pH/O2 dual optical sensor.	siloxane polymer	141-157	phenylalanine hydroxylase	Homo sapiens	96-98
35535664-3	2022	It was found that a design concept with an oxygen-responsive dye in polymer nanoparticles and a pH-responsive dye in an organically modified siloxane polymer resulted in a robust pH/O2 dual optical sensor.	siloxane polymer	141-157	phenylalanine hydroxylase	Homo sapiens	179-181
35535664-3	2022	It was found that a design concept with an oxygen-responsive dye in polymer nanoparticles and a pH-responsive dye in an organically modified siloxane polymer resulted in a robust pH/O2 dual optical sensor.	Oxygen	182-184	phenylalanine hydroxylase	Homo sapiens	96-98
35535664-3	2022	It was found that a design concept with an oxygen-responsive dye in polymer nanoparticles and a pH-responsive dye in an organically modified siloxane polymer resulted in a robust pH/O2 dual optical sensor.	Oxygen	182-184	phenylalanine hydroxylase	Homo sapiens	179-181
35608856-0	2022	Unveiling the pH-Dependent Yields of H2O2 and OH by Aqueous-Phase Ozonolysis of m-Cresol in the Atmosphere.	3-cresol	80-88	phenylalanine hydroxylase	Homo sapiens	14-16
35608856-4	2022	Here, we show that the aqueous-phase reaction of dissolved ozone (O3) with substituted phenols such as m-cresol represents an important source of H2O2 and OH exhibiting pH-dependent yields.	Ozone	59-64	phenylalanine hydroxylase	Homo sapiens	169-171
35608856-4	2022	Here, we show that the aqueous-phase reaction of dissolved ozone (O3) with substituted phenols such as m-cresol represents an important source of H2O2 and OH exhibiting pH-dependent yields.	Ozone	66-68	phenylalanine hydroxylase	Homo sapiens	169-171
35608856-4	2022	Here, we show that the aqueous-phase reaction of dissolved ozone (O3) with substituted phenols such as m-cresol represents an important source of H2O2 and OH exhibiting pH-dependent yields.	Phenols	87-94	phenylalanine hydroxylase	Homo sapiens	169-171
35608856-4	2022	Here, we show that the aqueous-phase reaction of dissolved ozone (O3) with substituted phenols such as m-cresol represents an important source of H2O2 and OH exhibiting pH-dependent yields.	3-cresol	103-111	phenylalanine hydroxylase	Homo sapiens	169-171
35608856-4	2022	Here, we show that the aqueous-phase reaction of dissolved ozone (O3) with substituted phenols such as m-cresol represents an important source of H2O2 and OH exhibiting pH-dependent yields.	Hydrogen Peroxide	146-150	phenylalanine hydroxylase	Homo sapiens	169-171
35608856-5	2022	Intriguingly, the formation of H2O2 through the ring-opening mechanism is strongly promoted under lower pH conditions (pH 2.5-3.5), while higher pH favors the ring-retaining pathways yielding OH.	Hydrogen Peroxide	31-35	phenylalanine hydroxylase	Homo sapiens	104-106
35235698-3	2022	Combined GPC and 31 P DOSY NMR spectroscopic analyses, quantum chemical computations, and stoichiometric reactions disclose a P-H bond activation by the cooperative action of the square-planar aluminate and the electron-rich ligand framework.	Aluminate	193-202	phenylalanine hydroxylase	Homo sapiens	126-129
35608856-5	2022	Intriguingly, the formation of H2O2 through the ring-opening mechanism is strongly promoted under lower pH conditions (pH 2.5-3.5), while higher pH favors the ring-retaining pathways yielding OH.	Hydrogen Peroxide	31-35	phenylalanine hydroxylase	Homo sapiens	119-121
35608856-5	2022	Intriguingly, the formation of H2O2 through the ring-opening mechanism is strongly promoted under lower pH conditions (pH 2.5-3.5), while higher pH favors the ring-retaining pathways yielding OH.	Hydrogen Peroxide	31-35	phenylalanine hydroxylase	Homo sapiens	145-147
35608856-6	2022	The rate constant of the reaction of O3 with m-cresol increases with increasing pH.	Ozone	37-39	phenylalanine hydroxylase	Homo sapiens	80-82
35608856-6	2022	The rate constant of the reaction of O3 with m-cresol increases with increasing pH.	3-cresol	45-53	phenylalanine hydroxylase	Homo sapiens	80-82
35588340-5	2022	Lactate plays a critical role in normal physiology of humans including an energy source, a signaling molecule and a pH regulator.	Lactic Acid	0-7	phenylalanine hydroxylase	Homo sapiens	116-118
35588340-6	2022	Depending on the pH, lactate exists as the protonated acidic form (lactic acid) at low pH or as sodium salt (sodium lactate) at basic pH.	Lactic Acid	21-28	phenylalanine hydroxylase	Homo sapiens	17-19
35589004-0	2022	Biosynthesis of folic acid appended PHBV modified copper oxide nanorods for pH sensitive drug release in targeted breast cancer therapy.	Folic Acid	16-26	phenylalanine hydroxylase	Homo sapiens	76-78
35585102-0	2022	Quantifying local pH changes in carbonate electrolyte during copper-catalysed (Formula: see text) electroreduction using in operando (Formula: see text) NMR.	Carbonates	32-41	phenylalanine hydroxylase	Homo sapiens	18-20
35585102-0	2022	Quantifying local pH changes in carbonate electrolyte during copper-catalysed (Formula: see text) electroreduction using in operando (Formula: see text) NMR.	Copper	61-67	phenylalanine hydroxylase	Homo sapiens	18-20
35151973-0	2022	A dual-functional polyaniline film-based flexible electrochemical sensor for the detection of pH and lactate in sweat of the human body.	polyaniline	18-29	phenylalanine hydroxylase	Homo sapiens	94-96
35589004-0	2022	Biosynthesis of folic acid appended PHBV modified copper oxide nanorods for pH sensitive drug release in targeted breast cancer therapy.	cupric oxide	50-62	phenylalanine hydroxylase	Homo sapiens	76-78
35589004-4	2022	The pH-sensitive CuO-PTX@PHBV-PEG-FA nanosystem was successfully developed, as evidenced by number of characterizations.	cuo-ptx	17-24	phenylalanine hydroxylase	Homo sapiens	4-6
35589004-4	2022	The pH-sensitive CuO-PTX@PHBV-PEG-FA nanosystem was successfully developed, as evidenced by number of characterizations.	peg-fa	30-36	phenylalanine hydroxylase	Homo sapiens	4-6
35562544-3	2022	Soda lakes are natural environments rich in carbonate and bicarbonate water, resulting in elevated pH and salinities that frequently approach saturation.	Carbonates	44-53	phenylalanine hydroxylase	Homo sapiens	99-101
35588340-6	2022	Depending on the pH, lactate exists as the protonated acidic form (lactic acid) at low pH or as sodium salt (sodium lactate) at basic pH.	Lactic Acid	21-28	phenylalanine hydroxylase	Homo sapiens	87-89
35588340-6	2022	Depending on the pH, lactate exists as the protonated acidic form (lactic acid) at low pH or as sodium salt (sodium lactate) at basic pH.	Lactic Acid	21-28	phenylalanine hydroxylase	Homo sapiens	134-136
35562544-3	2022	Soda lakes are natural environments rich in carbonate and bicarbonate water, resulting in elevated pH and salinities that frequently approach saturation.	Bicarbonates	58-69	phenylalanine hydroxylase	Homo sapiens	99-101
35562544-3	2022	Soda lakes are natural environments rich in carbonate and bicarbonate water, resulting in elevated pH and salinities that frequently approach saturation.	Water	70-75	phenylalanine hydroxylase	Homo sapiens	99-101
35560241-4	2022	The initial viscosity of thickened water samples (pH 5.3 and 7.4) was reduced by 80% after only 5 s of in vitro oral digestion.	Water	35-40	phenylalanine hydroxylase	Homo sapiens	50-52
35600090-2	2022	Without a functional copy of PAH, levels of Phe in the blood and tissues rise, resulting in potentially life-threatening damage to the central nervous system.	Phenylalanine	44-47	phenylalanine hydroxylase	Homo sapiens	29-32
35629830-5	2022	At present, existing pH-sensitive materials are mainly based on polyaniline (PANI), hydrogen ionophores (HIs) and metal oxides (MOx).	metal oxides	114-126	phenylalanine hydroxylase	Homo sapiens	21-23
35471651-0	2022	T- and pH-dependent OH radical reaction kinetics with glycine, alanine, serine, and threonine in the aqueous phase.	Glycine	54-61	phenylalanine hydroxylase	Homo sapiens	7-9
35471651-0	2022	T- and pH-dependent OH radical reaction kinetics with glycine, alanine, serine, and threonine in the aqueous phase.	Alanine	63-70	phenylalanine hydroxylase	Homo sapiens	7-9
35471651-0	2022	T- and pH-dependent OH radical reaction kinetics with glycine, alanine, serine, and threonine in the aqueous phase.	Serine	72-78	phenylalanine hydroxylase	Homo sapiens	7-9
35471651-0	2022	T- and pH-dependent OH radical reaction kinetics with glycine, alanine, serine, and threonine in the aqueous phase.	Threonine	84-93	phenylalanine hydroxylase	Homo sapiens	7-9
35471651-3	2022	In the present study, the aqueous phase reaction kinetics of hydroxyl radicals ( OH) with the four amino acids is investigated using the competition kinetics method under controlled temperature and pH conditions.	Hydroxyl Radical	61-78	phenylalanine hydroxylase	Homo sapiens	198-200
35467846-4	2022	The core analytical design of these smart bandages integrated wound dressing of poly(vinyl acrylic) gel@PANI/Cu2O NPs for instigating pH-responsive current during the wound healing process.	poly(vinyl acrylic)	80-99	phenylalanine hydroxylase	Homo sapiens	134-136
35007589-7	2022	The immobilized colloids can be more easily released by alkaline DI-water (pH 11.0) than acidic one (pH 6.0) as a result of the more negative surface charges of the immobilized bentonite colloids.	Water	68-73	phenylalanine hydroxylase	Homo sapiens	75-77
35629830-5	2022	At present, existing pH-sensitive materials are mainly based on polyaniline (PANI), hydrogen ionophores (HIs) and metal oxides (MOx).	MOX	128-131	phenylalanine hydroxylase	Homo sapiens	21-23
35120400-4	2022	The red and green luminescence of a novel dendritic polyamine Pt-porphyrin and fluorescein conjugate quantitatively responds to oxygen and pH, respectively, and enables robust sensing.	pt-porphyrin	62-74	phenylalanine hydroxylase	Homo sapiens	139-141
35218123-2	2022	Previously, we reported an ultra-pH-sensitive (UPS) nanoprobe library with a sharp pH response using co-polymerization of two tertiary amine-containing monomers with distinct pKa .	Amines	135-140	phenylalanine hydroxylase	Homo sapiens	33-35
35218123-2	2022	Previously, we reported an ultra-pH-sensitive (UPS) nanoprobe library with a sharp pH response using co-polymerization of two tertiary amine-containing monomers with distinct pKa .	Amines	135-140	phenylalanine hydroxylase	Homo sapiens	83-85
35218123-3	2022	Currently, we have generalized the UPS nanoparticle library with tunable pH transitions (pHt ) by copolymerization of a tertiary amine-containing monomer with a series of non-ionizable monomers.	Amines	129-134	phenylalanine hydroxylase	Homo sapiens	73-75
35120400-4	2022	The red and green luminescence of a novel dendritic polyamine Pt-porphyrin and fluorescein conjugate quantitatively responds to oxygen and pH, respectively, and enables robust sensing.	Polyamines	52-61	phenylalanine hydroxylase	Homo sapiens	139-141
35120400-4	2022	The red and green luminescence of a novel dendritic polyamine Pt-porphyrin and fluorescein conjugate quantitatively responds to oxygen and pH, respectively, and enables robust sensing.	Fluorescein	79-90	phenylalanine hydroxylase	Homo sapiens	139-141
35120400-7	2022	The hydrogel formulation exhibits a robust and validated visible red-orange-green "traffic light" spectrum in response to oxygen changes, regardless of swelling state, pH, or autofluorescence from skin, thereby enabling clinician friendly naked-eye feedback.	Oxygen	122-128	phenylalanine hydroxylase	Homo sapiens	168-170
35122829-7	2022	Moreover, 5-FU could gradually release from chitosan at a more acidic pH (tumor tissues) environment.	Fluorouracil	10-14	phenylalanine hydroxylase	Homo sapiens	70-72
35351554-0	2022	Response of nitrogen removal performance and microbial community to a wide range of pH in thermophilic denitrification system.	Nitrogen	12-20	phenylalanine hydroxylase	Homo sapiens	84-86
35351554-3	2022	The results showed that thermophilic denitrification could adapt to pH 5-11, but suffered from obvious nitrite and ammonia accumulation at pH 3.	Ammonia	115-122	phenylalanine hydroxylase	Homo sapiens	139-141
35351554-5	2022	Besides, the potential selecting advantage of nitrate reducing bacteria over nitrite reducing bacteria and the enrichment of dissimilatory nitrate reduction to ammonium (DNRA) bacteria could be responsible for the nitrite and ammonia accumulation at pH 3.	Nitrates	46-53	phenylalanine hydroxylase	Homo sapiens	250-252
35351554-5	2022	Besides, the potential selecting advantage of nitrate reducing bacteria over nitrite reducing bacteria and the enrichment of dissimilatory nitrate reduction to ammonium (DNRA) bacteria could be responsible for the nitrite and ammonia accumulation at pH 3.	Nitrites	77-84	phenylalanine hydroxylase	Homo sapiens	250-252
35351554-5	2022	Besides, the potential selecting advantage of nitrate reducing bacteria over nitrite reducing bacteria and the enrichment of dissimilatory nitrate reduction to ammonium (DNRA) bacteria could be responsible for the nitrite and ammonia accumulation at pH 3.	Nitrates	139-146	phenylalanine hydroxylase	Homo sapiens	250-252
35351554-5	2022	Besides, the potential selecting advantage of nitrate reducing bacteria over nitrite reducing bacteria and the enrichment of dissimilatory nitrate reduction to ammonium (DNRA) bacteria could be responsible for the nitrite and ammonia accumulation at pH 3.	Ammonium Compounds	160-168	phenylalanine hydroxylase	Homo sapiens	250-252
35351554-5	2022	Besides, the potential selecting advantage of nitrate reducing bacteria over nitrite reducing bacteria and the enrichment of dissimilatory nitrate reduction to ammonium (DNRA) bacteria could be responsible for the nitrite and ammonia accumulation at pH 3.	dnra	170-174	phenylalanine hydroxylase	Homo sapiens	250-252
35351554-5	2022	Besides, the potential selecting advantage of nitrate reducing bacteria over nitrite reducing bacteria and the enrichment of dissimilatory nitrate reduction to ammonium (DNRA) bacteria could be responsible for the nitrite and ammonia accumulation at pH 3.	Nitrites	214-221	phenylalanine hydroxylase	Homo sapiens	250-252
35351554-5	2022	Besides, the potential selecting advantage of nitrate reducing bacteria over nitrite reducing bacteria and the enrichment of dissimilatory nitrate reduction to ammonium (DNRA) bacteria could be responsible for the nitrite and ammonia accumulation at pH 3.	Ammonia	226-233	phenylalanine hydroxylase	Homo sapiens	250-252
35168105-2	2022	In this study, redox and pH dual-responsive nanocarriers (CPNPs) were prepared through molecular assembly by utilizing the Schiff base interactions of cystamine (Cys), PEG-NH2 and formaldehyde (FA) under aqueous conditions with a one-pot, one-step technique.	Schiff Bases	123-134	phenylalanine hydroxylase	Homo sapiens	25-27
35168105-2	2022	In this study, redox and pH dual-responsive nanocarriers (CPNPs) were prepared through molecular assembly by utilizing the Schiff base interactions of cystamine (Cys), PEG-NH2 and formaldehyde (FA) under aqueous conditions with a one-pot, one-step technique.	Cystamine	151-160	phenylalanine hydroxylase	Homo sapiens	25-27
35168105-2	2022	In this study, redox and pH dual-responsive nanocarriers (CPNPs) were prepared through molecular assembly by utilizing the Schiff base interactions of cystamine (Cys), PEG-NH2 and formaldehyde (FA) under aqueous conditions with a one-pot, one-step technique.	Cystamine	162-165	phenylalanine hydroxylase	Homo sapiens	25-27
35168105-2	2022	In this study, redox and pH dual-responsive nanocarriers (CPNPs) were prepared through molecular assembly by utilizing the Schiff base interactions of cystamine (Cys), PEG-NH2 and formaldehyde (FA) under aqueous conditions with a one-pot, one-step technique.	peg-nh2	168-175	phenylalanine hydroxylase	Homo sapiens	25-27
35168105-2	2022	In this study, redox and pH dual-responsive nanocarriers (CPNPs) were prepared through molecular assembly by utilizing the Schiff base interactions of cystamine (Cys), PEG-NH2 and formaldehyde (FA) under aqueous conditions with a one-pot, one-step technique.	Formaldehyde	180-192	phenylalanine hydroxylase	Homo sapiens	25-27
35168105-4	2022	In addition, doxorubicin (DOX) was encapsulated in CPNPs simply by changing the pH (DOX@CPNPs), and pH/GSH-responsive release behaviour was confirmed.	Doxorubicin	13-24	phenylalanine hydroxylase	Homo sapiens	80-82
35168105-4	2022	In addition, doxorubicin (DOX) was encapsulated in CPNPs simply by changing the pH (DOX@CPNPs), and pH/GSH-responsive release behaviour was confirmed.	Doxorubicin	13-24	phenylalanine hydroxylase	Homo sapiens	100-102
35168105-4	2022	In addition, doxorubicin (DOX) was encapsulated in CPNPs simply by changing the pH (DOX@CPNPs), and pH/GSH-responsive release behaviour was confirmed.	Doxorubicin	26-29	phenylalanine hydroxylase	Homo sapiens	80-82
35168105-4	2022	In addition, doxorubicin (DOX) was encapsulated in CPNPs simply by changing the pH (DOX@CPNPs), and pH/GSH-responsive release behaviour was confirmed.	Doxorubicin	26-29	phenylalanine hydroxylase	Homo sapiens	100-102
35168105-4	2022	In addition, doxorubicin (DOX) was encapsulated in CPNPs simply by changing the pH (DOX@CPNPs), and pH/GSH-responsive release behaviour was confirmed.	Doxorubicin	84-87	phenylalanine hydroxylase	Homo sapiens	80-82
35168105-4	2022	In addition, doxorubicin (DOX) was encapsulated in CPNPs simply by changing the pH (DOX@CPNPs), and pH/GSH-responsive release behaviour was confirmed.	Glutathione	103-106	phenylalanine hydroxylase	Homo sapiens	100-102
35325557-1	2022	Phenylketonuria (PKU) is an autosomal recessive disease caused by variants in the gene that encodes phenylalanine hydroxylase (PAH), limiting the metabolism of phenylalanine (Phe).	Phenylalanine	160-173	phenylalanine hydroxylase	Homo sapiens	100-125
35325557-1	2022	Phenylketonuria (PKU) is an autosomal recessive disease caused by variants in the gene that encodes phenylalanine hydroxylase (PAH), limiting the metabolism of phenylalanine (Phe).	Phenylalanine	160-173	phenylalanine hydroxylase	Homo sapiens	127-130
35325557-1	2022	Phenylketonuria (PKU) is an autosomal recessive disease caused by variants in the gene that encodes phenylalanine hydroxylase (PAH), limiting the metabolism of phenylalanine (Phe).	Phenylalanine	175-178	phenylalanine hydroxylase	Homo sapiens	100-125
35325557-1	2022	Phenylketonuria (PKU) is an autosomal recessive disease caused by variants in the gene that encodes phenylalanine hydroxylase (PAH), limiting the metabolism of phenylalanine (Phe).	Phenylalanine	175-178	phenylalanine hydroxylase	Homo sapiens	127-130
35325557-2	2022	When PAH activity is absent or hindered, Phe is not converted to tyrosine, leading to an accumulation of Phe in the blood, which can cause serious neurological complications.	Phenylalanine	41-44	phenylalanine hydroxylase	Homo sapiens	5-8
35325557-2	2022	When PAH activity is absent or hindered, Phe is not converted to tyrosine, leading to an accumulation of Phe in the blood, which can cause serious neurological complications.	Phenylalanine	105-108	phenylalanine hydroxylase	Homo sapiens	5-8
35631542-6	2022	Metronidazole was released from the NCHGs within 12 h, but chlorhexidine showed a much longer elution time with strong pH dependence, which lasted more than 7 days as it was corroborated by the bactericidal effect.	Chlorhexidine	59-72	phenylalanine hydroxylase	Homo sapiens	119-121
35449354-4	2022	However, recent evidence revealed that PAH tetramers exist as a mixture of resting state and activated state whose transition depends upon the phenylalanine concentration and certain PAH variants that fail to modulate the structural equilibrium are associated with PKU disease.	Phenylalanine	143-156	phenylalanine hydroxylase	Homo sapiens	39-42
35486460-5	2022	The conditions of pH, biomass concentration, temperature, time, agitation and Initial concentration of metal for biosorption of Pb (II) were optimized.	pb (ii)	128-135	phenylalanine hydroxylase	Homo sapiens	18-20
35080964-1	2022	Inherent characteristics of native starches such as water insolubility, retrogradation and syneresis, and instability in harsh processing conditions (e.g., high temperature and shearing, low pH) limit their industrial applications.	Starch	35-43	phenylalanine hydroxylase	Homo sapiens	191-193
35323087-8	2022	Glycolate concentrations were related to categorical clinical outcomes (acute kidney injury, mortality), and correlated with continuous surrogate biochemical measurements (anion gap, base excess, bicarbonate concentration and pH).	glycolic acid	0-9	phenylalanine hydroxylase	Homo sapiens	226-228
35324974-7	2022	The effects of pH, concentration, temperature, and time on the adsorption of methylene blue dye using BC-COF bio-leather were also evaluated using ultraviolet-visible spectroscopy and zeta potential measurement.	Methylene Blue	77-91	phenylalanine hydroxylase	Homo sapiens	15-17
35324974-8	2022	The results showed that BC-COF was found to be most effective when pH 6 of methylene blue solution with a concentration of 50 mg/L was adsorbed for 30 minutes at 25 C. Moreover, BC-COF could be reused for multiple times and had better dye adsorption rate compared to the original BC.	Methylene Blue	75-89	phenylalanine hydroxylase	Homo sapiens	67-69
35392227-0	2022	pH-Responsive Polymer Nanomaterials for Tumor Therapy.	Polymers	14-21	phenylalanine hydroxylase	Homo sapiens	0-2
35392227-6	2022	In this review, recent advances in, and common applications of, pH-responsive polymer nanomaterials for drug delivery in cancer therapy are summarized, with a focus on the different types of pH-responsive polymers.	Polymers	78-85	phenylalanine hydroxylase	Homo sapiens	64-66
35392227-6	2022	In this review, recent advances in, and common applications of, pH-responsive polymer nanomaterials for drug delivery in cancer therapy are summarized, with a focus on the different types of pH-responsive polymers.	Polymers	78-85	phenylalanine hydroxylase	Homo sapiens	191-193
35382283-4	2022	The scavenger was found to adsorb only Ag(I), Pd(II), and Au(III) from an aqueous media in the presence of coexisting ions of different bases and precious metals at wide ranges of pH and acid concentration.	poly-4-dioxan-2-one	46-52	phenylalanine hydroxylase	Homo sapiens	180-182
35382283-4	2022	The scavenger was found to adsorb only Ag(I), Pd(II), and Au(III) from an aqueous media in the presence of coexisting ions of different bases and precious metals at wide ranges of pH and acid concentration.	au(iii)	58-65	phenylalanine hydroxylase	Homo sapiens	180-182
35335706-0	2022	Impact of Fluorinated Ionic Liquids on Human Phenylalanine Hydroxylase-A Potential Drug Delivery System.	fluorinated ionic liquids	10-35	phenylalanine hydroxylase	Homo sapiens	45-70
35335706-4	2022	In this work, biophysical methods were used to evaluate the potential of (N1112(OH))(C4F9SO3), a biocompatible fluorinated ionic liquid (FIL), as a delivery system of hPAH.	(n1112(oh))(c4f9so3	73-92	phenylalanine hydroxylase	Homo sapiens	167-171
35335706-5	2022	The results herein presented show that (N1112(OH))(C4F9SO3) spontaneously forms micelles in a solution that can encapsulate hPAH.	(n1112(oh))(c4f9so3	39-58	phenylalanine hydroxylase	Homo sapiens	124-128
35335706-7	2022	The influence of (N1112(OH))(C4F9SO3) on the complex oligomerization equilibrium of hPAH was also assessed.	(n1112(oh))(c4f9so3)	17-37	phenylalanine hydroxylase	Homo sapiens	84-88
35233669-6	2022	The lower residual oil on sand with coexisting nanoclay was found to be at pH 7.	Oils	19-22	phenylalanine hydroxylase	Homo sapiens	75-77
35353163-2	2022	Objective: To compare changes in the vaginal microbiota, metabolome, and pH among women using low-dose vaginal estradiol tablet or low pH moisturizer gel for 12-weeks vs low pH placebo.	Estradiol	111-120	phenylalanine hydroxylase	Homo sapiens	73-75
35353163-11	2022	The 12-week pH among women in the estradiol group was lower vs placebo (median (IQR) pH, 5 (4.5-6.0) vs 6 (5.5-7.0); P = .005) but not the moisturizer group vs placebo (median (IQR) pH, 6 (5.5-6.5); P = .28).	Estradiol	34-43	phenylalanine hydroxylase	Homo sapiens	12-14
35353163-11	2022	The 12-week pH among women in the estradiol group was lower vs placebo (median (IQR) pH, 5 (4.5-6.0) vs 6 (5.5-7.0); P = .005) but not the moisturizer group vs placebo (median (IQR) pH, 6 (5.5-6.5); P = .28).	Estradiol	34-43	phenylalanine hydroxylase	Homo sapiens	85-87
35353163-14	2022	Conclusions and Relevance: This secondary analysis of a randomized clinical trial found that use of vaginal estradiol tablets resulted in substantial changes in the vaginal microbiota and metabolome with a lowering in pH, particularly in women with high-diversity bacterial communities at baseline.	Estradiol	108-117	phenylalanine hydroxylase	Homo sapiens	218-220
35629830-5	2022	At present, existing pH-sensitive materials are mainly based on polyaniline (PANI), hydrogen ionophores (HIs) and metal oxides (MOx).	polyaniline	64-75	phenylalanine hydroxylase	Homo sapiens	21-23
35629830-5	2022	At present, existing pH-sensitive materials are mainly based on polyaniline (PANI), hydrogen ionophores (HIs) and metal oxides (MOx).	polyaniline	77-81	phenylalanine hydroxylase	Homo sapiens	21-23
35629830-5	2022	At present, existing pH-sensitive materials are mainly based on polyaniline (PANI), hydrogen ionophores (HIs) and metal oxides (MOx).	Hydrogen	84-92	phenylalanine hydroxylase	Homo sapiens	21-23
35629830-5	2022	At present, existing pH-sensitive materials are mainly based on polyaniline (PANI), hydrogen ionophores (HIs) and metal oxides (MOx).	Histidine	105-108	phenylalanine hydroxylase	Homo sapiens	21-23
35366497-3	2022	Landfill leachate with a high content of humic acids can be efficiently treated by pH sensitive flocculation at pH 2.0, reducing COD value in 86.1% and colour in 84.7%.	Humic Substances	41-52	phenylalanine hydroxylase	Homo sapiens	83-85
35366497-3	2022	Landfill leachate with a high content of humic acids can be efficiently treated by pH sensitive flocculation at pH 2.0, reducing COD value in 86.1% and colour in 84.7%.	Humic Substances	41-52	phenylalanine hydroxylase	Homo sapiens	112-114
35366497-4	2022	Mechanism of pH sensitive flocculation is based in protonation first of phenolic groups and later of carboxylic acid groups in the HAs molecules, resulting in a reduction of Zeta potential value.	Carboxylic Acids	101-116	phenylalanine hydroxylase	Homo sapiens	13-15
35501613-2	2022	Simultaneous detection of nitrates, phosphates, and pH is of importance in soil and water analysis, agriculture, and food quality assessment.	Water	84-89	phenylalanine hydroxylase	Homo sapiens	52-54
35501613-3	2022	This article demonstrates a suite of stainless steel microneedle electrochemical sensors for multiplexed measurement of pH, nitrate, and phosphate using faradaic capacitance derived from cyclic voltammetry as the mode of detection.	Stainless Steel	37-52	phenylalanine hydroxylase	Homo sapiens	120-122
35044732-7	2022	RESULTS: Multivariable linear regression analysis showed that except for 2-hydroxyphenanthrene, PAH metabolites correlated positively with In(HE4) after adjustment for relevant covariates (all P < 0.05).	Phenanthren-2-ol	73-94	phenylalanine hydroxylase	Homo sapiens	96-99
35449354-20	2022	USP19 increases the enzymatic activity of PAH, thus maintaining normal Phe levels.	Phenylalanine	71-74	phenylalanine hydroxylase	Homo sapiens	42-45
35445300-12	2022	In contrast, the N2O emissions from the growing season were controlled by soil temperature, water table level, pH, NH4+-N, NO3--N, total nitrogen, total organic carbon, and C/N ratio, which could explain 14.51-45.72% of the temporal variation of N2O emissions.	Nitrous Oxide	17-20	phenylalanine hydroxylase	Homo sapiens	111-113
35458077-0	2022	Interaction of Mg Alloy with PLA Electrospun Nanofibers Coating in Understanding Changes of Corrosion, Wettability, and pH.	Magnesium	15-17	phenylalanine hydroxylase	Homo sapiens	120-122
35458077-7	2022	Taking into account corrosion rate, wettability, and pH changes, an empiric model of the interaction of Mg alloy with PLA nanofibers is proposed.	Magnesium	104-106	phenylalanine hydroxylase	Homo sapiens	53-55
35114635-4	2022	Fluorescent investigation demonstrated that the probe is not only highly stable under interferences of pH, ionic strength, and irradiation, but also significantly selective toward ClO- amongst a variety of attractive bioactive species through the fluorescent quenching process which was correlative with the concentration of ClO- and linearly in the range of 0.1-50 mumol L-1 with the sensitivity of 0.03 mumol L-1.	Hypochlorous Acid	180-183	phenylalanine hydroxylase	Homo sapiens	103-105
35420780-4	2022	In addition, a precision targeted therapy system was designed based on the pH level and glutathione response, and it can be effectively used to target CD24high cells to induce lysosomal escape and drug burst release through CO2 production, resulting in enhanced ferroptosis and macrophage phagocytosis through FSP1 and CD24 inhibition mediated by the NF2-YAP signaling axis.	Carbon Dioxide	224-227	phenylalanine hydroxylase	Homo sapiens	75-77
35430250-8	2022	CONCLUSIONS: Empiric treatment with sildenafil in infants with BPD-PH is a superior strategy with both decreased costs and increased effectiveness when compared with catheterization-obligate treatment.	Sildenafil Citrate	36-46	phenylalanine hydroxylase	Homo sapiens	67-69
35445216-0	2022	Effect of pH on the Properties of Hydrogels Cross-Linked via Dynamic Thia-Michael Addition Bonds.	thia	69-73	phenylalanine hydroxylase	Homo sapiens	10-12
35445216-4	2022	Poly(ethylene glycol)-based hydrogels were cross-linked with a reversible thia-Michael addition reaction in aqueous buffer between pH 3 and pH 7.	Polyethylene Glycols	0-21	phenylalanine hydroxylase	Homo sapiens	131-133
35445216-4	2022	Poly(ethylene glycol)-based hydrogels were cross-linked with a reversible thia-Michael addition reaction in aqueous buffer between pH 3 and pH 7.	Polyethylene Glycols	0-21	phenylalanine hydroxylase	Homo sapiens	140-142
35445216-4	2022	Poly(ethylene glycol)-based hydrogels were cross-linked with a reversible thia-Michael addition reaction in aqueous buffer between pH 3 and pH 7.	thia	74-78	phenylalanine hydroxylase	Homo sapiens	131-133
35445216-4	2022	Poly(ethylene glycol)-based hydrogels were cross-linked with a reversible thia-Michael addition reaction in aqueous buffer between pH 3 and pH 7.	thia	74-78	phenylalanine hydroxylase	Homo sapiens	140-142
35458731-2	2022	Lignin samples were characterized by measuring their ash content, hydroxyl content (Phosphorus Nuclear Magnetic Resonance Spectroscopy), impurities (Inductively Coupled Plasma), and pH.	Lignin	0-6	phenylalanine hydroxylase	Homo sapiens	182-184
35458731-7	2022	Lignin-based foams that passed all required performance testing were made with lignins having higher pH, potassium, sodium, calcium, magnesium, and aliphatic/p-hydroxyphenyl hydroxyl group contents than those that failed.	Lignin	79-86	phenylalanine hydroxylase	Homo sapiens	101-103
35411999-1	2022	A series of oxidized di(indolyl)arylmethanes (DIAM) with polyaromatic signaling moieties have been designed for monitoring local pH at interfacial region of surfactant aggregates, such as micelles and vesicles etc.	diam	46-50	phenylalanine hydroxylase	Homo sapiens	129-131
35411999-7	2022	Thus, it is evident that probes can predict as well as quantify the local pH change using the pseudophase ion exchange formalism.	formalism	119-128	phenylalanine hydroxylase	Homo sapiens	74-76
35384399-6	2022	RESULTS: Calcium hydroxide group showed the highest median pH value at all time points (7, 14, and 28 days).	Calcium Hydroxide	9-26	phenylalanine hydroxylase	Homo sapiens	59-61
35384399-7	2022	Both calcium hydroxide and bioceramic sealer groups showed significantly higher median pH values compared with control (p < .001).	Calcium Hydroxide	5-22	phenylalanine hydroxylase	Homo sapiens	87-89
35384399-8	2022	Comparing within groups, both bioceramic sealer group and calcium hydroxide group showed significantly decreased median pH over time, while the median pH of the control did not show any significant difference among Days 7, 14, and 28.	Calcium Hydroxide	58-75	phenylalanine hydroxylase	Homo sapiens	120-122
35311850-2	2022	The result shows that with different grafting densities and grafting lengths, zwitterionic polymer brushes show typical pH- and salt-responsiveness features.	Polymers	91-98	phenylalanine hydroxylase	Homo sapiens	120-122
35311850-5	2022	Differently, compared with the pH effect, the salt concentration has an obvious impact on the switching effect, i.e., responsiveness emerges with a lower grafting density and length.	Salts	46-50	phenylalanine hydroxylase	Homo sapiens	31-33
35311850-6	2022	This work provides molecular level mechanism and theoretical guidance for the design of smart nanopores modified by zwitterionic polymer brushes, as well as plays an important role in the construction of nanopores with antifouling and pH/salt-responsive properties.	Polymers	129-136	phenylalanine hydroxylase	Homo sapiens	235-237
34999400-10	2022	Multi-linear regression analysis indicated that nitrogen release was closely related to biochar nitrogen content, pH and average pore width.	Nitrogen	48-56	phenylalanine hydroxylase	Homo sapiens	114-116
34999400-11	2022	Phosphate release was inversely related to pH and positively related to average pore width.	Phosphates	0-9	phenylalanine hydroxylase	Homo sapiens	43-45
34995593-7	2022	The major drawback of porous concrete is the high pH (>8.5) of the effluent water, decalcification of the porous concrete and leaching of adsorbed pollutants.	Water	76-81	phenylalanine hydroxylase	Homo sapiens	50-52
35124562-4	2022	Besides, the Cr(VI) reduction enhancement decreased with the increase of pH and initial Cr(VI) concentration or increased with the increase of ferric sludge dosage.	chromium hexavalent ion	13-19	phenylalanine hydroxylase	Homo sapiens	73-75
35408134-0	2022	Non-Destructive Measurement of Acetic Acid and Its Distribution in a Photovoltaic Module during Damp Heat Testing Using pH-Sensitive Fluorescent Dye Sensors.	Acetic Acid	31-42	phenylalanine hydroxylase	Homo sapiens	120-122
35408134-1	2022	An optical pH sensor that enables the non-destructive measurement of acetic acid and its distribution in a photovoltaic module during damp heat (DH) testing is reported.	Acetic Acid	69-80	phenylalanine hydroxylase	Homo sapiens	11-13
35335932-3	2022	An optimal SC formulation of ketamine would thus have a pH and osmolality close to physiological levels, without compromising on concentration and, thus, injection volume.	Ketamine	29-37	phenylalanine hydroxylase	Homo sapiens	56-58
35335932-6	2022	We describe the development of a novel Captisol -based formulation strategy to achieve an elevated pH, isosmotic and buffered formulation of ketamine (hence, three birds, one excipient) without compromising on concentration.	SBE4-beta-cyclodextrin	39-47	phenylalanine hydroxylase	Homo sapiens	99-101
35335932-6	2022	We describe the development of a novel Captisol -based formulation strategy to achieve an elevated pH, isosmotic and buffered formulation of ketamine (hence, three birds, one excipient) without compromising on concentration.	Ketamine	141-149	phenylalanine hydroxylase	Homo sapiens	99-101
35150337-0	2022	Not just a background: pH buffers do interact with lanthanide ions-a Europium(III) case study.	Lanthanoid Series Elements	51-61	phenylalanine hydroxylase	Homo sapiens	23-25
32233704-9	2022	More cesarean deliveries were performed in the lactate group (16.5 vs. 12.4%; RR: 1.33; 95% CI: 1.02-1.74).Conclusion: When analyzing lactate or pH in fetal scalp blood during second stage of labor neonatal outcomes were comparable.	Lactic Acid	47-54	phenylalanine hydroxylase	Homo sapiens	145-147
35356682-6	2022	We show that intravenous infusion of LUNAR-hPAH mRNA can generate high levels of hPAH protein in hepatocytes and restore the Phe metabolism in the Pah enu2 mouse model.	Phenylalanine	125-128	phenylalanine hydroxylase	Homo sapiens	43-47
35133360-3	2022	One typical molecule, HBT-ASD-2, emits three kinds of fluorescence output signal at 438 nm and 545 nm for NAS-DCE under different pH values (5.0, 7.4 and 10, respectively).	ethylene dichloride	110-113	phenylalanine hydroxylase	Homo sapiens	130-132
35142483-4	2022	The sensor was fabricated via a simple and facile approach using the cold atmospheric plasma technique in which a pH sensitive silica coating was deposited from a siloxane precursor onto a carbon electrode.	Silicon Dioxide	127-133	phenylalanine hydroxylase	Homo sapiens	114-116
35142483-4	2022	The sensor was fabricated via a simple and facile approach using the cold atmospheric plasma technique in which a pH sensitive silica coating was deposited from a siloxane precursor onto a carbon electrode.	Siloxanes	163-171	phenylalanine hydroxylase	Homo sapiens	114-116
35142483-4	2022	The sensor was fabricated via a simple and facile approach using the cold atmospheric plasma technique in which a pH sensitive silica coating was deposited from a siloxane precursor onto a carbon electrode.	Carbon	189-195	phenylalanine hydroxylase	Homo sapiens	114-116
35147033-7	2022	In addition, this adsorbent shows a high extraction efficiency for uranium under a wide range of pH conditions and exhibits good regeneration performance.	Uranium	67-74	phenylalanine hydroxylase	Homo sapiens	97-99
35167021-6	2022	Maximum phosphate removal and granulation efficiencies obtained were 91.25% and 82.55%, respectively, at 500 mg/L phosphate concentration, pH 12, and calcium to phosphorous molar ratio 1.65.	Phosphates	8-17	phenylalanine hydroxylase	Homo sapiens	139-141
35119286-0	2022	Complex pH-Dependent Interactions between Weak Polyelectrolyte Block Copolymer Micelles and Molecular Fluorophores.	copolymer	69-78	phenylalanine hydroxylase	Homo sapiens	8-10
35119286-4	2022	Here, we investigate whether the pH-driven morphological response of polyelectrolyte-bearing nanostructures also affects the interactions of these nanostructures with molecules in solution, using micelles of a short-chain polybutadiene-block-poly(acrylic acid) (pBd-pAA) as a model system.	polybutadiene-block-poly(acrylic acid)	222-260	phenylalanine hydroxylase	Homo sapiens	33-35
35119286-4	2022	Here, we investigate whether the pH-driven morphological response of polyelectrolyte-bearing nanostructures also affects the interactions of these nanostructures with molecules in solution, using micelles of a short-chain polybutadiene-block-poly(acrylic acid) (pBd-pAA) as a model system.	pbd-paa	262-269	phenylalanine hydroxylase	Homo sapiens	33-35
35425587-0	2022	Photoluminescent polymer micelles with thermo-/pH-/metal responsibility and their features in selective optical sensing of Pd(ii) cations.	Polymers	17-24	phenylalanine hydroxylase	Homo sapiens	47-49
35425587-0	2022	Photoluminescent polymer micelles with thermo-/pH-/metal responsibility and their features in selective optical sensing of Pd(ii) cations.	poly-4-dioxan-2-one	123-129	phenylalanine hydroxylase	Homo sapiens	47-49
35176311-9	2022	CONCLUSION: Intrinsic LV diastolic impairment is directly associated with higher indices of PH in infants with DS and may be a contributing factor to its evolution.	Deuterium	111-113	phenylalanine hydroxylase	Homo sapiens	92-94
35081310-0	2022	Structure and pH-Induced Swelling of Polymer Films Prepared from Sequentially Grafted Polyelectrolytes.	Polyelectrolytes	86-102	phenylalanine hydroxylase	Homo sapiens	14-16
35122829-8	2022	These results revealed the underlying atomic interaction mechanism between 5-FU and chitosan at various pH levels, and may be helpful in the design of chitosan-based drug delivery systems.	Fluorouracil	75-79	phenylalanine hydroxylase	Homo sapiens	104-106
35068137-6	2022	Taking advantage of the excellent dual pH-/photo-responsive color switching properties, we demonstrated the potential applications of the TiO2-x nanoparticles/NR/agarose gel film in dynamic rewritable paper, in which the created patterns by photo-printing produce dynamic color changing upon applying an acidic or a basic vapor.	titanium dioxide	138-142	phenylalanine hydroxylase	Homo sapiens	39-41
35068137-6	2022	Taking advantage of the excellent dual pH-/photo-responsive color switching properties, we demonstrated the potential applications of the TiO2-x nanoparticles/NR/agarose gel film in dynamic rewritable paper, in which the created patterns by photo-printing produce dynamic color changing upon applying an acidic or a basic vapor.	Sepharose	162-169	phenylalanine hydroxylase	Homo sapiens	39-41
35200648-4	2022	A major challenge is to account for the highly dynamic microenvironmental conditions experienced by Prochloron&nbsp;in hospite, where light-dark cycles drive rapid shifts between hyperoxia and anoxia as well as pH variations from pH ~6 to ~10.	prochloron&nbsp	100-115	phenylalanine hydroxylase	Homo sapiens	211-213
35200648-4	2022	A major challenge is to account for the highly dynamic microenvironmental conditions experienced by Prochloron&nbsp;in hospite, where light-dark cycles drive rapid shifts between hyperoxia and anoxia as well as pH variations from pH ~6 to ~10.	prochloron&nbsp	100-115	phenylalanine hydroxylase	Homo sapiens	230-232
34653468-6	2022	In addition, the key factors influencing secondary formation of imidazoles, such as relative humidity, water-soluble inorganic ions, and pH, were analyzed.	Imidazoles	64-74	phenylalanine hydroxylase	Homo sapiens	137-139
35093398-9	2022	CONCLUSIONS: Hypocitraturia and elevated pH is seen during topiramate use with resultant higher rate of calcium phosphate stone formation compared to the general population.	Topiramate	59-69	phenylalanine hydroxylase	Homo sapiens	41-43
35093398-10	2022	Stopping topiramate leads to significant increase in citrate excretion and normalization of pH.	Topiramate	9-19	phenylalanine hydroxylase	Homo sapiens	92-94
35091541-0	2022	Venetoclax-ponatinib for T315I/compound-mutated Ph+ acute lymphoblastic leukemia.	ponatinib	11-20	phenylalanine hydroxylase	Homo sapiens	48-50
35160450-5	2022	Firstly, we investigated albumin dynamics and calculated electrostatic surfaces at experimental pH values in water by using molecular dynamics methods.	Water	109-114	phenylalanine hydroxylase	Homo sapiens	96-98
35060541-9	2022	In addition, PH may be also associated with all-cause mortality, although it was statistically attenuated after IPTW adjustment.	iptw	112-116	phenylalanine hydroxylase	Homo sapiens	13-15
35000378-1	2022	In this work, a T2-T1 switchable superparamagnetic iron oxide nanoprobe with a pH/H2O2 dual response was obtained using a microemulsion method.	ferric oxide	51-61	phenylalanine hydroxylase	Homo sapiens	79-81
35000378-1	2022	In this work, a T2-T1 switchable superparamagnetic iron oxide nanoprobe with a pH/H2O2 dual response was obtained using a microemulsion method.	Hydrogen Peroxide	82-86	phenylalanine hydroxylase	Homo sapiens	79-81
35000378-5	2022	When this occurred, the T2 MRI signal was converted into a T1 MRI signal, achieving specific detection of tumors by a pH/H2O2 dual-response T2-T1 MRI.	Hydrogen Peroxide	121-125	phenylalanine hydroxylase	Homo sapiens	118-120
34904988-3	2022	Over the past few decades, the addition of P-H bonds to alkenes, alkynes, arenes, heteroarenes and other unsaturated substrates in hydrophosphination and other related reactions via the above-mentioned catalytic processes has emerged as an atom economical approach to obtain organophosphorus compounds.	Alkenes	56-63	phenylalanine hydroxylase	Homo sapiens	43-46
34904988-3	2022	Over the past few decades, the addition of P-H bonds to alkenes, alkynes, arenes, heteroarenes and other unsaturated substrates in hydrophosphination and other related reactions via the above-mentioned catalytic processes has emerged as an atom economical approach to obtain organophosphorus compounds.	Alkynes	65-72	phenylalanine hydroxylase	Homo sapiens	43-46
34904988-3	2022	Over the past few decades, the addition of P-H bonds to alkenes, alkynes, arenes, heteroarenes and other unsaturated substrates in hydrophosphination and other related reactions via the above-mentioned catalytic processes has emerged as an atom economical approach to obtain organophosphorus compounds.	arenes	74-80	phenylalanine hydroxylase	Homo sapiens	43-46
34904988-3	2022	Over the past few decades, the addition of P-H bonds to alkenes, alkynes, arenes, heteroarenes and other unsaturated substrates in hydrophosphination and other related reactions via the above-mentioned catalytic processes has emerged as an atom economical approach to obtain organophosphorus compounds.	heteroarenes	82-94	phenylalanine hydroxylase	Homo sapiens	43-46
34904988-3	2022	Over the past few decades, the addition of P-H bonds to alkenes, alkynes, arenes, heteroarenes and other unsaturated substrates in hydrophosphination and other related reactions via the above-mentioned catalytic processes has emerged as an atom economical approach to obtain organophosphorus compounds.	organophosphorus	275-291	phenylalanine hydroxylase	Homo sapiens	43-46
34904988-4	2022	In most of the catalytic cycles, the P-H bond is cleaved to yield a phosphorus-based radical, which adds onto the unsaturated substrate followed by reduction of the corresponding radical yielding the product.	Phosphorus	68-78	phenylalanine hydroxylase	Homo sapiens	37-40
35159647-1	2022	In this study, we report the realization of drug-loaded smart magnetic nanocarriers constituted by superparamagnetic iron oxide nanoparticles encapsulated in a dual pH- and temperature-responsive poly (N-vinylcaprolactam-co-acrylic acid) copolymer to achieve highly controlled drug release and localized magnetic hyperthermia.	ferric oxide	117-127	phenylalanine hydroxylase	Homo sapiens	165-167
35159647-1	2022	In this study, we report the realization of drug-loaded smart magnetic nanocarriers constituted by superparamagnetic iron oxide nanoparticles encapsulated in a dual pH- and temperature-responsive poly (N-vinylcaprolactam-co-acrylic acid) copolymer to achieve highly controlled drug release and localized magnetic hyperthermia.	poly (n-vinylcaprolactam-co-acrylic acid) copolymer	196-247	phenylalanine hydroxylase	Homo sapiens	165-167
35159647-4	2022	The efficacy of the system was proved by loading doxorubicin with very high encapsulation efficiency (>96.0%) at neutral pH.	Doxorubicin	49-60	phenylalanine hydroxylase	Homo sapiens	121-123
35159647-5	2022	The double pH- and temperature-responsive nature of the magnetic nanocarriers facilitated a burst, almost complete release of the drug at acidic pH under hyperthermia conditions, while a negligible amount of doxorubicin was released at physiological body temperature at neutral pH, confirming that in addition to pH variation, drug release can be improved by hyperthermia treatment.	Doxorubicin	208-219	phenylalanine hydroxylase	Homo sapiens	278-280
35159647-5	2022	The double pH- and temperature-responsive nature of the magnetic nanocarriers facilitated a burst, almost complete release of the drug at acidic pH under hyperthermia conditions, while a negligible amount of doxorubicin was released at physiological body temperature at neutral pH, confirming that in addition to pH variation, drug release can be improved by hyperthermia treatment.	Doxorubicin	208-219	phenylalanine hydroxylase	Homo sapiens	313-315
35022664-13	2022	TRANSLATIONAL PERSPECTIVE: In heart failure (HF) related (Group 2) PH, despite remodeling of pulmonary veins (PV) and arteries (PA), therapies targeting PA biology altered in Group 1 PH have not shown consistent benefit.	Protactinium	153-155	phenylalanine hydroxylase	Homo sapiens	183-185
35022299-9	2022	CONCLUSIONS: In Chinese patients with AIS caused by anterior circulation LVO, the risk of PH was positively associated with low admission ASPECTS, serum glucose >7 mmol/L, and NLR, but negatively related to underlying ICAS and intracranial angioplasty/stenting.	Glucose	153-160	phenylalanine hydroxylase	Homo sapiens	90-92
35062515-3	2022	The pH of the local environment is shown to be determined by the chemistry and the electrochemical response of the redox active species on the surface of the electrode; the local pH can be controlled by the electropolymerized salicylic acid moieties due to the acid concentration on the surface, avoiding any perturbation in environmental pH and leading to a stable novel reference system.	Salicylic Acid	226-240	phenylalanine hydroxylase	Homo sapiens	179-181
35062515-0	2022	Electropolymerised pH Insensitive Salicylic Acid Reference Systems: Utilization in a Novel pH Sensor for Food and Environmental Monitoring.	Salicylic Acid	34-48	phenylalanine hydroxylase	Homo sapiens	19-21
35062515-0	2022	Electropolymerised pH Insensitive Salicylic Acid Reference Systems: Utilization in a Novel pH Sensor for Food and Environmental Monitoring.	Salicylic Acid	34-48	phenylalanine hydroxylase	Homo sapiens	91-93
35062515-1	2022	This work summarizes the electrochemical response of a salicylic acid-based carbon electrode for use as a novel solid-state reference electrode in a redox-based pH sensor.	Salicylic Acid	55-69	phenylalanine hydroxylase	Homo sapiens	161-163
35062515-1	2022	This work summarizes the electrochemical response of a salicylic acid-based carbon electrode for use as a novel solid-state reference electrode in a redox-based pH sensor.	Carbon	76-82	phenylalanine hydroxylase	Homo sapiens	161-163
35062515-3	2022	The pH of the local environment is shown to be determined by the chemistry and the electrochemical response of the redox active species on the surface of the electrode; the local pH can be controlled by the electropolymerized salicylic acid moieties due to the acid concentration on the surface, avoiding any perturbation in environmental pH and leading to a stable novel reference system.	Salicylic Acid	226-240	phenylalanine hydroxylase	Homo sapiens	4-6
35082602-1	2021	Phenylketonuria is a recessive genetic disorder of amino-acid metabolism, where impaired phenylalanine hydroxylase function leads to the accumulation of neurotoxic phenylalanine levels in the brain.	Phenylalanine	164-177	phenylalanine hydroxylase	Homo sapiens	89-114
35056740-3	2022	Here, we designed and synthesized a novel theranostic agent H6M based on the "double-locked" strategy by introducing an electron-withdrawing nitro group into 1-position of a pH-responsive 3-amino-beta-carboline and further covalently linking the hydroxamic acid group, a zinc-binding group (ZBG), to the 3-position of beta-carboline to obtain histone deacetylase (HDAC) inhibitory effect for combined HDAC-targeted therapy.	nitro	141-146	phenylalanine hydroxylase	Homo sapiens	174-176
35056740-3	2022	Here, we designed and synthesized a novel theranostic agent H6M based on the "double-locked" strategy by introducing an electron-withdrawing nitro group into 1-position of a pH-responsive 3-amino-beta-carboline and further covalently linking the hydroxamic acid group, a zinc-binding group (ZBG), to the 3-position of beta-carboline to obtain histone deacetylase (HDAC) inhibitory effect for combined HDAC-targeted therapy.	3-Amino-9H-pyrido[3,4-b]indole	188-210	phenylalanine hydroxylase	Homo sapiens	174-176
35056740-3	2022	Here, we designed and synthesized a novel theranostic agent H6M based on the "double-locked" strategy by introducing an electron-withdrawing nitro group into 1-position of a pH-responsive 3-amino-beta-carboline and further covalently linking the hydroxamic acid group, a zinc-binding group (ZBG), to the 3-position of beta-carboline to obtain histone deacetylase (HDAC) inhibitory effect for combined HDAC-targeted therapy.	norharman	318-332	phenylalanine hydroxylase	Homo sapiens	174-176
35056740-4	2022	We found that H6M can be specifically reduced under overexpressed nitroreductase (NTR) to produce H6AQ, which emits bright fluorescence at low pH.	h6aq	98-102	phenylalanine hydroxylase	Homo sapiens	143-145
35056714-3	2022	Regarding the release of the entrapped amino acids and di-peptides, their hydrophobicity and the pH had a significant effect, whereas the concentration of the dissolved compound did not lead to different release kinetics.	Dipeptides	55-66	phenylalanine hydroxylase	Homo sapiens	97-99
35071907-3	2022	The influences of the pH, ion category, and concentration on methylene blue adsorption were investigated.	Methylene Blue	61-75	phenylalanine hydroxylase	Homo sapiens	22-24
34988841-3	2022	Also, the probe absorption spectrum shows a clear pH dependence, and the probe aqueous solution (ethanol/water = 1:2, borate buffer) responds selectively and sensitively through its fluorescence spectrum to the presence of Cu2+.	cupric ion	223-227	phenylalanine hydroxylase	Homo sapiens	50-52
35062515-3	2022	The pH of the local environment is shown to be determined by the chemistry and the electrochemical response of the redox active species on the surface of the electrode; the local pH can be controlled by the electropolymerized salicylic acid moieties due to the acid concentration on the surface, avoiding any perturbation in environmental pH and leading to a stable novel reference system.	Salicylic Acid	226-240	phenylalanine hydroxylase	Homo sapiens	339-341
35062515-5	2022	This reference system is paired with a new pH sensing element based on electropolymerized flavanone to provide a calibration free, pH sensitive sensor to effectively and accurately measure the pH of various media with high viscosity, low conductivity, low/high buffer concentration or cell-culture environment, presenting a maximum error of +/-0.03 pH units.	flavanone	90-99	phenylalanine hydroxylase	Homo sapiens	43-45
35062515-5	2022	This reference system is paired with a new pH sensing element based on electropolymerized flavanone to provide a calibration free, pH sensitive sensor to effectively and accurately measure the pH of various media with high viscosity, low conductivity, low/high buffer concentration or cell-culture environment, presenting a maximum error of +/-0.03 pH units.	flavanone	90-99	phenylalanine hydroxylase	Homo sapiens	131-133
35062515-5	2022	This reference system is paired with a new pH sensing element based on electropolymerized flavanone to provide a calibration free, pH sensitive sensor to effectively and accurately measure the pH of various media with high viscosity, low conductivity, low/high buffer concentration or cell-culture environment, presenting a maximum error of +/-0.03 pH units.	flavanone	90-99	phenylalanine hydroxylase	Homo sapiens	193-195
35062515-5	2022	This reference system is paired with a new pH sensing element based on electropolymerized flavanone to provide a calibration free, pH sensitive sensor to effectively and accurately measure the pH of various media with high viscosity, low conductivity, low/high buffer concentration or cell-culture environment, presenting a maximum error of +/-0.03 pH units.	flavanone	90-99	phenylalanine hydroxylase	Homo sapiens	349-351
2611059-0	1989	Effect of diatrizoate on renal extraction of PAH in man.	Diatrizoate	10-21	phenylalanine hydroxylase	Homo sapiens	45-48
35140568-0	2022	Formulation and evaluation of pH activated dosage form as minitablets in capsule for delivery of fesoterodine.	fesoterodine	97-109	phenylalanine hydroxylase	Homo sapiens	30-32
35187277-5	2022	The sensor consists of different electrodes printed on polydimethylsiloxane (PDMS) substrate for pH and moisture sensing.	baysilon	55-75	phenylalanine hydroxylase	Homo sapiens	97-99
35187277-5	2022	The sensor consists of different electrodes printed on polydimethylsiloxane (PDMS) substrate for pH and moisture sensing.	baysilon	77-81	phenylalanine hydroxylase	Homo sapiens	97-99
2574153-1	1989	The coding region of the phenylalanine hydroxylase (PAH) gene contains 22 CpG dinucleotides, including five doublets in the seventh exon of the gene.	cytidylyl-3'-5'-guanosine	74-91	phenylalanine hydroxylase	Homo sapiens	25-50
2574153-1	1989	The coding region of the phenylalanine hydroxylase (PAH) gene contains 22 CpG dinucleotides, including five doublets in the seventh exon of the gene.	cytidylyl-3'-5'-guanosine	74-91	phenylalanine hydroxylase	Homo sapiens	52-55
2840952-2	1988	Molecular cloning and DNA sequence analyses revealed that the MspI polymorphism was created by a T to C transition in exon 9 of the human PAH gene, which also resulted in the conversion of a leucine codon to a proline codon.	Proline	210-217	phenylalanine hydroxylase	Homo sapiens	138-141
2675639-8	1989	Organic anion (p-aminohippurate; PAH) uptake is driven by exchange for certain divalent organic anions, e.g., glutarate and alpha-ketoglutarate.	p-Aminohippuric Acid	15-31	phenylalanine hydroxylase	Homo sapiens	33-36
2675639-8	1989	Organic anion (p-aminohippurate; PAH) uptake is driven by exchange for certain divalent organic anions, e.g., glutarate and alpha-ketoglutarate.	Glutarates	110-119	phenylalanine hydroxylase	Homo sapiens	33-36
2675639-8	1989	Organic anion (p-aminohippurate; PAH) uptake is driven by exchange for certain divalent organic anions, e.g., glutarate and alpha-ketoglutarate.	Ketoglutaric Acids	124-143	phenylalanine hydroxylase	Homo sapiens	33-36
3146175-0	1988	[Nitrated polycyclic aromatic hydrocarbons (nitro-PAH) in suspended particles in the atmosphere.	Polycyclic Aromatic Hydrocarbons	10-42	phenylalanine hydroxylase	Homo sapiens	50-53
3186165-6	1988	Hence, the major part of phenylalanine oxidizing activity in the embryonic liver is related to the enzyme immunochemically identical with the PH of adult liver but differing from it in some structural and functional properties.	Phenylalanine	25-38	phenylalanine hydroxylase	Homo sapiens	142-144
3054749-12	1988	We did not observe any variation of creatinine, inulin clearances or variation of urinary electrolytes output PAH clearance was significantly decreased during alpacilline infusion.	alpacilline	159-170	phenylalanine hydroxylase	Homo sapiens	110-113
2889273-4	1987	The locations of these genes and the evolutionary distance between their sequences suggest that at least three distinct genetic events have occurred during the evolution of the aromatic amino acid hydroxylase superfamily: two sequential gene duplications giving rise to the three distinct hydroxylase loci, and a translocation which separated the tryptophan and tyrosine hydroxylase loci on chromosome 11 from the phenylalanine hydroxylase locus on chromosome 12.	Tryptophan	347-357	phenylalanine hydroxylase	Homo sapiens	414-439
3370253-1	1988	Phenylalanine hydroxylase was detected among human liver bioptats and autoptats extracted with 0.4% Triton X-100 from the 105,000 g homogenate fraction.	Octoxynol	100-112	phenylalanine hydroxylase	Homo sapiens	0-25
2888478-3	1987	These results are in accord with shared mechanisms of oxygen activation by TH and the more commonly studied tetrahydropterin-dependent enzyme phenylalanine hydroxylase (PAH) and strongly suggest that a peroxytetrahydropterin is the hydroxylating species generated during TH turnover.	Oxygen	54-60	phenylalanine hydroxylase	Homo sapiens	142-167
2888478-3	1987	These results are in accord with shared mechanisms of oxygen activation by TH and the more commonly studied tetrahydropterin-dependent enzyme phenylalanine hydroxylase (PAH) and strongly suggest that a peroxytetrahydropterin is the hydroxylating species generated during TH turnover.	Oxygen	54-60	phenylalanine hydroxylase	Homo sapiens	169-172
2888478-3	1987	These results are in accord with shared mechanisms of oxygen activation by TH and the more commonly studied tetrahydropterin-dependent enzyme phenylalanine hydroxylase (PAH) and strongly suggest that a peroxytetrahydropterin is the hydroxylating species generated during TH turnover.	tetrahydropterin	108-124	phenylalanine hydroxylase	Homo sapiens	142-167
2888478-3	1987	These results are in accord with shared mechanisms of oxygen activation by TH and the more commonly studied tetrahydropterin-dependent enzyme phenylalanine hydroxylase (PAH) and strongly suggest that a peroxytetrahydropterin is the hydroxylating species generated during TH turnover.	tetrahydropterin	108-124	phenylalanine hydroxylase	Homo sapiens	169-172
2888478-3	1987	These results are in accord with shared mechanisms of oxygen activation by TH and the more commonly studied tetrahydropterin-dependent enzyme phenylalanine hydroxylase (PAH) and strongly suggest that a peroxytetrahydropterin is the hydroxylating species generated during TH turnover.	peroxytetrahydropterin	202-224	phenylalanine hydroxylase	Homo sapiens	142-167
2888478-3	1987	These results are in accord with shared mechanisms of oxygen activation by TH and the more commonly studied tetrahydropterin-dependent enzyme phenylalanine hydroxylase (PAH) and strongly suggest that a peroxytetrahydropterin is the hydroxylating species generated during TH turnover.	peroxytetrahydropterin	202-224	phenylalanine hydroxylase	Homo sapiens	169-172
2888478-4	1987	In addition, TH can also utilize H2O2 as a cofactor for substrate hydroxylation, a result not previously established for PAH.	Hydrogen Peroxide	33-37	phenylalanine hydroxylase	Homo sapiens	121-124
3768311-0	1986	Pyrimidodiazepine, a ring-strained cofactor for phenylalanine hydroxylase.	pyrimidodiazepine	0-17	phenylalanine hydroxylase	Homo sapiens	48-73
3546287-2	1987	Transformed bacteria express phenylalanine hydroxylase immunoreactive protein and pterin-dependent conversion of phenylalanine to tyrosine.	Tyrosine	130-138	phenylalanine hydroxylase	Homo sapiens	29-54
3546287-4	1987	The optimal reaction conditions, kinetic constants, and sensitivity to inhibition by aromatic amino acids are the same for recombinant phenylalanine hydroxylase and native phenylalanine hydroxylase.	Amino Acids, Aromatic	85-105	phenylalanine hydroxylase	Homo sapiens	135-160
3546287-4	1987	The optimal reaction conditions, kinetic constants, and sensitivity to inhibition by aromatic amino acids are the same for recombinant phenylalanine hydroxylase and native phenylalanine hydroxylase.	Amino Acids, Aromatic	85-105	phenylalanine hydroxylase	Homo sapiens	172-197
2949745-2	1987	We investigated the effect of p-chlorophenylalanine on production of human phenylalanine hydroxylase in human hepatoma cells and cells transformed with the recombinant human phenylalanine hydroxylase gene.	Fenclonine	30-51	phenylalanine hydroxylase	Homo sapiens	75-100
3026504-1	1987	Lineshape simulations are presented for the multiple, overlapping X-band electron paramagnetic resonance (EPR) spectra in two non-heme, high-spin iron proteins: phenylalanine hydroxylase (PAH) and diferric transferrin.	Heme	130-134	phenylalanine hydroxylase	Homo sapiens	188-191
3026504-1	1987	Lineshape simulations are presented for the multiple, overlapping X-band electron paramagnetic resonance (EPR) spectra in two non-heme, high-spin iron proteins: phenylalanine hydroxylase (PAH) and diferric transferrin.	Iron	146-150	phenylalanine hydroxylase	Homo sapiens	161-186
3026504-1	1987	Lineshape simulations are presented for the multiple, overlapping X-band electron paramagnetic resonance (EPR) spectra in two non-heme, high-spin iron proteins: phenylalanine hydroxylase (PAH) and diferric transferrin.	Iron	146-150	phenylalanine hydroxylase	Homo sapiens	188-191
3026504-4	1987	In both PAH and transferrin, at least one of the iron sites is characterized by the ratio of zero-field splitting parameters, E/D, near 1/3 and a broad, asymmetric lineshape.	Iron	49-53	phenylalanine hydroxylase	Homo sapiens	8-11
3026504-9	1987	When applied to spectra of PAH in the resting state, the E/D-distribution approach accounts for the intensity of one of the two major species of iron.	Iron	145-149	phenylalanine hydroxylase	Homo sapiens	27-30
3326734-1	1987	The phenylalanine-hydroxylating system consists of 3 essential components, phenylalanine hydroxylase (PAH), dihydropteridine reductase (DHPR) and the coenzyme, tetrahydrobiopterin (BH4).	Phenylalanine	4-17	phenylalanine hydroxylase	Homo sapiens	75-100
3326734-1	1987	The phenylalanine-hydroxylating system consists of 3 essential components, phenylalanine hydroxylase (PAH), dihydropteridine reductase (DHPR) and the coenzyme, tetrahydrobiopterin (BH4).	Phenylalanine	4-17	phenylalanine hydroxylase	Homo sapiens	102-105
3326734-1	1987	The phenylalanine-hydroxylating system consists of 3 essential components, phenylalanine hydroxylase (PAH), dihydropteridine reductase (DHPR) and the coenzyme, tetrahydrobiopterin (BH4).	sapropterin	181-184	phenylalanine hydroxylase	Homo sapiens	102-105
2884570-7	1987	Direct hybridization analysis of the point mutation using a specific oligonucleotide probe demonstrated that this mutation is also in linkage disequilibrium with RFLP haplotype 2 alleles that make up about 20% of mutant PAH genes.	Oligonucleotides	69-84	phenylalanine hydroxylase	Homo sapiens	220-223
3297709-8	1987	It is concluded that "peripheral" tetrahydrobiopterin deficiency is caused by a partial PTS deficiency with sufficient activity to cover the tetrahydrobiopterin requirement of tyrosine 3-hydroxylase and trytophan 5-hydroxylase in brain but not enough for phenylalanine 4-hydroxylase in liver.	sapropterin	34-53	phenylalanine hydroxylase	Homo sapiens	255-282
3768311-10	1986	Although phenylalanine hydroxylase utilizes 6-Me-PDH4 (Km = 0.15 mM), the maximum velocity of tyrosine production is 20 times slower than that with 6-Me-PH4, indicating that a ring opening reaction is not a rate-limiting step in the hydroxylase pathway.	6-me-pdh4	44-53	phenylalanine hydroxylase	Homo sapiens	9-34
3772017-3	1986	The method has been used to determine the stoichiometry of iron for nanomole quantities of heme-iron proteins, iron-sulfur proteins, complex iron-sulfur proteins, as well as in phenylalanine hydroxylase, an enzyme with iron in an undetermined coordination.	Iron	59-63	phenylalanine hydroxylase	Homo sapiens	177-202
3749064-0	1986	Metabolic activation pathways of cyclopenta-fused PAH and their relationship to genetic and carcinogenic activity.	cyclopenta	33-43	phenylalanine hydroxylase	Homo sapiens	50-53
3751555-7	1986	It seems likely that those of our patients who markedly increased their phenylalanine tolerance during childhood had a regulatory mutation of the phenylalanine hydroxylase system.	Phenylalanine	72-85	phenylalanine hydroxylase	Homo sapiens	146-171
3800881-0	1986	The polyamine-dependent modulation of phenylalanine hydroxylase phosphorylation state and enzymic activity in isolated liver cells.	Polyamines	4-13	phenylalanine hydroxylase	Homo sapiens	38-63
3800881-1	1986	The role of polyamines in the control of phenylalanine hydroxylase phosphorylation state and enzymic activity was investigated.	Polyamines	12-22	phenylalanine hydroxylase	Homo sapiens	41-66
3008810-1	1986	Human phenylalanine hydroxylase is a liver-specific enzyme that catalyzes the conversion of phenylalanine to tyrosine.	Tyrosine	109-117	phenylalanine hydroxylase	Homo sapiens	6-31
3019383-1	1986	Iron can be bound to phenylalanine hydroxylase (PAH) in two environments.	Iron	0-4	phenylalanine hydroxylase	Homo sapiens	21-46
3019383-1	1986	Iron can be bound to phenylalanine hydroxylase (PAH) in two environments.	Iron	0-4	phenylalanine hydroxylase	Homo sapiens	48-51
3019383-2	1986	The assignment of the electron paramagnetic resonance spectrum of PAH to two, overlapping high-spin ferric signals is confirmed by computer simulation.	Ferric enterobactin ion	100-106	phenylalanine hydroxylase	Homo sapiens	66-69
3019383-5	1986	Oxygen consumption during PAH reduction by tetrahydropterin in the absence of phenylalanine but not in its presence explains the different reduction stoichiometries (tetrahydropterin:enzyme) that have been observed.	Oxygen	0-6	phenylalanine hydroxylase	Homo sapiens	26-29
3019383-5	1986	Oxygen consumption during PAH reduction by tetrahydropterin in the absence of phenylalanine but not in its presence explains the different reduction stoichiometries (tetrahydropterin:enzyme) that have been observed.	tetrahydropterin	43-59	phenylalanine hydroxylase	Homo sapiens	26-29
3019383-5	1986	Oxygen consumption during PAH reduction by tetrahydropterin in the absence of phenylalanine but not in its presence explains the different reduction stoichiometries (tetrahydropterin:enzyme) that have been observed.	Phenylalanine	78-91	phenylalanine hydroxylase	Homo sapiens	26-29
2427069-5	1986	PH5, PH10, PH12 and PH6 recognise sites on phenylalanine hydroxylase affected by lysolecithin activation.	Lysophosphatidylcholines	81-93	phenylalanine hydroxylase	Homo sapiens	43-68
3814104-1	1986	Phenylalanine hydroxylase activity, determined by fluorimetric procedure in human kidney (cortex) of 17 patients, who had a kidney operation, was on the average 4.7 nkat tyr/g protein (25 degrees C), which is 28% in comparison to the enzyme activity in human liver.	Tyrosine	170-173	phenylalanine hydroxylase	Homo sapiens	0-25
2872999-1	1986	Phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH) are consecutive enzymes in the metabolic pathway leading to the production of catecholamine neurotransmitters.	Catecholamines	140-153	phenylalanine hydroxylase	Homo sapiens	0-25
2872999-1	1986	Phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH) are consecutive enzymes in the metabolic pathway leading to the production of catecholamine neurotransmitters.	Catecholamines	140-153	phenylalanine hydroxylase	Homo sapiens	27-30
3862128-5	1985	The PAH map position on chromosome 12 was further localized by in situ hybridization of 125I-labeled human PAH cDNA to chromosomes prepared from a human lymphoblastoid cell line.	Iodine-125	88-92	phenylalanine hydroxylase	Homo sapiens	4-7
4084494-0	1985	Mechanism of "uncoupled" tetrahydropterin oxidation by phenylalanine hydroxylase.	tetrahydropterin	23-41	phenylalanine hydroxylase	Homo sapiens	55-80
4084494-1	1985	Phenylalanine hydroxylase can catalyze the oxidation of its tetrahydropterin cofactor without concomitant substrate hydroxylation.	tetrahydropterin	60-76	phenylalanine hydroxylase	Homo sapiens	0-25
4084494-8	1985	A mechanism is proposed for the uncoupled oxidation of tetrahydropterins by phenylalanine hydroxylase, and the significance of these findings is discussed.	tetrahydropterin	55-72	phenylalanine hydroxylase	Homo sapiens	76-101
3862128-5	1985	The PAH map position on chromosome 12 was further localized by in situ hybridization of 125I-labeled human PAH cDNA to chromosomes prepared from a human lymphoblastoid cell line.	Iodine-125	88-92	phenylalanine hydroxylase	Homo sapiens	107-110
4049788-1	1985	Activated and nonactivated forms of phenylalanine hydroxylase varied in the activity within the first minutes of the reaction initiated by means of a synthetic coenzyme 6,7-dimethyl-5,6,7,8-tetrahydropteridine.	6,7-dimethyl-5,6,7,8-tetrahydropteridine	169-209	phenylalanine hydroxylase	Homo sapiens	36-61
4049788-5	1985	Activation of phenylalanine hydroxylase altered the enzyme affinity to hydroxyapatite.	Durapatite	71-85	phenylalanine hydroxylase	Homo sapiens	14-39
3888282-6	1985	Dyspropterin could also serve as a cofactor in phenylalanine hydroxylase (EC 1.14.16.1) system.	dyspropterin	0-12	phenylalanine hydroxylase	Homo sapiens	47-72
6679751-2	1983	Phenylalanine hydroxylase from fresh human liver was purified to homogeneity with a 60% yield by a three steps procedure involving hydrophobic chromatography on Phenyl-Sepharose, ion exchange chromatography on DEAE-Cellulose and High Performance gel permeation chromatography.	phenyl-sepharose	161-177	phenylalanine hydroxylase	Homo sapiens	0-25
4041562-0	1985	Effect of glucagon on hepatic phenylalanine hydroxylase in vivo.	Glucagon	10-18	phenylalanine hydroxylase	Homo sapiens	30-55
4041562-3	1985	In addition, the stimulation of the tetrahydrobiopterin-dependent phenylalanine hydroxylase activity in livers of animals fed on a high-protein diet has been correlated with an elevated phosphate content.	sapropterin	36-55	phenylalanine hydroxylase	Homo sapiens	66-91
4041562-3	1985	In addition, the stimulation of the tetrahydrobiopterin-dependent phenylalanine hydroxylase activity in livers of animals fed on a high-protein diet has been correlated with an elevated phosphate content.	Phosphates	186-195	phenylalanine hydroxylase	Homo sapiens	66-91
3994703-0	1985	Effects of phenylalanine on phenylalanine hydroxylase separation and stability.	Phenylalanine	11-24	phenylalanine hydroxylase	Homo sapiens	28-53
2857123-4	1985	6,6,8-Trimethyl-5,6,7,8-tetrahydropterin is a cofactor for phenylalanine hydroxylase (EC 1.14.16.1) with an apparent Km of 0.33 mM, but no cofactor activity could be detected with tyrosine hydroxylase (EC 1.14.16.2).	6,6,8-trimethyl-5,6,7,8-tetrahydropterin	0-40	phenylalanine hydroxylase	Homo sapiens	59-84
2866676-1	1985	The metabolic pathways of pterin de novo synthesis, interconversion and salvage which lead to the tetrahydrobiopterin cofactor of phenylalanine 4-monooxygenase, tyrosine 2-monooxygenase and tryptophan 5-monooxygenase are reviewed and data on the enzymes which catalyze the individual steps are presented.	Pterins	26-32	phenylalanine hydroxylase	Homo sapiens	130-159
2866676-1	1985	The metabolic pathways of pterin de novo synthesis, interconversion and salvage which lead to the tetrahydrobiopterin cofactor of phenylalanine 4-monooxygenase, tyrosine 2-monooxygenase and tryptophan 5-monooxygenase are reviewed and data on the enzymes which catalyze the individual steps are presented.	sapropterin	98-117	phenylalanine hydroxylase	Homo sapiens	130-159
2858216-1	1985	Intravenous loading with 500 ml of 2.7% saline increased the clearance of PAH and inulin and urine sodium excretion in 14 healthy subjects.	Sodium Chloride	40-46	phenylalanine hydroxylase	Homo sapiens	74-77
2858216-4	1985	Intravenous nadolol (0.05 and 0.75 mg/kg) reduced resting PAH and inulin clearances by up to 25%.	Nadolol	12-19	phenylalanine hydroxylase	Homo sapiens	58-61
6530447-4	1984	This methodology is used to study the electrochemistry of q-BH2 formed by oxidation of BH4 and in the hydroxylation of phenylalanine by phenylalanine hydroxylase.	7,8-dihydrobiopterin	58-63	phenylalanine hydroxylase	Homo sapiens	136-161
6530447-4	1984	This methodology is used to study the electrochemistry of q-BH2 formed by oxidation of BH4 and in the hydroxylation of phenylalanine by phenylalanine hydroxylase.	Phenylalanine	119-132	phenylalanine hydroxylase	Homo sapiens	136-161
6509772-4	1984	The results suggest that the low-plasma tyrosine levels observed in patients with chronic renal failure are due, at least in part, to the inhibition of phenylalanine hydroxylase.	Tyrosine	40-48	phenylalanine hydroxylase	Homo sapiens	152-177
6395558-5	1984	By means of an on principle other method by determination of the 125J-hippuran clearance under infusion of PAH the Tm-PAH may be indirectly calculated without investigation of the urine.	125j-hippuran	65-78	phenylalanine hydroxylase	Homo sapiens	107-110
6395558-5	1984	By means of an on principle other method by determination of the 125J-hippuran clearance under infusion of PAH the Tm-PAH may be indirectly calculated without investigation of the urine.	125j-hippuran	65-78	phenylalanine hydroxylase	Homo sapiens	118-121
6518276-2	1984	Analysis of 3H2O production and fluorimetric estimation of tyrosine production has allowed calculation of flux through phenylalanine hydroxylase and homogentisate oxidase.	3h2o	12-16	phenylalanine hydroxylase	Homo sapiens	119-144
6518276-2	1984	Analysis of 3H2O production and fluorimetric estimation of tyrosine production has allowed calculation of flux through phenylalanine hydroxylase and homogentisate oxidase.	Tyrosine	59-67	phenylalanine hydroxylase	Homo sapiens	119-144
6088538-1	1984	Two-dimensional polyacrylamide gel analyses of purified human and monkey liver phenylalanine hydroxylase reveal that the enzyme consists of two different apparent molecular weight forms of polypeptide, designated H (Mr = 50,000) and L (Mr = 49,000), each containing three isoelectric forms.	polyacrylamide	16-30	phenylalanine hydroxylase	Homo sapiens	79-104
6470001-0	1984	The effect of ligands of phenylalanine 4-monooxygenase on the cAMP-dependent phosphorylation of the enzyme.	Cyclic AMP	62-66	phenylalanine hydroxylase	Homo sapiens	25-54
6470001-1	1984	The rate of phosphorylation of phenylalanine 4-monooxygenase by the cAMP-dependent protein kinase was found to be under substrate-directed regulation.	Cyclic AMP	68-72	phenylalanine hydroxylase	Homo sapiens	31-60
6487579-2	1984	Incubation of native phenylalanine hydroxylase with phenylalanine or lysophosphatidylcholine results in an increase in the fluorescence emission of the enzyme at 360 nm, which closely parallels the increase in tetrahydrobiopterin-dependent activity observed under these conditions.	Lysophosphatidylcholines	69-92	phenylalanine hydroxylase	Homo sapiens	21-46
6487579-2	1984	Incubation of native phenylalanine hydroxylase with phenylalanine or lysophosphatidylcholine results in an increase in the fluorescence emission of the enzyme at 360 nm, which closely parallels the increase in tetrahydrobiopterin-dependent activity observed under these conditions.	sapropterin	210-229	phenylalanine hydroxylase	Homo sapiens	21-46
6487579-9	1984	These results suggest that activation of phenylalanine hydroxylase results in a conformation change and the exposure of buried tryptophan(s) and possibly a cysteine residue.	Tryptophan	127-137	phenylalanine hydroxylase	Homo sapiens	41-66
6487579-9	1984	These results suggest that activation of phenylalanine hydroxylase results in a conformation change and the exposure of buried tryptophan(s) and possibly a cysteine residue.	Cysteine	156-164	phenylalanine hydroxylase	Homo sapiens	41-66
6495818-0	1984	Studies on the possible mechanism of inactivation of phenylalanine hydroxylase by destructive oxygen species.	Oxygen	94-100	phenylalanine hydroxylase	Homo sapiens	53-78
6495818-1	1984	The enzymic hydroxylation of phenylalanine by phenylalanine hydroxylase (E.C.	Phenylalanine	29-42	phenylalanine hydroxylase	Homo sapiens	46-71
6495818-6	1984	These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H2O2 and the tetrahydropterin cofactor.	Phenylalanine	47-60	phenylalanine hydroxylase	Homo sapiens	213-238
6495818-6	1984	These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H2O2 and the tetrahydropterin cofactor.	Hydrogen Peroxide	93-110	phenylalanine hydroxylase	Homo sapiens	213-238
6495818-6	1984	These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H2O2 and the tetrahydropterin cofactor.	Oxygen	161-167	phenylalanine hydroxylase	Homo sapiens	213-238
6495818-6	1984	These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H2O2 and the tetrahydropterin cofactor.	Hydrogen Peroxide	258-262	phenylalanine hydroxylase	Homo sapiens	213-238
6495818-6	1984	These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H2O2 and the tetrahydropterin cofactor.	tetrahydropterin	271-287	phenylalanine hydroxylase	Homo sapiens	213-238
6721866-3	1984	Glucagon increased flux through phenylalanine hydroxylase; a half-maximal response was obtained at 0.7 nM.	Glucagon	0-8	phenylalanine hydroxylase	Homo sapiens	32-57
3930837-1	1985	The hepatic phenylalanine hydroxylating system consists of three essential components, phenylalanine hydroxylase, dihydropteridine reductase and the non-protein coenzyme, tetrahydrobiopterin.	Phenylalanine	12-25	phenylalanine hydroxylase	Homo sapiens	87-112
6489353-0	1984	Some aspects of the phosphorylation of phenylalanine 4-monooxygenase by a calcium-dependent and calmodulin-dependent protein kinase.	Calcium	74-81	phenylalanine hydroxylase	Homo sapiens	39-68
6489353-1	1984	A calmodulin-dependent protein kinase purified from liver catalyzed the incorporation of up to 0.7 mol of phosphate per mol subunit of phenylalanine 4-monooxygenase.	Phosphates	106-115	phenylalanine hydroxylase	Homo sapiens	135-164
6489353-4	1984	Phenylalanine 4-monooxygenase was also a substrate for the cGMP-dependent protein kinase, but in this system phenylalanine stimulated the rate of phosphorylation to a similar extent as that observed in the reaction catalyzed by cAMP-dependent protein kinase.	Phenylalanine	109-122	phenylalanine hydroxylase	Homo sapiens	0-29
6489353-4	1984	Phenylalanine 4-monooxygenase was also a substrate for the cGMP-dependent protein kinase, but in this system phenylalanine stimulated the rate of phosphorylation to a similar extent as that observed in the reaction catalyzed by cAMP-dependent protein kinase.	Cyclic AMP	228-232	phenylalanine hydroxylase	Homo sapiens	0-29
6547271-1	1984	Classical phenylketonuria (PKU) is a typical example of inborn errors in metabolism and is characterized by a complete lack of the hepatic enzyme phenylalanine hydroxylase, which normally converts phenylalanine to tyrosine.	Tyrosine	214-222	phenylalanine hydroxylase	Homo sapiens	146-171
6324864-0	1984	Reductive activation of phenylalanine hydroxylase and its effect on the redox state of the non-heme iron.	Heme	95-99	phenylalanine hydroxylase	Homo sapiens	24-49
6324864-0	1984	Reductive activation of phenylalanine hydroxylase and its effect on the redox state of the non-heme iron.	Iron	100-104	phenylalanine hydroxylase	Homo sapiens	24-49
6324864-1	1984	Phenylalanine hydroxylase undergoes an obligatory prereduction step in order to become catalytically active as shown by stopped-flow kinetics and by measuring tyrosine formation at limiting 6-methyltetrahydropterin levels.	Tyrosine	159-167	phenylalanine hydroxylase	Homo sapiens	0-25
6324864-1	1984	Phenylalanine hydroxylase undergoes an obligatory prereduction step in order to become catalytically active as shown by stopped-flow kinetics and by measuring tyrosine formation at limiting 6-methyltetrahydropterin levels.	6-methyltetrahydropterin	190-214	phenylalanine hydroxylase	Homo sapiens	0-25
6324864-7	1984	Dithionite can substitute for 6-methyltetrahydropterin in an anaerobic prereduction step, generating a catalytically active phenylalanine hydroxylase containing Fe2+ that functions aerobically to produce tyrosine from added 6-methyltetrahydropterin in a 1/1 stoichiometry.	Dithionite	0-10	phenylalanine hydroxylase	Homo sapiens	124-149
6324864-7	1984	Dithionite can substitute for 6-methyltetrahydropterin in an anaerobic prereduction step, generating a catalytically active phenylalanine hydroxylase containing Fe2+ that functions aerobically to produce tyrosine from added 6-methyltetrahydropterin in a 1/1 stoichiometry.	6-methyltetrahydropterin	30-54	phenylalanine hydroxylase	Homo sapiens	124-149
6324864-7	1984	Dithionite can substitute for 6-methyltetrahydropterin in an anaerobic prereduction step, generating a catalytically active phenylalanine hydroxylase containing Fe2+ that functions aerobically to produce tyrosine from added 6-methyltetrahydropterin in a 1/1 stoichiometry.	ammonium ferrous sulfate	161-165	phenylalanine hydroxylase	Homo sapiens	124-149
6324864-7	1984	Dithionite can substitute for 6-methyltetrahydropterin in an anaerobic prereduction step, generating a catalytically active phenylalanine hydroxylase containing Fe2+ that functions aerobically to produce tyrosine from added 6-methyltetrahydropterin in a 1/1 stoichiometry.	Tyrosine	204-212	phenylalanine hydroxylase	Homo sapiens	124-149
6324864-7	1984	Dithionite can substitute for 6-methyltetrahydropterin in an anaerobic prereduction step, generating a catalytically active phenylalanine hydroxylase containing Fe2+ that functions aerobically to produce tyrosine from added 6-methyltetrahydropterin in a 1/1 stoichiometry.	6-methyltetrahydropterin	224-248	phenylalanine hydroxylase	Homo sapiens	124-149
6698976-1	1984	The effects of substrate and cofactors on the phosphorylation of hepatic phenylalanine hydroxylase by cAMP-dependent protein kinase and on dephosphorylation by phosphoprotein phosphatase have been examined.	Cyclic AMP	102-106	phenylalanine hydroxylase	Homo sapiens	73-98
6698976-7	1984	Both phenylalanine and (6R)-tetrahydrobiopterin inhibit to a small extent the dephosphorylation of phosphorylated phenylalanine hydroxylase catalyzed by phosphoprotein phosphatase.	Phenylalanine	5-18	phenylalanine hydroxylase	Homo sapiens	114-139
6698976-7	1984	Both phenylalanine and (6R)-tetrahydrobiopterin inhibit to a small extent the dephosphorylation of phosphorylated phenylalanine hydroxylase catalyzed by phosphoprotein phosphatase.	sapropterin	23-47	phenylalanine hydroxylase	Homo sapiens	114-139
6679751-2	1983	Phenylalanine hydroxylase from fresh human liver was purified to homogeneity with a 60% yield by a three steps procedure involving hydrophobic chromatography on Phenyl-Sepharose, ion exchange chromatography on DEAE-Cellulose and High Performance gel permeation chromatography.	DEAE-Cellulose	210-224	phenylalanine hydroxylase	Homo sapiens	0-25
6679751-6	1983	Moreover, the purified human liver phenylalanine hydroxylase was found to be devoid of protein-bound phosphate and no phosphate could be incorporated from [32P]-ATP in the presence of cyclic-AMP - dependent protein kinase.	Phosphates	101-110	phenylalanine hydroxylase	Homo sapiens	35-60
20487919-1	1983	The activities of three pterin-requiring monooxygenases, phenylalanine hydroxylase, tyrosine hydroxylase and tryptophan hydroxylase, are regulated by the level of the pterin cofactor, (6R)- l -erythro- tetrahydrobiopterin , which is synthesized from guanosine triphosphate (GTP).	Pterins	24-30	phenylalanine hydroxylase	Homo sapiens	57-82
6844469-6	1983	Half of the patients showed some reduction in inulin and PAH clearance, which was greatest in those patients who had been taking lithium for over 10 years.	Lithium	129-136	phenylalanine hydroxylase	Homo sapiens	57-60
20487919-1	1983	The activities of three pterin-requiring monooxygenases, phenylalanine hydroxylase, tyrosine hydroxylase and tryptophan hydroxylase, are regulated by the level of the pterin cofactor, (6R)- l -erythro- tetrahydrobiopterin , which is synthesized from guanosine triphosphate (GTP).	Guanosine Triphosphate	274-277	phenylalanine hydroxylase	Homo sapiens	57-82
6337829-6	1983	So far the studies carried out among the Finnish working population exposed to PAH compounds reveal an association between the lung cancer risk and exposure to PAHs.	Polycyclic Aromatic Hydrocarbons	160-164	phenylalanine hydroxylase	Homo sapiens	79-82
20487919-1	1983	The activities of three pterin-requiring monooxygenases, phenylalanine hydroxylase, tyrosine hydroxylase and tryptophan hydroxylase, are regulated by the level of the pterin cofactor, (6R)- l -erythro- tetrahydrobiopterin , which is synthesized from guanosine triphosphate (GTP).	(6r)- l	184-191	phenylalanine hydroxylase	Homo sapiens	57-82
20487919-1	1983	The activities of three pterin-requiring monooxygenases, phenylalanine hydroxylase, tyrosine hydroxylase and tryptophan hydroxylase, are regulated by the level of the pterin cofactor, (6R)- l -erythro- tetrahydrobiopterin , which is synthesized from guanosine triphosphate (GTP).	erythro- tetrahydrobiopterin	193-221	phenylalanine hydroxylase	Homo sapiens	57-82
20487919-1	1983	The activities of three pterin-requiring monooxygenases, phenylalanine hydroxylase, tyrosine hydroxylase and tryptophan hydroxylase, are regulated by the level of the pterin cofactor, (6R)- l -erythro- tetrahydrobiopterin , which is synthesized from guanosine triphosphate (GTP).	Guanosine Triphosphate	250-272	phenylalanine hydroxylase	Homo sapiens	57-82
7132735-15	1982	This supports the existence of some type of substance activation of the enzyme as reflected in the previously reported exponential relationship between phenylalanine concentration and phenylalanine hydroxylase activity in vitro.	Phenylalanine	152-165	phenylalanine hydroxylase	Homo sapiens	184-209
7132735-16	1982	The use of continuous simultaneous infusions of tracer amounts of stable isotope-labeled phenylalanine and tyrosine provides a direct means for studying physiological regulation of phenylalanine hydroxylase activity in vivo.	Phenylalanine	89-102	phenylalanine hydroxylase	Homo sapiens	181-206
7132735-16	1982	The use of continuous simultaneous infusions of tracer amounts of stable isotope-labeled phenylalanine and tyrosine provides a direct means for studying physiological regulation of phenylalanine hydroxylase activity in vivo.	Tyrosine	107-115	phenylalanine hydroxylase	Homo sapiens	181-206
7101818-1	1982	Activity of phenylalanine hydroxylase from human leukocytes was shown to depend on concentration of phenylalanine and pteridine cofactor; optimal concentrations of the substances were estimated.	Pteridines	118-127	phenylalanine hydroxylase	Homo sapiens	12-37
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	sapropterin	305-324	phenylalanine hydroxylase	Homo sapiens	61-64
6282659-4	1982	PAH also requires 1.0 iron per 50,000-dalton subunit for maximal activity.	Iron	22-26	phenylalanine hydroxylase	Homo sapiens	0-3
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	Oxygen	12-18	phenylalanine hydroxylase	Homo sapiens	34-59
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	Oxygen	12-18	phenylalanine hydroxylase	Homo sapiens	61-64
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	Phenylalanine	34-47	phenylalanine hydroxylase	Homo sapiens	61-64
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	Tyrosine	105-113	phenylalanine hydroxylase	Homo sapiens	34-59
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	Tyrosine	105-113	phenylalanine hydroxylase	Homo sapiens	61-64
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	tetrahydropterin	172-188	phenylalanine hydroxylase	Homo sapiens	34-59
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	tetrahydropterin	172-188	phenylalanine hydroxylase	Homo sapiens	61-64
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	6-methyltetrahydropterin	276-300	phenylalanine hydroxylase	Homo sapiens	34-59
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	6-methyltetrahydropterin	276-300	phenylalanine hydroxylase	Homo sapiens	61-64
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	sapropterin	305-324	phenylalanine hydroxylase	Homo sapiens	34-59
7096201-0	1982	Inhibition of phenylalanine hydroxylase, a pterin-requiring monooxygenase, by oudenone and its derivatives.	oudenone	78-86	phenylalanine hydroxylase	Homo sapiens	14-39
7096201-1	1982	Phenylalanine hydroxylase was shown to be inhibited by oudenone and its derivatives in vitro.	oudenone	55-63	phenylalanine hydroxylase	Homo sapiens	0-25
7096201-2	1982	At a concentration of 2.3 x 10(-3) M, oudenone inhibited phenylalanine hydroxylase by 50%, and some of the oudenone derivatives showed more potent inhibition.	oudenone	38-46	phenylalanine hydroxylase	Homo sapiens	57-82
7096201-7	1982	It inhibited phenylalanine hydroxylase by 50% at a concentration of 1.8 x 10(-5) M. This inhibition was a mixed type with either a tetrahydropterin cofactor, DMPH4, or with the substrate phenylalanine, which was different from the inhibition by oudenone.	tetrahydropterin	131-147	phenylalanine hydroxylase	Homo sapiens	13-38
7096201-7	1982	It inhibited phenylalanine hydroxylase by 50% at a concentration of 1.8 x 10(-5) M. This inhibition was a mixed type with either a tetrahydropterin cofactor, DMPH4, or with the substrate phenylalanine, which was different from the inhibition by oudenone.	2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine	158-163	phenylalanine hydroxylase	Homo sapiens	13-38
7096201-7	1982	It inhibited phenylalanine hydroxylase by 50% at a concentration of 1.8 x 10(-5) M. This inhibition was a mixed type with either a tetrahydropterin cofactor, DMPH4, or with the substrate phenylalanine, which was different from the inhibition by oudenone.	oudenone	245-253	phenylalanine hydroxylase	Homo sapiens	13-38
6820408-0	1982	The use of deuterated phenylalanine for the in vivo assay of phenylalanine hydroxylase activity in children.	deuterated phenylalanine	11-35	phenylalanine hydroxylase	Homo sapiens	61-86
7054185-2	1982	Phenylalanine hydroxylase requires 1.0 mol of iron/Mr = 50,000 subunit for maximal activity.	Iron	46-50	phenylalanine hydroxylase	Homo sapiens	0-25
7054185-5	1982	A comparison of the native and reconstituted phenylalanine hydroxylase shows the latter behaves identically upon affinity and Chelex column chromatography as well as precipitation with ammonium sulfate supporting its close similarity to the native enzyme.	Ammonium Sulfate	185-201	phenylalanine hydroxylase	Homo sapiens	45-70
7104147-3	1982	2 The long-term administration of pindolol (5--20 mg/day) to hypertensive patients with normal renal function was not associated with changes in renal function but in patients with a decreased renal function, pindolol caused an increase in PAH clearance but no change in inulin clearance.	Pindolol	34-42	phenylalanine hydroxylase	Homo sapiens	240-243
7104147-3	1982	2 The long-term administration of pindolol (5--20 mg/day) to hypertensive patients with normal renal function was not associated with changes in renal function but in patients with a decreased renal function, pindolol caused an increase in PAH clearance but no change in inulin clearance.	Pindolol	209-217	phenylalanine hydroxylase	Homo sapiens	240-243
7317357-1	1981	The oxidation of 6-methyltetrahydropterin and tetrahydrobiopterin coupled to the formation of tyrosine by phenylalanine hydroxylase generates a precursor species to the quinonoid product that is tentatively identified as a 4a-hydroxy adduct based on its spectral similarity to the 4a-hydroxy-6-methyl-5-deazatetrahydropterin.	6-methyltetrahydropterin	17-41	phenylalanine hydroxylase	Homo sapiens	106-131
7317357-1	1981	The oxidation of 6-methyltetrahydropterin and tetrahydrobiopterin coupled to the formation of tyrosine by phenylalanine hydroxylase generates a precursor species to the quinonoid product that is tentatively identified as a 4a-hydroxy adduct based on its spectral similarity to the 4a-hydroxy-6-methyl-5-deazatetrahydropterin.	sapropterin	46-65	phenylalanine hydroxylase	Homo sapiens	106-131
7317357-1	1981	The oxidation of 6-methyltetrahydropterin and tetrahydrobiopterin coupled to the formation of tyrosine by phenylalanine hydroxylase generates a precursor species to the quinonoid product that is tentatively identified as a 4a-hydroxy adduct based on its spectral similarity to the 4a-hydroxy-6-methyl-5-deazatetrahydropterin.	Tyrosine	94-102	phenylalanine hydroxylase	Homo sapiens	106-131
7317357-1	1981	The oxidation of 6-methyltetrahydropterin and tetrahydrobiopterin coupled to the formation of tyrosine by phenylalanine hydroxylase generates a precursor species to the quinonoid product that is tentatively identified as a 4a-hydroxy adduct based on its spectral similarity to the 4a-hydroxy-6-methyl-5-deazatetrahydropterin.	quinonoid	169-178	phenylalanine hydroxylase	Homo sapiens	106-131
7317357-1	1981	The oxidation of 6-methyltetrahydropterin and tetrahydrobiopterin coupled to the formation of tyrosine by phenylalanine hydroxylase generates a precursor species to the quinonoid product that is tentatively identified as a 4a-hydroxy adduct based on its spectral similarity to the 4a-hydroxy-6-methyl-5-deazatetrahydropterin.	4a-hydroxy-6-methyl-5-deazatetrahydropterin	281-324	phenylalanine hydroxylase	Homo sapiens	106-131
7435950-0	1980	An assay for picomole levels of tyrosine and related phenols and its application to the measurement of phenylalanine hydroxylase activity.	Tyrosine	32-40	phenylalanine hydroxylase	Homo sapiens	103-128
6803767-5	1981	The binding of PH alpha 1-1 antibody to phenylalanine hydroxylase is dependent on substrate phenylalanine, whereas the binding of the others is not influenced by phenylalanine.	Phenylalanine	92-105	phenylalanine hydroxylase	Homo sapiens	40-65
7435950-0	1980	An assay for picomole levels of tyrosine and related phenols and its application to the measurement of phenylalanine hydroxylase activity.	Phenols	53-60	phenylalanine hydroxylase	Homo sapiens	103-128
7400145-0	1980	Cleavage of the 5-amino substituent of pyrimidine cofactors by phenylalanine hydroxylase.	pyrimidine	39-49	phenylalanine hydroxylase	Homo sapiens	63-88
7394510-1	1980	Two methods for extraction and determination of benzo[a]pyrene and other PAH in liquid and white soft paraffins, widely used for medicinal and cosmetic purposes, are compared.	Paraffin	102-111	phenylalanine hydroxylase	Homo sapiens	73-76
6933904-1	1980	After single administration of potassium dichromate or glycerol, renal PAH excretion was markedly reduced in adult, but not in newborn and infant rats.	Potassium Dichromate	31-51	phenylalanine hydroxylase	Homo sapiens	71-74
6933904-1	1980	After single administration of potassium dichromate or glycerol, renal PAH excretion was markedly reduced in adult, but not in newborn and infant rats.	Glycerol	55-63	phenylalanine hydroxylase	Homo sapiens	71-74
511154-2	1979	Phenylalanine is converted to tyrosine by phenylalanine hydroxylase, which is located mainly in the liver.	Phenylalanine	0-13	phenylalanine hydroxylase	Homo sapiens	42-67
489556-7	1979	Phenylalanine hydroxylase half-life in the H4 cells was investigated under both normal and hydrocortisone-induced growth conditions.	Hydrocortisone	91-105	phenylalanine hydroxylase	Homo sapiens	0-25
489556-9	1979	Although these measured enzyme half-lives were not essentially different, the steady state level of phenylalanine hydroxylase was increased 6.2-fold upon hydrocortisone induction, from 0.076 to 0.47 microgram/10(6) cells.	Hydrocortisone	154-168	phenylalanine hydroxylase	Homo sapiens	100-125
489556-10	1979	The results demonstrated that hydrocortisone induces phenylalanine hydroxylase in the H4 cells by causing an increase in the rate of enzyme synthesis.	Hydrocortisone	30-44	phenylalanine hydroxylase	Homo sapiens	53-78
511154-2	1979	Phenylalanine is converted to tyrosine by phenylalanine hydroxylase, which is located mainly in the liver.	Tyrosine	30-38	phenylalanine hydroxylase	Homo sapiens	42-67
484489-4	1979	The results obtained show that, A benzene extraction time of 250 hours is necessary to obtain complete extraction, but for practical purposes, an extraction time of 150 hours is sufficient to extract more than 95% of the PAH.	Benzene	34-41	phenylalanine hydroxylase	Homo sapiens	221-224
496890-2	1979	Phenylalanine hydroxylase was purified from crude extracts of human livers which show enzyme activity by usine two different methods: (a) affinity chromatography and (b) immunoprecipitation with an antiserum against highly purified monkey liver phenylalanine hydroxylase.	usine	105-110	phenylalanine hydroxylase	Homo sapiens	0-25
221463-0	1979	The activity of 2,4,5-triamino-6-hydroxypyrimidine in the phenylalanine hydroxylase system.	6-hydroxy-2,4,5-triaminopyrimidine	16-50	phenylalanine hydroxylase	Homo sapiens	58-83
221463-2	1979	The phenylalanine-dependent, phenylalanine hydroxylase-catalyzed reaction in the presence of the pyrimidine is largely, but not completely, uncoupled; the ratio of DPNH oxidized to tyrosine formed is about 20 to 1.	pyrimidine	97-107	phenylalanine hydroxylase	Homo sapiens	29-54
221463-2	1979	The phenylalanine-dependent, phenylalanine hydroxylase-catalyzed reaction in the presence of the pyrimidine is largely, but not completely, uncoupled; the ratio of DPNH oxidized to tyrosine formed is about 20 to 1.	NAD	164-168	phenylalanine hydroxylase	Homo sapiens	29-54
221463-2	1979	The phenylalanine-dependent, phenylalanine hydroxylase-catalyzed reaction in the presence of the pyrimidine is largely, but not completely, uncoupled; the ratio of DPNH oxidized to tyrosine formed is about 20 to 1.	Tyrosine	181-189	phenylalanine hydroxylase	Homo sapiens	29-54
221463-3	1979	In addition to the pyrimidine having activity with phenylalanine hydroxylase, a product of the pyrimidine is also a substrate for dihydropteridine reductase.	pyrimidine	19-29	phenylalanine hydroxylase	Homo sapiens	51-76
221463-3	1979	In addition to the pyrimidine having activity with phenylalanine hydroxylase, a product of the pyrimidine is also a substrate for dihydropteridine reductase.	pyrimidine	95-105	phenylalanine hydroxylase	Homo sapiens	51-76
84153-1	1979	A patient with atypical phenylketonuria and normal liver dihydropteridine reductase and phenylalanine-4-hydroxylase activities excreted neopterin but not biopterin or dihydrobiopterin in urine.	Neopterin	136-145	phenylalanine hydroxylase	Homo sapiens	88-115
743318-0	1978	Pyrimidines as cofactors for phenylalanine hydroxylase.	Pyrimidines	0-11	phenylalanine hydroxylase	Homo sapiens	29-54
683251-6	1978	The phenylalanine hydroxylase activity in this child, as determined by an in vivo tritium-release assay, was 2.3 per cent of the normal value.	Tritium	82-89	phenylalanine hydroxylase	Homo sapiens	4-29
221463-2	1979	The phenylalanine-dependent, phenylalanine hydroxylase-catalyzed reaction in the presence of the pyrimidine is largely, but not completely, uncoupled; the ratio of DPNH oxidized to tyrosine formed is about 20 to 1.	Phenylalanine	4-17	phenylalanine hydroxylase	Homo sapiens	29-54
648526-7	1978	Two novel adsorbents, 5-formyl-tetrahydrofolate--AH-Sepharose and 5-methyl-tetrahydrofolate--AH-Sepharose, are described which may be useful not only in the study of phenylalanine hydroxylase but also in the study of folate-metabolizing enzymes.	5-methyl-tetrahydrofolate--ah-sepharose	66-105	phenylalanine hydroxylase	Homo sapiens	166-191
627558-0	1978	Separation and properties of the 6-diastereoisomers of l-erythro-tetrahydrobiopterin and their reactivities with phenylalanine hydroxylase.	Sapropterin	55-84	phenylalanine hydroxylase	Homo sapiens	113-138
624182-1	1978	Consideration of the flow of phenylalanine within the body shows that classical phenylalanine load tests for assessing phenylalanine hydroxylase activity cannot usefully be replaced by tracer techniques.	Phenylalanine	80-93	phenylalanine hydroxylase	Homo sapiens	119-144
988698-0	1976	[In-vivo studies on the activation possibility of the phenylalanine hydroxylase system in hyperphenylalaninemia through treatment with pterins].	Pterins	135-142	phenylalanine hydroxylase	Homo sapiens	54-79
732825-0	1978	In vivo determination of phenylalanine hydroxylase activity using heptadeutero-phenylalanine and comparison to the in vitro assay values.	heptadeutero-phenylalanine	66-92	phenylalanine hydroxylase	Homo sapiens	25-50
843338-0	1977	The use of dithiothreitol in the assay of phenylalanine hydroxylase.	Dithiothreitol	11-25	phenylalanine hydroxylase	Homo sapiens	42-67
1011298-6	1976	Application of the procedure for 42 consecutive days on the daily diet records of 43 adult carriers of the phenylalanine hydroxylase enzyme formed the data base used to determine if aspartame significantly increased levels of phenylalanine in the blood.	Aspartame	182-191	phenylalanine hydroxylase	Homo sapiens	107-132
145862-0	1977	Entrapment of phenylalanine hydroxylase in a polyacrylamide matrix.	polyacrylamide	45-59	phenylalanine hydroxylase	Homo sapiens	14-39
914934-9	1977	Using this method, an in vivo determination of phenylalanine-4-monooxygenase activity in humans is possible by loading the subjects with deuterated L-phenylalanine-d5 (accepted as substrate by phenylalanine-4-monooxygenase E.C.	L-Phenyl-d5-alanine	148-166	phenylalanine hydroxylase	Homo sapiens	47-76
914934-9	1977	Using this method, an in vivo determination of phenylalanine-4-monooxygenase activity in humans is possible by loading the subjects with deuterated L-phenylalanine-d5 (accepted as substrate by phenylalanine-4-monooxygenase E.C.	L-Phenyl-d5-alanine	148-166	phenylalanine hydroxylase	Homo sapiens	193-222
15461325-3	1977	It is possible that a lack of phenylalanine hydroxylase in the peripheral lymphocytes of PKU patients prevents oxidation of phenylalanine to tyrosine.	Tyrosine	141-149	phenylalanine hydroxylase	Homo sapiens	30-55
835603-1	1977	In vitro concentrative transport to tritiated p-aminohippuric acid (3H-PAH) was evaluated in renal biopsy specimens from human subjects by section freeze-dry autoradiography.	p-Aminohippuric Acid	46-66	phenylalanine hydroxylase	Homo sapiens	71-74
835603-7	1977	The frequency of proximal tubules showing 3H-PAH uptake in the cortex varied directly with the glomerular filtration rate and inversely with the degree of interstitial involvement.	Tritium	42-44	phenylalanine hydroxylase	Homo sapiens	45-48
68906-10	1977	Six unknown PAH were found: cyclopenteno[cd]pyrene (mol wt 226), methylenebenzo[a]pyrene (mol 264), methylenebenzo[e]pyrene (mol wt 264), methylenebenzo[ghi]perylene (mol wt 288), PAH mol wt 300A and PAH mol wt 300B.	cyclopenta(c,d)pyrene	28-50	phenylalanine hydroxylase	Homo sapiens	12-15
68906-10	1977	Six unknown PAH were found: cyclopenteno[cd]pyrene (mol wt 226), methylenebenzo[a]pyrene (mol 264), methylenebenzo[e]pyrene (mol wt 264), methylenebenzo[ghi]perylene (mol wt 288), PAH mol wt 300A and PAH mol wt 300B.	methylenebenzo[ghi]perylene	138-165	phenylalanine hydroxylase	Homo sapiens	12-15
8429-4	1976	Both dihydropteridine reductase and phenylalanine hydroxylase activities were found to be higher in cells adapted to a medium containing L-phenylalanine or L-tyrosine as the sole carbon source than in those grown in L-asparagine.	Phenylalanine	137-152	phenylalanine hydroxylase	Homo sapiens	36-61
8429-4	1976	Both dihydropteridine reductase and phenylalanine hydroxylase activities were found to be higher in cells adapted to a medium containing L-phenylalanine or L-tyrosine as the sole carbon source than in those grown in L-asparagine.	Tyrosine	156-166	phenylalanine hydroxylase	Homo sapiens	36-61
8429-4	1976	Both dihydropteridine reductase and phenylalanine hydroxylase activities were found to be higher in cells adapted to a medium containing L-phenylalanine or L-tyrosine as the sole carbon source than in those grown in L-asparagine.	Carbon	179-185	phenylalanine hydroxylase	Homo sapiens	36-61
8429-4	1976	Both dihydropteridine reductase and phenylalanine hydroxylase activities were found to be higher in cells adapted to a medium containing L-phenylalanine or L-tyrosine as the sole carbon source than in those grown in L-asparagine.	Asparagine	216-228	phenylalanine hydroxylase	Homo sapiens	36-61
8429-5	1976	The substrate of the reductase is quinonoid dihydropteridine, and the product is tentatively identified as a tetrahydropteridine through its ability to serve as a cofactor for phenylalanine hydroxylase.	quinonoid dihydropteridine	34-60	phenylalanine hydroxylase	Homo sapiens	176-201
8429-5	1976	The substrate of the reductase is quinonoid dihydropteridine, and the product is tentatively identified as a tetrahydropteridine through its ability to serve as a cofactor for phenylalanine hydroxylase.	5,6,7,8-tetrahydropteridine	109-128	phenylalanine hydroxylase	Homo sapiens	176-201
177008-0	1976	Hydrocortisone induction of phenylalanine hydroxylase isozymes in cultured hepatoma cells.	Hydrocortisone	0-14	phenylalanine hydroxylase	Homo sapiens	28-53
3704-0	1975	Inhibition of phenylalanine hydroxylase activity by alpha-methyl tyrosine, a potent inhibitor of tyrosine hydroxylase.	alpha-Methyltyrosine	52-73	phenylalanine hydroxylase	Homo sapiens	14-39
136660-0	1976	What is the mechanism of the irreversible inhibition of phenylalanine hydroxylase by p-chlorophenylalanine?	Fenclonine	85-106	phenylalanine hydroxylase	Homo sapiens	56-81
1196708-1	1975	The phenylalanine hydroxylase assay was modified by using biopterin, lysolecithin, and dithioerythritol.	Dithioerythritol	87-103	phenylalanine hydroxylase	Homo sapiens	4-29
1196708-1	1975	The phenylalanine hydroxylase assay was modified by using biopterin, lysolecithin, and dithioerythritol.	Biopterin	58-67	phenylalanine hydroxylase	Homo sapiens	4-29
1196708-1	1975	The phenylalanine hydroxylase assay was modified by using biopterin, lysolecithin, and dithioerythritol.	Lysophosphatidylcholines	69-81	phenylalanine hydroxylase	Homo sapiens	4-29
172500-7	1975	Three lines of evidence suggest that serum contains a nonsteroidal phenylalanine hydroxylase stimulatory components(s): (a) glucocorticoid antagonists inhibit less than one-half of the biological activity of serum; (b) exhaustive extraction of endogenous serum glucocorticoids with charcoal reduces the activity of serum to about one-half of control values; and (c) the stimulatory effects of charcoal reduces the values; and (c) the stimulatory effects of charcoal-extracted serum and hydrocortisone are additive.	Charcoal	282-290	phenylalanine hydroxylase	Homo sapiens	67-92
172500-7	1975	Three lines of evidence suggest that serum contains a nonsteroidal phenylalanine hydroxylase stimulatory components(s): (a) glucocorticoid antagonists inhibit less than one-half of the biological activity of serum; (b) exhaustive extraction of endogenous serum glucocorticoids with charcoal reduces the activity of serum to about one-half of control values; and (c) the stimulatory effects of charcoal reduces the values; and (c) the stimulatory effects of charcoal-extracted serum and hydrocortisone are additive.	Charcoal	393-401	phenylalanine hydroxylase	Homo sapiens	67-92
172500-7	1975	Three lines of evidence suggest that serum contains a nonsteroidal phenylalanine hydroxylase stimulatory components(s): (a) glucocorticoid antagonists inhibit less than one-half of the biological activity of serum; (b) exhaustive extraction of endogenous serum glucocorticoids with charcoal reduces the activity of serum to about one-half of control values; and (c) the stimulatory effects of charcoal reduces the values; and (c) the stimulatory effects of charcoal-extracted serum and hydrocortisone are additive.	Charcoal	393-401	phenylalanine hydroxylase	Homo sapiens	67-92
172500-7	1975	Three lines of evidence suggest that serum contains a nonsteroidal phenylalanine hydroxylase stimulatory components(s): (a) glucocorticoid antagonists inhibit less than one-half of the biological activity of serum; (b) exhaustive extraction of endogenous serum glucocorticoids with charcoal reduces the activity of serum to about one-half of control values; and (c) the stimulatory effects of charcoal reduces the values; and (c) the stimulatory effects of charcoal-extracted serum and hydrocortisone are additive.	Hydrocortisone	486-500	phenylalanine hydroxylase	Homo sapiens	67-92
1160969-2	1975	In assays of the components of the phenylalanine hydroxylating system (open liver biopsy at 14 months), the activity of phenylalanine hydroxylase was 20 per cent of the average normal adult value.	Phenylalanine	35-48	phenylalanine hydroxylase	Homo sapiens	120-145
1093910-0	1975	A tyrosine-free medium for the selective growth of cells expressing phenylalanine hydroxylase activity.	Tyrosine	2-10	phenylalanine hydroxylase	Homo sapiens	68-93
234440-0	1975	p-Chlorphenylalanine effect on phenylalanine hydroxylase in hepatoma cells in culture.	Fenclonine	0-20	phenylalanine hydroxylase	Homo sapiens	31-56
234440-2	1975	The similarity of the effect of p-chlorophenylalanine on phenylalanine hydroxylase in the hepatoma cells and that reported from studies in vivo indicates that the loss of phenylalanine hydroxylase activity is due to a direct interaction of the amino acid analogue with the liver.	Fenclonine	32-53	phenylalanine hydroxylase	Homo sapiens	57-82
234440-2	1975	The similarity of the effect of p-chlorophenylalanine on phenylalanine hydroxylase in the hepatoma cells and that reported from studies in vivo indicates that the loss of phenylalanine hydroxylase activity is due to a direct interaction of the amino acid analogue with the liver.	Fenclonine	32-53	phenylalanine hydroxylase	Homo sapiens	171-196
234440-7	1975	To measure very low levels of phenylalanine hydroxylase activity, a new procedure, based on isotope dilution, was developed for isolating the tyrosine formed during the enzymatic reaction.	Tyrosine	142-150	phenylalanine hydroxylase	Homo sapiens	30-55
1111363-1	1975	Cultured human lymphocytes treated with phytohemagglutinin (PAH) ahd higher rates of RNA and protein synthesis, as judged by incorporation of the labelled precursors -3H-URIDINE AND -14C-leucine, than did control cultures without PHA.	3h-uridine	167-177	phenylalanine hydroxylase	Homo sapiens	60-63
1111363-1	1975	Cultured human lymphocytes treated with phytohemagglutinin (PAH) ahd higher rates of RNA and protein synthesis, as judged by incorporation of the labelled precursors -3H-URIDINE AND -14C-leucine, than did control cultures without PHA.	14c-leucine	183-194	phenylalanine hydroxylase	Homo sapiens	60-63
4280309-0	1974	Inhibition of phenylalanine hydroxylase by p-chlorophenylalanine; dependence on cofactor structure.	Fenclonine	43-64	phenylalanine hydroxylase	Homo sapiens	14-39
4854919-9	1974	As with the rat enzyme, human phenylalanine hydroxylase acted also on p-fluorophenylalanine, which was inhibitory at high concentrations, and p-chlorophenylalanine acted as an inhibitor competing with phenylalanine.	p-Fluorophenylalanine	70-91	phenylalanine hydroxylase	Homo sapiens	30-55
4854919-10	1974	Iron-chelating and copper-chelating agents inhibited human phenylalanine hydroxylase.	Iron	0-4	phenylalanine hydroxylase	Homo sapiens	59-84
4854919-10	1974	Iron-chelating and copper-chelating agents inhibited human phenylalanine hydroxylase.	Copper	19-25	phenylalanine hydroxylase	Homo sapiens	59-84
4152249-2	1974	The rationale for selection is that tyrosine is an essential amino acid for most mammalian cells and that three enzymes from mammalian sources can catalyze the synthesis of tyrosine: phenylalanine hydroxylase (EC 1.14.16.1), tyrosine hydroxylase (EC 1.14.16.2), and tryptophan hydroxylase (EC 1.14.16.4).	Tyrosine	36-44	phenylalanine hydroxylase	Homo sapiens	183-208
4269912-0	1973	Studies on the stimulation of phenylalanine hydroxylase activity by short-chain alcohols.	Alcohols	80-88	phenylalanine hydroxylase	Homo sapiens	30-55
4705985-0	1973	Kinetics of phenylalanine hydroxylase with analogs of tetrahydrobiopterin.	sapropterin	54-73	phenylalanine hydroxylase	Homo sapiens	12-37
4785942-0	1973	[Relationship between radioimmunologically determined serum-digoxin concentration and kidney function (serum-creatinine, inulin, and PAH clearance)].	Digoxin	60-67	phenylalanine hydroxylase	Homo sapiens	133-136
4281155-0	1973	Control of liver and brain aromatic amino-acid metabolism by phenylalanine hydroxylase.	Amino Acids, Aromatic	27-46	phenylalanine hydroxylase	Homo sapiens	61-86
5165490-0	1971	Two mechanisms for the inhibition in vitro of phenylalanine hydroxylase by catecholamines.	Catecholamines	75-89	phenylalanine hydroxylase	Homo sapiens	46-71
4335693-0	1971	The inactivation of phenylalanine hydroxylase by 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine and the aerobic oxidation of the latter.	2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine	49-98	phenylalanine hydroxylase	Homo sapiens	20-45
4335693-3	1971	Phenylalanine hydroxylase is inhibited by its cofactor, 6,7-dimethyltetrahydropterin.	6,7-dimethyltetrahydropterin	56-84	phenylalanine hydroxylase	Homo sapiens	0-25
4335693-16	1971	It is suggested that either hydrogen peroxide or an organic peroxide formed by oxidation in air of the cofactor is the substance attacking phenylalanine hydroxylase, dithiothreitol and cofactor.	Hydrogen Peroxide	28-45	phenylalanine hydroxylase	Homo sapiens	139-164
4335693-16	1971	It is suggested that either hydrogen peroxide or an organic peroxide formed by oxidation in air of the cofactor is the substance attacking phenylalanine hydroxylase, dithiothreitol and cofactor.	Peroxides	37-45	phenylalanine hydroxylase	Homo sapiens	139-164
5004199-8	1971	l-[(14)C]Phenylalanine</compound-id> as purchased or soon after purification contains p- and m-tyrosine, both of which can cause errors in the assay of phenylalanine hydroxylase.	p- and m-tyrosine	86-103	phenylalanine hydroxylase	Homo sapiens	152-177
5317637-0	1971	The effects of some nucleosides and dithiothreitol on the stability and activity of liver phenylalanine hydroxylase.	Nucleosides	20-31	phenylalanine hydroxylase	Homo sapiens	90-115
5289888-4	1971	The isomerization of 1,4-dimethylbenzene oxide to 2,4-dimethylphenol is analogous to the methyl migration observed in the enzymatic conversion of 4-methylphenylalanine to 3-methyltyrosine with phenylalanine hydroxylase.	1,4-dimethylbenzene oxide	21-46	phenylalanine hydroxylase	Homo sapiens	193-218
5289888-4	1971	The isomerization of 1,4-dimethylbenzene oxide to 2,4-dimethylphenol is analogous to the methyl migration observed in the enzymatic conversion of 4-methylphenylalanine to 3-methyltyrosine with phenylalanine hydroxylase.	2,4-dimethylphenol	50-68	phenylalanine hydroxylase	Homo sapiens	193-218
5289888-4	1971	The isomerization of 1,4-dimethylbenzene oxide to 2,4-dimethylphenol is analogous to the methyl migration observed in the enzymatic conversion of 4-methylphenylalanine to 3-methyltyrosine with phenylalanine hydroxylase.	4-methylphenylalanine	146-167	phenylalanine hydroxylase	Homo sapiens	193-218
5289888-4	1971	The isomerization of 1,4-dimethylbenzene oxide to 2,4-dimethylphenol is analogous to the methyl migration observed in the enzymatic conversion of 4-methylphenylalanine to 3-methyltyrosine with phenylalanine hydroxylase.	methyl-3-tyrosine	171-187	phenylalanine hydroxylase	Homo sapiens	193-218
5317637-0	1971	The effects of some nucleosides and dithiothreitol on the stability and activity of liver phenylalanine hydroxylase.	Dithiothreitol	36-50	phenylalanine hydroxylase	Homo sapiens	90-115
5649509-0	1968	Production of m-methyltyrosine and p-hydroxymethylphenylalanine from p-methylphenylalanine by phenylalanine hydroxylase.	m-methyltyrosine	14-30	phenylalanine hydroxylase	Homo sapiens	94-119
5455644-0	1970	Comparison of renal tubular transport of urate and PAH in water snakes: evidence for differences in mechanisms and sites of transport.	Water	58-63	phenylalanine hydroxylase	Homo sapiens	51-54
5686299-0	1968	Phenylalanine hydroxylase activity towards two substrates simultaneously: enhancement of inhibition by phenylalanine, tryptophan and their derivatives.	Phenylalanine	103-116	phenylalanine hydroxylase	Homo sapiens	0-25
5686299-0	1968	Phenylalanine hydroxylase activity towards two substrates simultaneously: enhancement of inhibition by phenylalanine, tryptophan and their derivatives.	Tryptophan	118-128	phenylalanine hydroxylase	Homo sapiens	0-25
5649509-0	1968	Production of m-methyltyrosine and p-hydroxymethylphenylalanine from p-methylphenylalanine by phenylalanine hydroxylase.	4-hydroxymethylphenylalanine	35-63	phenylalanine hydroxylase	Homo sapiens	94-119
5690961-2	1968	Inhibitors of phenylalanine hydroxylase related to esculetin.	esculetin	51-60	phenylalanine hydroxylase	Homo sapiens	14-39
5649509-0	1968	Production of m-methyltyrosine and p-hydroxymethylphenylalanine from p-methylphenylalanine by phenylalanine hydroxylase.	4-methylphenylalanine	69-90	phenylalanine hydroxylase	Homo sapiens	94-119
14031389-0	1962	The source of oxygen in the phenylalanine hydroxylase and the copamine-beta-hydroxylase catalyzed rections.	Oxygen	14-20	phenylalanine hydroxylase	Homo sapiens	28-53
6048017-0	1967	Dependence of m-fluorophenylalanine toxicity on phenylalanine hydroxylase activity.	fluorophenylalanine	16-35	phenylalanine hydroxylase	Homo sapiens	48-73
5971770-0	1966	The production of meta-tritiotyrosine from p-tritiophenylalanine by phenylalanine hydroxylase.	meta-tritiotyrosine	18-37	phenylalanine hydroxylase	Homo sapiens	68-93
5971770-0	1966	The production of meta-tritiotyrosine from p-tritiophenylalanine by phenylalanine hydroxylase.	p-tritiophenylalanine	43-64	phenylalanine hydroxylase	Homo sapiens	68-93
14491500-0	1961	Conversion of tryptopan to 5-hydroxytryptophan by phenylalanine hydroxylase.	tryptopan	14-23	phenylalanine hydroxylase	Homo sapiens	50-75
14491501-0	1962	Hydroxylation of tryptophan by phenylalanine hydroxylase.	Tryptophan	17-27	phenylalanine hydroxylase	Homo sapiens	31-56
13894152-0	1961	Relationship between renal succinoxidase activity and maximal transport rates of paminohippurate (Tm-PAH) in various representative vertebrates.	p-Aminohippuric Acid	81-96	phenylalanine hydroxylase	Homo sapiens	101-104
14491500-0	1961	Conversion of tryptopan to 5-hydroxytryptophan by phenylalanine hydroxylase.	5-Hydroxytryptophan	27-46	phenylalanine hydroxylase	Homo sapiens	50-75
33933945-3	2021	At physiological pH, it undergoes conversion to MTIC (methyltriazine imidazole carboxamide) and AIC (amino imidazole carboxamide), resulting in only 20-30% brain bioavailability.	Aminoimidazole Carboxamide	101-128	phenylalanine hydroxylase	Homo sapiens	17-19
13532310-0	1958	Determination of unilateral renal function in urology; unilateral selective clearances and the extraction ratio of PAH (Epah) determined by renal vein catheterization.	epah	120-124	phenylalanine hydroxylase	Homo sapiens	115-118
33894546-0	2021	pH-responsive pickering foam created from self-aggregate polymer using dynamic covalent bond.	Polymers	57-64	phenylalanine hydroxylase	Homo sapiens	0-2
33894546-4	2021	The covalent imine bonds between originally hydrophilic PAH and hydrophobic BA are dynamic in that their formation and breakage is a function of solution pH, confirmed by 1H NMR and dynamic interfacial tension measurement.	polyallylamine	56-59	phenylalanine hydroxylase	Homo sapiens	154-156
33894546-4	2021	The covalent imine bonds between originally hydrophilic PAH and hydrophobic BA are dynamic in that their formation and breakage is a function of solution pH, confirmed by 1H NMR and dynamic interfacial tension measurement.	Barium	76-78	phenylalanine hydroxylase	Homo sapiens	154-156
33933945-5	2021	In this research study, analytical methods were developed for the estimation of TMZ using two media pH 1.2 (0.1 N HCl) and pH 4.5 acetate buffer, which were validated for linearity, range, precision, accuracy, limit of detection, limit of quantification, and specificity as per ICH guidelines.	Temozolomide	80-83	phenylalanine hydroxylase	Homo sapiens	100-102
33894546-4	2021	The covalent imine bonds between originally hydrophilic PAH and hydrophobic BA are dynamic in that their formation and breakage is a function of solution pH, confirmed by 1H NMR and dynamic interfacial tension measurement.	Hydrogen	171-173	phenylalanine hydroxylase	Homo sapiens	154-156
33894546-5	2021	FINDINGS: At pH 7.4, a stable foam is achieved in the PAH-BA (amino to aldehyde ratio at 1:0.2) solution; while at pH 2.5, it defoams due to breakage of dynamic bonds corresponding to the measured diminishing surface activity.	pah-ba	54-60	phenylalanine hydroxylase	Homo sapiens	13-15
33894546-5	2021	FINDINGS: At pH 7.4, a stable foam is achieved in the PAH-BA (amino to aldehyde ratio at 1:0.2) solution; while at pH 2.5, it defoams due to breakage of dynamic bonds corresponding to the measured diminishing surface activity.	amino	62-67	phenylalanine hydroxylase	Homo sapiens	13-15
33894546-5	2021	FINDINGS: At pH 7.4, a stable foam is achieved in the PAH-BA (amino to aldehyde ratio at 1:0.2) solution; while at pH 2.5, it defoams due to breakage of dynamic bonds corresponding to the measured diminishing surface activity.	Aldehydes	71-79	phenylalanine hydroxylase	Homo sapiens	13-15
33933945-0	2021	UV spectroscopic method for estimation of temozolomide: Application in stability studies in simulated plasma pH, degradation rate kinetics, formulation design, and selection of dissolution media.	Temozolomide	42-54	phenylalanine hydroxylase	Homo sapiens	109-111
33933945-2	2021	The major drawback associated with TMZ is pH-dependent stability and short half-life.	Temozolomide	35-38	phenylalanine hydroxylase	Homo sapiens	42-44
33933945-5	2021	In this research study, analytical methods were developed for the estimation of TMZ using two media pH 1.2 (0.1 N HCl) and pH 4.5 acetate buffer, which were validated for linearity, range, precision, accuracy, limit of detection, limit of quantification, and specificity as per ICH guidelines.	Temozolomide	80-83	phenylalanine hydroxylase	Homo sapiens	123-125
33933945-3	2021	At physiological pH, it undergoes conversion to MTIC (methyltriazine imidazole carboxamide) and AIC (amino imidazole carboxamide), resulting in only 20-30% brain bioavailability.	5-(3-methyl-1-triazeno)imidazole-4-carboxamide	48-52	phenylalanine hydroxylase	Homo sapiens	17-19
33933945-8	2021	The stability of TMZ in three pH conditions (1.2, 4.5, and 7.4) and the respective degradation rate kinetics was studied.	Temozolomide	17-20	phenylalanine hydroxylase	Homo sapiens	30-32
33933945-3	2021	At physiological pH, it undergoes conversion to MTIC (methyltriazine imidazole carboxamide) and AIC (amino imidazole carboxamide), resulting in only 20-30% brain bioavailability.	methyltriazine imidazole carboxamide	54-90	phenylalanine hydroxylase	Homo sapiens	17-19
33933945-9	2021	Conversion of TMZ was found to follow first order kinetics with the conversion rate of 0.0011, 0.0011, and 0.0453 h-1 in pH 1.2, 4.5, and 7.4 respectively.	Temozolomide	14-17	phenylalanine hydroxylase	Homo sapiens	121-123
33933945-3	2021	At physiological pH, it undergoes conversion to MTIC (methyltriazine imidazole carboxamide) and AIC (amino imidazole carboxamide), resulting in only 20-30% brain bioavailability.	Aminoimidazole Carboxamide	96-99	phenylalanine hydroxylase	Homo sapiens	17-19
33933945-11	2021	Acetate buffer (pH 4.5) was found to be an appropriate dissolution media for TMZ loaded lipid nanoformulations.	Acetates	0-7	phenylalanine hydroxylase	Homo sapiens	16-18
33933945-11	2021	Acetate buffer (pH 4.5) was found to be an appropriate dissolution media for TMZ loaded lipid nanoformulations.	Temozolomide	77-80	phenylalanine hydroxylase	Homo sapiens	16-18
33957451-0	2021	Development of the fluorescent carbon nanosensor for pH and temperature of liquid media with artificial neural networks.	Carbon	31-37	phenylalanine hydroxylase	Homo sapiens	53-55
33957451-1	2021	The present study is devoted to the creation of optical nanosensors for pH and temperature of liquid media based on carbon dots (CD) prepared via hydrothermal synthesis.	Methane	116-127	phenylalanine hydroxylase	Homo sapiens	72-74
33957451-1	2021	The present study is devoted to the creation of optical nanosensors for pH and temperature of liquid media based on carbon dots (CD) prepared via hydrothermal synthesis.	Cadmium	129-131	phenylalanine hydroxylase	Homo sapiens	72-74
33957451-2	2021	The application of artificial neural networks to the CD fluorescence spectra database provided simultaneous determination of pH and ambient temperature values with an accuracy of 0.005 pH units and 0.67  C, respectively.	Cadmium	53-55	phenylalanine hydroxylase	Homo sapiens	125-127
33957451-2	2021	The application of artificial neural networks to the CD fluorescence spectra database provided simultaneous determination of pH and ambient temperature values with an accuracy of 0.005 pH units and 0.67  C, respectively.	Cadmium	53-55	phenylalanine hydroxylase	Homo sapiens	185-187
33957451-3	2021	The obtained results are unique since they indicate the possibility of creating a multifunctional CD-based nanosensor that operates in a wide temperature range (22-81  C) and provides an accuracy of pH determination exceeding the accuracy of nanoscale analogs by an order of magnitude.	Cadmium	98-100	phenylalanine hydroxylase	Homo sapiens	199-201
33887313-1	2021	The determination of pH in fermented milk is an important parameter for monitoring the production of acid by lactic acid bacteria (LAB).	Lactic Acid	109-120	phenylalanine hydroxylase	Homo sapiens	21-23
33789191-0	2021	Selective, pH sensitive, "turn on" fluorescence sensing of carbonate ions by a benzimidazole.	Carbonates	59-68	phenylalanine hydroxylase	Homo sapiens	11-13
33789191-0	2021	Selective, pH sensitive, "turn on" fluorescence sensing of carbonate ions by a benzimidazole.	benzimidazole	79-92	phenylalanine hydroxylase	Homo sapiens	11-13
33789191-3	2021	A pH-sensitive & selective benzimidazole-based fluorescent sensor has been developed for rapid detection of carbonate ions which can detect carbonate ions in low nanomolar concentrations.	benzimidazole	27-40	phenylalanine hydroxylase	Homo sapiens	2-4
33789191-3	2021	A pH-sensitive & selective benzimidazole-based fluorescent sensor has been developed for rapid detection of carbonate ions which can detect carbonate ions in low nanomolar concentrations.	Carbonates	108-117	phenylalanine hydroxylase	Homo sapiens	2-4
33789191-3	2021	A pH-sensitive & selective benzimidazole-based fluorescent sensor has been developed for rapid detection of carbonate ions which can detect carbonate ions in low nanomolar concentrations.	Carbonates	140-149	phenylalanine hydroxylase	Homo sapiens	2-4
33690059-3	2021	Low pH (5.0) and low substrate concentration (20 mM and 40 mM) effectively decreased propionate production via restrained acrylate pathway, resulting in higher electron efficiency of caproate.	Propionates	85-95	phenylalanine hydroxylase	Homo sapiens	4-6
33690059-3	2021	Low pH (5.0) and low substrate concentration (20 mM and 40 mM) effectively decreased propionate production via restrained acrylate pathway, resulting in higher electron efficiency of caproate.	acrylic acid	122-130	phenylalanine hydroxylase	Homo sapiens	4-6
33690059-3	2021	Low pH (5.0) and low substrate concentration (20 mM and 40 mM) effectively decreased propionate production via restrained acrylate pathway, resulting in higher electron efficiency of caproate.	hexanoic acid	183-191	phenylalanine hydroxylase	Homo sapiens	4-6
33690059-6	2021	Compared with the batch operation, the caproate production in semi-continuous operation was enhanced by 3.45 times to 30.91 +- 1.07 mM as the acrylate pathway was successfully inhibited in semi-continuous experiments due to low pH and low lactate concentration.	hexanoic acid	39-47	phenylalanine hydroxylase	Homo sapiens	228-230
33690059-6	2021	Compared with the batch operation, the caproate production in semi-continuous operation was enhanced by 3.45 times to 30.91 +- 1.07 mM as the acrylate pathway was successfully inhibited in semi-continuous experiments due to low pH and low lactate concentration.	acrylic acid	142-150	phenylalanine hydroxylase	Homo sapiens	228-230
33887313-3	2021	The proposed method uses spectrophotometry to measure the pH change by bacteria and uses bromocresol purple as a pH indicator dye.	Bromcresol Purple	89-107	phenylalanine hydroxylase	Homo sapiens	113-115
33887313-4	2021	The absorbance at 430 nm of a buffer solution with bromocresol purple was found to be correlated with pH values.	Bromcresol Purple	51-69	phenylalanine hydroxylase	Homo sapiens	102-104
33518692-6	2021	We also found that a 1% TiF4 solution adjusted to a pH 4-6 can reduce demineralization as effectively as a similar concentration of NaF.	titanium tetrafluoride	24-28	phenylalanine hydroxylase	Homo sapiens	52-54
33550493-3	2021	Other forms of HPA also characterized by neurological symptoms occur in rare instances due to defects in the metabolism of the PAH cofactor tetrahydrobiopterin.	sapropterin	140-159	phenylalanine hydroxylase	Homo sapiens	127-130
33491267-9	2021	We also identify important residues in the BH4 binding pocket that may be of interest for the rational drug design of other PAH drug-based therapies.	sapropterin	43-46	phenylalanine hydroxylase	Homo sapiens	124-127
34057292-1	2021	Phenylketonuria (PKU), a deficiency in the activity of the enzyme phenylalanine hydroxylase, leads to toxic levels of phenylalanine (Phe) in the blood and brain.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	66-91
33845278-7	2021	Secondly, pH increase was evaluated to be the major cause for the formation of a mixed scaling (a majority of oxidized vivianite with some iron hydroxides) around dewatering centrifuges of undigested sludge.	ferrous phosphate	119-128	phenylalanine hydroxylase	Homo sapiens	10-12
33845278-7	2021	Secondly, pH increase was evaluated to be the major cause for the formation of a mixed scaling (a majority of oxidized vivianite with some iron hydroxides) around dewatering centrifuges of undigested sludge.	iron hydroxides	139-154	phenylalanine hydroxylase	Homo sapiens	10-12
33934496-0	2021	Influences of pH and substrate supply on the ratio of iron to sulfate reduction.	Iron	54-58	phenylalanine hydroxylase	Homo sapiens	14-16
34058475-11	2021	We also used physicochemical measurements and molecular dynamics simulations to analyze the effects of supercharging mutations in sodium phosphate buffer with different pH and ion concentrations, which revealed preferential solvation of phosphate ions to the supercharged surface relative to the wild-type surface.	sodium phosphate	130-146	phenylalanine hydroxylase	Homo sapiens	169-171
34058475-11	2021	We also used physicochemical measurements and molecular dynamics simulations to analyze the effects of supercharging mutations in sodium phosphate buffer with different pH and ion concentrations, which revealed preferential solvation of phosphate ions to the supercharged surface relative to the wild-type surface.	Phosphates	137-146	phenylalanine hydroxylase	Homo sapiens	169-171
33977874-6	2021	Carbopol 934 did not significantly affect sol-gel transition temperature in optimized concentration (< 0.3%) but altered gelling capacity, pH, and transparency of the formulations.	carbopol 934P	0-12	phenylalanine hydroxylase	Homo sapiens	139-141
33845472-0	2021	Role of pH in the synthesis and growth of gold nanoparticles using L-Asparagine: A combined experimental and simulation study.	Asparagine	67-79	phenylalanine hydroxylase	Homo sapiens	8-10
33845472-3	2021	In this work, we use L-Asparagine (Asn), an amino acid building block of large biomolecular systems, to synthesise gold nanoparticles (AuNPs) in aqueous solution at controlled pH.	Asparagine	21-33	phenylalanine hydroxylase	Homo sapiens	176-178
33845472-3	2021	In this work, we use L-Asparagine (Asn), an amino acid building block of large biomolecular systems, to synthesise gold nanoparticles (AuNPs) in aqueous solution at controlled pH.	Asparagine	35-38	phenylalanine hydroxylase	Homo sapiens	176-178
33845472-7	2021	A combined analysis suggests that the underlying mechanism controlling AuNPs geometry correlates with amine"s preferential adsorption over ammonium groups, enhanced upon increasing pH.	Amines	102-107	phenylalanine hydroxylase	Homo sapiens	181-183
33845472-7	2021	A combined analysis suggests that the underlying mechanism controlling AuNPs geometry correlates with amine"s preferential adsorption over ammonium groups, enhanced upon increasing pH.	Ammonium Compounds	139-147	phenylalanine hydroxylase	Homo sapiens	181-183
33845472-10	2021	These results indicate that pH is a relevant parameter in green-synthesis protocols with the capability to control the nanoparticle"s geometry, and pave the way to computational studies exploring the effect of water monolayers on the adsorption of small molecules on wet gold surfaces.	Water	210-215	phenylalanine hydroxylase	Homo sapiens	28-30
33257072-2	2021	Current knowledge gaps include how nitrification-related N2O is associated with soil microbes in different pH soils.	Nitrous Oxide	57-60	phenylalanine hydroxylase	Homo sapiens	107-109
33257072-9	2021	The results showed that N2O yield for AOA and AOB varied with soil pH.	Nitrous Oxide	24-27	phenylalanine hydroxylase	Homo sapiens	67-69
33257072-14	2021	To conclude, soil pH was a key factor affecting the contribution of ammonia oxidizers to nitrification-related N2O emissions.	Ammonia	68-75	phenylalanine hydroxylase	Homo sapiens	18-20
33257072-14	2021	To conclude, soil pH was a key factor affecting the contribution of ammonia oxidizers to nitrification-related N2O emissions.	Nitrous Oxide	111-114	phenylalanine hydroxylase	Homo sapiens	18-20
33739584-1	2021	A novel charge-reversible surfactant, (CH 3 ) 2 N-(CH 2 ) 10 COONa, was designed and synthesized, which together with silica nanoparticles can stabilize a smart n -octane-in-water emulsion responsive to pH.	Water	174-179	phenylalanine hydroxylase	Homo sapiens	203-205
33712157-1	2021	A dual pH-/thermo-responsive hydrogel was designed based on a polyelectrolyte complex of polyacrylic acid (PAA) and norbornene-functionalized chitosan (CsNb), which was synergized with chemical crosslinking using bistetrazine-poly(N-isopropyl acrylamide) (bisTz-PNIPAM).	2-norbornene	116-126	phenylalanine hydroxylase	Homo sapiens	7-9
33712157-1	2021	A dual pH-/thermo-responsive hydrogel was designed based on a polyelectrolyte complex of polyacrylic acid (PAA) and norbornene-functionalized chitosan (CsNb), which was synergized with chemical crosslinking using bistetrazine-poly(N-isopropyl acrylamide) (bisTz-PNIPAM).	Chitosan	142-150	phenylalanine hydroxylase	Homo sapiens	7-9
33712157-1	2021	A dual pH-/thermo-responsive hydrogel was designed based on a polyelectrolyte complex of polyacrylic acid (PAA) and norbornene-functionalized chitosan (CsNb), which was synergized with chemical crosslinking using bistetrazine-poly(N-isopropyl acrylamide) (bisTz-PNIPAM).	csnb	152-156	phenylalanine hydroxylase	Homo sapiens	7-9
33712157-5	2021	The hydrogel (COOH/NH2 mole ratio of 3:1) exhibited limited drug release (8.5 %) of 5-ASA at a pH of 2.2, but it provided an almost complete release (92 %) at pH 7.4 and 37  C within 48 h due to the pH responsiveness of PAA, hydrogel porosity, and shrinkage behavior of PNIPAM.	Carbonic Acid	14-18	phenylalanine hydroxylase	Homo sapiens	95-97
33712157-5	2021	The hydrogel (COOH/NH2 mole ratio of 3:1) exhibited limited drug release (8.5 %) of 5-ASA at a pH of 2.2, but it provided an almost complete release (92 %) at pH 7.4 and 37  C within 48 h due to the pH responsiveness of PAA, hydrogel porosity, and shrinkage behavior of PNIPAM.	Carbonic Acid	14-18	phenylalanine hydroxylase	Homo sapiens	159-161
33712157-5	2021	The hydrogel (COOH/NH2 mole ratio of 3:1) exhibited limited drug release (8.5 %) of 5-ASA at a pH of 2.2, but it provided an almost complete release (92 %) at pH 7.4 and 37  C within 48 h due to the pH responsiveness of PAA, hydrogel porosity, and shrinkage behavior of PNIPAM.	Carbonic Acid	14-18	phenylalanine hydroxylase	Homo sapiens	159-161
33712157-5	2021	The hydrogel (COOH/NH2 mole ratio of 3:1) exhibited limited drug release (8.5 %) of 5-ASA at a pH of 2.2, but it provided an almost complete release (92 %) at pH 7.4 and 37  C within 48 h due to the pH responsiveness of PAA, hydrogel porosity, and shrinkage behavior of PNIPAM.	Amido radical	19-22	phenylalanine hydroxylase	Homo sapiens	159-161
33712157-5	2021	The hydrogel (COOH/NH2 mole ratio of 3:1) exhibited limited drug release (8.5 %) of 5-ASA at a pH of 2.2, but it provided an almost complete release (92 %) at pH 7.4 and 37  C within 48 h due to the pH responsiveness of PAA, hydrogel porosity, and shrinkage behavior of PNIPAM.	Amido radical	19-22	phenylalanine hydroxylase	Homo sapiens	159-161
33524719-0	2021	Effect of pH and urea on the proteins secondary structure at the water/air interface and in solution.	Water	65-70	phenylalanine hydroxylase	Homo sapiens	10-12
33609931-4	2021	Long-term trends of bacterial concentrations and community structures were likely caused by changes in the water physical-chemical quality (i.e. pH and conductivity).	Water	107-112	phenylalanine hydroxylase	Homo sapiens	145-147
33609931-9	2021	On the other hand, FCM data correlated with water pH and conductivity, underlining the relation between physical-chemical and microbiological water quality.	Water	44-49	phenylalanine hydroxylase	Homo sapiens	50-52
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	Polyethylene Glycols	82-103	phenylalanine hydroxylase	Homo sapiens	34-36
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	Polyethylene Glycols	82-103	phenylalanine hydroxylase	Homo sapiens	310-312
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	Polyethylene Glycols	105-108	phenylalanine hydroxylase	Homo sapiens	34-36
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	Polyethylene Glycols	105-108	phenylalanine hydroxylase	Homo sapiens	310-312
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	ylated phospholipid	109-128	phenylalanine hydroxylase	Homo sapiens	34-36
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	ylated phospholipid	109-128	phenylalanine hydroxylase	Homo sapiens	310-312
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	DSPE-PEG	130-138	phenylalanine hydroxylase	Homo sapiens	34-36
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	DSPE-PEG	130-138	phenylalanine hydroxylase	Homo sapiens	310-312
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	Phenol	146-152	phenylalanine hydroxylase	Homo sapiens	34-36
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	Phenol	146-152	phenylalanine hydroxylase	Homo sapiens	310-312
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	Phospholipids	116-128	phenylalanine hydroxylase	Homo sapiens	34-36
33904297-2	2021	Herein, we engineered an original pH sensor by a simple one-step self-assembly of poly(ethylene glycol) (PEG)ylated phospholipid (DSPE-PEG) and a phenol red small molecule on the surface of upconversion nanoparticles (UCNPs) to form a phospholipid monolayer for sensing and imaging the change of intracellular pH.	Phospholipids	116-128	phenylalanine hydroxylase	Homo sapiens	310-312
33724816-0	2021	Thiol-Thioester Exchange Reactions in Precursors Enable pH-Triggered Hydrogel Formation.	Sulfhydryl Compounds	0-5	phenylalanine hydroxylase	Homo sapiens	56-58
33724816-3	2021	In particular, thiopeptolide/thio-depsipeptides were capable of pH-sensitive thiol-thioester exchange reactions to yield alpha,omega-dithiols, which react with maleimide-functionalized multi-arm polyethylene glycol to polymer networks.	thiopeptolide	15-28	phenylalanine hydroxylase	Homo sapiens	64-66
33724816-3	2021	In particular, thiopeptolide/thio-depsipeptides were capable of pH-sensitive thiol-thioester exchange reactions to yield alpha,omega-dithiols, which react with maleimide-functionalized multi-arm polyethylene glycol to polymer networks.	Sulfhydryl Compounds	77-82	phenylalanine hydroxylase	Homo sapiens	64-66
33724816-3	2021	In particular, thiopeptolide/thio-depsipeptides were capable of pH-sensitive thiol-thioester exchange reactions to yield alpha,omega-dithiols, which react with maleimide-functionalized multi-arm polyethylene glycol to polymer networks.	Cy5-benzyl thioester	83-92	phenylalanine hydroxylase	Homo sapiens	64-66
33724816-3	2021	In particular, thiopeptolide/thio-depsipeptides were capable of pH-sensitive thiol-thioester exchange reactions to yield alpha,omega-dithiols, which react with maleimide-functionalized multi-arm polyethylene glycol to polymer networks.	alpha,omega-dithiols	121-141	phenylalanine hydroxylase	Homo sapiens	64-66
33724816-3	2021	In particular, thiopeptolide/thio-depsipeptides were capable of pH-sensitive thiol-thioester exchange reactions to yield alpha,omega-dithiols, which react with maleimide-functionalized multi-arm polyethylene glycol to polymer networks.	maleimide	160-169	phenylalanine hydroxylase	Homo sapiens	64-66
33724816-3	2021	In particular, thiopeptolide/thio-depsipeptides were capable of pH-sensitive thiol-thioester exchange reactions to yield alpha,omega-dithiols, which react with maleimide-functionalized multi-arm polyethylene glycol to polymer networks.	Polyethylene Glycols	195-214	phenylalanine hydroxylase	Homo sapiens	64-66
33958651-4	2021	Differential substrate preference at different pH (i.e. peroxidised phospholipids at neutral pH and reduced phospholipids at acidic pH) is considered to be the reason for this behavior.	Phospholipids	68-81	phenylalanine hydroxylase	Homo sapiens	47-49
33958651-4	2021	Differential substrate preference at different pH (i.e. peroxidised phospholipids at neutral pH and reduced phospholipids at acidic pH) is considered to be the reason for this behavior.	Phospholipids	68-81	phenylalanine hydroxylase	Homo sapiens	93-95
33958651-4	2021	Differential substrate preference at different pH (i.e. peroxidised phospholipids at neutral pH and reduced phospholipids at acidic pH) is considered to be the reason for this behavior.	Phospholipids	68-81	phenylalanine hydroxylase	Homo sapiens	93-95
33958651-4	2021	Differential substrate preference at different pH (i.e. peroxidised phospholipids at neutral pH and reduced phospholipids at acidic pH) is considered to be the reason for this behavior.	Phospholipids	108-121	phenylalanine hydroxylase	Homo sapiens	47-49
33950296-0	2021	Computational studies on binding, solvent, and pH effects on (S)-propranolol and methacrylic acid complex.	Propranolol	61-76	phenylalanine hydroxylase	Homo sapiens	47-49
33950296-0	2021	Computational studies on binding, solvent, and pH effects on (S)-propranolol and methacrylic acid complex.	methacrylic acid	81-97	phenylalanine hydroxylase	Homo sapiens	47-49
33950296-2	2021	The model has been expanded to study the effect of various pH by adding hydronium and hydroxide ions solvated by water molecules to the template-monomer system, to mimic acidic and basic environments, respectively.	Hydronium	72-81	phenylalanine hydroxylase	Homo sapiens	59-61
33950296-2	2021	The model has been expanded to study the effect of various pH by adding hydronium and hydroxide ions solvated by water molecules to the template-monomer system, to mimic acidic and basic environments, respectively.	hydroxide ion	86-95	phenylalanine hydroxylase	Homo sapiens	59-61
33950296-2	2021	The model has been expanded to study the effect of various pH by adding hydronium and hydroxide ions solvated by water molecules to the template-monomer system, to mimic acidic and basic environments, respectively.	Water	113-118	phenylalanine hydroxylase	Homo sapiens	59-61
33934496-0	2021	Influences of pH and substrate supply on the ratio of iron to sulfate reduction.	Sulfates	62-69	phenylalanine hydroxylase	Homo sapiens	14-16
33934496-3	2021	This study examines impacts of pH and the supply of acetate, sulfate, and goethite on the ratio of iron to sulfate reduction in semi-continuous sediment bioreactors.	Iron	99-103	phenylalanine hydroxylase	Homo sapiens	31-33
33934496-5	2021	Results show that pH had a greater influence than acetate supply on the ratio of iron to sulfate reduction, and that the impact of acetate supply on the ratio depended on pH.	Iron	81-85	phenylalanine hydroxylase	Homo sapiens	18-20
33934496-5	2021	Results show that pH had a greater influence than acetate supply on the ratio of iron to sulfate reduction, and that the impact of acetate supply on the ratio depended on pH.	Acetates	131-138	phenylalanine hydroxylase	Homo sapiens	171-173
33934496-6	2021	In acidic reactors (pH 6.0 media), the ratio of iron to sulfate reduction decreased from 3:1 to 2:1 as acetate supply increased (0-1 mM).	Iron	48-52	phenylalanine hydroxylase	Homo sapiens	20-22
33934496-6	2021	In acidic reactors (pH 6.0 media), the ratio of iron to sulfate reduction decreased from 3:1 to 2:1 as acetate supply increased (0-1 mM).	Sulfates	56-63	phenylalanine hydroxylase	Homo sapiens	20-22
33934496-6	2021	In acidic reactors (pH 6.0 media), the ratio of iron to sulfate reduction decreased from 3:1 to 2:1 as acetate supply increased (0-1 mM).	Acetates	103-110	phenylalanine hydroxylase	Homo sapiens	20-22
33934496-9	2021	Thus, the influence of sulfate supply on iron reduction extent also depended on pH and suggests that iron reduction grows more dependent on sulfate reduction as pH increases.	Sulfates	23-30	phenylalanine hydroxylase	Homo sapiens	80-82
33934496-9	2021	Thus, the influence of sulfate supply on iron reduction extent also depended on pH and suggests that iron reduction grows more dependent on sulfate reduction as pH increases.	Sulfates	23-30	phenylalanine hydroxylase	Homo sapiens	161-163
33934496-9	2021	Thus, the influence of sulfate supply on iron reduction extent also depended on pH and suggests that iron reduction grows more dependent on sulfate reduction as pH increases.	Iron	41-45	phenylalanine hydroxylase	Homo sapiens	80-82
33934496-9	2021	Thus, the influence of sulfate supply on iron reduction extent also depended on pH and suggests that iron reduction grows more dependent on sulfate reduction as pH increases.	Iron	41-45	phenylalanine hydroxylase	Homo sapiens	161-163
33934496-9	2021	Thus, the influence of sulfate supply on iron reduction extent also depended on pH and suggests that iron reduction grows more dependent on sulfate reduction as pH increases.	Iron	101-105	phenylalanine hydroxylase	Homo sapiens	80-82
33934496-9	2021	Thus, the influence of sulfate supply on iron reduction extent also depended on pH and suggests that iron reduction grows more dependent on sulfate reduction as pH increases.	Iron	101-105	phenylalanine hydroxylase	Homo sapiens	161-163
33934496-9	2021	Thus, the influence of sulfate supply on iron reduction extent also depended on pH and suggests that iron reduction grows more dependent on sulfate reduction as pH increases.	Sulfates	140-147	phenylalanine hydroxylase	Homo sapiens	161-163
33934496-10	2021	Our results compare well to trends in groundwater geochemistry and provide further evidence that pH is a major control on iron and sulfate reduction in systems with crystalline (oxyhydr)oxides.	Iron	122-126	phenylalanine hydroxylase	Homo sapiens	97-99
33934496-10	2021	Our results compare well to trends in groundwater geochemistry and provide further evidence that pH is a major control on iron and sulfate reduction in systems with crystalline (oxyhydr)oxides.	Sulfates	131-138	phenylalanine hydroxylase	Homo sapiens	97-99
33934496-10	2021	Our results compare well to trends in groundwater geochemistry and provide further evidence that pH is a major control on iron and sulfate reduction in systems with crystalline (oxyhydr)oxides.	(oxyhydr)oxides	177-192	phenylalanine hydroxylase	Homo sapiens	97-99
33609882-1	2021	This study focused on the nitrous oxide (N2O) generation from the biological nitrogen removal process under different pH levels.	Nitrous Oxide	26-39	phenylalanine hydroxylase	Homo sapiens	118-120
33609882-1	2021	This study focused on the nitrous oxide (N2O) generation from the biological nitrogen removal process under different pH levels.	Nitrous Oxide	41-44	phenylalanine hydroxylase	Homo sapiens	118-120
33609882-1	2021	This study focused on the nitrous oxide (N2O) generation from the biological nitrogen removal process under different pH levels.	Nitrogen	77-85	phenylalanine hydroxylase	Homo sapiens	118-120
33609882-3	2021	The mean gaseous N2O emission accounted for 0.329%, 0.103%, 0.085%, and 0.793% of the influent total nitrogen at pH of 5, 6, 8, and 9, respectively.	Nitrous Oxide	17-20	phenylalanine hydroxylase	Homo sapiens	113-115
33609882-6	2021	The impacts of pH on N2O generation were more likely related to the response of bacterial enzymes and nitrogen compounds, rather than the feedback of bacterial community structure itself.	Nitrous Oxide	21-24	phenylalanine hydroxylase	Homo sapiens	15-17
33609882-6	2021	The impacts of pH on N2O generation were more likely related to the response of bacterial enzymes and nitrogen compounds, rather than the feedback of bacterial community structure itself.	Nitrogen	102-110	phenylalanine hydroxylase	Homo sapiens	15-17
33609882-7	2021	Above all, an influent pH range of 6-8 is recommended for nitrogen removal and N2O mitigation in anoxic-oxic process.	Nitrogen	58-66	phenylalanine hydroxylase	Homo sapiens	23-25
33609882-7	2021	Above all, an influent pH range of 6-8 is recommended for nitrogen removal and N2O mitigation in anoxic-oxic process.	Nitrous Oxide	79-82	phenylalanine hydroxylase	Homo sapiens	23-25
33685581-2	2021	Anecdotally, low rectal pH could reduce rectal azithromycin concentrations, with in vitro studies reporting higher minimum inhibitory concentrations (MICs) with lower pHs for antibiotics used to treat sexually transmissible infections (STIs).	Azithromycin	47-59	phenylalanine hydroxylase	Homo sapiens	24-26
33129860-4	2021	The photoreduction rate of U(VI) significantly decreased with increasing pH, H2O2 radicals and photo-generated electrons play an important role in U(VI) photoreduction by quenching experiments and ESR analysis.	Hydrogen Peroxide	77-81	phenylalanine hydroxylase	Homo sapiens	73-75
33485250-5	2021	For the model substances maleic acid and phenylalanine, we demonstrate that a custom-made genetic algorithm is able to extract up to nine parameters of a multispecies isotherm from experimental data covering a broad pH-range.	maleic acid	25-36	phenylalanine hydroxylase	Homo sapiens	216-218
33485250-5	2021	For the model substances maleic acid and phenylalanine, we demonstrate that a custom-made genetic algorithm is able to extract up to nine parameters of a multispecies isotherm from experimental data covering a broad pH-range.	Phenylalanine	41-54	phenylalanine hydroxylase	Homo sapiens	216-218
33685581-10	2021	And 50% had a rectal pH <8.0, with 27% reporting a pH between 6.0 and 6.5 where treatment failure is thought to occur for azithromycin.	Azithromycin	122-134	phenylalanine hydroxylase	Homo sapiens	51-53
33685581-12	2021	CONCLUSIONS: Lower rectal pH among MSM is associated with older age and could influence the rectal pharmacokinetics of azithromycin and other drugs influenced by pH and may therefore affect treatment outcomes.	Azithromycin	119-131	phenylalanine hydroxylase	Homo sapiens	26-28
33685581-12	2021	CONCLUSIONS: Lower rectal pH among MSM is associated with older age and could influence the rectal pharmacokinetics of azithromycin and other drugs influenced by pH and may therefore affect treatment outcomes.	Azithromycin	119-131	phenylalanine hydroxylase	Homo sapiens	162-164
33946988-4	2021	The hydrosols with MC water were characterized by a lower pH, decreased viscosity, a lower contact angle, and only slightly lower antioxidant activity than control samples.	Water	22-27	phenylalanine hydroxylase	Homo sapiens	58-60
33997408-2	2021	Although numerous chemical species such as water soluble ionic species (e.g. Na+, K+, Cl-, Ca2+, Mg2+) and acid leachable heavy metal fractions (e.g. Fe, Cd, Al, Mo, Sb, As, Cu, Zn, Pb, and Mn) can be used to characterize tsunami deposits, the knowledge of PAH congeners as alternative chemical species for identifying tsunami backwash deposits is strictly limited.	Water	43-48	phenylalanine hydroxylase	Homo sapiens	257-260
33997408-2	2021	Although numerous chemical species such as water soluble ionic species (e.g. Na+, K+, Cl-, Ca2+, Mg2+) and acid leachable heavy metal fractions (e.g. Fe, Cd, Al, Mo, Sb, As, Cu, Zn, Pb, and Mn) can be used to characterize tsunami deposits, the knowledge of PAH congeners as alternative chemical species for identifying tsunami backwash deposits is strictly limited.	Aluminum	0-2	phenylalanine hydroxylase	Homo sapiens	257-260
33394414-3	2021	A general formula for P adsorption was proposed that considers mineral composition through the component additivity method, also incorporating the effects of environmental factors, including the aqueous P concentration (Ce), pH, sediment concentration (S), and ionic strength (IS).	Phosphorus	22-23	phenylalanine hydroxylase	Homo sapiens	225-227
34047298-0	2021	The pH and Bismuth Oxide Particle Size can Affect Diametral Tensile Strength of Mineral Trioxide Aggregate.	mineral trioxide	80-96	phenylalanine hydroxylase	Homo sapiens	4-6
34047298-9	2021	RESULTS: The comparison of DTS in pH groups were: 8.4>7.4>9.4>6.4>5.4>4.4 (P<0.05); and in bismuth oxide groups were: fine particles > medium particles > coarse particles (P<0.05).	dibenzyl trisulfide	27-30	phenylalanine hydroxylase	Homo sapiens	34-36
34047298-10	2021	Acidic pH, negatively affected the distribution of Ca2+ and Si4+ ions, while bismuth oxide with fine particles enhanced it.	si4+	60-64	phenylalanine hydroxylase	Homo sapiens	7-9
34047298-11	2021	CONCLUSION: Acidic pH can decline the DTS of MTA significantly.	dibenzyl trisulfide	38-41	phenylalanine hydroxylase	Homo sapiens	19-21
33221376-1	2021	Phenylalanine hydroxylase (PAH) is an allosteric enzyme that maintains phenylalanine (Phe) below neurotoxic levels; its failure results in phenylketonuria, an inborn error of amino acid metabolism.	Phenylalanine	71-84	phenylalanine hydroxylase	Homo sapiens	0-25
33394453-7	2021	In general, PAH concentrations in the samples were low and may reflect baseline levels for this Amazon estuarine system.	estuarine	103-112	phenylalanine hydroxylase	Homo sapiens	12-15
33920688-0	2021	Development of a New Deodorization Method of Herring Milt Hydrolysate: Impacts of pH, Stirring with Nitrogen and Deaerator Treatment on the Odorous Content.	milt hydrolysate	53-69	phenylalanine hydroxylase	Homo sapiens	82-84
33920688-4	2021	Results showed that pH had a huge impact on the targeted compounds resulting in higher detected concentrations of DMA, TMA and TMAO at pH 10 than at pH 7 (p < 0.05) while the opposite trend was observed for the most potent odor-active compounds of HMH (p < 0.05).	dimethylamine	114-117	phenylalanine hydroxylase	Homo sapiens	20-22
33920688-4	2021	Results showed that pH had a huge impact on the targeted compounds resulting in higher detected concentrations of DMA, TMA and TMAO at pH 10 than at pH 7 (p < 0.05) while the opposite trend was observed for the most potent odor-active compounds of HMH (p < 0.05).	dimethylamine	114-117	phenylalanine hydroxylase	Homo sapiens	135-137
33920688-4	2021	Results showed that pH had a huge impact on the targeted compounds resulting in higher detected concentrations of DMA, TMA and TMAO at pH 10 than at pH 7 (p < 0.05) while the opposite trend was observed for the most potent odor-active compounds of HMH (p < 0.05).	dimethylamine	114-117	phenylalanine hydroxylase	Homo sapiens	135-137
33920688-4	2021	Results showed that pH had a huge impact on the targeted compounds resulting in higher detected concentrations of DMA, TMA and TMAO at pH 10 than at pH 7 (p < 0.05) while the opposite trend was observed for the most potent odor-active compounds of HMH (p < 0.05).	trimethyloxamine	127-131	phenylalanine hydroxylase	Homo sapiens	20-22
33920688-4	2021	Results showed that pH had a huge impact on the targeted compounds resulting in higher detected concentrations of DMA, TMA and TMAO at pH 10 than at pH 7 (p < 0.05) while the opposite trend was observed for the most potent odor-active compounds of HMH (p < 0.05).	trimethyloxamine	127-131	phenylalanine hydroxylase	Homo sapiens	135-137
33920688-4	2021	Results showed that pH had a huge impact on the targeted compounds resulting in higher detected concentrations of DMA, TMA and TMAO at pH 10 than at pH 7 (p < 0.05) while the opposite trend was observed for the most potent odor-active compounds of HMH (p < 0.05).	trimethyloxamine	127-131	phenylalanine hydroxylase	Homo sapiens	135-137
33920688-6	2021	Finally, the deaerator treatment was more effective to remove TMA and DMA at pH 10 than at pH 7 (p < 0.05) while the opposite trend was observed for the most potent odor-active compounds (p < 0.05).	dimethylamine	70-73	phenylalanine hydroxylase	Homo sapiens	77-79
33860893-0	2021	A study on the effects of anion, cation, organic compounds, and pH on the release behaviors of As and Sb from sediments.	Arsenic	95-97	phenylalanine hydroxylase	Homo sapiens	64-66
33860893-7	2021	The stability of As and Sb in the sediment was found to be the best at pH 5.	Arsenic	17-19	phenylalanine hydroxylase	Homo sapiens	71-73
33860893-7	2021	The stability of As and Sb in the sediment was found to be the best at pH 5.	Antimony	24-26	phenylalanine hydroxylase	Homo sapiens	71-73
33861488-6	2021	The urease-urea reaction can be used to control hydrogel properties by a uniform and controlled pH increase as well as to set up pH cycles.	Urea	4-8	phenylalanine hydroxylase	Homo sapiens	96-98
33861488-6	2021	The urease-urea reaction can be used to control hydrogel properties by a uniform and controlled pH increase as well as to set up pH cycles.	Urea	4-8	phenylalanine hydroxylase	Homo sapiens	129-131
33861488-7	2021	The reaction involves hydrolysis of urea by urease and production of ammonia which increases the pH.	Urea	36-40	phenylalanine hydroxylase	Homo sapiens	97-99
33861488-7	2021	The reaction involves hydrolysis of urea by urease and production of ammonia which increases the pH.	Ammonia	69-76	phenylalanine hydroxylase	Homo sapiens	97-99
34017389-9	2021	In conclusion, miR-320-3p plays a certain role in the progression of hypoxic PH via KLF5 and HIF1alpha and might be a potent therapeutic tool for PH.	mir-320-3p	15-25	phenylalanine hydroxylase	Homo sapiens	77-79
33401050-0	2021	Associative structures formed from cellulose nanofibrils and nanochitins are pH-responsive and exhibit tunable rheology.	nanochitins	61-72	phenylalanine hydroxylase	Homo sapiens	77-79
33394414-7	2021	Multivariable regression analysis was used to show that the amount of P adsorption was strongly correlated with Ce, followed by S, IS, and pH.	Phosphorus	70-71	phenylalanine hydroxylase	Homo sapiens	139-141
33345720-0	2021	A core-shell structured alginate hydrogel beads with tunable thickness of Carboxymethyl cellulose coating for pH responsive drug delivery.	Alginates	24-32	phenylalanine hydroxylase	Homo sapiens	110-112
33345720-0	2021	A core-shell structured alginate hydrogel beads with tunable thickness of Carboxymethyl cellulose coating for pH responsive drug delivery.	Carboxymethylcellulose Sodium	74-97	phenylalanine hydroxylase	Homo sapiens	110-112
33345720-1	2021	pH-responsive core-shell structured composite hydrogel beads, composed of a alginate (ALG) core coated with carboxymethyl cellulose (CMC) shell (ALG@CMC), were prepared by using in-situ gel preparation technology as a drug delivery system.	Alginates	76-84	phenylalanine hydroxylase	Homo sapiens	0-2
33345720-1	2021	pH-responsive core-shell structured composite hydrogel beads, composed of a alginate (ALG) core coated with carboxymethyl cellulose (CMC) shell (ALG@CMC), were prepared by using in-situ gel preparation technology as a drug delivery system.	Alginates	86-89	phenylalanine hydroxylase	Homo sapiens	0-2
33345720-1	2021	pH-responsive core-shell structured composite hydrogel beads, composed of a alginate (ALG) core coated with carboxymethyl cellulose (CMC) shell (ALG@CMC), were prepared by using in-situ gel preparation technology as a drug delivery system.	Carboxymethylcellulose Sodium	108-131	phenylalanine hydroxylase	Homo sapiens	0-2
33345720-1	2021	pH-responsive core-shell structured composite hydrogel beads, composed of a alginate (ALG) core coated with carboxymethyl cellulose (CMC) shell (ALG@CMC), were prepared by using in-situ gel preparation technology as a drug delivery system.	Carboxymethylcellulose Sodium	133-136	phenylalanine hydroxylase	Homo sapiens	0-2
33345720-1	2021	pH-responsive core-shell structured composite hydrogel beads, composed of a alginate (ALG) core coated with carboxymethyl cellulose (CMC) shell (ALG@CMC), were prepared by using in-situ gel preparation technology as a drug delivery system.	Alginates	145-148	phenylalanine hydroxylase	Homo sapiens	0-2
33345720-1	2021	pH-responsive core-shell structured composite hydrogel beads, composed of a alginate (ALG) core coated with carboxymethyl cellulose (CMC) shell (ALG@CMC), were prepared by using in-situ gel preparation technology as a drug delivery system.	Carboxymethylcellulose Sodium	149-152	phenylalanine hydroxylase	Homo sapiens	0-2
33345720-6	2021	The swelling and drug release behaviors revealed that the swelling and drug release rate of ALG@CMC beads were obviously slower than that of simple-ALG and both have significant pH responsiveness.	Alginates	92-95	phenylalanine hydroxylase	Homo sapiens	178-180
33345720-6	2021	The swelling and drug release behaviors revealed that the swelling and drug release rate of ALG@CMC beads were obviously slower than that of simple-ALG and both have significant pH responsiveness.	Carboxymethylcellulose Sodium	96-99	phenylalanine hydroxylase	Homo sapiens	178-180
33728720-7	2021	Additionally, extracellular basic pH and KGF treatment up-regulated Nrf2 activation and its regulation of the oxidative defence system in the 3HSE.	3hse	142-146	phenylalanine hydroxylase	Homo sapiens	34-36
33513404-2	2021	Ibuprofen (pKa=5.3) is in its anionic form, whereas paracetamol (pKa 9.4) is only partially ionized at the synthesis pH (9.0), and thus intercalation is expected to be different in the two cases.	Acetaminophen	52-63	phenylalanine hydroxylase	Homo sapiens	117-119
33728720-6	2021	Extracellular basic pH decreased KGF expression and enhanced the oxidative defence system, and thus activated Nrf2 in the 3HSE.	3hse	122-126	phenylalanine hydroxylase	Homo sapiens	20-22
33130281-5	2021	The correlation between the pH and lactates was studied using Pearson coefficient.	Lactates	35-43	phenylalanine hydroxylase	Homo sapiens	28-30
33576028-5	2021	The relationship between [ADP] and muscle power output was augmented at workloads above the pH threshold (pHT ; proxy for LT), whereas increases in ATPOX were attenuated.	Adenosine Diphosphate	26-29	phenylalanine hydroxylase	Homo sapiens	92-94
33001224-5	2021	Concentrations of extractable calcium, iron, and phosphorus also varied significantly across the pH gradients.	Calcium	30-37	phenylalanine hydroxylase	Homo sapiens	97-99
33833848-0	2021	Optimizing CO Coverage on Rough Copper Electrodes: Effect of the Partial Pressure of CO and Electrolyte Anions (pH) on Selectivity toward Ethylene.	Copper	32-38	phenylalanine hydroxylase	Homo sapiens	112-114
33833848-0	2021	Optimizing CO Coverage on Rough Copper Electrodes: Effect of the Partial Pressure of CO and Electrolyte Anions (pH) on Selectivity toward Ethylene.	Carbon Monoxide	11-13	phenylalanine hydroxylase	Homo sapiens	112-114
33833848-0	2021	Optimizing CO Coverage on Rough Copper Electrodes: Effect of the Partial Pressure of CO and Electrolyte Anions (pH) on Selectivity toward Ethylene.	ethylene	138-146	phenylalanine hydroxylase	Homo sapiens	112-114
33833848-1	2021	The conversion of the initial intermediate CO in the electrochemical reduction reaction of CO2 on the surface of oxide-derived Cu electrodes has been investigated as a function of partial pressure and pH, manipulated by the composition of the electrolyte.	Carbon Monoxide	43-45	phenylalanine hydroxylase	Homo sapiens	201-203
33833848-1	2021	The conversion of the initial intermediate CO in the electrochemical reduction reaction of CO2 on the surface of oxide-derived Cu electrodes has been investigated as a function of partial pressure and pH, manipulated by the composition of the electrolyte.	Carbon Dioxide	91-94	phenylalanine hydroxylase	Homo sapiens	201-203
33833848-7	2021	Collectively, the data herein outline the critical role of reactant partial pressures and the significant effect of anion composition (pH) on the surface coverage of CO and concomitant selectivity in electrochemical reduction of CO2 to ethylene.	Carbon Monoxide	166-168	phenylalanine hydroxylase	Homo sapiens	135-137
33833848-7	2021	Collectively, the data herein outline the critical role of reactant partial pressures and the significant effect of anion composition (pH) on the surface coverage of CO and concomitant selectivity in electrochemical reduction of CO2 to ethylene.	Carbon Dioxide	229-232	phenylalanine hydroxylase	Homo sapiens	135-137
33833848-7	2021	Collectively, the data herein outline the critical role of reactant partial pressures and the significant effect of anion composition (pH) on the surface coverage of CO and concomitant selectivity in electrochemical reduction of CO2 to ethylene.	ethylene	236-244	phenylalanine hydroxylase	Homo sapiens	135-137
33001224-5	2021	Concentrations of extractable calcium, iron, and phosphorus also varied significantly across the pH gradients.	Phosphorus	49-59	phenylalanine hydroxylase	Homo sapiens	97-99
33838420-6	2021	Results revealed that pinewood-derived biochar had its maximum performance at pH 2, with predicted equilibrium uptakes of 20.5 and 4.20 mg/g for phosphate and nitrate, respectively at initial solute concentrations of 60 mg/L within 360 min.	Nitrates	159-166	phenylalanine hydroxylase	Homo sapiens	78-80
33739227-5	2021	Moreover, employed as an effective catalyst in Fenton oxidation, over 99%, 95% and 97% of rhodamine B, methyl orange and reactive black V were rapidly degraded without the assistance of additional irradiation, and degradation conditions like pH, H2O2 and initial pollutant concentrations as well as the reaction kinetic was investigated, indicating the hydroxyl radical generated in the presence of TFMOF and H2O2 was able to degrade the pollutants into non-toxic molecular.	methyl orange	103-116	phenylalanine hydroxylase	Homo sapiens	242-244
33759670-10	2021	Hyaluronic acid was generally found to be effective in improving vulvovaginal symptoms (dyspareunia, itching, burning, dryness) and signs (bleeding, atrophy, vaginal pH).	Hyaluronic Acid	0-15	phenylalanine hydroxylase	Homo sapiens	166-168
33481326-0	2021	Delivering the Full Potential of Oxygen Evolving Electrocatalyst by Conditioning Electrolytes at Near-Neutral pH.	Oxygen	33-39	phenylalanine hydroxylase	Homo sapiens	110-112
33606865-1	2021	Amphotericin B incorporating 2,2"-bipyridine (bpy-AmB) forms a membrane channel exhibiting pH-dependent Ca2+ ion permeability with a selective response to Cu2+ ions.	cupric ion	155-159	phenylalanine hydroxylase	Homo sapiens	91-93
33606865-0	2021	pH-Dependent ion permeability control of a modified amphotericin B channel through metal complexation.	Amphotericin B	52-66	phenylalanine hydroxylase	Homo sapiens	0-2
33606865-0	2021	pH-Dependent ion permeability control of a modified amphotericin B channel through metal complexation.	Metals	83-88	phenylalanine hydroxylase	Homo sapiens	0-2
33606865-1	2021	Amphotericin B incorporating 2,2"-bipyridine (bpy-AmB) forms a membrane channel exhibiting pH-dependent Ca2+ ion permeability with a selective response to Cu2+ ions.	Amphotericin B	0-14	phenylalanine hydroxylase	Homo sapiens	91-93
33606865-1	2021	Amphotericin B incorporating 2,2"-bipyridine (bpy-AmB) forms a membrane channel exhibiting pH-dependent Ca2+ ion permeability with a selective response to Cu2+ ions.	2,2'-Dipyridyl	29-44	phenylalanine hydroxylase	Homo sapiens	91-93
33606865-1	2021	Amphotericin B incorporating 2,2"-bipyridine (bpy-AmB) forms a membrane channel exhibiting pH-dependent Ca2+ ion permeability with a selective response to Cu2+ ions.	bpy-amb	46-53	phenylalanine hydroxylase	Homo sapiens	91-93
33599654-0	2021	Reaction of carbon oxides with an ethylene-bridged PH/B Lewis pair.	carbon oxides	12-25	phenylalanine hydroxylase	Homo sapiens	51-53
33599654-0	2021	Reaction of carbon oxides with an ethylene-bridged PH/B Lewis pair.	ethylene	34-42	phenylalanine hydroxylase	Homo sapiens	51-53
33599654-2	2021	It is a monomer at high temperature (>323 K), but exists as an associated 12-membered macrocyclic trimer below 273 K. The PH/B FLP splits dihydrogen and serves as a metal-free hydrogenation catalyst.	Hydrogen	138-148	phenylalanine hydroxylase	Homo sapiens	122-124
33599654-2	2021	It is a monomer at high temperature (>323 K), but exists as an associated 12-membered macrocyclic trimer below 273 K. The PH/B FLP splits dihydrogen and serves as a metal-free hydrogenation catalyst.	Metals	165-170	phenylalanine hydroxylase	Homo sapiens	122-124
33599654-4	2021	It serves as a PH/B template for the reduction of carbon monoxide by the HB(C6F5)2 borane to the formyl stage.	Carbon Monoxide	50-65	phenylalanine hydroxylase	Homo sapiens	15-17
33646759-1	2021	Bioneutralization of pH by microbial fermentation of added carbon substrates is a promising new method for remediation of the 1.7 GT/yr of alkaline mining tailings produced globally.	Carbon	59-65	phenylalanine hydroxylase	Homo sapiens	21-23
33646759-2	2021	Here, we present the first study to systematically compare and optimize the efficacy of microbial inocula of varying diversities, structures, and provenance and organic carbon substrates of varying complexities on the rate and extent of pH bioneutralization in alkaline bauxite residue tailings.	Carbon	169-175	phenylalanine hydroxylase	Homo sapiens	237-239
33646759-2	2021	Here, we present the first study to systematically compare and optimize the efficacy of microbial inocula of varying diversities, structures, and provenance and organic carbon substrates of varying complexities on the rate and extent of pH bioneutralization in alkaline bauxite residue tailings.	Aluminum Oxide	270-277	phenylalanine hydroxylase	Homo sapiens	237-239
33646759-3	2021	Laboratory-scale bioreactors inoculated with soda lake sediments or with monosaccharide substrates added had a significantly lower minimum pH (<8) and a significantly higher maximum rate of pH neutralization (>0.02 mumol H+ day-1) and achieved these in significantly less time (<26 days) compared to bioreactors with other inocula or substrates.	Monosaccharides	73-87	phenylalanine hydroxylase	Homo sapiens	139-141
33646759-3	2021	Laboratory-scale bioreactors inoculated with soda lake sediments or with monosaccharide substrates added had a significantly lower minimum pH (<8) and a significantly higher maximum rate of pH neutralization (>0.02 mumol H+ day-1) and achieved these in significantly less time (<26 days) compared to bioreactors with other inocula or substrates.	Monosaccharides	73-87	phenylalanine hydroxylase	Homo sapiens	190-192
33507734-7	2021	The influence of pH (pH of human saliva, 6.7-7.4) on the uptake of uranyl was negligible.	uranyl	67-73	phenylalanine hydroxylase	Homo sapiens	17-19
33507734-7	2021	The influence of pH (pH of human saliva, 6.7-7.4) on the uptake of uranyl was negligible.	uranyl	67-73	phenylalanine hydroxylase	Homo sapiens	21-23
33198983-4	2021	Here, we discuss a fundamentally different approach, in which changes in pH modify the nonspecific interparticle interaction between Au nanorods conjugated with single-stranded (ss) DNA.	Gold	133-135	phenylalanine hydroxylase	Homo sapiens	73-75
33198983-6	2021	Analysis of in-situ electron microscopy of ssDNA-Au nanorods in solution is consistent with a van der Waals attraction of charge-neutral monomers at acidic pH.	Gold	49-51	phenylalanine hydroxylase	Homo sapiens	156-158
33465714-5	2021	Maximum Cu(II) removal efficiency (92%) was observed at pH 6.	cu(ii)	8-14	phenylalanine hydroxylase	Homo sapiens	56-58
33465714-6	2021	By decreasing the pH from 6 to 2, a log 5 reduction in bacteria was observed and Carboxyl groups transformed from -COO- to -COOH.	carboxyl radical	115-119	phenylalanine hydroxylase	Homo sapiens	18-20
33465714-6	2021	By decreasing the pH from 6 to 2, a log 5 reduction in bacteria was observed and Carboxyl groups transformed from -COO- to -COOH.	Carbonic Acid	124-128	phenylalanine hydroxylase	Homo sapiens	18-20
33533365-3	2021	The effect of pH, contact time, and initial dye concentration has been investigated on MO to find the optimum pH, equilibrium and adsorption capacity of the synthesized BNNSs.	bnnss	169-174	phenylalanine hydroxylase	Homo sapiens	14-16
33533365-3	2021	The effect of pH, contact time, and initial dye concentration has been investigated on MO to find the optimum pH, equilibrium and adsorption capacity of the synthesized BNNSs.	bnnss	169-174	phenylalanine hydroxylase	Homo sapiens	110-112
33710842-6	2021	To date, multiple PAH-specific therapies have been developed, and all currently target one of 3 pathways that contribute to the endothelial dysfunction pathogenesis of PAH (prostacyclin, endothelin, and nitric oxide pathways).	Epoprostenol	173-185	phenylalanine hydroxylase	Homo sapiens	168-171
32883659-1	2021	OBJECTIVES: Severe pulmonary hypertension (PH) causing right heart failure can occur due to thiamine deficiency in exclusively breastfeeding infants.	Thiamine	92-100	phenylalanine hydroxylase	Homo sapiens	43-45
33216297-5	2021	However, a slight overdosing of GO was observed for dosages of more than 20 mg/L under pH values of less than about 4.	graphene oxide	32-34	phenylalanine hydroxylase	Homo sapiens	87-89
33216297-8	2021	The most significant interaction effect was also observed between pH and GO dosage.	graphene oxide	73-75	phenylalanine hydroxylase	Homo sapiens	66-68
33216297-10	2021	Under basic pH levels, the sweeping effect was recognized as the main coagulation mechanism occurred between the negatively surface charged particles of GO and soil.	graphene oxide	153-155	phenylalanine hydroxylase	Homo sapiens	12-14
33219502-12	2021	The spent adsorbent was successfully regenerated at high pH by flushing with NaOH.	Sodium Hydroxide	77-81	phenylalanine hydroxylase	Homo sapiens	57-59
32066882-4	2021	This study analysed creatinine-adjusted urinary PAH metabolite concentrations and questionnaire data from ~1200 individuals aged 16 years and older surveyed in Cycle 2 of the Canadian Health Measures Survey (CHMS).	Creatinine	20-30	phenylalanine hydroxylase	Homo sapiens	48-51
32929770-0	2021	Quantifying the effect of dobutamine stress on myocardial Pi and pH in healthy volunteers: A 31 P MRS study at 7T.	Dobutamine	26-36	phenylalanine hydroxylase	Homo sapiens	65-67
32929770-3	2021	We focus on another 31 P signal: inorganic phosphate (Pi), whose chemical shift allows computation of myocardial pH, with Pi/PCr providing additional insight into cardiac energetics.	Phosphates	33-52	phenylalanine hydroxylase	Homo sapiens	113-115
32929770-13	2021	CONCLUSION: We introduced a method that can resolve Pi using 7 Tesla STEAM 31 P-MRS. We demonstrate the stability of Pi/PCr and myocardial pH in volunteers at rest and during catecholamine stress.	Catecholamines	175-188	phenylalanine hydroxylase	Homo sapiens	139-141
33354836-8	2021	Glucose addition significantly further decreased pHe in hyperglycolytic cell lines (VX2, HepG2, and Huh7, by 0.28, 0.06, and 0.11, respectively, all p < 0.001), whereas 3-bromopyruvate normalized tumor pHe in a dose-dependent manner without affecting viability.	Glucose	0-7	phenylalanine hydroxylase	Homo sapiens	49-52
33354836-8	2021	Glucose addition significantly further decreased pHe in hyperglycolytic cell lines (VX2, HepG2, and Huh7, by 0.28, 0.06, and 0.11, respectively, all p < 0.001), whereas 3-bromopyruvate normalized tumor pHe in a dose-dependent manner without affecting viability.	Glucose	0-7	phenylalanine hydroxylase	Homo sapiens	202-205
33670952-0	2021	Multi-Component Hydrogel Beads Incorporated with Reduced Graphene Oxide for pH-Responsive and Controlled Co-Delivery of Multiple Agents.	graphene oxide	57-71	phenylalanine hydroxylase	Homo sapiens	76-78
33707087-9	2021	Adding pH and P/F ratio to the ABA criteria improved their sensitivity in detecting appropriate intubations (sensitivity: ABA + pH + P/F = 0.97 vs ABA = 0.86; p = 0.013), without altering their specificity.	Abscisic Acid	31-34	phenylalanine hydroxylase	Homo sapiens	128-130
33673467-0	2021	Influences of pH and EDTA Additive on the Structure of Ni Films Electrodeposited by Using Bubble Templates as Electrocatalysts for Hydrogen Evolution Reaction.	Hydrogen	131-139	phenylalanine hydroxylase	Homo sapiens	14-16
33673467-2	2021	The pH value and EDTA (ethylene diamine tetraacetic acid) additive are important factors for the structure control of electrodeposited metal films due to their adjustment of metal electrocrystallization and hydrogen evolution side reactions.	Metals	135-140	phenylalanine hydroxylase	Homo sapiens	4-6
33673467-2	2021	The pH value and EDTA (ethylene diamine tetraacetic acid) additive are important factors for the structure control of electrodeposited metal films due to their adjustment of metal electrocrystallization and hydrogen evolution side reactions.	Metals	174-179	phenylalanine hydroxylase	Homo sapiens	4-6
33673467-2	2021	The pH value and EDTA (ethylene diamine tetraacetic acid) additive are important factors for the structure control of electrodeposited metal films due to their adjustment of metal electrocrystallization and hydrogen evolution side reactions.	Hydrogen	207-215	phenylalanine hydroxylase	Homo sapiens	4-6
33673467-6	2021	When pH <= 7.7, hydrogen bubbles with large break-off diameter are easily adsorbed on film surface acting as porous structure templates, and the electroactive ion species, Ni2+ and Ni(NH3)n2+ complexes with low coordination number (n <= 3), possess high reduction overpotential, which is beneficial to forming protrusions and smaller particles.	Hydrogen	16-24	phenylalanine hydroxylase	Homo sapiens	5-7
33673467-6	2021	When pH <= 7.7, hydrogen bubbles with large break-off diameter are easily adsorbed on film surface acting as porous structure templates, and the electroactive ion species, Ni2+ and Ni(NH3)n2+ complexes with low coordination number (n <= 3), possess high reduction overpotential, which is beneficial to forming protrusions and smaller particles.	Nickel(2+)	172-176	phenylalanine hydroxylase	Homo sapiens	5-7
33673467-6	2021	When pH <= 7.7, hydrogen bubbles with large break-off diameter are easily adsorbed on film surface acting as porous structure templates, and the electroactive ion species, Ni2+ and Ni(NH3)n2+ complexes with low coordination number (n <= 3), possess high reduction overpotential, which is beneficial to forming protrusions and smaller particles.	ni(nh3)n2+	181-191	phenylalanine hydroxylase	Homo sapiens	5-7
33673467-8	2021	In solutions with pH >= 8.1 or 0.1 M EDTA, Ni(NH3)n2+ complexes with high coordination number (6 >= n >= 3) and hexadentate chelate are formed.	ni(nh3)n2+	43-53	phenylalanine hydroxylase	Homo sapiens	18-20
32997426-0	2021	Effect of hydrophilic monomer distribution on self-assembly of a pH-responsive copolymer: Spheres, worms and vesicles from a single copolymer composition.	copolymer	79-88	phenylalanine hydroxylase	Homo sapiens	65-67
32997426-0	2021	Effect of hydrophilic monomer distribution on self-assembly of a pH-responsive copolymer: Spheres, worms and vesicles from a single copolymer composition.	copolymer	132-141	phenylalanine hydroxylase	Homo sapiens	65-67
32997426-3	2021	In particular, a diblock copolymer consisting of two random copolymer segments of equal length (16 mol% and 84 mol% AA respectively) formed spherical micelles at pH > 5, a mix of spherical and worm-like micelles at pH 5 and vesicles at pH 4.	diblock copolymer	17-34	phenylalanine hydroxylase	Homo sapiens	162-164
32997426-3	2021	In particular, a diblock copolymer consisting of two random copolymer segments of equal length (16 mol% and 84 mol% AA respectively) formed spherical micelles at pH > 5, a mix of spherical and worm-like micelles at pH 5 and vesicles at pH 4.	diblock copolymer	17-34	phenylalanine hydroxylase	Homo sapiens	215-217
32997426-3	2021	In particular, a diblock copolymer consisting of two random copolymer segments of equal length (16 mol% and 84 mol% AA respectively) formed spherical micelles at pH > 5, a mix of spherical and worm-like micelles at pH 5 and vesicles at pH 4.	diblock copolymer	17-34	phenylalanine hydroxylase	Homo sapiens	215-217
33671501-8	2021	When high levels of amine concentration are used, the initial pH values in the reaction are also high which leads to agglomeration.	Amines	20-25	phenylalanine hydroxylase	Homo sapiens	62-64
33671501-9	2021	This study provides a possible explanation to the aggregation based on the kinetic and thermodynamic controls in reactions and shows that the pH measurements account for the polyurea reaction and carbamate formation, which is a reason why this is not a suitable method to study kinetics of polymerization.	polyurea	174-182	phenylalanine hydroxylase	Homo sapiens	142-144
33671501-9	2021	This study provides a possible explanation to the aggregation based on the kinetic and thermodynamic controls in reactions and shows that the pH measurements account for the polyurea reaction and carbamate formation, which is a reason why this is not a suitable method to study kinetics of polymerization.	Carbamates	196-205	phenylalanine hydroxylase	Homo sapiens	142-144
33868536-4	2021	The pH sensitivity, drift coefficient, and hysteresis width of the Si3N4 LAPS are 52.8 mV/pH, -3.2 mV/h, and 10.5 mV, respectively, which are comparable to the results from the conventional setup.	silicon nitride	67-72	phenylalanine hydroxylase	Homo sapiens	4-6
33868536-4	2021	The pH sensitivity, drift coefficient, and hysteresis width of the Si3N4 LAPS are 52.8 mV/pH, -3.2 mV/h, and 10.5 mV, respectively, which are comparable to the results from the conventional setup.	silicon nitride	67-72	phenylalanine hydroxylase	Homo sapiens	90-92
33676393-8	2021	RESULTS: After addition of Rennie, the gastric medium reached a pH of 3.0 within 40 s. The maximum pH of 5.24 was maintained for almost 10 min.	Rennie	27-33	phenylalanine hydroxylase	Homo sapiens	64-66
33676393-8	2021	RESULTS: After addition of Rennie, the gastric medium reached a pH of 3.0 within 40 s. The maximum pH of 5.24 was maintained for almost 10 min.	Rennie	27-33	phenylalanine hydroxylase	Homo sapiens	99-101
33577340-0	2021	The pH-Induced Specific Area Changes of Unsaturated Lipids Deposited onto a Bubble Interface.	unsaturated lipids	40-58	phenylalanine hydroxylase	Homo sapiens	4-6
33867534-11	2021	Since theobromine had the added benefits of increasing the salivary pH and decreasing the S.mutans levels, theobromine containing toothpastes can be considered effective agents in remineralizing white spot lesions and can be used in prevention of early enamel lesions.	Theobromine	6-17	phenylalanine hydroxylase	Homo sapiens	68-70
33462659-0	2021	Water-stable perovskite-on-polymer fluorescent microspheres for simultaneous monitoring of pH, urea, and urease.	Water	0-5	phenylalanine hydroxylase	Homo sapiens	91-93
33462659-0	2021	Water-stable perovskite-on-polymer fluorescent microspheres for simultaneous monitoring of pH, urea, and urease.	perovskite	13-23	phenylalanine hydroxylase	Homo sapiens	91-93
33462659-4	2021	Additionally, a real-time pH monitoring platform was constructed based on the prepared PDPS composites and dopamine, and the system showed a good linear relationship in a pH range of 4-12.	Dopamine	107-115	phenylalanine hydroxylase	Homo sapiens	26-28
33462659-4	2021	Additionally, a real-time pH monitoring platform was constructed based on the prepared PDPS composites and dopamine, and the system showed a good linear relationship in a pH range of 4-12.	Dopamine	107-115	phenylalanine hydroxylase	Homo sapiens	171-173
33462659-5	2021	Furthermore, urea could be hydrolyzed to produce hydroxyl groups, thereby increasing the pH of the solution.	Urea	13-17	phenylalanine hydroxylase	Homo sapiens	89-91
33417911-0	2021	Photo transformation of 5-methylbenzotriazole and 5-chlorobenzotriazole by UV irradiation: influences of pH, salinity, metal species and humic acid.	5-tolyltriazole	24-45	phenylalanine hydroxylase	Homo sapiens	105-107
33417911-0	2021	Photo transformation of 5-methylbenzotriazole and 5-chlorobenzotriazole by UV irradiation: influences of pH, salinity, metal species and humic acid.	5-Chlorobenzotriazole	50-71	phenylalanine hydroxylase	Homo sapiens	105-107
33417911-4	2021	The photolysis rates for both 5-TTri and CBT were strongly dependent on the solution pH value, and decreased with increasing solution pH.	5-tolyltriazole	30-36	phenylalanine hydroxylase	Homo sapiens	85-87
33417911-4	2021	The photolysis rates for both 5-TTri and CBT were strongly dependent on the solution pH value, and decreased with increasing solution pH.	5-tolyltriazole	30-36	phenylalanine hydroxylase	Homo sapiens	134-136
33417911-4	2021	The photolysis rates for both 5-TTri and CBT were strongly dependent on the solution pH value, and decreased with increasing solution pH.	N,N-BIS(4-CHLOROBENZYL)-1H-1,2,3,4-TETRAAZOL-5-AMINE	41-44	phenylalanine hydroxylase	Homo sapiens	85-87
33417911-4	2021	The photolysis rates for both 5-TTri and CBT were strongly dependent on the solution pH value, and decreased with increasing solution pH.	N,N-BIS(4-CHLOROBENZYL)-1H-1,2,3,4-TETRAAZOL-5-AMINE	41-44	phenylalanine hydroxylase	Homo sapiens	134-136
33678882-3	2021	The 4 weeks of storage had a statistically significant (P < 0.05) effect on every tested parameter, while the addition of citric acid had a statistically significant (P < 0.05) effect on pH, conductivity, L* and b* values, protein solubility, emulsion activity index, emulsion capacity, emulsion stability, and an increase in foaming and texture parameters, but not on rheological parameters.	Citric Acid	122-133	phenylalanine hydroxylase	Homo sapiens	187-189
33678882-4	2021	Citric acid addition and a storage period of 4 weeks resulted in a change of pH and an increase in protein solubility.	Citric Acid	0-11	phenylalanine hydroxylase	Homo sapiens	77-79
33404065-4	2021	The cerebrovascular responses to changes in arterial H+ /pH were altered in keeping with the altered relationship between PaCO2 and H+ /pH following NaHCO3 - infusion (i.e., changes in buffering capacity).	paco2	122-127	phenylalanine hydroxylase	Homo sapiens	57-59
33404065-4	2021	The cerebrovascular responses to changes in arterial H+ /pH were altered in keeping with the altered relationship between PaCO2 and H+ /pH following NaHCO3 - infusion (i.e., changes in buffering capacity).	paco2	122-127	phenylalanine hydroxylase	Homo sapiens	136-138
33404065-4	2021	The cerebrovascular responses to changes in arterial H+ /pH were altered in keeping with the altered relationship between PaCO2 and H+ /pH following NaHCO3 - infusion (i.e., changes in buffering capacity).	Sodium Bicarbonate	149-155	phenylalanine hydroxylase	Homo sapiens	57-59
33404065-4	2021	The cerebrovascular responses to changes in arterial H+ /pH were altered in keeping with the altered relationship between PaCO2 and H+ /pH following NaHCO3 - infusion (i.e., changes in buffering capacity).	Sodium Bicarbonate	149-155	phenylalanine hydroxylase	Homo sapiens	136-138
33404065-6	2021	ABSTRACT: Cerebral blood flow (CBF) regulation is dependent on the integrative relationship between arterial PCO2 (PaCO2 ), pH, and cerebrovascular tone; however, pre-clinical studies indicate that intrinsic sensitivity to pH - independent of changes in PaCO2 or intravascular bicarbonate ([HCO3 - ]) - principally influences cerebrovascular tone.	Bicarbonates	277-288	phenylalanine hydroxylase	Homo sapiens	223-225
33404065-6	2021	ABSTRACT: Cerebral blood flow (CBF) regulation is dependent on the integrative relationship between arterial PCO2 (PaCO2 ), pH, and cerebrovascular tone; however, pre-clinical studies indicate that intrinsic sensitivity to pH - independent of changes in PaCO2 or intravascular bicarbonate ([HCO3 - ]) - principally influences cerebrovascular tone.	Bicarbonates	291-297	phenylalanine hydroxylase	Homo sapiens	223-225
33404065-11	2021	These changes in reactivity to [H+ ] were, however, explained by alterations in buffering between PaCO2 and arterial H+ /pH consequent to NaHCO3 - .	Sodium Bicarbonate	138-144	phenylalanine hydroxylase	Homo sapiens	121-123
33465300-1	2021	BACKGROUND: The impairment of the hepatic enzyme phenylalanine hydroxylase (PAH) causes elevation of phenylalanine levels in blood and other body fluids resulting in the most common inborn error of amino acid metabolism (phenylketonuria).	Phenylalanine	49-62	phenylalanine hydroxylase	Homo sapiens	76-79
32738166-1	2021	In the last two decades, environmental experts have focused on the development of several biological, chemical, physical and thermal methods/technologies for remediation of PAH polluted water.	Water	186-191	phenylalanine hydroxylase	Homo sapiens	173-176
32738166-5	2021	Water is an essential component of the ecosystem and highly susceptible to PAH contamination due to crude oil exploration and spillage, and improper municipal and industrial waste management, yet comprehensive reviews on PAH remediation are only available for contaminated soils, despite the several treatment methods developed for the remediation of PAH polluted water.	Water	0-5	phenylalanine hydroxylase	Homo sapiens	75-78
32738166-5	2021	Water is an essential component of the ecosystem and highly susceptible to PAH contamination due to crude oil exploration and spillage, and improper municipal and industrial waste management, yet comprehensive reviews on PAH remediation are only available for contaminated soils, despite the several treatment methods developed for the remediation of PAH polluted water.	Oils	106-109	phenylalanine hydroxylase	Homo sapiens	75-78
33865236-8	2021	Excretion of ammonia in the urine and urine pH levels increased after treatment of DKA, which resulted in the formation of AAU crystals.	Uric Acid	123-126	phenylalanine hydroxylase	Homo sapiens	44-46
33606865-2	2021	The coordination structure at bpy sites depends on the pH and metal ions can control the association state of bpy-AmB in the membrane.	bpy-amb	110-117	phenylalanine hydroxylase	Homo sapiens	55-57
33272657-1	2021	In order to assess the performance of anaerobic ammonium oxidation (anammox) bioreactors, it is necessary to study the stoichiometry of the anammox reaction and pH.	Ammonium Compounds	48-56	phenylalanine hydroxylase	Homo sapiens	161-163
33272657-4	2021	It was concluded that under varying HRT conditions, the decrease in effluent pH did not indicate the deterioration of nitrogen removal, but did indicate that the nitrogen removal efficiency was reduced owing to a sudden increase in the nitrogen loading rate resulting from the decrease in HRT.	Nitrogen	162-170	phenylalanine hydroxylase	Homo sapiens	77-79
33272657-4	2021	It was concluded that under varying HRT conditions, the decrease in effluent pH did not indicate the deterioration of nitrogen removal, but did indicate that the nitrogen removal efficiency was reduced owing to a sudden increase in the nitrogen loading rate resulting from the decrease in HRT.	Nitrogen	162-170	phenylalanine hydroxylase	Homo sapiens	77-79
33352382-0	2021	Nitrate and nitrite bacterial reduction at alkaline pH and high nitrate concentrations, comparison of acetate versus dihydrogen as electron donors.	Nitrites	12-19	phenylalanine hydroxylase	Homo sapiens	52-54
33352382-3	2021	With both types of electron donors, nitrite reduction was the key step, likely to increase the pH and lead to nitrite accumulation.	Nitrites	36-43	phenylalanine hydroxylase	Homo sapiens	95-97
33352382-4	2021	Firstly, an acclimation process was used: nitrate was progressively increased in three cultures set at pH 9, 10, or 11.	Nitrates	42-49	phenylalanine hydroxylase	Homo sapiens	103-105
33352382-5	2021	This method allowed to observe for the first time nitrate reduction up to pH 10 and 100 mM nitrate with dihydrogen, or up to pH 10 and 400 mM nitrate with acetate.	Nitrates	50-57	phenylalanine hydroxylase	Homo sapiens	74-76
33352382-5	2021	This method allowed to observe for the first time nitrate reduction up to pH 10 and 100 mM nitrate with dihydrogen, or up to pH 10 and 400 mM nitrate with acetate.	Nitrates	91-98	phenylalanine hydroxylase	Homo sapiens	74-76
33352382-5	2021	This method allowed to observe for the first time nitrate reduction up to pH 10 and 100 mM nitrate with dihydrogen, or up to pH 10 and 400 mM nitrate with acetate.	Hydrogen	104-114	phenylalanine hydroxylase	Homo sapiens	74-76
33352382-5	2021	This method allowed to observe for the first time nitrate reduction up to pH 10 and 100 mM nitrate with dihydrogen, or up to pH 10 and 400 mM nitrate with acetate.	Nitrates	91-98	phenylalanine hydroxylase	Homo sapiens	74-76
33352382-5	2021	This method allowed to observe for the first time nitrate reduction up to pH 10 and 100 mM nitrate with dihydrogen, or up to pH 10 and 400 mM nitrate with acetate.	Acetates	155-162	phenylalanine hydroxylase	Homo sapiens	125-127
33352382-8	2021	Denitrification with dihydrogen strongly increases the pH while with acetate the pH evolution depends on the initial pH.	Hydrogen	21-31	phenylalanine hydroxylase	Homo sapiens	55-57
33352382-8	2021	Denitrification with dihydrogen strongly increases the pH while with acetate the pH evolution depends on the initial pH.	Hydrogen	21-31	phenylalanine hydroxylase	Homo sapiens	81-83
33352382-8	2021	Denitrification with dihydrogen strongly increases the pH while with acetate the pH evolution depends on the initial pH.	Hydrogen	21-31	phenylalanine hydroxylase	Homo sapiens	81-83
33352382-8	2021	Denitrification with dihydrogen strongly increases the pH while with acetate the pH evolution depends on the initial pH.	Acetates	69-76	phenylalanine hydroxylase	Homo sapiens	81-83
33352382-8	2021	Denitrification with dihydrogen strongly increases the pH while with acetate the pH evolution depends on the initial pH.	Acetates	69-76	phenylalanine hydroxylase	Homo sapiens	81-83
33352382-10	2021	Finally, the use of long duration cultures with a highly alkaline pH allowed a nitrate reduction up to pH 11.5 with acetate.	Nitrates	79-86	phenylalanine hydroxylase	Homo sapiens	66-68
33352382-10	2021	Finally, the use of long duration cultures with a highly alkaline pH allowed a nitrate reduction up to pH 11.5 with acetate.	Nitrates	79-86	phenylalanine hydroxylase	Homo sapiens	103-105
33352382-10	2021	Finally, the use of long duration cultures with a highly alkaline pH allowed a nitrate reduction up to pH 11.5 with acetate.	Acetates	116-123	phenylalanine hydroxylase	Homo sapiens	66-68
33352382-10	2021	Finally, the use of long duration cultures with a highly alkaline pH allowed a nitrate reduction up to pH 11.5 with acetate.	Acetates	116-123	phenylalanine hydroxylase	Homo sapiens	103-105
33352382-12	2021	Instead, bacteria used organic matter from inoculum to reduce nitrate at pH 11.5.	Nitrates	62-69	phenylalanine hydroxylase	Homo sapiens	73-75
33573668-11	2021	CONCLUSIONS: In the successful management of Ph-positive ALL, dasatinib, a second-generation Abl-tyrosine kinase inhibitor, is crucial.	Dasatinib	62-71	phenylalanine hydroxylase	Homo sapiens	45-47
33475345-3	2021	As an example, we have applied it to glutamic acid in aqueous solution and have demonstrated that it can work to generate reasonably the pH-dependent microscopic configuration ensemble compatible with the experimental pKa value and also to show interestingly the molecular diffusivity correlated with pH-dependent solvation shell.	Glutamic Acid	37-50	phenylalanine hydroxylase	Homo sapiens	137-139
33475345-3	2021	As an example, we have applied it to glutamic acid in aqueous solution and have demonstrated that it can work to generate reasonably the pH-dependent microscopic configuration ensemble compatible with the experimental pKa value and also to show interestingly the molecular diffusivity correlated with pH-dependent solvation shell.	Glutamic Acid	37-50	phenylalanine hydroxylase	Homo sapiens	301-303
33405910-1	2021	Vaginal films featuring the pH-dependent release of tenofovir (TFV) were developed for the prevention of sexual transmission of human immunodeficiency syndrome (HIV).	Tenofovir	52-61	phenylalanine hydroxylase	Homo sapiens	28-30
33405910-1	2021	Vaginal films featuring the pH-dependent release of tenofovir (TFV) were developed for the prevention of sexual transmission of human immunodeficiency syndrome (HIV).	Tenofovir	63-66	phenylalanine hydroxylase	Homo sapiens	28-30
33542361-1	2021	The pH-CO2-HCO3- system is a ubiquitous biological regulator with important functional implications for reproduction.	Carbon Dioxide	7-10	phenylalanine hydroxylase	Homo sapiens	4-6
33542361-1	2021	The pH-CO2-HCO3- system is a ubiquitous biological regulator with important functional implications for reproduction.	Bicarbonates	11-15	phenylalanine hydroxylase	Homo sapiens	4-6
33542361-10	2021	This study contributes to a better understanding of the in vivo regulation of the pH-CO2-HCO3- system in the uterus and may help to optimize the protocols of sperm treatment for in vitro fertilization.	Carbon Dioxide	85-88	phenylalanine hydroxylase	Homo sapiens	82-84
33542361-10	2021	This study contributes to a better understanding of the in vivo regulation of the pH-CO2-HCO3- system in the uterus and may help to optimize the protocols of sperm treatment for in vitro fertilization.	Bicarbonates	89-93	phenylalanine hydroxylase	Homo sapiens	82-84
33536517-0	2021	Exceptional antibacterial and cytotoxic potency of monodisperse greener AgNPs prepared under optimized pH and temperature.	agnps	72-77	phenylalanine hydroxylase	Homo sapiens	103-105
33285465-3	2021	Formulated [18F]MK-6240 maintained stability, as measured by radio-high-performance liquid chromatography (HPLC), as well as clarity and pH, over a period of 8 h. Our established method can facilitate multi-center trials and widespread use of [18F]MK-6240.	MK-6240	16-23	phenylalanine hydroxylase	Homo sapiens	137-139
32997426-3	2021	In particular, a diblock copolymer consisting of two random copolymer segments of equal length (16 mol% and 84 mol% AA respectively) formed spherical micelles at pH > 5, a mix of spherical and worm-like micelles at pH 5 and vesicles at pH 4.	copolymer	25-34	phenylalanine hydroxylase	Homo sapiens	162-164
32997426-3	2021	In particular, a diblock copolymer consisting of two random copolymer segments of equal length (16 mol% and 84 mol% AA respectively) formed spherical micelles at pH > 5, a mix of spherical and worm-like micelles at pH 5 and vesicles at pH 4.	copolymer	25-34	phenylalanine hydroxylase	Homo sapiens	215-217
32997426-3	2021	In particular, a diblock copolymer consisting of two random copolymer segments of equal length (16 mol% and 84 mol% AA respectively) formed spherical micelles at pH > 5, a mix of spherical and worm-like micelles at pH 5 and vesicles at pH 4.	copolymer	25-34	phenylalanine hydroxylase	Homo sapiens	215-217
33570037-1	2021	Phenylketonuria is an inherited metabolic disease, of autosomal recessive transmission, due to the enzymatic deficit of phenylalanine hydroxylase, which transforms phenylalanine into tyrosine.	Tyrosine	183-191	phenylalanine hydroxylase	Homo sapiens	120-145
33164127-12	2021	The effects of pH, Eh, and total suspended solids (TSS) on suspended Pd were reduced in the response process of the receiving water body.	Water	126-131	phenylalanine hydroxylase	Homo sapiens	15-17
33246627-0	2021	Short communication: Chemical structure, concentration, and pH are key factors influencing antimicrobial activity of conjugated bile acids against lactobacilli.	Bile Acids and Salts	128-138	phenylalanine hydroxylase	Homo sapiens	60-62
33051847-8	2021	The effects of citrate and SRNOM on the transport and retention of QDs were pH dependent as reflected in the influence of the electrostatic and steric interactions between QDs and sand surfaces.	Citric Acid	15-22	phenylalanine hydroxylase	Homo sapiens	76-78
33051847-8	2021	The effects of citrate and SRNOM on the transport and retention of QDs were pH dependent as reflected in the influence of the electrostatic and steric interactions between QDs and sand surfaces.	srnom	27-32	phenylalanine hydroxylase	Homo sapiens	76-78
33246627-1	2021	Effects of chemical structure, concentration, and pH on antimicrobial activity of conjugated bile acids were investigated in 4 strains of lactobacilli.	Bile Acids and Salts	93-103	phenylalanine hydroxylase	Homo sapiens	50-52
33246627-5	2021	Additionally, the antimicrobial activity of glycochenodeoxycholic acid was also observed to be pH-dependent, and it was significantly enhanced with the decreasing pH, with the result that all the strains of lactobacilli were unable to grow at pH 5.0.	Glycochenodeoxycholic Acid	44-70	phenylalanine hydroxylase	Homo sapiens	95-97
33246627-5	2021	Additionally, the antimicrobial activity of glycochenodeoxycholic acid was also observed to be pH-dependent, and it was significantly enhanced with the decreasing pH, with the result that all the strains of lactobacilli were unable to grow at pH 5.0.	Glycochenodeoxycholic Acid	44-70	phenylalanine hydroxylase	Homo sapiens	163-165
33246627-5	2021	Additionally, the antimicrobial activity of glycochenodeoxycholic acid was also observed to be pH-dependent, and it was significantly enhanced with the decreasing pH, with the result that all the strains of lactobacilli were unable to grow at pH 5.0.	Glycochenodeoxycholic Acid	44-70	phenylalanine hydroxylase	Homo sapiens	163-165
33246627-6	2021	In conclusion, chemical structure, concentration, and pH are key factors influencing antimicrobial activity of conjugated bile acids against lactobacilli.	Bile Acids and Salts	122-132	phenylalanine hydroxylase	Homo sapiens	54-56
33221423-5	2021	A reduction in time (from 24 to 12 h) and temperature (from 37 to 20 or 4  C) and an increase in pH (from 5.5 to 7) resulted in a decline in antimony mobilization from textiles, while altering textile mass to solution volume and the presence of lactate had little impact on the results.	Lactic Acid	245-252	phenylalanine hydroxylase	Homo sapiens	97-99
33350421-0	2021	Defect-assisted electronic metal-support interactions: tuning the interplay between Ru nanoparticles and CuO supports for pH-neutral oxygen evolution.	Metals	27-32	phenylalanine hydroxylase	Homo sapiens	122-124
33579470-0	2021	Tumor microenvironment responsive VEGF-antibody functionalized pH sensitive liposomes of docetaxel for augmented breast cancer therapy.	Docetaxel	89-98	phenylalanine hydroxylase	Homo sapiens	63-65
33579470-6	2021	The in vitro release study revealed biphasic release pattern of DTX from VEGF-PEG-pH-Lipo-DTX.	Docetaxel	64-67	phenylalanine hydroxylase	Homo sapiens	82-84
33579470-6	2021	The in vitro release study revealed biphasic release pattern of DTX from VEGF-PEG-pH-Lipo-DTX.	Polyethylene Glycols	78-81	phenylalanine hydroxylase	Homo sapiens	82-84
33579470-6	2021	The in vitro release study revealed biphasic release pattern of DTX from VEGF-PEG-pH-Lipo-DTX.	lipo-dtx	85-93	phenylalanine hydroxylase	Homo sapiens	82-84
33579470-8	2021	In case of VEGF-PEG-pH-Lipo-DTX the cellular uptake in MCF-7 cell line was augmented ~3.17-fold as compared to free DTX probably due to the VEGF-positive nature of MCF-7 cell (increased affinity for VEGF).	Docetaxel	28-31	phenylalanine hydroxylase	Homo sapiens	20-22
33579470-9	2021	Further, it was evident from the cytotoxicity assay that VEGF-PEG-pH-Lipo-DTX showed higher cytotoxicity in MCF-7 cells and ~5.78-fold reduction in IC50 value as compared to free DTX.	Docetaxel	74-77	phenylalanine hydroxylase	Homo sapiens	66-68
33579470-10	2021	The apoptotic index observed in case of VEGF-PEG-pH-Lipo-DTX was ~1.70-fold higher than free DTX.	Docetaxel	57-60	phenylalanine hydroxylase	Homo sapiens	49-51
33579470-12	2021	Furthermore, pharmacokinetic profile of VEGF-PEG-pH-Lipo-DTX revealed a ~2.94-fold increase in t1/2 and a ~1.25-fold higher AUC (0  ) as compared to marketed formulation Taxotere .	Docetaxel	170-178	phenylalanine hydroxylase	Homo sapiens	49-51
33579470-14	2021	Finally, treatment with VEGF-PEG-pH-Lipo-DTX demonstrated significant reduction in % tumor burden (~35%) as compared to Taxotere  (~75%).	Docetaxel	120-128	phenylalanine hydroxylase	Homo sapiens	33-35
33584618-0	2021	Antarctic Water Tracks: Microbial Community Responses to Variation in Soil Moisture, pH, and Salinity.	Water	10-15	phenylalanine hydroxylase	Homo sapiens	85-87
33513731-3	2021	Sulfuric acid, citric acid, and acetic acid were used to maintain the pH level, which varied from 5 to 2 for the precipitation process.	sulfuric acid	0-13	phenylalanine hydroxylase	Homo sapiens	70-72
33513731-3	2021	Sulfuric acid, citric acid, and acetic acid were used to maintain the pH level, which varied from 5 to 2 for the precipitation process.	Citric Acid	15-26	phenylalanine hydroxylase	Homo sapiens	70-72
33513731-3	2021	Sulfuric acid, citric acid, and acetic acid were used to maintain the pH level, which varied from 5 to 2 for the precipitation process.	Acetic Acid	32-43	phenylalanine hydroxylase	Homo sapiens	70-72
33513731-5	2021	The finding showed that the lignin isolated using citric acid maintained to pH 3 resulted in briquette with 72% fixed carbon content, excellent 99.7% DSI, and a calorific value equivalent to coal-based briquette.	Lignin	28-34	phenylalanine hydroxylase	Homo sapiens	76-78
33513731-5	2021	The finding showed that the lignin isolated using citric acid maintained to pH 3 resulted in briquette with 72% fixed carbon content, excellent 99.7% DSI, and a calorific value equivalent to coal-based briquette.	Citric Acid	50-61	phenylalanine hydroxylase	Homo sapiens	76-78
33513731-5	2021	The finding showed that the lignin isolated using citric acid maintained to pH 3 resulted in briquette with 72% fixed carbon content, excellent 99.7% DSI, and a calorific value equivalent to coal-based briquette.	Carbon	118-124	phenylalanine hydroxylase	Homo sapiens	76-78
33614016-7	2021	The main ions involved in PH are calcium ion (Ca2+), potassium ion (K+), sodium ion (Na+) and chloride ion (Cl-).	Calcium	33-40	phenylalanine hydroxylase	Homo sapiens	26-28
33614016-7	2021	The main ions involved in PH are calcium ion (Ca2+), potassium ion (K+), sodium ion (Na+) and chloride ion (Cl-).	Potassium	53-62	phenylalanine hydroxylase	Homo sapiens	26-28
33614016-7	2021	The main ions involved in PH are calcium ion (Ca2+), potassium ion (K+), sodium ion (Na+) and chloride ion (Cl-).	Sodium	73-79	phenylalanine hydroxylase	Homo sapiens	26-28
33614016-7	2021	The main ions involved in PH are calcium ion (Ca2+), potassium ion (K+), sodium ion (Na+) and chloride ion (Cl-).	Chlorides	94-102	phenylalanine hydroxylase	Homo sapiens	26-28
33564607-2	2021	The properties of silver nanostructures, such as size, size distribution, and morphology, are strongly dependent on synthesis process conditions such as the process type, equipment type, reagent type, precursor concentration, temperature, process duration, and pH.	Silver	18-24	phenylalanine hydroxylase	Homo sapiens	261-263
33564607-7	2021	Recent studies are then reviewed in detail and the effects of essential reaction parameters, such as temperature, pH, precursor, and reagent concentration, on silver nanostructure size and morphology are discussed.	Silver	159-165	phenylalanine hydroxylase	Homo sapiens	114-116
33628696-1	2021	Metabolic alkalosis is an increase in blood pH to >7.45 due to a primary increase in serum bicarbonate (HCO3 -).	Bicarbonates	91-102	phenylalanine hydroxylase	Homo sapiens	44-46
33628696-1	2021	Metabolic alkalosis is an increase in blood pH to >7.45 due to a primary increase in serum bicarbonate (HCO3 -).	Bicarbonates	104-110	phenylalanine hydroxylase	Homo sapiens	44-46
33207438-2	2021	In the EC process, the electro-dissolution of sacrificial metallic anodes through direct application of current/cell potential dissolves the metals, which precipitate as oxides and hydroxides depending on the electrolyte pH.	as oxides	167-176	phenylalanine hydroxylase	Homo sapiens	221-223
33207438-2	2021	In the EC process, the electro-dissolution of sacrificial metallic anodes through direct application of current/cell potential dissolves the metals, which precipitate as oxides and hydroxides depending on the electrolyte pH.	Hydroxides	181-191	phenylalanine hydroxylase	Homo sapiens	221-223
33564327-1	2021	Light- and pH-responsive nano-assemblies with switchable size and structure are formed by the association of a photoacid, anthocyanidin, and a linear polyelectrolyte in aqueous solution.	Anthocyanins	122-135	phenylalanine hydroxylase	Homo sapiens	11-13
32871296-8	2021	FINDINGS: By reducing pH of a concentrated kaolinite suspension from 8 to 5 and 3, the dispersed kaolinite particles were self-assembled to a well-stacked configuration and card-house structure, respectively.	Kaolin	43-52	phenylalanine hydroxylase	Homo sapiens	22-24
32871296-8	2021	FINDINGS: By reducing pH of a concentrated kaolinite suspension from 8 to 5 and 3, the dispersed kaolinite particles were self-assembled to a well-stacked configuration and card-house structure, respectively.	Kaolin	97-106	phenylalanine hydroxylase	Homo sapiens	22-24
32871296-9	2021	Current study demonstrates that the pH-dependent surface properties of platy kaolinite nanoparticles can be successfully used to understand the macroscopic behavior (rheology) of kaolinite nanoparticle suspensions and design nanostructures of clay products (catalysts and sorbents).	Kaolin	77-86	phenylalanine hydroxylase	Homo sapiens	36-38
32871296-9	2021	Current study demonstrates that the pH-dependent surface properties of platy kaolinite nanoparticles can be successfully used to understand the macroscopic behavior (rheology) of kaolinite nanoparticle suspensions and design nanostructures of clay products (catalysts and sorbents).	Kaolin	179-188	phenylalanine hydroxylase	Homo sapiens	36-38
33162063-3	2021	We explored the risk of PH associated with standard antiplatelet therapy (sAP: acetylsalicylic acid, and/or clopidogrel) in the context of aneurysmal subarachnoid hemorrhage (aSAH).	Aspirin	79-99	phenylalanine hydroxylase	Homo sapiens	24-26
33162063-3	2021	We explored the risk of PH associated with standard antiplatelet therapy (sAP: acetylsalicylic acid, and/or clopidogrel) in the context of aneurysmal subarachnoid hemorrhage (aSAH).	Clopidogrel	108-119	phenylalanine hydroxylase	Homo sapiens	24-26
33167215-5	2021	An iridium oxide film was electrodeposited onto the graphite working electrode providing the pH sensitive layer, while the integrated circuit board allows for data acquisition and storing.	iridium oxide	3-16	phenylalanine hydroxylase	Homo sapiens	93-95
33167215-5	2021	An iridium oxide film was electrodeposited onto the graphite working electrode providing the pH sensitive layer, while the integrated circuit board allows for data acquisition and storing.	Graphite	52-60	phenylalanine hydroxylase	Homo sapiens	93-95
33325709-4	2021	Experiments conducted under varying bias potential, pH, illumination intensity, and scan rate reveal two distinct mechanisms of photoelectrochemical hydrogen production.	Hydrogen	149-157	phenylalanine hydroxylase	Homo sapiens	52-54
33325709-6	2021	At relatively high polarization or pH, the limiting photoactivity shows a linear response to increasing photon flux and is attributed to a mechanism involving reduction of substrate water.	Water	182-187	phenylalanine hydroxylase	Homo sapiens	35-37
33373178-0	2021	In Vivo Regenerable Cerium Oxide Nanozyme-Loaded pH/H2O2-Responsive Nanovesicle for Tumor-Targeted Photothermal and Photodynamic Therapies.	ceric oxide	20-32	phenylalanine hydroxylase	Homo sapiens	49-51
33505976-1	2020	The ability of phagosomes to halt microbial growth is intimately linked to their ability to acidify their luminal pH.	Phenobarbital	106-113	phenylalanine hydroxylase	Homo sapiens	114-116
33313631-3	2021	The resulting hybrid of a metal-organic framework and conjugated polymer featured robust crystalline order that withstood long-term air exposure and broad pH (from 0 to 12) conditions.	Metals	26-31	phenylalanine hydroxylase	Homo sapiens	155-157
33313631-3	2021	The resulting hybrid of a metal-organic framework and conjugated polymer featured robust crystalline order that withstood long-term air exposure and broad pH (from 0 to 12) conditions.	Polymers	65-72	phenylalanine hydroxylase	Homo sapiens	155-157
33215623-0	2021	Lysosome-targeting pH indicator based on peri-fused naphthalene monoimide with superior stability for long term live cell imaging.	naphthalene monoimide	52-73	phenylalanine hydroxylase	Homo sapiens	19-21
33215623-2	2021	Their dysfunction is associated with a number of diseases, which are often related to an altered localization or luminal pH.	Phenobarbital	113-120	phenylalanine hydroxylase	Homo sapiens	121-123
33215623-5	2021	Here, we describe the synthesis and spectroscopic properties of a novel small molecule marker for lysosomes based on naphthalene monoimide with reversible, pH-dependent spectral shifts in both the absorption and the emission spectrum and acidity-associated changes in fluorescence lifetime.	naphthalene monoimide	117-138	phenylalanine hydroxylase	Homo sapiens	156-158
33579470-15	2021	Thus, the combined approach of using PEGylated pH sensitive liposomes along with VEGF antibody functionalization for efficient targeting can improve current standards of DTX therapy for treatment of breast cancer.	Docetaxel	170-173	phenylalanine hydroxylase	Homo sapiens	47-49
33350421-0	2021	Defect-assisted electronic metal-support interactions: tuning the interplay between Ru nanoparticles and CuO supports for pH-neutral oxygen evolution.	Ruthenium	84-86	phenylalanine hydroxylase	Homo sapiens	122-124
33350421-0	2021	Defect-assisted electronic metal-support interactions: tuning the interplay between Ru nanoparticles and CuO supports for pH-neutral oxygen evolution.	Oxygen	133-139	phenylalanine hydroxylase	Homo sapiens	122-124
33401641-0	2021	Selective Extraction of Sinapic Acid Derivatives from Mustard Seed Meal by Acting on pH: Toward a High Antioxidant Activity Rich Extract.	sinapinic acid	24-36	phenylalanine hydroxylase	Homo sapiens	85-87
33325232-0	2021	Molecular Dynamics Simulations of the pH-Dependent Adsorption of Doxorubicin on Carbon Quantum Dots.	Doxorubicin	65-76	phenylalanine hydroxylase	Homo sapiens	38-40
33325232-0	2021	Molecular Dynamics Simulations of the pH-Dependent Adsorption of Doxorubicin on Carbon Quantum Dots.	Carbon	80-86	phenylalanine hydroxylase	Homo sapiens	38-40
33325232-2	2021	Molecular dynamics simulations of loading and release of doxorubicin (DOX) molecules on the CQD surface at pH = 7.4 and pH = 5 were carried out, followed by binding free energy calculations with steered molecular dynamics.	Doxorubicin	70-73	phenylalanine hydroxylase	Homo sapiens	107-109
33325232-3	2021	The results indicate that the CQDs-DOX interaction strength increases with the surface coverage and pH, as well as that the electrostatic interaction between DOX and CQDs plays a significant role in the drug-loading process.	cqds	30-34	phenylalanine hydroxylase	Homo sapiens	100-102
33325232-3	2021	The results indicate that the CQDs-DOX interaction strength increases with the surface coverage and pH, as well as that the electrostatic interaction between DOX and CQDs plays a significant role in the drug-loading process.	Doxorubicin	35-38	phenylalanine hydroxylase	Homo sapiens	100-102
33325232-3	2021	The results indicate that the CQDs-DOX interaction strength increases with the surface coverage and pH, as well as that the electrostatic interaction between DOX and CQDs plays a significant role in the drug-loading process.	Doxorubicin	158-161	phenylalanine hydroxylase	Homo sapiens	100-102
33401641-1	2021	The aim of this paper is to study the effect of the pH on the extraction of sinapic acid and its derivatives from mustard seed meal.	sinapinic acid	76-88	phenylalanine hydroxylase	Homo sapiens	52-54
33401641-3	2021	The maximum extraction yield for sinapic acid (13.22 micromol/g of dry matter (DM)) was obtained with a buffered aqueous solution at pH 12.	sinapinic acid	33-45	phenylalanine hydroxylase	Homo sapiens	133-135
33401641-4	2021	For ethyl sinapate, the maximum extraction yield reached 9.81 micromol/g DM with 70% ethanol/buffered aqueous solution at pH 12.	ethyl 3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate	4-18	phenylalanine hydroxylase	Homo sapiens	122-124
33401641-5	2021	The maximum extraction yield of sinapine (15.73 micromol/g DM) was achieved with 70% ethanol/buffered aqueous solution at pH 2.	sinapine	32-40	phenylalanine hydroxylase	Homo sapiens	122-124
33401641-7	2021	Maximum antioxidant activity was reached at pH 12 with buffer solution (11.37 mg of Trolox Equivalent/g DM), which confirms that sinapic acid-rich fractions exhibit a higher antioxidant activity.	sinapinic acid	129-141	phenylalanine hydroxylase	Homo sapiens	44-46
33390524-0	2021	Development of Novel Bead Milling Technology with Less Metal Contamination by pH Optimization of the Suspension Medium.	Metals	55-60	phenylalanine hydroxylase	Homo sapiens	78-80
33297218-7	2021	The use of biochar results in a decrease (i.e. up to 20%) of the PAH degradation during bioaugmentation and phytoremediation of sediments, as a consequence of the reduction of PAH bioavailability and an increase of water and nutrient retention.	Water	215-220	phenylalanine hydroxylase	Homo sapiens	65-68
33297218-8	2021	In contrast, PAH degradation has been reported to increase up to 54% when nitrate is used as electron acceptor in low-temperature biochar-amended sediments.	Nitrates	74-81	phenylalanine hydroxylase	Homo sapiens	13-16
33390524-5	2021	Among the various pH values tested, the metal contamination generated during the grinding process could be significantly reduced in the optimized pH range without significant differences in the particle size of the phenytoin suspension after pulverization.	Metals	40-45	phenylalanine hydroxylase	Homo sapiens	18-20
33390524-5	2021	Among the various pH values tested, the metal contamination generated during the grinding process could be significantly reduced in the optimized pH range without significant differences in the particle size of the phenytoin suspension after pulverization.	Metals	40-45	phenylalanine hydroxylase	Homo sapiens	146-148
33249568-7	2021	A characteristic U-shaped solubility curve observed within pH 2.0 to 8.0 at low ionic strengths (I < 0.01) was altered by increasing the salt concentration.	Salts	137-141	phenylalanine hydroxylase	Homo sapiens	59-61
32820436-4	2021	PAH contamination was observed slightly lower in the summer season from the pollution characteristics of water bodies in most areas of the Baiyangdian Lake, and the levels of PAH pollution in the water body of urban residential regions and rural residential regions were relatively higher than those in tourist regions and low human disturbance regions.	Water	105-110	phenylalanine hydroxylase	Homo sapiens	0-3
32820436-4	2021	PAH contamination was observed slightly lower in the summer season from the pollution characteristics of water bodies in most areas of the Baiyangdian Lake, and the levels of PAH pollution in the water body of urban residential regions and rural residential regions were relatively higher than those in tourist regions and low human disturbance regions.	Water	196-201	phenylalanine hydroxylase	Homo sapiens	175-178
33296998-6	2021	Results showed that when pH was adjusted in the range of 2.5 to 2 by HCl (1.2 M), Microcystis unicells aggregated to form flocs as large as 28 mum, which are easy to remove by filtration or sedimentation.	Hydrochloric Acid	69-72	phenylalanine hydroxylase	Homo sapiens	25-27
33296998-8	2021	Thus, pH regulation is an environment-friendly and cost-effective method to remove Microcystis unicells, which can be potentially applied to water treatment.	Water	141-146	phenylalanine hydroxylase	Homo sapiens	6-8
33063214-8	2021	During these processes, key factors are multi-metallic components, metal doping, temperature, and pH.	Metals	46-51	phenylalanine hydroxylase	Homo sapiens	98-100
33152365-3	2021	Batch adsorption experiments were carried out as pH function, and the highest adsorption capacities and removal percentages were, respectively, 216 mg g-1 and 65% for chitosan beads at pH 8, and 126.4 mg g-1 and 38% for alginate beads at pH 4.	Chitosan	167-175	phenylalanine hydroxylase	Homo sapiens	49-51
33152365-3	2021	Batch adsorption experiments were carried out as pH function, and the highest adsorption capacities and removal percentages were, respectively, 216 mg g-1 and 65% for chitosan beads at pH 8, and 126.4 mg g-1 and 38% for alginate beads at pH 4.	Chitosan	167-175	phenylalanine hydroxylase	Homo sapiens	185-187
33152365-3	2021	Batch adsorption experiments were carried out as pH function, and the highest adsorption capacities and removal percentages were, respectively, 216 mg g-1 and 65% for chitosan beads at pH 8, and 126.4 mg g-1 and 38% for alginate beads at pH 4.	Chitosan	167-175	phenylalanine hydroxylase	Homo sapiens	185-187
33249568-11	2021	This study highlights the relationship between ionic strength of the two salts and oat protein solubility at different pH levels, providing useful information for selecting proper salt concentrations in the manufacture of oat protein-based food products.	Salts	73-78	phenylalanine hydroxylase	Homo sapiens	119-121
33335340-2	2020	Here, we investigate how the pH and temperature responses of the rheology of hyaluronan hydrogels are connected to the underlying molecular interactions.	Hyaluronic Acid	77-87	phenylalanine hydroxylase	Homo sapiens	29-31
33375644-1	2020	Phenylketonuria (PKU) is a common inborn error of amino acid metabolism in which the enzyme phenylalanine hydroxylase, which converts phenylalanine to tyrosine, is functionally impaired due to pathogenic variants in the PAH gene.	Tyrosine	151-159	phenylalanine hydroxylase	Homo sapiens	92-117
33206746-1	2020	New amphiphilic carbosilane dendrons with pH-dependent behaviour based on the presence of carboxylate (propionate or succinate) groups at their peripheries and a fatty acid at the focal point were developed.	carboxylate	90-101	phenylalanine hydroxylase	Homo sapiens	42-44
33206746-1	2020	New amphiphilic carbosilane dendrons with pH-dependent behaviour based on the presence of carboxylate (propionate or succinate) groups at their peripheries and a fatty acid at the focal point were developed.	Propionates	103-113	phenylalanine hydroxylase	Homo sapiens	42-44
33206746-1	2020	New amphiphilic carbosilane dendrons with pH-dependent behaviour based on the presence of carboxylate (propionate or succinate) groups at their peripheries and a fatty acid at the focal point were developed.	Succinic Acid	117-126	phenylalanine hydroxylase	Homo sapiens	42-44
33206746-1	2020	New amphiphilic carbosilane dendrons with pH-dependent behaviour based on the presence of carboxylate (propionate or succinate) groups at their peripheries and a fatty acid at the focal point were developed.	Fatty Acids	162-172	phenylalanine hydroxylase	Homo sapiens	42-44
33206746-5	2020	No significant differences were found for the propionate and succinate based dendron micelles at basic or acidic pH, but the succinate dendron assemblies were more stable at neutral pH.	Succinic Acid	125-134	phenylalanine hydroxylase	Homo sapiens	182-184
33336311-3	2020	Hypo/hypercapnia, as well as mechanical ventilation during and after resuscitation, can affect CO2 levels and trigger a dangerous pathophysiological vicious circle related to the relationship between pH, cellular demand, and catecholamine levels.	Carbon Dioxide	95-98	phenylalanine hydroxylase	Homo sapiens	200-202
33336311-3	2020	Hypo/hypercapnia, as well as mechanical ventilation during and after resuscitation, can affect CO2 levels and trigger a dangerous pathophysiological vicious circle related to the relationship between pH, cellular demand, and catecholamine levels.	Catecholamines	225-238	phenylalanine hydroxylase	Homo sapiens	200-202
33336311-5	2020	The aim of this review was to describe the pathophysiology and clinical consequences of arterial blood gases and pH after cardiac arrest.According to our findings, the optimal ventilator strategies in post cardiac arrest patients are not fully understood, and oxygen and carbon dioxide targets should take in consideration a complex pattern of pathophysiological factors.	Oxygen	260-266	phenylalanine hydroxylase	Homo sapiens	113-115
32979721-0	2020	Granular activated carbon-supported titanium dioxide nanoparticles as an amendment for amending copper-contaminated sediments: Effect on the pH in sediments and enzymatic activities.	Carbon	19-25	phenylalanine hydroxylase	Homo sapiens	141-143
32979721-0	2020	Granular activated carbon-supported titanium dioxide nanoparticles as an amendment for amending copper-contaminated sediments: Effect on the pH in sediments and enzymatic activities.	titanium dioxide	36-52	phenylalanine hydroxylase	Homo sapiens	141-143
33376867-4	2020	The peroxone process had 75-88.5% chemical oxygen demand (COD) reduction efficiency at pH 5-11 in 3 h. Adsorption by activated char further reduced the COD to 85.4-92.7% for pH 5-11 in 2.5 h. All other water quality parameters were significantly decreased (>73% removal) during ozonation.	Water	202-207	phenylalanine hydroxylase	Homo sapiens	174-176
33237716-0	2020	On the Origin of the Effect of pH in Oxygen Reduction Reaction for Nondoped and Edge-Type Quaternary N-Doped Metal-Free Carbon-Based Catalysts.	Oxygen	37-43	phenylalanine hydroxylase	Homo sapiens	31-33
33237716-0	2020	On the Origin of the Effect of pH in Oxygen Reduction Reaction for Nondoped and Edge-Type Quaternary N-Doped Metal-Free Carbon-Based Catalysts.	Metals	109-114	phenylalanine hydroxylase	Homo sapiens	31-33
33237716-0	2020	On the Origin of the Effect of pH in Oxygen Reduction Reaction for Nondoped and Edge-Type Quaternary N-Doped Metal-Free Carbon-Based Catalysts.	Carbon	120-126	phenylalanine hydroxylase	Homo sapiens	31-33
33237716-6	2020	We address this matter through a combined experimental and modeling study, which yields fundamental principles on the origin of the pH effects in ORR for carbon-based materials.	Carbon	154-160	phenylalanine hydroxylase	Homo sapiens	132-134
33237716-7	2020	This is relevant for the design of pH-independent metal-free carbon-based catalysts.	Metals	50-55	phenylalanine hydroxylase	Homo sapiens	35-37
33237716-7	2020	This is relevant for the design of pH-independent metal-free carbon-based catalysts.	Carbon	61-67	phenylalanine hydroxylase	Homo sapiens	35-37
33335340-4	2020	Using two-dimensional infrared spectroscopy, we show that hyaluronan chains become connected by hydrogen bonds when the pH is changed from 7.0 to 2.5 and that the bond density at pH 2.5 is independent of temperature.	Hyaluronic Acid	58-68	phenylalanine hydroxylase	Homo sapiens	120-122
33335340-4	2020	Using two-dimensional infrared spectroscopy, we show that hyaluronan chains become connected by hydrogen bonds when the pH is changed from 7.0 to 2.5 and that the bond density at pH 2.5 is independent of temperature.	Hydrogen	96-104	phenylalanine hydroxylase	Homo sapiens	120-122
33335340-5	2020	Temperature-dependent rheology measurements show that because of this hydrogen bonding the stress relaxation at pH 2.5 is strongly slowed down in comparison to pH 7.0, consistent with the sticky reptation model of associative polymers.	Hydrogen	70-78	phenylalanine hydroxylase	Homo sapiens	112-114
33335340-5	2020	Temperature-dependent rheology measurements show that because of this hydrogen bonding the stress relaxation at pH 2.5 is strongly slowed down in comparison to pH 7.0, consistent with the sticky reptation model of associative polymers.	Hydrogen	70-78	phenylalanine hydroxylase	Homo sapiens	160-162
32949982-8	2020	The modeling of the contaminants of concern mobility, namely pH and concentrations of sulfate, uranium and 226Ra, is based on several key complementary mechanisms: density flow, cation exchange with clay minerals and co-precipitation of 226Ra in the barite.	Radium-226	237-242	phenylalanine hydroxylase	Homo sapiens	61-63
33287208-0	2020	Fluorescein Derivatives as Fluorescent Probes for pH Monitoring along Recent Biological Applications.	Fluorescein	0-11	phenylalanine hydroxylase	Homo sapiens	50-52
33287208-1	2020	Potential of hydrogen (pH) is one of the most relevant parameters characterizing aqueous solutions.	Hydrogen	13-21	phenylalanine hydroxylase	Homo sapiens	23-25
33287208-6	2020	One of the most notorious pH-sensitive probes is fluorescein.	Fluorescein	49-60	phenylalanine hydroxylase	Homo sapiens	26-28
33287208-8	2020	This review intends to shed new light on the recent use of fluorescein as pH-sensitive probes for biological applications, including targeted probes for specific imaging, flexible monitoring of bacterial growth, and biomedical applications.	Fluorescein	59-70	phenylalanine hydroxylase	Homo sapiens	74-76
33161754-4	2020	For suspicious samples, the genotypes of the PAH gene were amplified by biotin labeled oligonucleotide primers.	Biotin	72-78	phenylalanine hydroxylase	Homo sapiens	45-48
33140638-0	2020	Voltammetric pH Measurements in Unadulterated Foodstuffs, Urine, and Serum with 3D-Printed Graphene/Poly(Lactic Acid) Electrodes.	Graphite	91-99	phenylalanine hydroxylase	Homo sapiens	13-15
33251361-6	2020	The swelling of the polymer composite beads was found to be maximum at pH of 5.6 when compared to that of pH conditions, 7 and 8.5.	Polymers	20-27	phenylalanine hydroxylase	Homo sapiens	71-73
33251361-6	2020	The swelling of the polymer composite beads was found to be maximum at pH of 5.6 when compared to that of pH conditions, 7 and 8.5.	Polymers	20-27	phenylalanine hydroxylase	Homo sapiens	106-108
33187224-6	2020	Furthermore, we report the ability of chondroitin sulphate C to bind EDIII and induce higher-order dynamic molecular changes at the tertiary and quaternary structure levels which are dependent on pH, GAG species, and the GAG sulphation state.	Chondroitin Sulfates	38-58	phenylalanine hydroxylase	Homo sapiens	196-198
32996541-0	2020	pH-Responsive aggregates transition from spherical micelles to WLMs induced by hydrotropes based on the dynamic imine bond.	Imines	112-117	phenylalanine hydroxylase	Homo sapiens	0-2
32996541-3	2020	In this study, a novel pH-responsive worm-like micelle system was constructed by mixing cetyltrimethylammonium bromide (CTAB), 4-hydroxybenzaldehyde (HB) and p-toluidine (MB) at the molar ratio of 60 mM : 40 mM : 40 mM.	Cetrimonium	88-118	phenylalanine hydroxylase	Homo sapiens	23-25
32996541-3	2020	In this study, a novel pH-responsive worm-like micelle system was constructed by mixing cetyltrimethylammonium bromide (CTAB), 4-hydroxybenzaldehyde (HB) and p-toluidine (MB) at the molar ratio of 60 mM : 40 mM : 40 mM.	Cetrimonium	120-124	phenylalanine hydroxylase	Homo sapiens	23-25
32996541-3	2020	In this study, a novel pH-responsive worm-like micelle system was constructed by mixing cetyltrimethylammonium bromide (CTAB), 4-hydroxybenzaldehyde (HB) and p-toluidine (MB) at the molar ratio of 60 mM : 40 mM : 40 mM.	4-hydroxybenzaldehyde	127-148	phenylalanine hydroxylase	Homo sapiens	23-25
32996541-3	2020	In this study, a novel pH-responsive worm-like micelle system was constructed by mixing cetyltrimethylammonium bromide (CTAB), 4-hydroxybenzaldehyde (HB) and p-toluidine (MB) at the molar ratio of 60 mM : 40 mM : 40 mM.	4-hydroxybenzaldehyde	150-152	phenylalanine hydroxylase	Homo sapiens	23-25
32996541-3	2020	In this study, a novel pH-responsive worm-like micelle system was constructed by mixing cetyltrimethylammonium bromide (CTAB), 4-hydroxybenzaldehyde (HB) and p-toluidine (MB) at the molar ratio of 60 mM : 40 mM : 40 mM.	4-toluidine	158-169	phenylalanine hydroxylase	Homo sapiens	23-25
32996541-3	2020	In this study, a novel pH-responsive worm-like micelle system was constructed by mixing cetyltrimethylammonium bromide (CTAB), 4-hydroxybenzaldehyde (HB) and p-toluidine (MB) at the molar ratio of 60 mM : 40 mM : 40 mM.	Methylene Blue	171-173	phenylalanine hydroxylase	Homo sapiens	23-25
33135229-3	2020	Arsenic retention can be affected by changes in soil pH and the presence of competing anions, like phosphate.	Arsenic	0-7	phenylalanine hydroxylase	Homo sapiens	53-55
33135229-5	2020	The efficiency of InsP6 in displacing adsorbed As(III) decreased with increasing pH values and interaction time, which may be attributed to the increase in bonding strength of the As(III) complexes on the surface of goethite.	as(iii)	47-54	phenylalanine hydroxylase	Homo sapiens	81-83
33135229-6	2020	Adsorption and retention of As(V) by goethite generally decreased with increasing pH, particularly in the presence of InsP6 due to the similar pKa values and the competition for the same binding sites.	asunaprevir	28-33	phenylalanine hydroxylase	Homo sapiens	82-84
33135229-6	2020	Adsorption and retention of As(V) by goethite generally decreased with increasing pH, particularly in the presence of InsP6 due to the similar pKa values and the competition for the same binding sites.	goethite	37-45	phenylalanine hydroxylase	Homo sapiens	82-84
33423362-1	2021	IMPORTANCE: Sapropterin hydrochloride, a natural coenzyme (6R-tetrahydrobiopterin) of phenylalanine hydroxylase, was first approved as a treatment for tetrahydrobiopterin deficiency in 1992 in Japan, and was then approved as a treatment for a tetrahydrobiopterin-responsive hyperphenylalaninemia in 2007 and 2008, in the USA and Japan, respectively.	sapropterin	12-37	phenylalanine hydroxylase	Homo sapiens	86-111
33423362-1	2021	IMPORTANCE: Sapropterin hydrochloride, a natural coenzyme (6R-tetrahydrobiopterin) of phenylalanine hydroxylase, was first approved as a treatment for tetrahydrobiopterin deficiency in 1992 in Japan, and was then approved as a treatment for a tetrahydrobiopterin-responsive hyperphenylalaninemia in 2007 and 2008, in the USA and Japan, respectively.	(6r-tetrahydrobiopterin	58-81	phenylalanine hydroxylase	Homo sapiens	86-111
33423362-1	2021	IMPORTANCE: Sapropterin hydrochloride, a natural coenzyme (6R-tetrahydrobiopterin) of phenylalanine hydroxylase, was first approved as a treatment for tetrahydrobiopterin deficiency in 1992 in Japan, and was then approved as a treatment for a tetrahydrobiopterin-responsive hyperphenylalaninemia in 2007 and 2008, in the USA and Japan, respectively.	sapropterin	62-81	phenylalanine hydroxylase	Homo sapiens	86-111
33423362-1	2021	IMPORTANCE: Sapropterin hydrochloride, a natural coenzyme (6R-tetrahydrobiopterin) of phenylalanine hydroxylase, was first approved as a treatment for tetrahydrobiopterin deficiency in 1992 in Japan, and was then approved as a treatment for a tetrahydrobiopterin-responsive hyperphenylalaninemia in 2007 and 2008, in the USA and Japan, respectively.	sapropterin	151-170	phenylalanine hydroxylase	Homo sapiens	86-111
33397057-8	2020	Potassium citrate treatment caused a significant increase in urine pH levels (p<0.001).	Potassium Citrate	0-17	phenylalanine hydroxylase	Homo sapiens	67-69
33080489-4	2020	Pimobendan administration improved right ventricular (RV) function and lowered pulmonary arterial pressure in some human patients with precapillary PH.	pimobendan	0-10	phenylalanine hydroxylase	Homo sapiens	148-150
33260659-2	2020	Amongst a variety of parameters such as level (or depth), temperature, conductivity, turbidity, and pH, the water level is the most fundamental one that needs to be monitored on a real-time basis for securing the water management system.	Water	108-113	phenylalanine hydroxylase	Homo sapiens	100-102
33260674-2	2020	Alterations in the level of PAH leads to the toxic accumulation of phenylalanine in the blood and brain.	Phenylalanine	67-80	phenylalanine hydroxylase	Homo sapiens	28-31
33185198-0	2020	Molecular level picture of the interplay between pH and phosphate binding at the goethite-water interface.	Water	90-95	phenylalanine hydroxylase	Homo sapiens	49-51
33185198-1	2020	The soil pH plays a substantial role in controlling phosphorus (P) adsorption and mobilization.	Phosphorus	52-62	phenylalanine hydroxylase	Homo sapiens	9-11
33185198-1	2020	The soil pH plays a substantial role in controlling phosphorus (P) adsorption and mobilization.	Phosphorus	64-66	phenylalanine hydroxylase	Homo sapiens	9-11
33185198-3	2020	The target of the current contribution is to draw a molecular level picture of the interplay between pH and phosphate binding at the goethite-water interface via a joint experimental-theoretical approach.	Water	142-147	phenylalanine hydroxylase	Homo sapiens	101-103
33185198-4	2020	Periodic density functional theory (DFT) calculations were carried out to provide a molecular level understanding of the pH dependence of P adsorption.	Phosphorus	0-1	phenylalanine hydroxylase	Homo sapiens	121-123
33185198-13	2020	Furthermore, the results point to a decrease of pH upon phosphate sorption due to an induced acidification of soil solution.	Phosphates	56-65	phenylalanine hydroxylase	Homo sapiens	48-50
33170718-0	2020	Tuning the Photothermal Effect of Carboxylated-Coated Silver Nanoparticles through pH-Induced Reversible Aggregation.	Silver	54-60	phenylalanine hydroxylase	Homo sapiens	83-85
33170718-1	2020	The photothermal response of mercaptoundecanoic acid (MUA)-coated Ag nanoparticles (Ag@MUA NPs) in both aqueous dispersions and paper substrates was determined as a function of pH when irradiated with a green laser or a blue LED source.	mercaptoundecanoic acid	29-52	phenylalanine hydroxylase	Homo sapiens	177-179
33170718-3	2020	Aggregation was induced by changing the pH across the apparent pKa of the acid, higher than the pKa of the free acid.	streptolydigin	107-116	phenylalanine hydroxylase	Homo sapiens	40-42
33581706-1	2020	OBJECTIVES: Phenylalanine (Phe) hydroxylase (PAH) deficiency leads to hyperphenylalaninemia (HPA) and tyrosine (Tyr) depletion.	Tyrosine	102-110	phenylalanine hydroxylase	Homo sapiens	12-43
33581706-1	2020	OBJECTIVES: Phenylalanine (Phe) hydroxylase (PAH) deficiency leads to hyperphenylalaninemia (HPA) and tyrosine (Tyr) depletion.	Tyrosine	112-115	phenylalanine hydroxylase	Homo sapiens	12-43
33140638-0	2020	Voltammetric pH Measurements in Unadulterated Foodstuffs, Urine, and Serum with 3D-Printed Graphene/Poly(Lactic Acid) Electrodes.	poly(lactide)	100-117	phenylalanine hydroxylase	Homo sapiens	13-15
33140638-4	2020	In this work, we describe a voltammetric pH sensor that uses a three-dimensional (3D)-printed graphene/poly(lactic acid) filament electrode that is pretreated to introduce quinone functional groups to the graphene surface.	Graphite	94-102	phenylalanine hydroxylase	Homo sapiens	41-43
33140638-4	2020	In this work, we describe a voltammetric pH sensor that uses a three-dimensional (3D)-printed graphene/poly(lactic acid) filament electrode that is pretreated to introduce quinone functional groups to the graphene surface.	poly(lactide)	103-120	phenylalanine hydroxylase	Homo sapiens	41-43
33140638-4	2020	In this work, we describe a voltammetric pH sensor that uses a three-dimensional (3D)-printed graphene/poly(lactic acid) filament electrode that is pretreated to introduce quinone functional groups to the graphene surface.	quinone	172-179	phenylalanine hydroxylase	Homo sapiens	41-43
33140638-4	2020	In this work, we describe a voltammetric pH sensor that uses a three-dimensional (3D)-printed graphene/poly(lactic acid) filament electrode that is pretreated to introduce quinone functional groups to the graphene surface.	Graphite	205-213	phenylalanine hydroxylase	Homo sapiens	41-43
33140638-5	2020	After thoroughly characterizing the pretreatment parameters using outer-sphere and inner-sphere redox couples, we measured pH by reducing the surface-bound quinones, which undergo a pH-dependent 2e-/2H+ reduction.	Quinones	156-164	phenylalanine hydroxylase	Homo sapiens	123-125
33140638-5	2020	After thoroughly characterizing the pretreatment parameters using outer-sphere and inner-sphere redox couples, we measured pH by reducing the surface-bound quinones, which undergo a pH-dependent 2e-/2H+ reduction.	Quinones	156-164	phenylalanine hydroxylase	Homo sapiens	182-184
33140638-5	2020	After thoroughly characterizing the pretreatment parameters using outer-sphere and inner-sphere redox couples, we measured pH by reducing the surface-bound quinones, which undergo a pH-dependent 2e-/2H+ reduction.	2e	195-197	phenylalanine hydroxylase	Homo sapiens	123-125
33140638-5	2020	After thoroughly characterizing the pretreatment parameters using outer-sphere and inner-sphere redox couples, we measured pH by reducing the surface-bound quinones, which undergo a pH-dependent 2e-/2H+ reduction.	2e	195-197	phenylalanine hydroxylase	Homo sapiens	182-184
33140638-5	2020	After thoroughly characterizing the pretreatment parameters using outer-sphere and inner-sphere redox couples, we measured pH by reducing the surface-bound quinones, which undergo a pH-dependent 2e-/2H+ reduction.	Deuterium	199-201	phenylalanine hydroxylase	Homo sapiens	123-125
33140638-5	2020	After thoroughly characterizing the pretreatment parameters using outer-sphere and inner-sphere redox couples, we measured pH by reducing the surface-bound quinones, which undergo a pH-dependent 2e-/2H+ reduction.	Deuterium	199-201	phenylalanine hydroxylase	Homo sapiens	182-184
33187145-7	2020	The variation of pH is correlated to the increase of lignan molecules in the extracted samples.	Lignans	53-59	phenylalanine hydroxylase	Homo sapiens	17-19
33167490-10	2020	When analyzing the technical condition of concrete treated with urea, pH could be an indicator due to the possibility of buffer reactions.	Urea	64-68	phenylalanine hydroxylase	Homo sapiens	70-72
33158221-0	2020	Influence of Buffers, Ionic Strength, and pH on the Volume Phase Transition Behavior of Acrylamide-Based Nanogels.	Acrylamide	88-98	phenylalanine hydroxylase	Homo sapiens	42-44
32949982-10	2020	Similarly, the changes in pH and 226Ra concentration are only correctly predicted when the cationic exchanges with the clays and the co-precipitation reaction within the barite using the solid solution theory are integrated into the models.	Barium Sulfate	170-176	phenylalanine hydroxylase	Homo sapiens	26-28
33080006-0	2020	Allogeneic transplantation for Ph+ acute lymphoblastic leukemia with posttransplantation cyclophosphamide.	Cyclophosphamide	89-105	phenylalanine hydroxylase	Homo sapiens	31-33
33101986-1	2020	Introduction: Phenylketonuria (PKU) is an inborn error of metabolism characterized by pathogenic variants of the phenylalanine hydroxylase (PAH) gene with a resulting accumulation of phenylalanine (Phe) to neurotoxic levels.	Phenylalanine	113-126	phenylalanine hydroxylase	Homo sapiens	140-143
33312658-4	2020	The results of 2,4DNP removal by high-performance liquid chromatography method at the wavelength of 360 nm in a batch mode were obtained by changing the influential factors including contact time, pH, initial concentration of the contaminant, and adsorbent dosage.	2,4-Dinitrophenol	15-21	phenylalanine hydroxylase	Homo sapiens	197-199
33312658-6	2020	In this research, the optimal time was obtained as 60 min and pH as seven for all three adsorbents.	adsorbents	88-98	phenylalanine hydroxylase	Homo sapiens	62-64
33312658-11	2020	At high pH, hydroxide ions (OH) compete with 2,4 DNP molecules for the adsorption sites.	hydroxide ion	12-21	phenylalanine hydroxylase	Homo sapiens	8-10
33312658-11	2020	At high pH, hydroxide ions (OH) compete with 2,4 DNP molecules for the adsorption sites.	2,4 dnp	45-52	phenylalanine hydroxylase	Homo sapiens	8-10
33091174-1	2021	BACKGROUND: Limited data are available on the effects of fermentable fiber in altering intestinal pH and transit to predict efficacy-based delivery profiles of pH-dependent mesalamine coatings in ulcerative colitis (UC).	Mesalamine	173-183	phenylalanine hydroxylase	Homo sapiens	160-162
33091174-11	2021	These have potentially detrimental effects on predicted luminal release patterns of pH-dependent 5-aminosalicylic acid release systems.	Phenobarbital	56-63	phenylalanine hydroxylase	Homo sapiens	84-86
33091174-11	2021	These have potentially detrimental effects on predicted luminal release patterns of pH-dependent 5-aminosalicylic acid release systems.	Mesalamine	97-118	phenylalanine hydroxylase	Homo sapiens	84-86
33101986-1	2020	Introduction: Phenylketonuria (PKU) is an inborn error of metabolism characterized by pathogenic variants of the phenylalanine hydroxylase (PAH) gene with a resulting accumulation of phenylalanine (Phe) to neurotoxic levels.	Phenylalanine	14-17	phenylalanine hydroxylase	Homo sapiens	113-138
33101986-1	2020	Introduction: Phenylketonuria (PKU) is an inborn error of metabolism characterized by pathogenic variants of the phenylalanine hydroxylase (PAH) gene with a resulting accumulation of phenylalanine (Phe) to neurotoxic levels.	Phenylalanine	14-17	phenylalanine hydroxylase	Homo sapiens	140-143
33070288-0	2020	Physiologically Based Pharmacokinetic Modeling of Oral Absorption, pH, and Food Effect in Healthy Volunteers to Drive Alpelisib Formulation Selection.	Alpelisib	118-127	phenylalanine hydroxylase	Homo sapiens	67-69
33022178-0	2020	A pH-Sensing Fluorescent Metal-Organic Framework: pH-Triggered Fluorescence Transition and Detection of Mycotoxin.	Metals	25-30	phenylalanine hydroxylase	Homo sapiens	2-4
33022178-0	2020	A pH-Sensing Fluorescent Metal-Organic Framework: pH-Triggered Fluorescence Transition and Detection of Mycotoxin.	Metals	25-30	phenylalanine hydroxylase	Homo sapiens	50-52
33022178-4	2020	Because the steric hindrance in the ligand prevents metal coordination with the pyridyl group, the MOF features free basic N sites accessible to the small H+ ions, which renders pH responsivity.	Metals	52-57	phenylalanine hydroxylase	Homo sapiens	178-180
33022178-9	2020	Moreover, by virtue of the pH-responsive fluorescence, the MOF shows appealing sensing performance for the detection of 3-nitropropionic acid, a major mycotoxin in moldy sugar cane.	3-nitropropionic acid	120-141	phenylalanine hydroxylase	Homo sapiens	27-29
33070288-7	2020	Ranitidine showed a significant pH-mediated DDI effect only in the fasted but not fed state.	Ranitidine	0-10	phenylalanine hydroxylase	Homo sapiens	32-34
33070288-14	2020	The alpelisib model for healthy subjects enables future bioequivalence formulation assessments, in fasted, fed, or altered pH conditions.	Alpelisib	4-13	phenylalanine hydroxylase	Homo sapiens	123-125
32937072-0	2020	Reductive Cleavage of the CO Molecule by a Reactive Vicinal Frustrated PH/BH Lewis Pair.	vicinal	52-59	phenylalanine hydroxylase	Homo sapiens	71-73
32937072-1	2020	An intramolecular ethylene-bridged PH/BH system, isolated as a dimer, reduces carbon monoxide to the -CH2-O- state.	ethylene	18-26	phenylalanine hydroxylase	Homo sapiens	35-37
32937072-1	2020	An intramolecular ethylene-bridged PH/BH system, isolated as a dimer, reduces carbon monoxide to the -CH2-O- state.	Carbon Monoxide	78-93	phenylalanine hydroxylase	Homo sapiens	35-37
32937072-2	2020	In the presence of B(C6F5)3 the frustrated PH/BH Lewis pair reacts with carbon monoxide to give the product of reductive coupling of two CO molecules at the template.	tris(pentafluorophenyl)borane	19-27	phenylalanine hydroxylase	Homo sapiens	43-45
32937072-2	2020	In the presence of B(C6F5)3 the frustrated PH/BH Lewis pair reacts with carbon monoxide to give the product of reductive coupling of two CO molecules at the template.	Carbon Monoxide	72-87	phenylalanine hydroxylase	Homo sapiens	43-45
33053708-2	2020	In this study, Azure A-modified poly(methacrylic acid) (AA-PMA) was synthesized used to prepare a layer-by-layer deposited film with poly(allylamine hydrochloride) (PAH) on a glassy carbon electrode via electrostatic interactions and the multilayer film-immobilized electrode was used to measure pH.	polymethacrylic acid	32-54	phenylalanine hydroxylase	Homo sapiens	296-298
33053708-2	2020	In this study, Azure A-modified poly(methacrylic acid) (AA-PMA) was synthesized used to prepare a layer-by-layer deposited film with poly(allylamine hydrochloride) (PAH) on a glassy carbon electrode via electrostatic interactions and the multilayer film-immobilized electrode was used to measure pH.	aa-pma	56-62	phenylalanine hydroxylase	Homo sapiens	296-298
33053708-2	2020	In this study, Azure A-modified poly(methacrylic acid) (AA-PMA) was synthesized used to prepare a layer-by-layer deposited film with poly(allylamine hydrochloride) (PAH) on a glassy carbon electrode via electrostatic interactions and the multilayer film-immobilized electrode was used to measure pH.	polyallylamine	165-168	phenylalanine hydroxylase	Homo sapiens	296-298
32901638-3	2020	For diblock weak polyampholytes grafted by their acidic blocks, we find that the acidic monomers increase their charge while the basic monomers decrease their charge with decreasing salt concentration for pH values less than the pKa value of both monomers and vice versa when the pH > pKa.	Salts	182-186	phenylalanine hydroxylase	Homo sapiens	205-207
32901638-3	2020	For diblock weak polyampholytes grafted by their acidic blocks, we find that the acidic monomers increase their charge while the basic monomers decrease their charge with decreasing salt concentration for pH values less than the pKa value of both monomers and vice versa when the pH > pKa.	Salts	182-186	phenylalanine hydroxylase	Homo sapiens	280-282
32901638-6	2020	In the case of poor solvent conditions to the basic block (the top block), we find lateral segregation of basic monomers into micelles, forming a two-dimensional hexagonal pattern on the surface at intermediate and high pH values for monovalent salt concentrations from 0.01 to 0.1 M. When the solvent is poor to both blocks, we find lateral segregation of the grafted acidic block into lamellae with longitudinal undulations of low and high acidic monomer density.	Salts	245-249	phenylalanine hydroxylase	Homo sapiens	220-222
32921661-1	2020	Diazoxide, a drug used to treat hyperinsulinemic hypoglycemia (HH), is associated with pulmonary hypertension (PH), as reported by the US Food and Drug Administration.	Diazoxide	0-9	phenylalanine hydroxylase	Homo sapiens	111-113
33143151-0	2020	Soft Template Electropolymerization of Polypyrrole for Improved pH-Induced Drug Delivery.	polypyrrole	39-50	phenylalanine hydroxylase	Homo sapiens	64-66
33143151-6	2020	Fluorescein release was measured using UV spectroscopy over a pH range of 2 to 11, showing increased release at higher pH values.	Fluorescein	0-11	phenylalanine hydroxylase	Homo sapiens	62-64
33143151-6	2020	Fluorescein release was measured using UV spectroscopy over a pH range of 2 to 11, showing increased release at higher pH values.	Fluorescein	0-11	phenylalanine hydroxylase	Homo sapiens	119-121
32960575-2	2020	Here we report the reactivity of selected nitro substrates RNO2 (R = Me, Ph, p-C6H4CHO) with pyrazolate-based dinickel(II) dihydride complexes [ML(NiH)2] (M = Na, K); the latter eliminate H2 upon substrate binding and serve as a masked dinickel(I) platform.	nitro	42-47	phenylalanine hydroxylase	Homo sapiens	73-75
32960575-2	2020	Here we report the reactivity of selected nitro substrates RNO2 (R = Me, Ph, p-C6H4CHO) with pyrazolate-based dinickel(II) dihydride complexes [ML(NiH)2] (M = Na, K); the latter eliminate H2 upon substrate binding and serve as a masked dinickel(I) platform.	pyrazolate-based dinickel	93-118	phenylalanine hydroxylase	Homo sapiens	73-75
32960575-2	2020	Here we report the reactivity of selected nitro substrates RNO2 (R = Me, Ph, p-C6H4CHO) with pyrazolate-based dinickel(II) dihydride complexes [ML(NiH)2] (M = Na, K); the latter eliminate H2 upon substrate binding and serve as a masked dinickel(I) platform.	(ii) dihydride	118-132	phenylalanine hydroxylase	Homo sapiens	73-75
32442796-0	2020	Synthesis of trans-dihydronaphthalene-diols and evaluation of their use as standards for PAH metabolite analysis in fish bile by GC-MS. Phenols and trans-1,2-dihydro-1,2-diols are metabolites commonly formed in vivo in fish upon exposure to polycyclic aromatic hydrocarbons (PAHs).	trans-dihydronaphthalene-diols	13-43	phenylalanine hydroxylase	Homo sapiens	89-92
32806443-0	2020	Activation of percarbonate by water treatment sludge-derived biochar for the remediation of PAH-contaminated sediments.	sodium percarbonate	14-26	phenylalanine hydroxylase	Homo sapiens	92-95
32806443-0	2020	Activation of percarbonate by water treatment sludge-derived biochar for the remediation of PAH-contaminated sediments.	Water	30-35	phenylalanine hydroxylase	Homo sapiens	92-95
32866289-1	2020	INTRODUCTION: Treprostinil is a prostacyclin analog used for treatment of pulmonary hypertension (PH) in adults and children, currently awaiting clinical assessment for use in neonates.	treprostinil	14-26	phenylalanine hydroxylase	Homo sapiens	98-100
32866289-1	2020	INTRODUCTION: Treprostinil is a prostacyclin analog used for treatment of pulmonary hypertension (PH) in adults and children, currently awaiting clinical assessment for use in neonates.	Epoprostenol	32-44	phenylalanine hydroxylase	Homo sapiens	98-100
32866289-2	2020	OBJECTIVES: We aimed to investigate the use of treprostinil in neonates with PH on extracorporeal membrane oxygenation (ECMO) support and measure plasma concentrations of the drug.	treprostinil	47-59	phenylalanine hydroxylase	Homo sapiens	77-79
32866289-10	2020	CONCLUSION: This is the first study to report clinically therapeutic treprostinil concentrations in circulating plasma following treprostinil administration in neonates on ECMO, with associated clinical improvement of PH and no signs of hemodynamic instability.	treprostinil	69-81	phenylalanine hydroxylase	Homo sapiens	218-220
32783831-1	2020	BACKGROUND: Although some studies have suggested that exposure to polycyclic aromatic hydrocarbons (PAHs) induces neurodevelopmental disturbances in children and neurodegeneration in animals, the neurotoxic effect of PAH exposure is unclear in adults.	Polycyclic Aromatic Hydrocarbons	66-98	phenylalanine hydroxylase	Homo sapiens	100-103
32996242-1	2021	In previous work, lab-scale reactors designed to study microbial Fe(II) oxidation rates at low pH were found to have stable rates under a wide range of pH and Fe(II) concentrations.	ammonium ferrous sulfate	65-71	phenylalanine hydroxylase	Homo sapiens	95-97
32996242-1	2021	In previous work, lab-scale reactors designed to study microbial Fe(II) oxidation rates at low pH were found to have stable rates under a wide range of pH and Fe(II) concentrations.	ammonium ferrous sulfate	65-71	phenylalanine hydroxylase	Homo sapiens	152-154
32996242-1	2021	In previous work, lab-scale reactors designed to study microbial Fe(II) oxidation rates at low pH were found to have stable rates under a wide range of pH and Fe(II) concentrations.	ammonium ferrous sulfate	159-165	phenylalanine hydroxylase	Homo sapiens	95-97
33003284-0	2020	Co-FeS2/CoS2 Heterostructured Nanomaterials for pH Sensing.	co-fes2	0-7	phenylalanine hydroxylase	Homo sapiens	48-50
33003284-0	2020	Co-FeS2/CoS2 Heterostructured Nanomaterials for pH Sensing.	cos2	8-12	phenylalanine hydroxylase	Homo sapiens	48-50
33003284-3	2020	In this study, we demonstrate the use of a one-step hydrothermal method to prepare Co-FeS2/CoS2 nanomaterials as pH sensor (pH vs. overpotential) for the first time.	co-fes2	83-90	phenylalanine hydroxylase	Homo sapiens	113-115
33003284-3	2020	In this study, we demonstrate the use of a one-step hydrothermal method to prepare Co-FeS2/CoS2 nanomaterials as pH sensor (pH vs. overpotential) for the first time.	co-fes2	83-90	phenylalanine hydroxylase	Homo sapiens	124-126
33003284-3	2020	In this study, we demonstrate the use of a one-step hydrothermal method to prepare Co-FeS2/CoS2 nanomaterials as pH sensor (pH vs. overpotential) for the first time.	cos2	91-95	phenylalanine hydroxylase	Homo sapiens	113-115
33003284-3	2020	In this study, we demonstrate the use of a one-step hydrothermal method to prepare Co-FeS2/CoS2 nanomaterials as pH sensor (pH vs. overpotential) for the first time.	cos2	91-95	phenylalanine hydroxylase	Homo sapiens	124-126
33003284-4	2020	The proposed pH sensor exhibits outstanding performance in KOH solutions via electrochemical methods with good stability.	potassium hydroxide	59-62	phenylalanine hydroxylase	Homo sapiens	13-15
32786449-5	2020	Pronounced differences in aggregation and aggregate stability were observed with silver nanoparticles (citrate-coated) with an initial hydrodynamic diameter (Dh) of 24.6 +- 0.4 nm examined under fasted (pH 2) and fed (pH 5) gastric conditions using nanoparticle tracking analysis (NTA) for size distributions and transmission electron microscopy with energy dispersive X-ray spectroscopy (TEM-EDX) for morphology and elemental composition.	Silver	81-87	phenylalanine hydroxylase	Homo sapiens	203-205
32786449-5	2020	Pronounced differences in aggregation and aggregate stability were observed with silver nanoparticles (citrate-coated) with an initial hydrodynamic diameter (Dh) of 24.6 +- 0.4 nm examined under fasted (pH 2) and fed (pH 5) gastric conditions using nanoparticle tracking analysis (NTA) for size distributions and transmission electron microscopy with energy dispersive X-ray spectroscopy (TEM-EDX) for morphology and elemental composition.	Silver	81-87	phenylalanine hydroxylase	Homo sapiens	218-220
32786449-5	2020	Pronounced differences in aggregation and aggregate stability were observed with silver nanoparticles (citrate-coated) with an initial hydrodynamic diameter (Dh) of 24.6 +- 0.4 nm examined under fasted (pH 2) and fed (pH 5) gastric conditions using nanoparticle tracking analysis (NTA) for size distributions and transmission electron microscopy with energy dispersive X-ray spectroscopy (TEM-EDX) for morphology and elemental composition.	Citric Acid	103-110	phenylalanine hydroxylase	Homo sapiens	203-205
32786449-5	2020	Pronounced differences in aggregation and aggregate stability were observed with silver nanoparticles (citrate-coated) with an initial hydrodynamic diameter (Dh) of 24.6 +- 0.4 nm examined under fasted (pH 2) and fed (pH 5) gastric conditions using nanoparticle tracking analysis (NTA) for size distributions and transmission electron microscopy with energy dispersive X-ray spectroscopy (TEM-EDX) for morphology and elemental composition.	Citric Acid	103-110	phenylalanine hydroxylase	Homo sapiens	218-220
33345499-0	2020	[Effect of nitrogen additions on soil pH, phosphorus contents and phosphatase activities in grassland].	Nitrogen	11-19	phenylalanine hydroxylase	Homo sapiens	38-40
33345499-5	2020	The results showed that nitrogen addition significantly reduced soil pH, TP and AlP activity, while significantly increased AcP activity, but had no significant effect on AP.	Nitrogen	24-32	phenylalanine hydroxylase	Homo sapiens	69-71
32921661-2	2020	However, no report has detailed the association between diazoxide dose and PH development.	Diazoxide	56-65	phenylalanine hydroxylase	Homo sapiens	75-77
33345499-6	2020	Soil pH and AlP activity significantly decreased under nitrogen addition >5 g m-2 a-1, and AcP activity significantly increased under high nitrogen addition (>10 g m-2 a-1).	Nitrogen	55-63	phenylalanine hydroxylase	Homo sapiens	5-7
32921661-3	2020	We report a case of an infant with HH, subsequently complicated by diazoxide-induced PH.	Diazoxide	67-76	phenylalanine hydroxylase	Homo sapiens	85-87
32921661-4	2020	When diazoxide was introduced, PH did not appear initially, but it developed during increased dosing.	Diazoxide	5-14	phenylalanine hydroxylase	Homo sapiens	31-33
32921661-6	2020	PH gradually improved with tapering of the diazoxide dose and disappeared after drug discontinuation.	Diazoxide	43-52	phenylalanine hydroxylase	Homo sapiens	0-2
32921661-7	2020	Our case suggests a diazoxide dose threshold might induce PH.	Diazoxide	20-29	phenylalanine hydroxylase	Homo sapiens	58-60
32917041-3	2020	This study investigated the zeta potentials of magnetite nanoparticles and Alloy 690 surfaces, which were dependent on the pH value, pH agent, and the presence of NaCl.	Ferrosoferric Oxide	47-56	phenylalanine hydroxylase	Homo sapiens	123-125
32927830-0	2020	Oxygen- and pH-Dependent Photophysics of Fluorinated Fluorescein Derivatives: Non-Symmetrical vs.	Fluorescein	53-64	phenylalanine hydroxylase	Homo sapiens	12-14
32927830-4	2020	Fluorination of the xanthene moiety can alter the molecule"s pKa such as to render a probe whose photophysics remains invariant over a wide pH range.	Xanthenes	20-28	phenylalanine hydroxylase	Homo sapiens	140-142
32917041-3	2020	This study investigated the zeta potentials of magnetite nanoparticles and Alloy 690 surfaces, which were dependent on the pH value, pH agent, and the presence of NaCl.	Ferrosoferric Oxide	47-56	phenylalanine hydroxylase	Homo sapiens	133-135
32917041-4	2020	The zeta potentials of the magnetite nanoparticles increased in the negative direction as the pH increased, regardless of the pH agent.	Ferrosoferric Oxide	27-36	phenylalanine hydroxylase	Homo sapiens	94-96
32917041-5	2020	At the same pH value, the absolute values of the zeta potentials with different pH agents were: ethanolamine < ammonia < morpholine.	Ethanolamine	96-108	phenylalanine hydroxylase	Homo sapiens	80-82
32917041-5	2020	At the same pH value, the absolute values of the zeta potentials with different pH agents were: ethanolamine < ammonia < morpholine.	Ammonia	111-118	phenylalanine hydroxylase	Homo sapiens	80-82
32917041-5	2020	At the same pH value, the absolute values of the zeta potentials with different pH agents were: ethanolamine < ammonia < morpholine.	morpholine	121-131	phenylalanine hydroxylase	Homo sapiens	80-82
32917041-9	2020	Furthermore, the empirical formulas for the pH-dependent zeta potentials of magnetite particles in each alkaline solution were suggested.	Ferrosoferric Oxide	76-85	phenylalanine hydroxylase	Homo sapiens	44-46
32883979-1	2020	Phenylalanine hydroxylase (PAH) deficiency leads to phenylalanine accumulation and results in phenylketonuria (PKU).	Phenylalanine	52-65	phenylalanine hydroxylase	Homo sapiens	0-25
32900872-2	2020	Using continuous culture anaerobic fermentor systems, we found that lactate concentrations remained low in communities of human colonic bacteria maintained at pH 6.5, even when dl-lactate was infused at 10 or 20 mM.	Lactic Acid	68-75	phenylalanine hydroxylase	Homo sapiens	159-161
32900872-3	2020	In contrast, lower pH (5.5) led to periodic lactate accumulation following lactate infusion in three fecal microbial communities examined.	Lactic Acid	44-51	phenylalanine hydroxylase	Homo sapiens	19-21
32900872-3	2020	In contrast, lower pH (5.5) led to periodic lactate accumulation following lactate infusion in three fecal microbial communities examined.	Lactic Acid	75-82	phenylalanine hydroxylase	Homo sapiens	19-21
32900872-12	2020	At pH 5.5 in particular, lactate tended to accumulate in tandem with decreases in butyrate and propionate and with corresponding changes in microbial composition.	Lactic Acid	25-32	phenylalanine hydroxylase	Homo sapiens	3-5
31993977-1	2020	PURPOSE: Defective function of phenylalanine hydroxylase in phenylketonuria (PKU) results in the accumulation of phenylalanine (Phe) and the reduction of tyrosine (Tyr) in the blood, interfering in the normal development and function of organs and tissues in the body.	leucyl-phenylalanine	128-131	phenylalanine hydroxylase	Homo sapiens	31-56
32957294-3	2020	In the system of iron-carbon internal electrolysis coupled with persulfate, the iron-carbon internal electrolysis and persulfate had a significant mutual influence, exhibiting a wide range of pH in the treatment process.	Iron	17-21	phenylalanine hydroxylase	Homo sapiens	192-194
32957294-3	2020	In the system of iron-carbon internal electrolysis coupled with persulfate, the iron-carbon internal electrolysis and persulfate had a significant mutual influence, exhibiting a wide range of pH in the treatment process.	Carbon	22-28	phenylalanine hydroxylase	Homo sapiens	192-194
32957294-3	2020	In the system of iron-carbon internal electrolysis coupled with persulfate, the iron-carbon internal electrolysis and persulfate had a significant mutual influence, exhibiting a wide range of pH in the treatment process.	Peroxydisulfate	64-74	phenylalanine hydroxylase	Homo sapiens	192-194
32957294-3	2020	In the system of iron-carbon internal electrolysis coupled with persulfate, the iron-carbon internal electrolysis and persulfate had a significant mutual influence, exhibiting a wide range of pH in the treatment process.	Iron	80-84	phenylalanine hydroxylase	Homo sapiens	192-194
32957294-3	2020	In the system of iron-carbon internal electrolysis coupled with persulfate, the iron-carbon internal electrolysis and persulfate had a significant mutual influence, exhibiting a wide range of pH in the treatment process.	Carbon	85-91	phenylalanine hydroxylase	Homo sapiens	192-194
32957294-3	2020	In the system of iron-carbon internal electrolysis coupled with persulfate, the iron-carbon internal electrolysis and persulfate had a significant mutual influence, exhibiting a wide range of pH in the treatment process.	Peroxydisulfate	118-128	phenylalanine hydroxylase	Homo sapiens	192-194
32885499-4	2020	We hypothesized that esomeprazole and lansoprazole would provide superior acid suppression compared to dexlansoprazole and reach pH goals extrapolated from people for the treatment of esophagitis and duodenal ulceration.	Esomeprazole	21-33	phenylalanine hydroxylase	Homo sapiens	129-131
32885499-4	2020	We hypothesized that esomeprazole and lansoprazole would provide superior acid suppression compared to dexlansoprazole and reach pH goals extrapolated from people for the treatment of esophagitis and duodenal ulceration.	Lansoprazole	38-50	phenylalanine hydroxylase	Homo sapiens	129-131
32885499-11	2020	Esomeprazole was the only treatment that achieved the goals defined for people for the treatment of duodenal ulceration by Day 4 of treatment (MPT +- SD of intragastric pH >=4 of 77.1 +- 29.2%).	Esomeprazole	0-12	phenylalanine hydroxylase	Homo sapiens	169-171
32885499-11	2020	Esomeprazole was the only treatment that achieved the goals defined for people for the treatment of duodenal ulceration by Day 4 of treatment (MPT +- SD of intragastric pH >=4 of 77.1 +- 29.2%).	mpt +- sd	143-152	phenylalanine hydroxylase	Homo sapiens	169-171
33345499-8	2020	NH4NO3 treatment significantly reduced soil TP and increased AcP activity, while urea treatment significantly reduced soil pH and AlP activity.	Urea	81-85	phenylalanine hydroxylase	Homo sapiens	123-125
33345499-10	2020	Soil pH was significantly reduced after three years nitrogen addition, and AcP activitiy was significantly increased after 10 years nitrogen addition.	Nitrogen	52-60	phenylalanine hydroxylase	Homo sapiens	5-7
33345499-13	2020	The significant negative correlation between soil pH and AcP activity indicated that change in soil pH caused by nitrogen addition may be an important factor for the variation of soil phosphatase activity.	Nitrogen	113-121	phenylalanine hydroxylase	Homo sapiens	50-52
33345499-13	2020	The significant negative correlation between soil pH and AcP activity indicated that change in soil pH caused by nitrogen addition may be an important factor for the variation of soil phosphatase activity.	Nitrogen	113-121	phenylalanine hydroxylase	Homo sapiens	100-102
32870937-12	2020	We identified additional risk factors for PH, such as blood pressure maxima, steroid treatment, and increased white blood cell count.	Steroids	77-84	phenylalanine hydroxylase	Homo sapiens	42-44
31993977-1	2020	PURPOSE: Defective function of phenylalanine hydroxylase in phenylketonuria (PKU) results in the accumulation of phenylalanine (Phe) and the reduction of tyrosine (Tyr) in the blood, interfering in the normal development and function of organs and tissues in the body.	Tyrosine	154-162	phenylalanine hydroxylase	Homo sapiens	31-56
31993977-1	2020	PURPOSE: Defective function of phenylalanine hydroxylase in phenylketonuria (PKU) results in the accumulation of phenylalanine (Phe) and the reduction of tyrosine (Tyr) in the blood, interfering in the normal development and function of organs and tissues in the body.	Tyrosine	164-167	phenylalanine hydroxylase	Homo sapiens	31-56
32224135-0	2020	Consistent gastric pH-dependent effects of suppressors of gastric acid secretion on the antihypertensive responses to oral nitrite.	Nitrites	123-130	phenylalanine hydroxylase	Homo sapiens	19-21
32668217-9	2020	PAH variants were scored using an allelic phenotype value and correlated with pre-treatment blood phenylalanine concentrations (n = 6,115) and tetrahydrobiopterin loading test results (n = 4,381), enabling prediction of both a genotype-based phenotype (88%) and tetrahydrobiopterin responsiveness (83%).	Phenylalanine	98-111	phenylalanine hydroxylase	Homo sapiens	0-3
32668217-9	2020	PAH variants were scored using an allelic phenotype value and correlated with pre-treatment blood phenylalanine concentrations (n = 6,115) and tetrahydrobiopterin loading test results (n = 4,381), enabling prediction of both a genotype-based phenotype (88%) and tetrahydrobiopterin responsiveness (83%).	sapropterin	143-162	phenylalanine hydroxylase	Homo sapiens	0-3
32668217-9	2020	PAH variants were scored using an allelic phenotype value and correlated with pre-treatment blood phenylalanine concentrations (n = 6,115) and tetrahydrobiopterin loading test results (n = 4,381), enabling prediction of both a genotype-based phenotype (88%) and tetrahydrobiopterin responsiveness (83%).	sapropterin	262-281	phenylalanine hydroxylase	Homo sapiens	0-3
31955601-9	2020	RESULT: After fully adjusting for covariables, PAH metabolites had negative relationship with muscle strength, especially 3-fluorene (beta=-0.021, 95%CI: -0.042, 0.000) and 2-fluorene (beta=-0.020, 95%CI: -0.034, -0.005).	fluorene	122-132	phenylalanine hydroxylase	Homo sapiens	47-50
31955601-9	2020	RESULT: After fully adjusting for covariables, PAH metabolites had negative relationship with muscle strength, especially 3-fluorene (beta=-0.021, 95%CI: -0.042, 0.000) and 2-fluorene (beta=-0.020, 95%CI: -0.034, -0.005).	fluorene	173-183	phenylalanine hydroxylase	Homo sapiens	47-50
32294599-5	2020	Results show that by increasing pH and carbon content in the organo-mineral composites, the released phosphate to the solution increases in both oxic and suboxic conditions.	Phosphates	101-110	phenylalanine hydroxylase	Homo sapiens	32-34
32505394-7	2020	We found that BGM readings were significantly affected by lower pH values at both lactose levels.	Lactose	82-89	phenylalanine hydroxylase	Homo sapiens	64-66
32742934-1	2020	Background: Accumulation of phenylalanine (Phe) due to deficiency in the enzyme phenylalanine hydroxylase (PAH), responsible for the conversion of Phe into tyrosine leads to Phenylketonuria (PKU), a rare autosomal recessive inborn error of metabolism with a mean prevalence of approximately 1:10,000 to 1:15,000 newborns.	Phenylalanine	28-41	phenylalanine hydroxylase	Homo sapiens	107-110
32742934-1	2020	Background: Accumulation of phenylalanine (Phe) due to deficiency in the enzyme phenylalanine hydroxylase (PAH), responsible for the conversion of Phe into tyrosine leads to Phenylketonuria (PKU), a rare autosomal recessive inborn error of metabolism with a mean prevalence of approximately 1:10,000 to 1:15,000 newborns.	Phenylalanine	43-46	phenylalanine hydroxylase	Homo sapiens	107-110
32742934-1	2020	Background: Accumulation of phenylalanine (Phe) due to deficiency in the enzyme phenylalanine hydroxylase (PAH), responsible for the conversion of Phe into tyrosine leads to Phenylketonuria (PKU), a rare autosomal recessive inborn error of metabolism with a mean prevalence of approximately 1:10,000 to 1:15,000 newborns.	Phenylalanine	147-150	phenylalanine hydroxylase	Homo sapiens	107-110
32742934-1	2020	Background: Accumulation of phenylalanine (Phe) due to deficiency in the enzyme phenylalanine hydroxylase (PAH), responsible for the conversion of Phe into tyrosine leads to Phenylketonuria (PKU), a rare autosomal recessive inborn error of metabolism with a mean prevalence of approximately 1:10,000 to 1:15,000 newborns.	Tyrosine	156-164	phenylalanine hydroxylase	Homo sapiens	107-110
32168152-1	2020	BACKGROUND: Add-on therapy with prostacyclin in pediatric refractory pulmonary hypertension (PH) poses a challenge, especially when considering continuous intravenous administration in younger children.	Epoprostenol	32-44	phenylalanine hydroxylase	Homo sapiens	93-95
32168152-3	2020	We reported 2 pediatric cases of PH treated with subcutaneous treprostinil and reviewed the literature on treprostinil use in children.	treprostinil	62-74	phenylalanine hydroxylase	Homo sapiens	33-35
32168152-7	2020	The literature review identified 19 studies reporting treprostinil use in 421 children with various types of PH (groups 1 and 3).	treprostinil	54-66	phenylalanine hydroxylase	Homo sapiens	109-111
32168152-9	2020	Overall, 12 clinical trials on treprostinil for children with PH were registered on the clinical trial registries.	treprostinil	31-43	phenylalanine hydroxylase	Homo sapiens	62-64
32168152-11	2020	CONCLUSIONS: Subcutaneous treprostinil may be a useful adjunct in the therapeutic algorithm for children with severe PH, refractory to oral drugs, and after a complete check-up for all PH etiologies.	treprostinil	26-38	phenylalanine hydroxylase	Homo sapiens	117-119
32168152-11	2020	CONCLUSIONS: Subcutaneous treprostinil may be a useful adjunct in the therapeutic algorithm for children with severe PH, refractory to oral drugs, and after a complete check-up for all PH etiologies.	treprostinil	26-38	phenylalanine hydroxylase	Homo sapiens	185-187
32601437-2	2020	We evaluated whether elevated glucose and severe hypoperfusion have synergistic effects in the promotion of parenchymal hemorrhage (PH) after mechanical thrombectomy (MT).	Glucose	30-37	phenylalanine hydroxylase	Homo sapiens	132-134
32601437-7	2020	In adjusted models, pretreatment glucose levels interacted significantly with VLCBV on the prediction of PH (p-interaction = 0.011).	Glucose	33-40	phenylalanine hydroxylase	Homo sapiens	105-107
32601437-8	2020	In patients with VLCBV-regions, higher glucose was significantly associated with PH (adjusted-OR = 3.15; 95% CI = 1.08-9.19, p = 0.036), whereas this association was not significant in patients without VLCBV-regions.	Glucose	39-46	phenylalanine hydroxylase	Homo sapiens	81-83
32592045-7	2020	The solubility of the drugs was significantly affected by the vehicle physicochemical properties and macronutrient composition, with the solubility of montelukast being driven by the pH, fat and protein content of the vehicles and the solubility of mesalazine by vehicle osmolality, viscosity and sugar content.	montelukast	151-162	phenylalanine hydroxylase	Homo sapiens	183-185
32279825-6	2020	In this review, the physicochemical properties and applications of thermo/pH-responsive CS-based hydrogels and their future perspectives in BTE are briefly outlined.	2,1,3-Benzothiadiazol-4-amine	140-143	phenylalanine hydroxylase	Homo sapiens	74-76
32450880-1	2020	BACKGROUND: Phenylketonuria (PKU) is an inherited metabolic disorder characterized by reduced activity of phenylalanine hydroxylase resulting in elevated blood phenylalanine (Phe) concentration.	Phenylalanine	12-15	phenylalanine hydroxylase	Homo sapiens	106-131
32213389-0	2020	The fate and toxicity of Pb-based perovskite nanoparticles on soil bacterial community: Impacts of pH, humic acid, and divalent cations.	Lead	25-27	phenylalanine hydroxylase	Homo sapiens	99-101
32213389-4	2020	Increasing pH decreased PbPNPs-particle aggregation as well as Pb-ion release.	Lead	24-26	phenylalanine hydroxylase	Homo sapiens	11-13
32092627-7	2020	We show that for some PAH congeners, for example, benzo[a]pyrene (BaP)-the forest-fire-induced air emissions are almost one order of magnitude higher than previous emission inventories in the Arctic.	Benzo(a)pyrene	50-64	phenylalanine hydroxylase	Homo sapiens	22-25
32092627-7	2020	We show that for some PAH congeners, for example, benzo[a]pyrene (BaP)-the forest-fire-induced air emissions are almost one order of magnitude higher than previous emission inventories in the Arctic.	Benzo(a)pyrene	66-69	phenylalanine hydroxylase	Homo sapiens	22-25
32224135-7	2020	These findings were reproduced in a second study using sodium acetate buffers at pH 3.5, 4.5, and 5.5 to mimic gastric pH found with vehicle, ranitidine, and omeprazole, respectively.	Sodium Acetate	55-69	phenylalanine hydroxylase	Homo sapiens	81-83
32224135-7	2020	These findings were reproduced in a second study using sodium acetate buffers at pH 3.5, 4.5, and 5.5 to mimic gastric pH found with vehicle, ranitidine, and omeprazole, respectively.	Omeprazole	158-168	phenylalanine hydroxylase	Homo sapiens	119-121
32224135-9	2020	Our results clearly indicate that SGAS impair nitrite-induced gastric formation of NO and vasoactive RXNO in a pH-dependent manner, thus resulting in impaired responses to oral nitrite.	Nitrites	46-53	phenylalanine hydroxylase	Homo sapiens	111-113
32440121-0	2020	Surface Engineering of Metal-Organic Framework as pH-/NIR-Responsive Nanocarrier for Imaging-Guided Chemo-Photothermal Therapy.	Metals	23-28	phenylalanine hydroxylase	Homo sapiens	50-52
32440121-3	2020	Materials and Methods: Herein, a pH/near-infrared (NIR) dual-responsive drug delivery system based on zeolitic imidazolate framework-8 (ZIF-8) is constructed for synergistic chemo-photothermal therapy and dual-modal magnetic resonance (MR)/photoacoustic (PA) imaging.	imidazolate	111-122	phenylalanine hydroxylase	Homo sapiens	33-35
32342967-0	2020	Photocyclization of diarylethylenes with a boronate moiety: a useful synthetic tool to soluble PAH building blocks.	diarylethylenes	20-35	phenylalanine hydroxylase	Homo sapiens	95-98
32440121-7	2020	The pH-dependent degradation and drug release behavior of prepared ZIF-8/DMPP are confirmed.	2-Methylimidazole zinc salt	67-72	phenylalanine hydroxylase	Homo sapiens	4-6
32440121-7	2020	The pH-dependent degradation and drug release behavior of prepared ZIF-8/DMPP are confirmed.	Dimethylphenylpiperazinium Iodide	73-77	phenylalanine hydroxylase	Homo sapiens	4-6
32342967-0	2020	Photocyclization of diarylethylenes with a boronate moiety: a useful synthetic tool to soluble PAH building blocks.	glutamyl-gamma-boronate	43-51	phenylalanine hydroxylase	Homo sapiens	95-98
32141284-0	2020	Engineered pH-Responsive Mesoporous Carbon Nanoparticles for Drug Delivery.	mesoporous	25-35	phenylalanine hydroxylase	Homo sapiens	11-13
32141284-0	2020	Engineered pH-Responsive Mesoporous Carbon Nanoparticles for Drug Delivery.	Carbon	36-42	phenylalanine hydroxylase	Homo sapiens	11-13
32141284-1	2020	In this work, two types of mesoporous carbon particles with different morphology, size, and pore structure have been functionalized with a self-immolative polymer sensitive to changes in pH and tested as drug nanocarriers.	Methane	27-44	phenylalanine hydroxylase	Homo sapiens	187-189
32141284-1	2020	In this work, two types of mesoporous carbon particles with different morphology, size, and pore structure have been functionalized with a self-immolative polymer sensitive to changes in pH and tested as drug nanocarriers.	Polymers	155-162	phenylalanine hydroxylase	Homo sapiens	187-189
32141284-3	2020	In vial release experiments of a model Ru dye at pH 7.4 and 5 confirm the pH-responsiveness of the hybrid systems, showing that only small amounts of the cargo are released at physiological pH, whereas at slightly acidic pH (e.g., that of lysosomes), self-immolation takes place and a significant amount of the cargo is released.	ru dye	39-45	phenylalanine hydroxylase	Homo sapiens	49-51
32141284-3	2020	In vial release experiments of a model Ru dye at pH 7.4 and 5 confirm the pH-responsiveness of the hybrid systems, showing that only small amounts of the cargo are released at physiological pH, whereas at slightly acidic pH (e.g., that of lysosomes), self-immolation takes place and a significant amount of the cargo is released.	ru dye	39-45	phenylalanine hydroxylase	Homo sapiens	74-76
32141284-3	2020	In vial release experiments of a model Ru dye at pH 7.4 and 5 confirm the pH-responsiveness of the hybrid systems, showing that only small amounts of the cargo are released at physiological pH, whereas at slightly acidic pH (e.g., that of lysosomes), self-immolation takes place and a significant amount of the cargo is released.	ru dye	39-45	phenylalanine hydroxylase	Homo sapiens	74-76
32141284-3	2020	In vial release experiments of a model Ru dye at pH 7.4 and 5 confirm the pH-responsiveness of the hybrid systems, showing that only small amounts of the cargo are released at physiological pH, whereas at slightly acidic pH (e.g., that of lysosomes), self-immolation takes place and a significant amount of the cargo is released.	ru dye	39-45	phenylalanine hydroxylase	Homo sapiens	74-76
32049604-5	2020	Notably, increase in C/N ratio led to decrease in total ammonia nitrogen (TAN) and alkalinity concentration (Alk), hence, treatments with the lowest C/N ratio had better reactor performance in terms of suitable process parameters such as Alk, pH, ORP, and TAN.	Carbon	21-22	phenylalanine hydroxylase	Homo sapiens	243-245
32059909-0	2020	pH-Responsive nanoparticles based on cholesterol/imidazole modified oxidized-starch for targeted anticancer drug delivery.	imidazole	49-58	phenylalanine hydroxylase	Homo sapiens	0-2
32059909-0	2020	pH-Responsive nanoparticles based on cholesterol/imidazole modified oxidized-starch for targeted anticancer drug delivery.	Starch	77-83	phenylalanine hydroxylase	Homo sapiens	0-2
32059909-8	2020	Curcumin was released faster at pH 5.5 than that at pH 7.4 from the curcumin-loaded nanoparticles (Cur-NPs), indicating the pH-triggered release capacity of Cur-NPs after endocytosis by endosomes since the pH is low to 5.0~6.0 in endosomes.	Curcumin	0-8	phenylalanine hydroxylase	Homo sapiens	32-34
32049604-5	2020	Notably, increase in C/N ratio led to decrease in total ammonia nitrogen (TAN) and alkalinity concentration (Alk), hence, treatments with the lowest C/N ratio had better reactor performance in terms of suitable process parameters such as Alk, pH, ORP, and TAN.	Nitrogen	0-1	phenylalanine hydroxylase	Homo sapiens	243-245
32049604-5	2020	Notably, increase in C/N ratio led to decrease in total ammonia nitrogen (TAN) and alkalinity concentration (Alk), hence, treatments with the lowest C/N ratio had better reactor performance in terms of suitable process parameters such as Alk, pH, ORP, and TAN.	Carbon	149-150	phenylalanine hydroxylase	Homo sapiens	243-245
32147842-6	2020	In addition, applying amino acids to meat surface significantly influenced (P < 0.05) pH and surface color change of beef crusts; particularly, lysine at 0.20% and 0.50% increased pH and a* (redness) but reduced b* (yellowness), while tryptophan and leucine at 0.50% increased L* (whiteness).	Lysine	144-150	phenylalanine hydroxylase	Homo sapiens	86-88
32147842-6	2020	In addition, applying amino acids to meat surface significantly influenced (P < 0.05) pH and surface color change of beef crusts; particularly, lysine at 0.20% and 0.50% increased pH and a* (redness) but reduced b* (yellowness), while tryptophan and leucine at 0.50% increased L* (whiteness).	Lysine	144-150	phenylalanine hydroxylase	Homo sapiens	180-182
32217972-7	2020	Although phenylalanine levels are increased in the breast milk of patients with PAH deficiency, breastfed infants who do not have PAH deficiency have normal enzyme levels and no dietary restriction.	Phenylalanine	9-22	phenylalanine hydroxylase	Homo sapiens	80-83
32235429-4	2020	A linear fit to the response of the sensing system to RH demonstrates a sensitivity of 3.02 mV/% (R2 = 0.96), hysteresis +- 1.17% RH when 11 bilayers of PAH/SiO2 NPs are coated on the tip of the fibre.	Rhodium	54-56	phenylalanine hydroxylase	Homo sapiens	153-156
32235429-4	2020	A linear fit to the response of the sensing system to RH demonstrates a sensitivity of 3.02 mV/% (R2 = 0.96), hysteresis +- 1.17% RH when 11 bilayers of PAH/SiO2 NPs are coated on the tip of the fibre.	Rhodium	130-132	phenylalanine hydroxylase	Homo sapiens	153-156
32168914-10	2020	The electrokinetic treatment of a sludge from a water treatment plant contaminated with Mn was effective when pH control on the cathode was used.	Water	48-53	phenylalanine hydroxylase	Homo sapiens	110-112
33558914-3	2020	Propofol was incorporated in the mixture of disodium edetate, sodium oleate, thioglycerol, glycerol, egg lecithin, soyabean oil and medium chain triglyceride oil, and homogenization was continued at controlled temperature of 20  C. The product did not show any significant change in visible extraneous particulate matter, pH, osmolality, bacterial endo-toxin, sterility, high performance liquid chromatography (HPLC) their stability and impurities after exposing at 40  C for 3 and 6 months.	Propofol	0-8	phenylalanine hydroxylase	Homo sapiens	322-324
31944002-1	2020	BACKGROUND: Previous studies suggested associations between maternal smoking, a source of exposure to polycyclic aromatic hydrocarbons (PAHs) and other chemicals, and central nervous system and face birth defects; however, no previous studies have evaluated maternal occupational PAH exposure itself.	Polycyclic Aromatic Hydrocarbons	102-134	phenylalanine hydroxylase	Homo sapiens	136-139
32059909-0	2020	pH-Responsive nanoparticles based on cholesterol/imidazole modified oxidized-starch for targeted anticancer drug delivery.	Cholesterol	37-48	phenylalanine hydroxylase	Homo sapiens	0-2
32115593-0	2020	Expanding the BN-embedded PAH family: 4a-aza-12a-borachrysene.	6-bromo-2-naphthyl sulfate	14-16	phenylalanine hydroxylase	Homo sapiens	26-29
32115593-0	2020	Expanding the BN-embedded PAH family: 4a-aza-12a-borachrysene.	4a-aza-12a-borachrysene	38-61	phenylalanine hydroxylase	Homo sapiens	26-29
32115593-2	2020	The reactions of this BN-embedded PAH with bromine and organolithium compounds proceed with complete regioselectivity, resulting in the formation of nine derivatives.	6-bromo-2-naphthyl sulfate	22-24	phenylalanine hydroxylase	Homo sapiens	34-37
32115593-2	2020	The reactions of this BN-embedded PAH with bromine and organolithium compounds proceed with complete regioselectivity, resulting in the formation of nine derivatives.	Bromine	43-50	phenylalanine hydroxylase	Homo sapiens	34-37
32115593-2	2020	The reactions of this BN-embedded PAH with bromine and organolithium compounds proceed with complete regioselectivity, resulting in the formation of nine derivatives.	organolithium	55-68	phenylalanine hydroxylase	Homo sapiens	34-37
32178414-0	2020	Zinc Binding to Fulvic acids: Assessing the Impact of pH, Metal Concentrations and Chemical Properties of Fulvic Acids on the Mechanism and Stability of Formed Soluble Complexes.	fulvic acid	16-28	phenylalanine hydroxylase	Homo sapiens	54-56
32178414-5	2020	The number of fluorophores available for Zn(II) increased from pH 3 to 7 by ~44%.	Zinc	41-47	phenylalanine hydroxylase	Homo sapiens	63-65
32178414-9	2020	A positive relationship was found between the fraction of accessible fluorophores and Zn(II) binding at pH 7 determined based on proton release (R = 0.91-0.97).	Zinc	86-92	phenylalanine hydroxylase	Homo sapiens	104-106
31896200-5	2020	Temperature and pH offer a synergistic effect on the adsorption of Cu (II), with maximum adsorption observed at pH 6.5 at 55  C. Kinetic, thermodynamic, and isotherm studies indicate that the adsorption of copper ions follows chemisorption and is thermodynamically favored at increasing temperature.	cu (ii)	67-74	phenylalanine hydroxylase	Homo sapiens	16-18
31896200-5	2020	Temperature and pH offer a synergistic effect on the adsorption of Cu (II), with maximum adsorption observed at pH 6.5 at 55  C. Kinetic, thermodynamic, and isotherm studies indicate that the adsorption of copper ions follows chemisorption and is thermodynamically favored at increasing temperature.	cu (ii)	67-74	phenylalanine hydroxylase	Homo sapiens	112-114
31896200-5	2020	Temperature and pH offer a synergistic effect on the adsorption of Cu (II), with maximum adsorption observed at pH 6.5 at 55  C. Kinetic, thermodynamic, and isotherm studies indicate that the adsorption of copper ions follows chemisorption and is thermodynamically favored at increasing temperature.	Copper	206-212	phenylalanine hydroxylase	Homo sapiens	16-18
31896200-6	2020	From the Langmuir isotherm model, the obtained maximum adsorption capacity, qm, was 161.30 mg g-1 at 55  C. From the desorption studies, results showed that the maximum desorption was observed at pH 3 at 25  C. In conclusion, PES-PDMAEMA has the capability to adsorb and desorb Cu (II) by adjusting both pH and temperature, hence it can be considered as an efficient and economical adsorbent for heavy metals such Cu (II).	cu (ii)	278-285	phenylalanine hydroxylase	Homo sapiens	196-198
31896200-6	2020	From the Langmuir isotherm model, the obtained maximum adsorption capacity, qm, was 161.30 mg g-1 at 55  C. From the desorption studies, results showed that the maximum desorption was observed at pH 3 at 25  C. In conclusion, PES-PDMAEMA has the capability to adsorb and desorb Cu (II) by adjusting both pH and temperature, hence it can be considered as an efficient and economical adsorbent for heavy metals such Cu (II).	cu (ii)	414-421	phenylalanine hydroxylase	Homo sapiens	196-198
31865166-3	2020	Geometric mean concentrations of 1-hydroxypyrene, the most common biomarker of PAH exposure, were 100 and 120 ng/L urine in 2014-2015 and 2016-2017, respectively.	1-hydroxypyrene	33-48	phenylalanine hydroxylase	Homo sapiens	79-82
31373030-3	2020	Tetrahydrobiopterin (BH4 ) could be one of those treatment options, as it may not only increase residual phenylalanine hydroxylase activity in BH4 -responsive PKU patients, but possibly also directly improves neurocognitive functioning in both BH4 -responsive and BH4 -unresponsive PKU patients.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	105-130
31373030-3	2020	Tetrahydrobiopterin (BH4 ) could be one of those treatment options, as it may not only increase residual phenylalanine hydroxylase activity in BH4 -responsive PKU patients, but possibly also directly improves neurocognitive functioning in both BH4 -responsive and BH4 -unresponsive PKU patients.	sapropterin	21-24	phenylalanine hydroxylase	Homo sapiens	105-130
31924016-0	2020	In vitro and in vivo evaluation of 3D biodegradable thermo/pH sensitive sol-gel reversible hydroxybutyl chitosan hydrogel.	hydroxybutyl chitosan	91-112	phenylalanine hydroxylase	Homo sapiens	59-61
31924016-5	2020	The HBCS hydrogel exhibited excellent thermo/pH sensitive sol-gel reversibility behavior from 4  C to the gelation temperature.	hydroxybutyl chitosan	4-8	phenylalanine hydroxylase	Homo sapiens	45-47
31924016-10	2020	These results demonstrated that the HBCS hydrogel with biodegradable thermo/pH sensitive sol-gel reversible properties had excellent cytocompatibility, histocompatibility, and biocompatibility as a drug carrier.	hydroxybutyl chitosan	36-40	phenylalanine hydroxylase	Homo sapiens	76-78
31883647-1	2020	BACKGROUND: Phenylketonuria (PKU) is an autosomal recessive disease caused by mutations in the PAH gene, resulting in deficiency of phenylalanine hydroxylase (PAH), an enzyme that converts phenylalanine (Phe) to tyrosine (Tyr).	Phenylalanine	132-145	phenylalanine hydroxylase	Homo sapiens	95-98
31883647-1	2020	BACKGROUND: Phenylketonuria (PKU) is an autosomal recessive disease caused by mutations in the PAH gene, resulting in deficiency of phenylalanine hydroxylase (PAH), an enzyme that converts phenylalanine (Phe) to tyrosine (Tyr).	Phenylalanine	132-145	phenylalanine hydroxylase	Homo sapiens	159-162
31883647-1	2020	BACKGROUND: Phenylketonuria (PKU) is an autosomal recessive disease caused by mutations in the PAH gene, resulting in deficiency of phenylalanine hydroxylase (PAH), an enzyme that converts phenylalanine (Phe) to tyrosine (Tyr).	Phenylalanine	12-15	phenylalanine hydroxylase	Homo sapiens	95-98
31883647-1	2020	BACKGROUND: Phenylketonuria (PKU) is an autosomal recessive disease caused by mutations in the PAH gene, resulting in deficiency of phenylalanine hydroxylase (PAH), an enzyme that converts phenylalanine (Phe) to tyrosine (Tyr).	Phenylalanine	12-15	phenylalanine hydroxylase	Homo sapiens	159-162
31892062-0	2020	A novel cell-penetrating Janus nanoprobe for ratiometric fluorescence detection of pH in living cells.	janus	25-30	phenylalanine hydroxylase	Homo sapiens	83-85
32106880-1	2020	BACKGROUND: Phenylketonuria (PKU; OMIM#261600) is a rare metabolic disorder caused by mutations in the phenylalanine hydroxylase (PAH) gene resulting in high phenylalanine (Phe) in blood and brain.	Phenylalanine	103-116	phenylalanine hydroxylase	Homo sapiens	130-133
32106880-1	2020	BACKGROUND: Phenylketonuria (PKU; OMIM#261600) is a rare metabolic disorder caused by mutations in the phenylalanine hydroxylase (PAH) gene resulting in high phenylalanine (Phe) in blood and brain.	Phenylalanine	12-15	phenylalanine hydroxylase	Homo sapiens	103-128
32106880-1	2020	BACKGROUND: Phenylketonuria (PKU; OMIM#261600) is a rare metabolic disorder caused by mutations in the phenylalanine hydroxylase (PAH) gene resulting in high phenylalanine (Phe) in blood and brain.	Phenylalanine	12-15	phenylalanine hydroxylase	Homo sapiens	130-133
32140415-1	2020	Background: Phenylketonuria (PKU) is a rare autosomal recessive disorder caused by mutations in the gene encoding phenylalanine hydroxylase, an enzyme that converts phenylalanine to tyrosine.	Tyrosine	182-190	phenylalanine hydroxylase	Homo sapiens	114-139
31600696-1	2020	The studies of the mechanism of Cd fixation by biochar have mainly focused on the pore size, pH, and oxygen-containing functional groups, and few researches have paid close attention to the effect of the negative charge in biochar surface.	Cadmium	32-34	phenylalanine hydroxylase	Homo sapiens	93-95
31422327-9	2019	More specifically, from the fifty-five studied molecules, only coronene (a PAH), 1,8-naphthalic anhydride, 6-H-benzo[cd]pyrene-6-one and 7H-benz[de]anthracence-7-one (three oxygenated-PAHs) provide relevant contributions to radiative forcing.	coronene	63-71	phenylalanine hydroxylase	Homo sapiens	75-78
31902521-0	2020	Normal brain aging and Alzheimer"s disease are associated with lower cerebral pH: an in vivo histidine 1H-MR spectroscopy study.	histidine 1h	93-105	phenylalanine hydroxylase	Homo sapiens	78-80
33335942-2	2020	Loss-of-function of PAH leads to accumulation of phenylalanine in the blood/body of an untreated patient, which damages the developing brain, causing severe mental retardation.	Phenylalanine	49-62	phenylalanine hydroxylase	Homo sapiens	20-23
31433959-1	2020	Biogeochemical-Argo (BGC-Argo) is a network of profiling floats carrying sensors that enable observation of as many as six essential biogeochemical and bio-optical variables: oxygen, nitrate, pH, chlorophyll a, suspended particles, and downwelling irradiance.	argo	15-19	phenylalanine hydroxylase	Homo sapiens	192-194
31433959-1	2020	Biogeochemical-Argo (BGC-Argo) is a network of profiling floats carrying sensors that enable observation of as many as six essential biogeochemical and bio-optical variables: oxygen, nitrate, pH, chlorophyll a, suspended particles, and downwelling irradiance.	argo	25-29	phenylalanine hydroxylase	Homo sapiens	192-194
31499302-0	2020	Phosphorus sorption and availability in an andosol after a decade of organic or mineral fertilizer applications: Importance of pH and organic carbon modifications in soil as compared to phosphorus accumulation.	Phosphorus	0-10	phenylalanine hydroxylase	Homo sapiens	127-129
31499302-2	2020	We aimed to highlight the impact of pH and organic C modifications in soil on the inorganic P (Pi) sorption capacity and availability as compared to the effect of P accumulation after mineral or organic fertilizers.	Phosphorus	92-93	phenylalanine hydroxylase	Homo sapiens	36-38
31499302-2	2020	We aimed to highlight the impact of pH and organic C modifications in soil on the inorganic P (Pi) sorption capacity and availability as compared to the effect of P accumulation after mineral or organic fertilizers.	Phosphorus	95-96	phenylalanine hydroxylase	Homo sapiens	36-38
31499302-10	2020	Our study demonstrated that, beyond the P fertilization rate, the increase in organic C content and even more so in pH induced by a decade of organic fertilizer applications in soil decreased the Pi sorption capacity and consequently increased Pi-water in soil.	Water	247-252	phenylalanine hydroxylase	Homo sapiens	116-118
31742798-1	2019	Herein, we have synthesized an enantiomerically pure propeller-shaped PAH, C90 H48 , possessing three [7]helicene and three [5]helicene subunits.	helicenes	102-113	phenylalanine hydroxylase	Homo sapiens	70-73
31742798-1	2019	Herein, we have synthesized an enantiomerically pure propeller-shaped PAH, C90 H48 , possessing three [7]helicene and three [5]helicene subunits.	helicenes	124-135	phenylalanine hydroxylase	Homo sapiens	70-73
31853950-6	2019	While the underlying physiological mechanisms are complex, unraveling the estrogen puzzle may reveal novel therapeutic strategies to treat and reverse the effects of PAH/PH.	Estrogens	74-82	phenylalanine hydroxylase	Homo sapiens	166-172
31883647-1	2020	BACKGROUND: Phenylketonuria (PKU) is an autosomal recessive disease caused by mutations in the PAH gene, resulting in deficiency of phenylalanine hydroxylase (PAH), an enzyme that converts phenylalanine (Phe) to tyrosine (Tyr).	Tyrosine	212-220	phenylalanine hydroxylase	Homo sapiens	95-98
31883647-1	2020	BACKGROUND: Phenylketonuria (PKU) is an autosomal recessive disease caused by mutations in the PAH gene, resulting in deficiency of phenylalanine hydroxylase (PAH), an enzyme that converts phenylalanine (Phe) to tyrosine (Tyr).	Tyrosine	212-220	phenylalanine hydroxylase	Homo sapiens	159-162
31883647-1	2020	BACKGROUND: Phenylketonuria (PKU) is an autosomal recessive disease caused by mutations in the PAH gene, resulting in deficiency of phenylalanine hydroxylase (PAH), an enzyme that converts phenylalanine (Phe) to tyrosine (Tyr).	Tyrosine	222-225	phenylalanine hydroxylase	Homo sapiens	95-98
31883647-1	2020	BACKGROUND: Phenylketonuria (PKU) is an autosomal recessive disease caused by mutations in the PAH gene, resulting in deficiency of phenylalanine hydroxylase (PAH), an enzyme that converts phenylalanine (Phe) to tyrosine (Tyr).	Tyrosine	222-225	phenylalanine hydroxylase	Homo sapiens	159-162
31846894-0	2020	Graphene aerogel nanoparticles for in-situ loading/pH sensitive releasing anticancer drugs.	Graphite	0-8	phenylalanine hydroxylase	Homo sapiens	51-53
31846894-9	2020	DOX-loaded GANPs showed high pH-sensitive release (equivalent to the carrier weight) after 5 days, which can indicate benefits in tumor cell acidic microenvironments in-vivo.	Doxorubicin	0-3	phenylalanine hydroxylase	Homo sapiens	29-31
31846894-9	2020	DOX-loaded GANPs showed high pH-sensitive release (equivalent to the carrier weight) after 5 days, which can indicate benefits in tumor cell acidic microenvironments in-vivo.	ganps	11-16	phenylalanine hydroxylase	Homo sapiens	29-31
32039316-0	2020	Screening of PAH Common Mutations in Chinese Phenylketonuria Patients Using iPLEX MALDI-TOF MS. Phenylketonuria (PKU) is caused by phenylalanine hydroxylase (PAH) gene variants.	phenylketonuria	45-60	phenylalanine hydroxylase	Homo sapiens	13-16
32039316-0	2020	Screening of PAH Common Mutations in Chinese Phenylketonuria Patients Using iPLEX MALDI-TOF MS. Phenylketonuria (PKU) is caused by phenylalanine hydroxylase (PAH) gene variants.	phenylketonuria	45-60	phenylalanine hydroxylase	Homo sapiens	131-156
32039316-0	2020	Screening of PAH Common Mutations in Chinese Phenylketonuria Patients Using iPLEX MALDI-TOF MS. Phenylketonuria (PKU) is caused by phenylalanine hydroxylase (PAH) gene variants.	phenylketonuria	45-60	phenylalanine hydroxylase	Homo sapiens	158-161
32039316-0	2020	Screening of PAH Common Mutations in Chinese Phenylketonuria Patients Using iPLEX MALDI-TOF MS. Phenylketonuria (PKU) is caused by phenylalanine hydroxylase (PAH) gene variants.	phenylketonuria	96-111	phenylalanine hydroxylase	Homo sapiens	13-16
32039316-0	2020	Screening of PAH Common Mutations in Chinese Phenylketonuria Patients Using iPLEX MALDI-TOF MS. Phenylketonuria (PKU) is caused by phenylalanine hydroxylase (PAH) gene variants.	phenylketonuria	96-111	phenylalanine hydroxylase	Homo sapiens	131-156
32039316-0	2020	Screening of PAH Common Mutations in Chinese Phenylketonuria Patients Using iPLEX MALDI-TOF MS. Phenylketonuria (PKU) is caused by phenylalanine hydroxylase (PAH) gene variants.	phenylketonuria	96-111	phenylalanine hydroxylase	Homo sapiens	158-161
31306961-0	2019	A near-infrared ratiometric fluorescence probe base on spiropyran derivative for pH and its application in living cells.	spiropyran	55-65	phenylalanine hydroxylase	Homo sapiens	81-83
31306961-4	2019	The spectroscopic responses of probe to pH variations were investigated in CH3OH/PBS (v/v, 1:1) mixed solution at different pH values.	Methanol	75-80	phenylalanine hydroxylase	Homo sapiens	40-42
31306961-4	2019	The spectroscopic responses of probe to pH variations were investigated in CH3OH/PBS (v/v, 1:1) mixed solution at different pH values.	Lead	81-84	phenylalanine hydroxylase	Homo sapiens	40-42
31355457-6	2019	KEY RESULTS: Low pH and the mutant receptor MOR-H2976.52 A impaired naloxone binding and antagonism of cAMP reduction.	Cyclic AMP	103-107	phenylalanine hydroxylase	Homo sapiens	17-19
31355457-9	2019	CONCLUSIONS AND IMPLICATIONS: Our investigations indicate that low pH selectively impairs mu-opioid receptor signalling modulated by ligands capable of forming hydrogen bonds with H2976.52 .	Hydrogen	160-168	phenylalanine hydroxylase	Homo sapiens	67-69
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	leucyl-phenylalanine	43-56	phenylalanine hydroxylase	Homo sapiens	70-73
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	leucyl-phenylalanine	43-56	phenylalanine hydroxylase	Homo sapiens	104-107
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	leucyl-phenylalanine	134-137	phenylalanine hydroxylase	Homo sapiens	43-68
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	leucyl-phenylalanine	134-137	phenylalanine hydroxylase	Homo sapiens	70-73
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	leucyl-phenylalanine	134-137	phenylalanine hydroxylase	Homo sapiens	104-107
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	Tyrosine	142-150	phenylalanine hydroxylase	Homo sapiens	43-68
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	Tyrosine	142-150	phenylalanine hydroxylase	Homo sapiens	70-73
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	Tyrosine	142-150	phenylalanine hydroxylase	Homo sapiens	104-107
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	Tyrosine	152-155	phenylalanine hydroxylase	Homo sapiens	43-68
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	Tyrosine	152-155	phenylalanine hydroxylase	Homo sapiens	70-73
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	Tyrosine	152-155	phenylalanine hydroxylase	Homo sapiens	104-107
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	leucyl-phenylalanine	171-174	phenylalanine hydroxylase	Homo sapiens	43-68
31233370-11	2020	Exhaustive investigation has identified the enzyme responsible for this S-oxygenation reaction as the tetrahydrobiopterin-dependent aromatic amino acid hydroxylase, phenylalanine 4-monooxygenase classically assigned the sole function of converting phenylalanine to tyrosine.	sapropterin	102-121	phenylalanine hydroxylase	Homo sapiens	165-194
31233370-11	2020	Exhaustive investigation has identified the enzyme responsible for this S-oxygenation reaction as the tetrahydrobiopterin-dependent aromatic amino acid hydroxylase, phenylalanine 4-monooxygenase classically assigned the sole function of converting phenylalanine to tyrosine.	Tyrosine	265-273	phenylalanine hydroxylase	Homo sapiens	165-194
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	leucyl-phenylalanine	171-174	phenylalanine hydroxylase	Homo sapiens	70-73
31648944-1	2019	In phenylketonuria (PKU), mutations of the phenylalanine hydroxylase (PAH) gene decrease the ability of PAH to convert phenylalanine (Phe) to tyrosine (Tyr), resulting in Phe accumulation in the blood and brain and disruption of neurotransmitter (NT) biosynthesis and metabolism.	leucyl-phenylalanine	171-174	phenylalanine hydroxylase	Homo sapiens	104-107
31703125-7	2019	CONCLUSION: Variants of the PAH gene identified in Jiangxi province mainly involve exons 7, 12, 11 and 6, with the most common variants being R243Q and R408Q.	99-408 compound	152-157	phenylalanine hydroxylase	Homo sapiens	28-31
31703458-1	2019	: Numerous studies have shown that genistein has a good therapeutic effect on pulmonary hypertension (PH).	Genistein	35-44	phenylalanine hydroxylase	Homo sapiens	102-104
31633936-1	2019	A series of homoleptic alkynyl-protected gold clusters Au22(C CR)18 were newly synthesized using 3-ethynylthiophene (ETP-H), phenylacetylene (PA-H), 3-ethynyltoluene (ET-H), and 3-ethynylanisole (EA-H).	peptide PVA	23-30	phenylalanine hydroxylase	Homo sapiens	142-146
31703458-3	2019	In this study, a systemic pharmacology approach was employed to analyze the anti-PH effect of genistein.	Genistein	94-103	phenylalanine hydroxylase	Homo sapiens	81-83
31633936-1	2019	A series of homoleptic alkynyl-protected gold clusters Au22(C CR)18 were newly synthesized using 3-ethynylthiophene (ETP-H), phenylacetylene (PA-H), 3-ethynyltoluene (ET-H), and 3-ethynylanisole (EA-H).	Gold	55-57	phenylalanine hydroxylase	Homo sapiens	142-146
31703458-5	2019	After that, the protein-protein interaction network was constructed, and the functional annotation and cluster analysis were performed to obtain the core targets and key pathways involved in exerting the anti-PH effect of genistein.	Genistein	222-231	phenylalanine hydroxylase	Homo sapiens	209-211
31759357-10	2019	In the other solutions, viscosity increase (propylene glycol solutions) and acidic pH were observed mainly in the glycerol group.	Glycerol	114-122	phenylalanine hydroxylase	Homo sapiens	83-85
31694851-6	2019	Intravenous sildenafil has reduced mortality in newborns with PH without CDH, but prospective data in CDH patients are lacking.	Sildenafil Citrate	12-22	phenylalanine hydroxylase	Homo sapiens	62-64
31789109-4	2019	Although a neglected clinical parameter, pH has implications for relatively all pathologies of wound healing affecting oxygen release, angiogenesis, protease activity, bacterial toxicity and antimicrobial activity.	Oxygen	119-125	phenylalanine hydroxylase	Homo sapiens	41-43
31255762-0	2019	Intracellularly stored polysulfur maintains homeostasis of pH and provides bioenergy for phosphorus metabolism in the sulfur-associated enhanced biological phosphorus removal (SEBPR) process.	trisulfur	23-33	phenylalanine hydroxylase	Homo sapiens	59-61
31255762-0	2019	Intracellularly stored polysulfur maintains homeostasis of pH and provides bioenergy for phosphorus metabolism in the sulfur-associated enhanced biological phosphorus removal (SEBPR) process.	Sulfur	27-33	phenylalanine hydroxylase	Homo sapiens	59-61
31255762-5	2019	The decrease in glycogen was likely because the accumulation of enough poly-S could replace glycogen to provide reducing power and buffer the inner pH.	Glycogen	16-24	phenylalanine hydroxylase	Homo sapiens	148-150
31255762-5	2019	The decrease in glycogen was likely because the accumulation of enough poly-S could replace glycogen to provide reducing power and buffer the inner pH.	poly-s	71-77	phenylalanine hydroxylase	Homo sapiens	148-150
31255762-6	2019	The results of batch tests confirmed that poly-S could adjust the intracellular protons under anaerobic conditions (pH always returned to neutral or neutral levels at the end of anaerobic phase) and provide cellular bioenergy (adenosine triphosphate, for P uptake, thereby maintaining net P removal).	poly-s	42-48	phenylalanine hydroxylase	Homo sapiens	116-118
31512136-6	2019	In range of 10.6-7.0, pH had no significant effect on CO2 absorption ratio (P > 0.05) when carbon concentration is below 9.52 mmol/L, while above 9.52 mmol/L, pH had significant effect on CO2 absorption ratio (P < 0.05).	Carbon Dioxide	188-191	phenylalanine hydroxylase	Homo sapiens	159-161
31512136-7	2019	It was found for the first time that the effect of pH on the CO2 absorption ratio was affected by carbon concentration.	Carbon Dioxide	61-64	phenylalanine hydroxylase	Homo sapiens	51-53
31512136-7	2019	It was found for the first time that the effect of pH on the CO2 absorption ratio was affected by carbon concentration.	Carbon	98-104	phenylalanine hydroxylase	Homo sapiens	51-53
31512136-8	2019	In addition, equilibrium pH, at which the CO2 partial pressure in the medium equals to that in the air, of medium with different carbon concentrations was also determined.	Carbon Dioxide	42-45	phenylalanine hydroxylase	Homo sapiens	25-27
31434173-1	2019	Phenylalanine hydroxylase from Chromobacterium violaceum (CvPAH) is a monomeric enzyme that converts phenylalanine to tyrosine.	Phenylalanine	101-114	phenylalanine hydroxylase	Homo sapiens	0-25
31512136-2	2019	However, most researches are only focused on microalgae; the effects of physicochemical factors, which are carbon concentration, medium pH, and bubbling depth, on absorption and utilization of supplied CO2 in culture is less known.	Carbon Dioxide	202-205	phenylalanine hydroxylase	Homo sapiens	136-138
31512136-4	2019	Results revealed that when medium carbon concentration increased from 4.76 to 95.24 mmol/L, CO2 absorption ratio increased by about 12%, 10%, 12%, and 11% at medium depths of 10, 20, 40, and 80 cm, with the initial pH 10.6 to 9.7 by bubbling CO2, respectively.	Carbon	34-40	phenylalanine hydroxylase	Homo sapiens	215-217
31512136-4	2019	Results revealed that when medium carbon concentration increased from 4.76 to 95.24 mmol/L, CO2 absorption ratio increased by about 12%, 10%, 12%, and 11% at medium depths of 10, 20, 40, and 80 cm, with the initial pH 10.6 to 9.7 by bubbling CO2, respectively.	Carbon Dioxide	92-95	phenylalanine hydroxylase	Homo sapiens	215-217
31512136-5	2019	As bubbling depth increased from 10 to 80 cm, CO2 absorption ratio increased by about 25%, 22%, and 25% at carbon concentrations of 4.76, 9.52, and 95.24 mmol/L, with the initial pH 10.6 to 9.7 by bubbling CO2, respectively.	Carbon Dioxide	46-49	phenylalanine hydroxylase	Homo sapiens	179-181
33015611-12	2020	Among paired samples in which predialysis total CO2 was < 22 mmol/L, the corresponding pH was acidemic (< 7.38) in just 3 of 13 (23%) instances.	Carbon Dioxide	48-51	phenylalanine hydroxylase	Homo sapiens	87-89
31621783-5	2019	Treatment with specific medication for PH (phosphodiesterase type 5 inhibitors, endothelin receptor antagonists and prostacyclin analogues) has been proven effective in patients with pulmonary arterial hypertension, but its use in patients with PH due to left heart disease can even be damaging.	Epoprostenol	116-128	phenylalanine hydroxylase	Homo sapiens	39-41
31490645-3	2019	The formulation of nanoparticulate carbon along with pH sensitive cellulose acetate phthalate as a polymeric binder is shown to produce conductive microneedles whose swelling/dissolution properties can be controlled electrochemically.	cellulose acetate phthalate	66-93	phenylalanine hydroxylase	Homo sapiens	53-55
31490645-4	2019	Through exploiting hydrogen evolution at the microneedle array, changes in local pH can induce swelling within the needle structure and could lay the foundations for a new approach to the smart device controlled delivery of therapeutic agents.	Hydrogen	19-27	phenylalanine hydroxylase	Homo sapiens	81-83
31389088-9	2019	CONCLUSIONS: Antithrombotic agent usage, postoperative pain, and two or more doses of ketorolac postoperatively were identified as independent risk factors for PH.	Ketorolac	86-95	phenylalanine hydroxylase	Homo sapiens	160-162
32186110-4	2019	The reabsorption of glucose and the excretion of para-aminohippuric acid (PAH) by HK-2 cells were also examined.	p-Aminohippuric Acid	49-72	phenylalanine hydroxylase	Homo sapiens	74-77
31434173-1	2019	Phenylalanine hydroxylase from Chromobacterium violaceum (CvPAH) is a monomeric enzyme that converts phenylalanine to tyrosine.	Tyrosine	118-126	phenylalanine hydroxylase	Homo sapiens	0-25
31541188-1	2019	Human phenylalanine hydroxylase (hPAH) hydroxylates L-phenylalanine (L-Phe) to L-tyrosine, a precursor for neurotransmitter biosynthesis.	leucyl-phenylalanine	39-67	phenylalanine hydroxylase	Homo sapiens	6-31
31541188-1	2019	Human phenylalanine hydroxylase (hPAH) hydroxylates L-phenylalanine (L-Phe) to L-tyrosine, a precursor for neurotransmitter biosynthesis.	leucyl-phenylalanine	39-67	phenylalanine hydroxylase	Homo sapiens	33-37
31541188-1	2019	Human phenylalanine hydroxylase (hPAH) hydroxylates L-phenylalanine (L-Phe) to L-tyrosine, a precursor for neurotransmitter biosynthesis.	phenylalanylphenylalanine	71-74	phenylalanine hydroxylase	Homo sapiens	6-31
31541188-1	2019	Human phenylalanine hydroxylase (hPAH) hydroxylates L-phenylalanine (L-Phe) to L-tyrosine, a precursor for neurotransmitter biosynthesis.	phenylalanylphenylalanine	71-74	phenylalanine hydroxylase	Homo sapiens	33-37
31448623-3	2019	Specifically, pH-driven charge reversal of zwitterionic carbon dots leads to immediate electrostatic conversion between the two building blocks from attraction to repulsion.	Carbon	56-62	phenylalanine hydroxylase	Homo sapiens	14-16
31551819-1	2019	Phenylketonuria (PKU) is a recessive disorder of phenylalanine metabolism due to mutations in the gene for phenylalanine hydroxylase (PAH).	phenylketonuria	0-15	phenylalanine hydroxylase	Homo sapiens	107-132
31230378-9	2019	Estimated BaPeq concentration averaged 0.072, 0.035, and 0.027 ng/m3 for outdoor, indoor, and indoor-generated individual PAH concentrations, respectively.	bapeq	10-15	phenylalanine hydroxylase	Homo sapiens	122-125
31195173-1	2019	Polycyclic aromatic hydrocarbons containing at least 24 carbon atoms (&gt;=C24-PAH) are often associated with pyrogenic processes such as combustion of fuel, wood or coal, and occur in the environment in diesel particulate matter, black carbon and coal tar.	Polycyclic Aromatic Hydrocarbons	0-32	phenylalanine hydroxylase	Homo sapiens	79-82
31195173-1	2019	Polycyclic aromatic hydrocarbons containing at least 24 carbon atoms (&gt;=C24-PAH) are often associated with pyrogenic processes such as combustion of fuel, wood or coal, and occur in the environment in diesel particulate matter, black carbon and coal tar.	Carbon	25-31	phenylalanine hydroxylase	Homo sapiens	79-82
31195173-1	2019	Polycyclic aromatic hydrocarbons containing at least 24 carbon atoms (&gt;=C24-PAH) are often associated with pyrogenic processes such as combustion of fuel, wood or coal, and occur in the environment in diesel particulate matter, black carbon and coal tar.	Carbon	56-62	phenylalanine hydroxylase	Homo sapiens	79-82
31195173-2	2019	Some of the &gt;=C24-PAH, particularly the group of dibenzopyrenes (five isomers, six aromatic rings) are known to show high mutagenic and carcinogenic activita.	dibenzopyrenes	52-66	phenylalanine hydroxylase	Homo sapiens	21-24
31203030-5	2019	The PAH concentrations in biochars ranged greatly, with the dominant proportion being 2-3 ringed PAHs (40%-71%).	pahs	97-101	phenylalanine hydroxylase	Homo sapiens	4-7
31267390-4	2019	As a result, the purified water, with lower total dissolved solids (TDS) and pH, was a suitable candidate for injection into the adjacent wells of the crude oil desalting unit.	Water	26-31	phenylalanine hydroxylase	Homo sapiens	77-79
31267390-8	2019	The analysis shows that the refined water from the reverse osmosis (RO) process was a suitable and low-cost economical option for injection in onshore and offshore fields, due to the low amount of salts, the concentration of susceptible ions in scaling formation, and the appropriate pH.	Water	36-41	phenylalanine hydroxylase	Homo sapiens	284-286
31535770-2	2019	This communication reports the facile reversible thermotriggered formation of novel pH-responsive supramolecular hydrogels based on poly(vinyl alcohol) (PVA) bonded via dynamic H-bridge with small phenolic biomolecules.	Polyvinyl Alcohol	132-151	phenylalanine hydroxylase	Homo sapiens	84-86
31535770-2	2019	This communication reports the facile reversible thermotriggered formation of novel pH-responsive supramolecular hydrogels based on poly(vinyl alcohol) (PVA) bonded via dynamic H-bridge with small phenolic biomolecules.	Polyvinyl Alcohol	153-156	phenylalanine hydroxylase	Homo sapiens	84-86
31208719-0	2019	Association between elevated placental polycyclic aromatic hydrocarbons (PAHs) and PAH-DNA adducts from Superfund sites in Harris County, and increased risk of preterm birth (PTB).	Polycyclic Aromatic Hydrocarbons	39-71	phenylalanine hydroxylase	Homo sapiens	73-76
31541188-1	2019	Human phenylalanine hydroxylase (hPAH) hydroxylates L-phenylalanine (L-Phe) to L-tyrosine, a precursor for neurotransmitter biosynthesis.	Tyrosine	79-89	phenylalanine hydroxylase	Homo sapiens	6-31
31541188-1	2019	Human phenylalanine hydroxylase (hPAH) hydroxylates L-phenylalanine (L-Phe) to L-tyrosine, a precursor for neurotransmitter biosynthesis.	Tyrosine	79-89	phenylalanine hydroxylase	Homo sapiens	33-37
31541188-4	2019	Each hPAH monomer comprises an N-terminal regulatory, a central catalytic and a C-terminal oligomerisation domain.	Nitrogen	31-32	phenylalanine hydroxylase	Homo sapiens	5-9
31541188-4	2019	Each hPAH monomer comprises an N-terminal regulatory, a central catalytic and a C-terminal oligomerisation domain.	Carbon	80-81	phenylalanine hydroxylase	Homo sapiens	5-9
31541188-5	2019	To maintain physiological L-Phe levels, hPAH employs complex regulatory mechanisms.	phenylalanylphenylalanine	28-31	phenylalanine hydroxylase	Homo sapiens	40-44
31541188-8	2019	Since a structure of activated wild-type hPAH is lacking, we addressed hPAH L-Phe-mediated conformational changes and report the first solution structure of the allosterically activated state.	phenylalanylphenylalanine	78-81	phenylalanine hydroxylase	Homo sapiens	71-75
31208719-3	2019	In this investigation, we tested the hypothesis that higher levels of exposure to PAHs and PAH-DNA adducts in placenta of women living near Superfund sites contribute to the increased rate of PTBs.	ptbs	192-196	phenylalanine hydroxylase	Homo sapiens	82-85
31208719-9	2019	In summary, this is the first report showing an association between PAH levels, DNA adducts, and modulation of endogenous metabolic pathways with PTBs in subjects residing near Superfund sites, and further studies could lead to novel strategies in the understanding of the mechanisms by which PAHs contribute to PTBs in women.	ptbs	146-150	phenylalanine hydroxylase	Homo sapiens	68-71
31208719-9	2019	In summary, this is the first report showing an association between PAH levels, DNA adducts, and modulation of endogenous metabolic pathways with PTBs in subjects residing near Superfund sites, and further studies could lead to novel strategies in the understanding of the mechanisms by which PAHs contribute to PTBs in women.	Polycyclic Aromatic Hydrocarbons	293-297	phenylalanine hydroxylase	Homo sapiens	68-71
31208719-9	2019	In summary, this is the first report showing an association between PAH levels, DNA adducts, and modulation of endogenous metabolic pathways with PTBs in subjects residing near Superfund sites, and further studies could lead to novel strategies in the understanding of the mechanisms by which PAHs contribute to PTBs in women.	ptbs	312-316	phenylalanine hydroxylase	Homo sapiens	68-71
31102715-3	2019	The residual activity of the PAH variants is the key determinant of the metabolic phenotype and BH4 responsiveness in PKU patients.	sapropterin	96-99	phenylalanine hydroxylase	Homo sapiens	29-32
31394804-8	2019	Several diagnostic PAH ratios indicated that the main sources of PAHs in Shenyang in the warm and cold seasons were not only coal burning but also vehicle emission.	Polycyclic Aromatic Hydrocarbons	65-69	phenylalanine hydroxylase	Homo sapiens	19-22
31152925-0	2019	Improving breast cancer therapy using doxorubicin loaded solid lipid nanoparticles: Synthesis of a novel arginine-glycine-aspartic tripeptide conjugated, pH sensitive lipid and evaluation of the nanomedicine in vitro and in vivo.	Doxorubicin	38-49	phenylalanine hydroxylase	Homo sapiens	154-156
31152925-0	2019	Improving breast cancer therapy using doxorubicin loaded solid lipid nanoparticles: Synthesis of a novel arginine-glycine-aspartic tripeptide conjugated, pH sensitive lipid and evaluation of the nanomedicine in vitro and in vivo.	Arginine	105-113	phenylalanine hydroxylase	Homo sapiens	154-156
31152925-0	2019	Improving breast cancer therapy using doxorubicin loaded solid lipid nanoparticles: Synthesis of a novel arginine-glycine-aspartic tripeptide conjugated, pH sensitive lipid and evaluation of the nanomedicine in vitro and in vivo.	Glycine	114-121	phenylalanine hydroxylase	Homo sapiens	154-156
31152925-0	2019	Improving breast cancer therapy using doxorubicin loaded solid lipid nanoparticles: Synthesis of a novel arginine-glycine-aspartic tripeptide conjugated, pH sensitive lipid and evaluation of the nanomedicine in vitro and in vivo.	tripeptide K-26	131-141	phenylalanine hydroxylase	Homo sapiens	154-156
31152925-2	2019	To overcome the toxic side effects and multidrug resistance (MDR) during doxorubicin (DOX) chemotherapy, an arginine-glycine-aspartic (RGD) tripeptide modified, pH-sensitive solid lipid nanoparticles (SLNs) is employed in this study.	Doxorubicin	73-84	phenylalanine hydroxylase	Homo sapiens	161-163
31152925-2	2019	To overcome the toxic side effects and multidrug resistance (MDR) during doxorubicin (DOX) chemotherapy, an arginine-glycine-aspartic (RGD) tripeptide modified, pH-sensitive solid lipid nanoparticles (SLNs) is employed in this study.	Doxorubicin	86-89	phenylalanine hydroxylase	Homo sapiens	161-163
31152925-2	2019	To overcome the toxic side effects and multidrug resistance (MDR) during doxorubicin (DOX) chemotherapy, an arginine-glycine-aspartic (RGD) tripeptide modified, pH-sensitive solid lipid nanoparticles (SLNs) is employed in this study.	Arginine	108-116	phenylalanine hydroxylase	Homo sapiens	161-163
31152925-2	2019	To overcome the toxic side effects and multidrug resistance (MDR) during doxorubicin (DOX) chemotherapy, an arginine-glycine-aspartic (RGD) tripeptide modified, pH-sensitive solid lipid nanoparticles (SLNs) is employed in this study.	Glycine	117-124	phenylalanine hydroxylase	Homo sapiens	161-163
31152925-3	2019	In this study, a RGD conjugated, pH sensitive lipid was synthesized using glycerin monostearate (GMS) and adipic acid dihydrazide (HZ) as lipid materials and named RGD-HZ-GMS.	arginyl-glycyl-aspartic acid	17-20	phenylalanine hydroxylase	Homo sapiens	33-35
31152925-3	2019	In this study, a RGD conjugated, pH sensitive lipid was synthesized using glycerin monostearate (GMS) and adipic acid dihydrazide (HZ) as lipid materials and named RGD-HZ-GMS.	glyceryl monostearate	74-95	phenylalanine hydroxylase	Homo sapiens	33-35
31152925-3	2019	In this study, a RGD conjugated, pH sensitive lipid was synthesized using glycerin monostearate (GMS) and adipic acid dihydrazide (HZ) as lipid materials and named RGD-HZ-GMS.	gms	97-100	phenylalanine hydroxylase	Homo sapiens	33-35
31152925-3	2019	In this study, a RGD conjugated, pH sensitive lipid was synthesized using glycerin monostearate (GMS) and adipic acid dihydrazide (HZ) as lipid materials and named RGD-HZ-GMS.	adipic dihydrazide	106-129	phenylalanine hydroxylase	Homo sapiens	33-35
31152925-3	2019	In this study, a RGD conjugated, pH sensitive lipid was synthesized using glycerin monostearate (GMS) and adipic acid dihydrazide (HZ) as lipid materials and named RGD-HZ-GMS.	hz	131-133	phenylalanine hydroxylase	Homo sapiens	33-35
31152925-3	2019	In this study, a RGD conjugated, pH sensitive lipid was synthesized using glycerin monostearate (GMS) and adipic acid dihydrazide (HZ) as lipid materials and named RGD-HZ-GMS.	gms	171-174	phenylalanine hydroxylase	Homo sapiens	33-35
30663162-2	2019	This technique, the most studied type of chemical exchange saturation transfer imaging, has been used successfully for imaging of protein content and pH, the latter being possible due to the strong dependence of the amide proton exchange rate on pH.	Amides	216-221	phenylalanine hydroxylase	Homo sapiens	150-152
30663162-2	2019	This technique, the most studied type of chemical exchange saturation transfer imaging, has been used successfully for imaging of protein content and pH, the latter being possible due to the strong dependence of the amide proton exchange rate on pH.	Amides	216-221	phenylalanine hydroxylase	Homo sapiens	246-248
30981068-8	2019	The stability studies conducted at room temperature suggested that carbamide peroxide nanoparticles could maintain all the parameters evaluated (size, polydispersity index, zeta potential, entrapment efficiency, pH and content) for at least 90 days.	Carbamide Peroxide	67-85	phenylalanine hydroxylase	Homo sapiens	212-214
31088083-2	2019	Herein, polynorepinephrine nanoparticles (PNE NPs) with a high photothermal conversion efficiency (eta) of 808 nm laser (67%), pH/thermal responsibility, and little to no long-term toxicity were synthesized from an endogenic neurotransmitter norepinephrine.	polynorepinephrine	8-26	phenylalanine hydroxylase	Homo sapiens	127-129
31088083-2	2019	Herein, polynorepinephrine nanoparticles (PNE NPs) with a high photothermal conversion efficiency (eta) of 808 nm laser (67%), pH/thermal responsibility, and little to no long-term toxicity were synthesized from an endogenic neurotransmitter norepinephrine.	Norepinephrine	12-26	phenylalanine hydroxylase	Homo sapiens	127-129
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Polyethylene Glycols	21-40	phenylalanine hydroxylase	Homo sapiens	163-165
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Polyethylene Glycols	21-40	phenylalanine hydroxylase	Homo sapiens	184-186
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Polyethylene Glycols	42-45	phenylalanine hydroxylase	Homo sapiens	163-165
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Polyethylene Glycols	42-45	phenylalanine hydroxylase	Homo sapiens	184-186
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Doxorubicin	64-75	phenylalanine hydroxylase	Homo sapiens	163-165
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Doxorubicin	64-75	phenylalanine hydroxylase	Homo sapiens	184-186
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Doxorubicin	77-80	phenylalanine hydroxylase	Homo sapiens	163-165
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Doxorubicin	77-80	phenylalanine hydroxylase	Homo sapiens	184-186
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	pne-peg	83-90	phenylalanine hydroxylase	Homo sapiens	163-165
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	pne-peg	83-90	phenylalanine hydroxylase	Homo sapiens	184-186
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Doxorubicin	91-94	phenylalanine hydroxylase	Homo sapiens	163-165
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Doxorubicin	91-94	phenylalanine hydroxylase	Homo sapiens	184-186
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Doxorubicin	91-94	phenylalanine hydroxylase	Homo sapiens	163-165
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Doxorubicin	91-94	phenylalanine hydroxylase	Homo sapiens	184-186
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Doxorubicin	91-94	phenylalanine hydroxylase	Homo sapiens	163-165
31088083-4	2019	After modifying with polyethylene glycol (PEG) and loading with doxorubicin (DOX), PNE-PEG@DOX could realize responsive release of DOX under either a cytolysosome pH microenvironment (pH 5.0) or an 808 nm laser irradiation, resulting in an enhanced chemotherapeutic efficacy of DOX.	Doxorubicin	91-94	phenylalanine hydroxylase	Homo sapiens	184-186
31362362-4	2019	Protection against varying pH and thermal treatments was more significant in the nanoemulsions at the elevated surfactant level, but at these high concentrations, the surface charges of the emulsions dramatically decreased under sodium salt addition, which may result in instability over time.	sodium salt	229-240	phenylalanine hydroxylase	Homo sapiens	27-29
31017011-2	2019	Urine pH is also of particular interest in stone formers, since it determines the presence of either calcium phosphate or uric acid content in stones.	calcium phosphate	101-118	phenylalanine hydroxylase	Homo sapiens	6-8
31017011-2	2019	Urine pH is also of particular interest in stone formers, since it determines the presence of either calcium phosphate or uric acid content in stones.	Uric Acid	122-131	phenylalanine hydroxylase	Homo sapiens	6-8
31017011-3	2019	Others have noted in epidemiological studies a rise in incidence of low pH-dependent uric acid stones with age, coinciding with a decrease in the incidence of high pH-dependent phosphate stones.	Uric Acid	85-94	phenylalanine hydroxylase	Homo sapiens	72-74
31017011-3	2019	Others have noted in epidemiological studies a rise in incidence of low pH-dependent uric acid stones with age, coinciding with a decrease in the incidence of high pH-dependent phosphate stones.	Phosphates	177-186	phenylalanine hydroxylase	Homo sapiens	164-166
31017011-10	2019	In fact, after adjustment for gastrointestinal anion absorption, urine pH declined more markedly, suggesting that bicarbonate-producing anion absorption is regulated in a manner that offsets the decline of urine pH.	Bicarbonates	114-125	phenylalanine hydroxylase	Homo sapiens	71-73
31017011-10	2019	In fact, after adjustment for gastrointestinal anion absorption, urine pH declined more markedly, suggesting that bicarbonate-producing anion absorption is regulated in a manner that offsets the decline of urine pH.	Bicarbonates	114-125	phenylalanine hydroxylase	Homo sapiens	212-214
31076506-5	2019	Allosteric Phe binding favors accumulation of an activated PAH tetramer conformation, which is biophysically distinct in solution.	Phenylalanine	11-14	phenylalanine hydroxylase	Homo sapiens	59-62
31076506-6	2019	Protein characterization with enzyme kinetics and intrinsic fluorescence revealed that the C29S variant and hPAH are otherwise equivalent in their response to Phe, further supported by their behavior on various chromatography resins and by analytical ultracentrifugation.	Phenylalanine	159-162	phenylalanine hydroxylase	Homo sapiens	108-112
31144503-6	2019	First, we show that the permeabilization ability of p3, but not p1, is strongly inhibited at pH 6.0 when the conserved histidines are partially charged and H17 is predominantly neutral.	p3	52-54	phenylalanine hydroxylase	Homo sapiens	93-95
31144503-6	2019	First, we show that the permeabilization ability of p3, but not p1, is strongly inhibited at pH 6.0 when the conserved histidines are partially charged and H17 is predominantly neutral.	Histidine	119-129	phenylalanine hydroxylase	Homo sapiens	93-95
31144503-11	2019	Overall, these results provide mechanistic insights into how differences in the histidine content and amphipathicity of peptides can elicit different directionality of membrane insertion and pH-dependent permeabilization.	Histidine	80-89	phenylalanine hydroxylase	Homo sapiens	191-193
31150248-0	2019	pH-Responsive Nano-Self-Assemblies of the Anticancer Drug 2-Hydroxyoleic Acid.	2-hydroxyoleic acid	58-77	phenylalanine hydroxylase	Homo sapiens	0-2
31150248-2	2019	Here, we present the design and characterization of pH-sensitive nano-self-assemblies of the poorly water-soluble anticancer drug 2-hydroxyoleic acid (2OHOA) with glycerol monooleate (GMO).	Water	100-105	phenylalanine hydroxylase	Homo sapiens	52-54
31150248-2	2019	Here, we present the design and characterization of pH-sensitive nano-self-assemblies of the poorly water-soluble anticancer drug 2-hydroxyoleic acid (2OHOA) with glycerol monooleate (GMO).	2-hydroxyoleic acid	130-149	phenylalanine hydroxylase	Homo sapiens	52-54
31150248-2	2019	Here, we present the design and characterization of pH-sensitive nano-self-assemblies of the poorly water-soluble anticancer drug 2-hydroxyoleic acid (2OHOA) with glycerol monooleate (GMO).	2-hydroxyoleic acid	151-156	phenylalanine hydroxylase	Homo sapiens	52-54
31150248-2	2019	Here, we present the design and characterization of pH-sensitive nano-self-assemblies of the poorly water-soluble anticancer drug 2-hydroxyoleic acid (2OHOA) with glycerol monooleate (GMO).	monoolein	163-182	phenylalanine hydroxylase	Homo sapiens	52-54
31150248-2	2019	Here, we present the design and characterization of pH-sensitive nano-self-assemblies of the poorly water-soluble anticancer drug 2-hydroxyoleic acid (2OHOA) with glycerol monooleate (GMO).	monoolein	184-187	phenylalanine hydroxylase	Homo sapiens	52-54
31150248-3	2019	pH-triggered nanostructural transformations from 2OHOA/GMO nanoparticles with an internal inverse hexagonal structure (hexosomes) at pH around 2.0-3.0, via nanocarriers with an internal inverse bicontinuous cubic structure (cubosomes) at pH 2.0-4.5, to vesicles at pH 4.5-7.4 were observed with synchrotron small-angle X-ray scattering, and cryogenic transmission electron microscopy.	2-hydroxyoleic acid	49-54	phenylalanine hydroxylase	Homo sapiens	0-2
31150248-3	2019	pH-triggered nanostructural transformations from 2OHOA/GMO nanoparticles with an internal inverse hexagonal structure (hexosomes) at pH around 2.0-3.0, via nanocarriers with an internal inverse bicontinuous cubic structure (cubosomes) at pH 2.0-4.5, to vesicles at pH 4.5-7.4 were observed with synchrotron small-angle X-ray scattering, and cryogenic transmission electron microscopy.	monoolein	55-58	phenylalanine hydroxylase	Homo sapiens	0-2
31150248-3	2019	pH-triggered nanostructural transformations from 2OHOA/GMO nanoparticles with an internal inverse hexagonal structure (hexosomes) at pH around 2.0-3.0, via nanocarriers with an internal inverse bicontinuous cubic structure (cubosomes) at pH 2.0-4.5, to vesicles at pH 4.5-7.4 were observed with synchrotron small-angle X-ray scattering, and cryogenic transmission electron microscopy.	monoolein	55-58	phenylalanine hydroxylase	Homo sapiens	133-135
31150248-3	2019	pH-triggered nanostructural transformations from 2OHOA/GMO nanoparticles with an internal inverse hexagonal structure (hexosomes) at pH around 2.0-3.0, via nanocarriers with an internal inverse bicontinuous cubic structure (cubosomes) at pH 2.0-4.5, to vesicles at pH 4.5-7.4 were observed with synchrotron small-angle X-ray scattering, and cryogenic transmission electron microscopy.	monoolein	55-58	phenylalanine hydroxylase	Homo sapiens	133-135
31150248-3	2019	pH-triggered nanostructural transformations from 2OHOA/GMO nanoparticles with an internal inverse hexagonal structure (hexosomes) at pH around 2.0-3.0, via nanocarriers with an internal inverse bicontinuous cubic structure (cubosomes) at pH 2.0-4.5, to vesicles at pH 4.5-7.4 were observed with synchrotron small-angle X-ray scattering, and cryogenic transmission electron microscopy.	monoolein	55-58	phenylalanine hydroxylase	Homo sapiens	133-135
31150248-4	2019	zeta-potential measurements highlight that the pH-driven deprotonation of the carboxylic group of 2OHOA, and the resulting charge-repulsions at the lipid-water interface account for these nanostructural alterations.	2-hydroxyoleic acid	98-103	phenylalanine hydroxylase	Homo sapiens	47-49
31150248-4	2019	zeta-potential measurements highlight that the pH-driven deprotonation of the carboxylic group of 2OHOA, and the resulting charge-repulsions at the lipid-water interface account for these nanostructural alterations.	Water	154-159	phenylalanine hydroxylase	Homo sapiens	47-49
31150248-5	2019	The study provides detailed insight into the pH-dependent self-assembly of 2OHOA with GMO in excess buffer at physiologically relevant pH values, and discusses the effects of pH alterations on modulating their nanostructure.	2-hydroxyoleic acid	75-80	phenylalanine hydroxylase	Homo sapiens	45-47
31150248-5	2019	The study provides detailed insight into the pH-dependent self-assembly of 2OHOA with GMO in excess buffer at physiologically relevant pH values, and discusses the effects of pH alterations on modulating their nanostructure.	2-hydroxyoleic acid	75-80	phenylalanine hydroxylase	Homo sapiens	135-137
31150248-5	2019	The study provides detailed insight into the pH-dependent self-assembly of 2OHOA with GMO in excess buffer at physiologically relevant pH values, and discusses the effects of pH alterations on modulating their nanostructure.	2-hydroxyoleic acid	75-80	phenylalanine hydroxylase	Homo sapiens	135-137
31150248-5	2019	The study provides detailed insight into the pH-dependent self-assembly of 2OHOA with GMO in excess buffer at physiologically relevant pH values, and discusses the effects of pH alterations on modulating their nanostructure.	monoolein	86-89	phenylalanine hydroxylase	Homo sapiens	45-47
31099374-3	2019	The present study aims to investigate the antitumor effect of photodynamic therapy (PDT) with PaH (PaH-PDT) on human OSCC cell lines both in vitro and in vivo.	palmatine	94-97	phenylalanine hydroxylase	Homo sapiens	99-106
31099374-6	2019	In addition, PaH-PDT markedly increased the generation of intracellular ROS, which can be suppressed using the ROS scavenger N-acetylcysteine (NAC).	ros	72-75	phenylalanine hydroxylase	Homo sapiens	13-20
31099374-6	2019	In addition, PaH-PDT markedly increased the generation of intracellular ROS, which can be suppressed using the ROS scavenger N-acetylcysteine (NAC).	ros	111-114	phenylalanine hydroxylase	Homo sapiens	13-20
31099374-6	2019	In addition, PaH-PDT markedly increased the generation of intracellular ROS, which can be suppressed using the ROS scavenger N-acetylcysteine (NAC).	Acetylcysteine	125-141	phenylalanine hydroxylase	Homo sapiens	13-20
31099374-6	2019	In addition, PaH-PDT markedly increased the generation of intracellular ROS, which can be suppressed using the ROS scavenger N-acetylcysteine (NAC).	Acetylcysteine	143-146	phenylalanine hydroxylase	Homo sapiens	13-20
31120459-1	2019	Disclosed herein is a rhodium(iii)-catalyzed novel one-step back-to-back double rollover annulation on pyridine and pyrazine backbones leading to a structurally and optoelectronically diverse class of nicely decorated multi-ring-fused, extensively pi-conjugated, N-enriched PAH molecules by virtue of orchestrated quadruple C-H activation events.	pyridine	103-111	phenylalanine hydroxylase	Homo sapiens	274-277
31120459-1	2019	Disclosed herein is a rhodium(iii)-catalyzed novel one-step back-to-back double rollover annulation on pyridine and pyrazine backbones leading to a structurally and optoelectronically diverse class of nicely decorated multi-ring-fused, extensively pi-conjugated, N-enriched PAH molecules by virtue of orchestrated quadruple C-H activation events.	Pyrazines	116-124	phenylalanine hydroxylase	Homo sapiens	274-277
31120459-1	2019	Disclosed herein is a rhodium(iii)-catalyzed novel one-step back-to-back double rollover annulation on pyridine and pyrazine backbones leading to a structurally and optoelectronically diverse class of nicely decorated multi-ring-fused, extensively pi-conjugated, N-enriched PAH molecules by virtue of orchestrated quadruple C-H activation events.	Nitrogen	263-264	phenylalanine hydroxylase	Homo sapiens	274-277
31117551-5	2019	Crystallographic, optical, electrochemical, and computational studies were performed to clarify the effect of boron-doped PAH shape, size, and structure on optoelectronic properties.	Boron	110-115	phenylalanine hydroxylase	Homo sapiens	122-125
31117551-7	2019	Finally, our study describes the first implementation of a precise three-coordinate boron-substituted PAH as an acceptor material in organic solar cells with power conversion efficiencies (PCEs) of up to 3%.	Boron	84-89	phenylalanine hydroxylase	Homo sapiens	102-105
31118288-0	2019	Structure of full-length human phenylalanine hydroxylase in complex with tetrahydrobiopterin.	sapropterin	73-92	phenylalanine hydroxylase	Homo sapiens	31-56
31118288-1	2019	Phenylalanine hydroxylase (PAH) is a key enzyme in the catabolism of phenylalanine, and mutations in this enzyme cause phenylketonuria (PKU), a genetic disorder that leads to brain damage and mental retardation if untreated.	Phenylalanine	69-82	phenylalanine hydroxylase	Homo sapiens	0-25
31118288-1	2019	Phenylalanine hydroxylase (PAH) is a key enzyme in the catabolism of phenylalanine, and mutations in this enzyme cause phenylketonuria (PKU), a genetic disorder that leads to brain damage and mental retardation if untreated.	Phenylalanine	69-82	phenylalanine hydroxylase	Homo sapiens	27-30
31118288-3	2019	Here we present structures of full-length human PAH (hPAH) both unbound and complexed with BH4 in the precatalytic state.	sapropterin	91-94	phenylalanine hydroxylase	Homo sapiens	48-51
31118288-3	2019	Here we present structures of full-length human PAH (hPAH) both unbound and complexed with BH4 in the precatalytic state.	sapropterin	91-94	phenylalanine hydroxylase	Homo sapiens	53-57
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	147-150	phenylalanine hydroxylase	Homo sapiens	96-99
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	147-150	phenylalanine hydroxylase	Homo sapiens	329-332
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	147-150	phenylalanine hydroxylase	Homo sapiens	329-332
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	96-99
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	329-332
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	329-332
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	96-99
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	329-332
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	329-332
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	96-99
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	329-332
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	329-332
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	96-99
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	329-332
31118288-4	2019	Crystal structures, solved at 3.18-A resolution, show the interactions between the cofactor and PAH, explaining the negative regulation exerted by BH4 BH4 forms several H-bonds with the N-terminal autoregulatory tail but is far from the catalytic FeII Upon BH4 binding a polar and salt-bridge interaction network links the three PAH domains, explaining the stability conferred by BH4 Importantly, BH4 binding modulates the interaction between subunits, providing information about PAH allostery.	sapropterin	151-154	phenylalanine hydroxylase	Homo sapiens	329-332
31118288-5	2019	Moreover, we also show that the cryo-EM structure of hPAH in absence of BH4 reveals a highly dynamic conformation for the tetramers.	sapropterin	72-75	phenylalanine hydroxylase	Homo sapiens	53-57
31118288-6	2019	Structural analyses of the hPAH:BH4 subunits revealed that the substrate-induced movement of Tyr138 into the active site could be coupled to the displacement of BH4 from the precatalytic toward the active conformation, a molecular mechanism that was supported by site-directed mutagenesis and targeted molecular dynamics simulations.	sapropterin	32-35	phenylalanine hydroxylase	Homo sapiens	27-31
31118288-6	2019	Structural analyses of the hPAH:BH4 subunits revealed that the substrate-induced movement of Tyr138 into the active site could be coupled to the displacement of BH4 from the precatalytic toward the active conformation, a molecular mechanism that was supported by site-directed mutagenesis and targeted molecular dynamics simulations.	sapropterin	161-164	phenylalanine hydroxylase	Homo sapiens	27-31
30831494-0	2019	Fenton-like and potassium permanganate oxidations of PAH-contaminated soils: Impact of oxidant doses on PAH and polar PAC (polycyclic aromatic compound) behavior.	Potassium	16-25	phenylalanine hydroxylase	Homo sapiens	53-56
30831494-1	2019	Potassium permanganate and Fenton-like oxidations were applied on two PAH-contaminated soils collected on former coking plant and gas plant sites.	Potassium Permanganate	0-22	phenylalanine hydroxylase	Homo sapiens	70-73
30831494-5	2019	However, permanganate treatment resulted in incomplete PAH degradation, leading to the formation of O-PACs, that was limited with the application of higher dose.	o-pacs	100-106	phenylalanine hydroxylase	Homo sapiens	55-58
30992364-0	2019	Tau repeat regions contain conserved histidine residues that modulate microtubule-binding in response to changes in pH.	Histidine	37-46	phenylalanine hydroxylase	Homo sapiens	116-118
31038957-0	2019	Uncovered Dynamic Coupling Resolves the Ambiguous Mechanism of Phenylalanine Hydroxylase Oxygen Binding.	Oxygen	89-95	phenylalanine hydroxylase	Homo sapiens	63-88
31038957-1	2019	Phenylalanine hydroxylase (PAH) is an iron enzyme catalyzing the oxidation of l-Phe to l-Tyr during phenylalanine catabolism.	Iron	38-42	phenylalanine hydroxylase	Homo sapiens	0-25
31038957-1	2019	Phenylalanine hydroxylase (PAH) is an iron enzyme catalyzing the oxidation of l-Phe to l-Tyr during phenylalanine catabolism.	Iron	38-42	phenylalanine hydroxylase	Homo sapiens	27-30
31038957-1	2019	Phenylalanine hydroxylase (PAH) is an iron enzyme catalyzing the oxidation of l-Phe to l-Tyr during phenylalanine catabolism.	Phenylalanine	78-83	phenylalanine hydroxylase	Homo sapiens	0-25
31038957-1	2019	Phenylalanine hydroxylase (PAH) is an iron enzyme catalyzing the oxidation of l-Phe to l-Tyr during phenylalanine catabolism.	Phenylalanine	78-83	phenylalanine hydroxylase	Homo sapiens	27-30
31038957-1	2019	Phenylalanine hydroxylase (PAH) is an iron enzyme catalyzing the oxidation of l-Phe to l-Tyr during phenylalanine catabolism.	Tyrosine	87-92	phenylalanine hydroxylase	Homo sapiens	0-25
31038957-1	2019	Phenylalanine hydroxylase (PAH) is an iron enzyme catalyzing the oxidation of l-Phe to l-Tyr during phenylalanine catabolism.	Tyrosine	87-92	phenylalanine hydroxylase	Homo sapiens	27-30
31038957-1	2019	Phenylalanine hydroxylase (PAH) is an iron enzyme catalyzing the oxidation of l-Phe to l-Tyr during phenylalanine catabolism.	Phenylalanine	100-113	phenylalanine hydroxylase	Homo sapiens	0-25
31038957-1	2019	Phenylalanine hydroxylase (PAH) is an iron enzyme catalyzing the oxidation of l-Phe to l-Tyr during phenylalanine catabolism.	Phenylalanine	100-113	phenylalanine hydroxylase	Homo sapiens	27-30
31038957-3	2019	Despite intensive study, there is no consensus on the atomistic details of the mechanism of O2 binding and splitting by wild-type (WT) PAH and how it varies with PKU-inducing mutations, Arg158Gln and Glu280Lys.	Oxygen	92-94	phenylalanine hydroxylase	Homo sapiens	135-138
30642159-0	2019	Dextran-Coated Iron Oxide Nanoparticles as Biomimetic Catalysts for Localized and pH-Activated Biofilm Disruption.	Dextrans	0-7	phenylalanine hydroxylase	Homo sapiens	82-84
30642159-0	2019	Dextran-Coated Iron Oxide Nanoparticles as Biomimetic Catalysts for Localized and pH-Activated Biofilm Disruption.	ferric oxide	15-25	phenylalanine hydroxylase	Homo sapiens	82-84
30642159-5	2019	Here, we report dextran-coated iron oxide nanoparticles termed nanozymes (Dex-NZM) that display strong catalytic (peroxidase-like) activity at acidic pH values, target biofilms with high specificity, and prevent severe caries without impacting surrounding oral tissues in vivo.	Dextrans	16-23	phenylalanine hydroxylase	Homo sapiens	150-152
30642159-5	2019	Here, we report dextran-coated iron oxide nanoparticles termed nanozymes (Dex-NZM) that display strong catalytic (peroxidase-like) activity at acidic pH values, target biofilms with high specificity, and prevent severe caries without impacting surrounding oral tissues in vivo.	ferric oxide	31-41	phenylalanine hydroxylase	Homo sapiens	150-152
30992364-4	2019	Here, we used molecular dynamics, microtubule-binding experiments, and live-cell microscopy, revealing that highly-conserved histidine residues near the C terminus of each microtubule-binding repeat are pH sensors that can modulate tau-microtubule interaction strength within the physiological intracellular pH range.	Histidine	125-134	phenylalanine hydroxylase	Homo sapiens	203-205
30992364-4	2019	Here, we used molecular dynamics, microtubule-binding experiments, and live-cell microscopy, revealing that highly-conserved histidine residues near the C terminus of each microtubule-binding repeat are pH sensors that can modulate tau-microtubule interaction strength within the physiological intracellular pH range.	Histidine	125-134	phenylalanine hydroxylase	Homo sapiens	308-310
30992364-5	2019	We observed that at low pH (<7.5), these histidines are positively charged and interact with phenylalanine residues in a hydrophobic cleft between adjacent tubulin dimers.	Histidine	41-51	phenylalanine hydroxylase	Homo sapiens	24-26
30992364-5	2019	We observed that at low pH (<7.5), these histidines are positively charged and interact with phenylalanine residues in a hydrophobic cleft between adjacent tubulin dimers.	Phenylalanine	93-106	phenylalanine hydroxylase	Homo sapiens	24-26
30916949-0	2019	Mechanism of Action of Peptides That Cause the pH-Triggered Macromolecular Poration of Lipid Bilayers.	Lipid Bilayers	87-101	phenylalanine hydroxylase	Homo sapiens	47-49
31042010-1	2019	BACKGROUND: Pulmonary arterial hypertension (PAH) is characterised by pulmonary vascular changes, leads to elevated pulmonary artery pressures, dyspnoea, a reduction in exercise tolerance, right heart failure, and ultimately death.Prostacyclin analogue drugs mimic endogenous prostacyclin which leads to vasodilation, inhibition of platelet aggregation, and reversal of vascular remodelling.	Epoprostenol	231-243	phenylalanine hydroxylase	Homo sapiens	45-48
31042010-1	2019	BACKGROUND: Pulmonary arterial hypertension (PAH) is characterised by pulmonary vascular changes, leads to elevated pulmonary artery pressures, dyspnoea, a reduction in exercise tolerance, right heart failure, and ultimately death.Prostacyclin analogue drugs mimic endogenous prostacyclin which leads to vasodilation, inhibition of platelet aggregation, and reversal of vascular remodelling.	Epoprostenol	276-288	phenylalanine hydroxylase	Homo sapiens	45-48
30916949-5	2019	In vesicles, 50% leakage of 40 kDa dextrans occurs at 1 bound peptide per 1300 lipids or only 75 peptides per vesicle, an observation that holds true across a wide range of acidic pH values.	Dextrans	35-43	phenylalanine hydroxylase	Homo sapiens	180-182
31105574-1	2019	Phenylketonuria (PKU) is an inherited metabolic disease characterized by abnormally high concentrations of the essential amino acid L-phenylalanine (Phe) in blood plasma caused by reduced activity of phenylalanine hydroxylase (PAH).	essential amino acid l-phenylalanine	111-147	phenylalanine hydroxylase	Homo sapiens	200-225
30901212-4	2019	We summarize developments of electrochemical pH sensors that by virtue of their optimized material chemistries (from metal oxides to polymers) and geometrical features (from thin films to quantum dots) enable their adoption in biomedical applications.	metal oxides	117-129	phenylalanine hydroxylase	Homo sapiens	45-47
30901212-4	2019	We summarize developments of electrochemical pH sensors that by virtue of their optimized material chemistries (from metal oxides to polymers) and geometrical features (from thin films to quantum dots) enable their adoption in biomedical applications.	Polymers	133-141	phenylalanine hydroxylase	Homo sapiens	45-47
31105574-1	2019	Phenylketonuria (PKU) is an inherited metabolic disease characterized by abnormally high concentrations of the essential amino acid L-phenylalanine (Phe) in blood plasma caused by reduced activity of phenylalanine hydroxylase (PAH).	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	200-225
31275726-5	2019	A significant reduction (35%) was observed in the PAH level as the perilla oil was removed from the mixed oil composition and roasting continued at 350  C for 10 s. These results show that the composition of the mixing oil and the parameters of the heat treatment are crucial factors that contribute to the formation of PAHs in roasted laver.	perilla seed oil	67-78	phenylalanine hydroxylase	Homo sapiens	50-53
30864096-1	2019	Phenylalanine hydroxylase (PAH) deficiency is an inborn error of metabolism that results in elevated phenylalanine levels in blood.	Phenylalanine	101-114	phenylalanine hydroxylase	Homo sapiens	0-25
30648773-1	2019	Phenylketonuria (PKU) is a genetic disorder caused by variants in the gene encoding phenylalanine hydroxylase (PAH), resulting in accumulation of phenylalanine to neurotoxic levels.	Phenylalanine	84-97	phenylalanine hydroxylase	Homo sapiens	111-114
30648773-5	2019	In all cases, PAH variants were stabilized by the cofactor tetrahydrobiopterin (BH4 ), a molecule known to alleviate symptoms in certain PKU patients.	sapropterin	59-78	phenylalanine hydroxylase	Homo sapiens	14-17
30648773-5	2019	In all cases, PAH variants were stabilized by the cofactor tetrahydrobiopterin (BH4 ), a molecule known to alleviate symptoms in certain PKU patients.	sapropterin	80-83	phenylalanine hydroxylase	Homo sapiens	14-17
30667594-4	2019	This is achieved by leveraging chitosan, a stimulus responsive polyaminosaccharide that undergoes a sol-gel transition driven by a change of pH.	polyaminosaccharide	63-82	phenylalanine hydroxylase	Homo sapiens	141-143
30485152-12	2019	Water only decontamination did not appear to be effective, resulting in an overall 42% increase in PAH contamination.	Water	0-5	phenylalanine hydroxylase	Homo sapiens	99-102
30504004-1	2019	Phenylketonuria (PKU) is an autosomal recessive inborn error of phenylalanine (phe) metabolism caused by a deficiency in the enzyme phenylalanine hydroxylase that converts phe into tyrosine.	Phenylalanine	64-67	phenylalanine hydroxylase	Homo sapiens	132-157
30504004-1	2019	Phenylketonuria (PKU) is an autosomal recessive inborn error of phenylalanine (phe) metabolism caused by a deficiency in the enzyme phenylalanine hydroxylase that converts phe into tyrosine.	Phenylalanine	79-82	phenylalanine hydroxylase	Homo sapiens	132-157
30504004-1	2019	Phenylketonuria (PKU) is an autosomal recessive inborn error of phenylalanine (phe) metabolism caused by a deficiency in the enzyme phenylalanine hydroxylase that converts phe into tyrosine.	Tyrosine	181-189	phenylalanine hydroxylase	Homo sapiens	132-157
30674554-4	2019	Analytical ultracentrifugation establishes that the isolated regulatory domain of R68S PheH is predominantly monomeric in the absence of phenylalanine and dimerizes in its presence, similar to the regulatory domain of the WT enzyme.	Phenylalanine	137-150	phenylalanine hydroxylase	Homo sapiens	87-91
33405653-1	2019	Hyperbranched polymer-derived drug nanocarriers have been synthesized that can change sizes selectively in response to pH.	Polymers	14-21	phenylalanine hydroxylase	Homo sapiens	119-121
33405653-4	2019	Upon lowering of pH, these larger aggregates disassembled into smaller nanoparticles with diameters of 3-5 nm as directed by protonation of tertiary amine side-chains.	Amines	149-154	phenylalanine hydroxylase	Homo sapiens	17-19
31275726-5	2019	A significant reduction (35%) was observed in the PAH level as the perilla oil was removed from the mixed oil composition and roasting continued at 350  C for 10 s. These results show that the composition of the mixing oil and the parameters of the heat treatment are crucial factors that contribute to the formation of PAHs in roasted laver.	Oils	75-78	phenylalanine hydroxylase	Homo sapiens	50-53
30293161-5	2019	This review summarized that (1) the roles of PAHs in asthma-work as risk factors; (2) the possible mechanisms involved in PAH-related asthma-through immunologic and oxidative stress changes; (3) the interactions between PAHs and EPHX1 involved in asthma-enzymatic activity of epoxide hydrolase 1, which affected by EPHX1 genotypes/SNPs/diplotypes, could influence human PAH metabolism and people"s vulnerability to PAH exposure.	Polycyclic Aromatic Hydrocarbons	45-49	phenylalanine hydroxylase	Homo sapiens	122-125
30718522-1	2019	Scleractinian corals promote the precipitation of their carbonate skeleton by elevating the pH and dissolved inorganic carbon (DIC) concentration of their calcifying fluid above that of seawater.	Carbonates	56-65	phenylalanine hydroxylase	Homo sapiens	92-94
30556205-7	2019	The applications of PA contrast agents as biosensors (in the sensing of metal ions, pH, enzymes, temperature, hypoxia, reactive oxygen species, and reactive nitrogen species) and in bioimaging (lymph nodes, vasculature, tumors, and brain tissue) are discussed in detail.	Protactinium	20-22	phenylalanine hydroxylase	Homo sapiens	84-86
30554387-4	2019	In this review, the genes involved in the biodegradation of hydrocarbons and several emerging plasticizer compounds in Rhodococcus strains are described in detail (aliphatic, aromatics, PAH, phthalate, polyethylene, and polyisoprene).	Hydrocarbons	60-72	phenylalanine hydroxylase	Homo sapiens	186-189
30293161-5	2019	This review summarized that (1) the roles of PAHs in asthma-work as risk factors; (2) the possible mechanisms involved in PAH-related asthma-through immunologic and oxidative stress changes; (3) the interactions between PAHs and EPHX1 involved in asthma-enzymatic activity of epoxide hydrolase 1, which affected by EPHX1 genotypes/SNPs/diplotypes, could influence human PAH metabolism and people"s vulnerability to PAH exposure.	Polycyclic Aromatic Hydrocarbons	45-49	phenylalanine hydroxylase	Homo sapiens	122-125
30293161-5	2019	This review summarized that (1) the roles of PAHs in asthma-work as risk factors; (2) the possible mechanisms involved in PAH-related asthma-through immunologic and oxidative stress changes; (3) the interactions between PAHs and EPHX1 involved in asthma-enzymatic activity of epoxide hydrolase 1, which affected by EPHX1 genotypes/SNPs/diplotypes, could influence human PAH metabolism and people"s vulnerability to PAH exposure.	Polycyclic Aromatic Hydrocarbons	220-224	phenylalanine hydroxylase	Homo sapiens	122-125
30293161-5	2019	This review summarized that (1) the roles of PAHs in asthma-work as risk factors; (2) the possible mechanisms involved in PAH-related asthma-through immunologic and oxidative stress changes; (3) the interactions between PAHs and EPHX1 involved in asthma-enzymatic activity of epoxide hydrolase 1, which affected by EPHX1 genotypes/SNPs/diplotypes, could influence human PAH metabolism and people"s vulnerability to PAH exposure.	Polycyclic Aromatic Hydrocarbons	220-224	phenylalanine hydroxylase	Homo sapiens	122-125
30353623-0	2019	Linaclotide increases cecal pH, accelerates colonic transit, and increases colonic motility in irritable bowel syndrome with constipation.	linaclotide	0-11	phenylalanine hydroxylase	Homo sapiens	28-30
30132871-3	2019	In this study, we found that treatment with human placental hydrolysate (hPH) significantly increased the viability (approximately 15%) of H2 O2 -stimulated C2C12 cells.	Hydrogen Peroxide	139-144	phenylalanine hydroxylase	Homo sapiens	73-76
30132871-5	2019	We further showed that hPH treatment effectively inhibited H2 O2 -induced cell death.	Hydrogen Peroxide	59-64	phenylalanine hydroxylase	Homo sapiens	23-26
30132871-7	2019	Exposure of C2C12 cells to H2 O2 induced abundant production of intracellular ROS, mitochondrial superoxide, and mitochondrial dysfunction as well as myostatin expression via nuclear factor-kappaB (NF-kappaB) signaling; these effects were attenuated by hPH.	Hydrogen Peroxide	27-32	phenylalanine hydroxylase	Homo sapiens	253-256
30353623-2	2019	The primary aim of the study was to examine the effect of linaclotide on change in pH across the ileocecal junction (ICJ), a proposed measure of cecal fermentation, and its relationship to symptoms and quality of life (QoL) in IBS-C. METHODS: A total of 13 participants with Rome III IBS-C underwent a standardized wireless motility capsule (WMC).	linaclotide	58-69	phenylalanine hydroxylase	Homo sapiens	83-85
30353623-6	2019	KEY RESULTS: Linaclotide reduced the change in pH across the ICJ (-2.4 +- 0.2 vs -2.1 +- 0.4, P = 0.01) as a function of a relative alkalinization of the cecum (5.2 +- 0.2 vs 5.5 +- 0.3, P = 0.02).	linaclotide	13-24	phenylalanine hydroxylase	Homo sapiens	47-49
30353623-9	2019	CONCLUSIONS & INFERENCES: Linaclotide"s effects are confined to the colon where it increases cecal pH, potentially representing a reduction in cecal fermentation and accelerates colonic motility.	linaclotide	26-37	phenylalanine hydroxylase	Homo sapiens	99-101
30592213-0	2019	Computational Study of the pH-Dependent Competition between Carbonate and Thymine Addition to the Guanine Radical.	Carbonates	60-69	phenylalanine hydroxylase	Homo sapiens	27-29
30592213-0	2019	Computational Study of the pH-Dependent Competition between Carbonate and Thymine Addition to the Guanine Radical.	Thymine	74-81	phenylalanine hydroxylase	Homo sapiens	27-29
30592213-0	2019	Computational Study of the pH-Dependent Competition between Carbonate and Thymine Addition to the Guanine Radical.	guanine radical	98-113	phenylalanine hydroxylase	Homo sapiens	27-29
30592213-2	2019	The ratio of thymine addition to carbonate addition depends strongly on the pH.	Thymine	13-20	phenylalanine hydroxylase	Homo sapiens	76-78
30592213-2	2019	The ratio of thymine addition to carbonate addition depends strongly on the pH.	Carbonates	33-42	phenylalanine hydroxylase	Homo sapiens	76-78
30592213-6	2019	Deprotonation of thymine is required for nucleophilic addition at C8 of guanine radical, and thus is favored at higher pH.	Thymine	17-24	phenylalanine hydroxylase	Homo sapiens	119-121
30592213-6	2019	Deprotonation of thymine is required for nucleophilic addition at C8 of guanine radical, and thus is favored at higher pH.	guanine radical	72-87	phenylalanine hydroxylase	Homo sapiens	119-121
30592213-9	2019	At pH 2.5, guanine radical cation can be formed by oxidization with sulfate radical.	guanine radical	11-26	phenylalanine hydroxylase	Homo sapiens	3-5
30592213-9	2019	At pH 2.5, guanine radical cation can be formed by oxidization with sulfate radical.	sulfate radical	68-83	phenylalanine hydroxylase	Homo sapiens	3-5
30592213-10	2019	Water addition to guanine radical cation is the preferred path for forming 8oxoG at pH 2.5.	Water	0-5	phenylalanine hydroxylase	Homo sapiens	84-86
30592213-10	2019	Water addition to guanine radical cation is the preferred path for forming 8oxoG at pH 2.5.	guanine radical	18-33	phenylalanine hydroxylase	Homo sapiens	84-86
30668579-3	2019	To date, BH4, a cofactor of PAH, has not been used to treat PKU in Russia.Genotype data of patients with PKU can be used to predict their sensitivity to BH4 therapy.	sapropterin	9-12	phenylalanine hydroxylase	Homo sapiens	28-31
30668579-3	2019	To date, BH4, a cofactor of PAH, has not been used to treat PKU in Russia.Genotype data of patients with PKU can be used to predict their sensitivity to BH4 therapy.	sapropterin	153-156	phenylalanine hydroxylase	Homo sapiens	28-31
31655738-0	2019	Dissimilatory reduction of sulfate and zero-valent sulfur at low pH and its significance for bioremediation and metal recovery.	Metals	112-117	phenylalanine hydroxylase	Homo sapiens	65-67
30668579-2	2019	Furthermore, numerous studies on BH4-sensitive PAH deficiency have been conducted.	sapropterin	33-36	phenylalanine hydroxylase	Homo sapiens	47-50
31655738-2	2019	In cases where zero-valent (elemental) sulfur, sulfate and other oxidized forms are used as electron acceptor in (primarily) anaerobic microbial metabolisms, the end product is hydrogen sulfide (HS- or H2S, dependent on pH).	Sulfur	39-45	phenylalanine hydroxylase	Homo sapiens	220-222
31655738-0	2019	Dissimilatory reduction of sulfate and zero-valent sulfur at low pH and its significance for bioremediation and metal recovery.	Sulfates	27-34	phenylalanine hydroxylase	Homo sapiens	65-67
31655738-2	2019	In cases where zero-valent (elemental) sulfur, sulfate and other oxidized forms are used as electron acceptor in (primarily) anaerobic microbial metabolisms, the end product is hydrogen sulfide (HS- or H2S, dependent on pH).	Sulfates	47-54	phenylalanine hydroxylase	Homo sapiens	220-222
31655738-0	2019	Dissimilatory reduction of sulfate and zero-valent sulfur at low pH and its significance for bioremediation and metal recovery.	Sulfur	51-57	phenylalanine hydroxylase	Homo sapiens	65-67
31655738-2	2019	In cases where zero-valent (elemental) sulfur, sulfate and other oxidized forms are used as electron acceptor in (primarily) anaerobic microbial metabolisms, the end product is hydrogen sulfide (HS- or H2S, dependent on pH).	Hydrogen Sulfide	177-193	phenylalanine hydroxylase	Homo sapiens	220-222
31655738-2	2019	In cases where zero-valent (elemental) sulfur, sulfate and other oxidized forms are used as electron acceptor in (primarily) anaerobic microbial metabolisms, the end product is hydrogen sulfide (HS- or H2S, dependent on pH).	Hydrogen	195-197	phenylalanine hydroxylase	Homo sapiens	220-222
31655738-2	2019	In cases where zero-valent (elemental) sulfur, sulfate and other oxidized forms are used as electron acceptor in (primarily) anaerobic microbial metabolisms, the end product is hydrogen sulfide (HS- or H2S, dependent on pH).	Deuterium	202-205	phenylalanine hydroxylase	Homo sapiens	220-222
31655738-4	2019	This review outlines the background and current status of the biodiversity and metabolisms of sulfate- and sulfur-reducing prokaryotes that are metabolically active in low pH environments, and describes the developing technologies in which they are being used to remediate acidic waste waters (which are often metal-contaminated) and to recover metal resources.	Sulfates	94-101	phenylalanine hydroxylase	Homo sapiens	172-174
31655738-4	2019	This review outlines the background and current status of the biodiversity and metabolisms of sulfate- and sulfur-reducing prokaryotes that are metabolically active in low pH environments, and describes the developing technologies in which they are being used to remediate acidic waste waters (which are often metal-contaminated) and to recover metal resources.	Sulfur	107-113	phenylalanine hydroxylase	Homo sapiens	172-174
29726916-12	2019	Histological changes in the epithelium and lamina propria, caused by fractional CO2 laser treatments, correlated with clinical restoration of vaginal hydration and pH to premenopausal levels.	Carbon Dioxide	80-83	phenylalanine hydroxylase	Homo sapiens	164-166
30578407-1	2018	Phenylalanine hydroxylase catalyzes a critical step in the phenylalanine catabolic pathway, and impairment of the human enzyme is linked to phenylketonuria.	Phenylalanine	59-72	phenylalanine hydroxylase	Homo sapiens	0-25
30562731-6	2019	CONCLUSION: The protein binding of PBUTs can be decreased by higher ionic strength, increased pH and the presence of some chemical displacers, including free fatty acids.	pbuts	35-40	phenylalanine hydroxylase	Homo sapiens	94-96
31208951-1	2019	BACKGROUND: Phenylketonuria (PKU) is due to the deficit of the enzyme phenylalanine hydroxylase, the first step of dopamine synthesis.	Dopamine	115-123	phenylalanine hydroxylase	Homo sapiens	70-95
30287685-0	2018	Simulations of the regulatory ACT domain of human phenylalanine hydroxylase (PAH) unveil its mechanism of phenylalanine binding.	Phenylalanine	50-63	phenylalanine hydroxylase	Homo sapiens	77-80
30287685-1	2018	Phenylalanine hydroxylase (PAH) regulates phenylalanine (Phe) levels in mammals to prevent neurotoxicity resulting from high Phe concentrations as observed in genetic disorders leading to hyperphenylalaninemia and phenylketonuria.	Phenylalanine	42-55	phenylalanine hydroxylase	Homo sapiens	0-25
30287685-1	2018	Phenylalanine hydroxylase (PAH) regulates phenylalanine (Phe) levels in mammals to prevent neurotoxicity resulting from high Phe concentrations as observed in genetic disorders leading to hyperphenylalaninemia and phenylketonuria.	Phenylalanine	42-55	phenylalanine hydroxylase	Homo sapiens	27-30
30287685-1	2018	Phenylalanine hydroxylase (PAH) regulates phenylalanine (Phe) levels in mammals to prevent neurotoxicity resulting from high Phe concentrations as observed in genetic disorders leading to hyperphenylalaninemia and phenylketonuria.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	27-30
30287685-1	2018	Phenylalanine hydroxylase (PAH) regulates phenylalanine (Phe) levels in mammals to prevent neurotoxicity resulting from high Phe concentrations as observed in genetic disorders leading to hyperphenylalaninemia and phenylketonuria.	Phenylalanine	57-60	phenylalanine hydroxylase	Homo sapiens	0-25
30287685-1	2018	Phenylalanine hydroxylase (PAH) regulates phenylalanine (Phe) levels in mammals to prevent neurotoxicity resulting from high Phe concentrations as observed in genetic disorders leading to hyperphenylalaninemia and phenylketonuria.	Phenylalanine	57-60	phenylalanine hydroxylase	Homo sapiens	27-30
30287685-2	2018	PAH senses elevated Phe concentrations by transient allosteric Phe binding to a protein-protein interface between ACT domains of different subunits in a PAH tetramer.	Phenylalanine	20-23	phenylalanine hydroxylase	Homo sapiens	0-3
30287685-2	2018	PAH senses elevated Phe concentrations by transient allosteric Phe binding to a protein-protein interface between ACT domains of different subunits in a PAH tetramer.	Phenylalanine	20-23	phenylalanine hydroxylase	Homo sapiens	153-156
30287685-2	2018	PAH senses elevated Phe concentrations by transient allosteric Phe binding to a protein-protein interface between ACT domains of different subunits in a PAH tetramer.	Phenylalanine	63-66	phenylalanine hydroxylase	Homo sapiens	0-3
30287685-2	2018	PAH senses elevated Phe concentrations by transient allosteric Phe binding to a protein-protein interface between ACT domains of different subunits in a PAH tetramer.	Phenylalanine	63-66	phenylalanine hydroxylase	Homo sapiens	153-156
30433759-3	2018	This work demonstrates that adsorption of protonated poly(allylamine) (PAH)/poly(4-styrenesulfonate) (PSS) multilayers on Nafion membranes leads to high K+/Li+ selectivities in Donnan dialysis, where K+ and Li+ ions in a source phase pass through the membrane and exchange with Na+ ions in a receiving phase.	polyallylamine	53-69	phenylalanine hydroxylase	Homo sapiens	71-74
30433759-3	2018	This work demonstrates that adsorption of protonated poly(allylamine) (PAH)/poly(4-styrenesulfonate) (PSS) multilayers on Nafion membranes leads to high K+/Li+ selectivities in Donnan dialysis, where K+ and Li+ ions in a source phase pass through the membrane and exchange with Na+ ions in a receiving phase.	poly(4-styrenesulfonate)	76-100	phenylalanine hydroxylase	Homo sapiens	71-74
30433759-3	2018	This work demonstrates that adsorption of protonated poly(allylamine) (PAH)/poly(4-styrenesulfonate) (PSS) multilayers on Nafion membranes leads to high K+/Li+ selectivities in Donnan dialysis, where K+ and Li+ ions in a source phase pass through the membrane and exchange with Na+ ions in a receiving phase.	perfluorosulfonic acid	122-128	phenylalanine hydroxylase	Homo sapiens	71-74
30433759-4	2018	Addition of 0.01 M HNO3 to a source phase containing 0.01 M KNO3 and 0.01 M LiNO3 increases the K+/Li+ selectivity from 8 to ~60 through (PAH/PSS)5PAH-coated Nafion membranes, primarily because of a &gt;=fivefold increase in K+ flux.	Nitric Acid	19-23	phenylalanine hydroxylase	Homo sapiens	138-141
30433759-4	2018	Addition of 0.01 M HNO3 to a source phase containing 0.01 M KNO3 and 0.01 M LiNO3 increases the K+/Li+ selectivity from 8 to ~60 through (PAH/PSS)5PAH-coated Nafion membranes, primarily because of a &gt;=fivefold increase in K+ flux.	Lithium nitrate	76-81	phenylalanine hydroxylase	Homo sapiens	138-141
30433759-4	2018	Addition of 0.01 M HNO3 to a source phase containing 0.01 M KNO3 and 0.01 M LiNO3 increases the K+/Li+ selectivity from 8 to ~60 through (PAH/PSS)5PAH-coated Nafion membranes, primarily because of a &gt;=fivefold increase in K+ flux.	5pah	146-150	phenylalanine hydroxylase	Homo sapiens	138-141
30433759-7	2018	In situ ellipsometry data indicate that PAH/PSS multilayers (assembled at pH 2.3, 7.5, or 9.3) swell at pH 2.0, and this swelling may open cation-exchange sites that preferentially bind K+ to enable highly selective transport.	pss	44-47	phenylalanine hydroxylase	Homo sapiens	40-43
30247042-1	2018	A molecular theory has been applied to study the equilibrium conditions of glyphosate and aminomethylphosphonic acid (AMPA) adsorption from aqueous solutions to hydrogel films of cross-linked polyallylamine (PAH).	glyphosate	75-85	phenylalanine hydroxylase	Homo sapiens	208-211
30346142-1	2018	Liver phenylalanine hydroxylase (PheH) is an allosteric enzyme that is activated by phenylalanine.	Phenylalanine	6-19	phenylalanine hydroxylase	Homo sapiens	33-37
30346142-9	2018	The kinetics of activation of PheH are biphasic over a range of phenylalanine concentrations.	Phenylalanine	64-77	phenylalanine hydroxylase	Homo sapiens	30-34
30201326-14	2018	However, PAH deficient MSCs cultured in 1200 muM PHE (metric defining classical PKU) show significantly reduced mineralization.	Phenylalanine	49-52	phenylalanine hydroxylase	Homo sapiens	9-12
30247042-1	2018	A molecular theory has been applied to study the equilibrium conditions of glyphosate and aminomethylphosphonic acid (AMPA) adsorption from aqueous solutions to hydrogel films of cross-linked polyallylamine (PAH).	2-amino-3-(3-hydrox-5(2-methyl-2H-tetrazol-5-yl)isoxazol-4-yl)propionic acid	90-116	phenylalanine hydroxylase	Homo sapiens	208-211
30247042-1	2018	A molecular theory has been applied to study the equilibrium conditions of glyphosate and aminomethylphosphonic acid (AMPA) adsorption from aqueous solutions to hydrogel films of cross-linked polyallylamine (PAH).	2-amino-3-(3-hydrox-5(2-methyl-2H-tetrazol-5-yl)isoxazol-4-yl)propionic acid	118-122	phenylalanine hydroxylase	Homo sapiens	208-211
30247042-1	2018	A molecular theory has been applied to study the equilibrium conditions of glyphosate and aminomethylphosphonic acid (AMPA) adsorption from aqueous solutions to hydrogel films of cross-linked polyallylamine (PAH).	polyallylamine	192-206	phenylalanine hydroxylase	Homo sapiens	208-211
30247042-9	2018	Thus, PAH hydrogel films can be considered as functional materials that combine glyphosate sequestration and in situ degradation.	glyphosate	80-90	phenylalanine hydroxylase	Homo sapiens	6-9
30961089-1	2018	Hydrogen peroxide (H2O2)-sensitive layer-by-layer films were prepared based on combining phenyl boronic acid (PBA)-modified poly(allylamine) (PAH) with shikimic acid (SA)-modified-PAH through boronate ester bonds.	Hydrogen Peroxide	0-17	phenylalanine hydroxylase	Homo sapiens	142-145
30961089-1	2018	Hydrogen peroxide (H2O2)-sensitive layer-by-layer films were prepared based on combining phenyl boronic acid (PBA)-modified poly(allylamine) (PAH) with shikimic acid (SA)-modified-PAH through boronate ester bonds.	Hydrogen Peroxide	0-17	phenylalanine hydroxylase	Homo sapiens	180-183
29721595-2	2018	Low hydrocarbon levels were observed and naphthalene was the most representative PAH.	naphthalene	41-52	phenylalanine hydroxylase	Homo sapiens	81-84
29654578-0	2018	Functional Characterization of Novel Phenylalanine Hydroxylase p.Gln226Lys Mutation Revealed Its Non-responsiveness to Tetrahydrobiopterin Treatment in Hepatoma Cellular Model.	sapropterin	119-138	phenylalanine hydroxylase	Homo sapiens	37-62
29654578-3	2018	Given that some PAH mutations are responsive to BH4 treatment while others are non-responsive, for every novel mutation that is discovered it is essential to confirm its pathogenic effect and to assess its responsiveness to a BH4 treatment in vitro, before the drug is administered to patients.	sapropterin	48-51	phenylalanine hydroxylase	Homo sapiens	16-19
29654578-3	2018	Given that some PAH mutations are responsive to BH4 treatment while others are non-responsive, for every novel mutation that is discovered it is essential to confirm its pathogenic effect and to assess its responsiveness to a BH4 treatment in vitro, before the drug is administered to patients.	sapropterin	226-229	phenylalanine hydroxylase	Homo sapiens	16-19
29654578-6	2018	Computational analyses proposed that glutamine at position 226 is an important, evolutionary conserved amino acid while the substitution with lysine probably disturbs tertiary protein structure and impacts posttranslational PAH modifications.	Lysine	142-148	phenylalanine hydroxylase	Homo sapiens	224-227
29906262-10	2018	Several cytosine-phosphoguanines, including those located on FHL2 and ELOVL2, were found associated with both aging indicators and monohydroxy-PAH levels.	cytosine-phosphoguanines	8-32	phenylalanine hydroxylase	Homo sapiens	143-146
30961089-1	2018	Hydrogen peroxide (H2O2)-sensitive layer-by-layer films were prepared based on combining phenyl boronic acid (PBA)-modified poly(allylamine) (PAH) with shikimic acid (SA)-modified-PAH through boronate ester bonds.	Hydrogen Peroxide	19-23	phenylalanine hydroxylase	Homo sapiens	142-145
30961089-1	2018	Hydrogen peroxide (H2O2)-sensitive layer-by-layer films were prepared based on combining phenyl boronic acid (PBA)-modified poly(allylamine) (PAH) with shikimic acid (SA)-modified-PAH through boronate ester bonds.	Hydrogen Peroxide	19-23	phenylalanine hydroxylase	Homo sapiens	180-183
30961089-1	2018	Hydrogen peroxide (H2O2)-sensitive layer-by-layer films were prepared based on combining phenyl boronic acid (PBA)-modified poly(allylamine) (PAH) with shikimic acid (SA)-modified-PAH through boronate ester bonds.	benzeneboronic acid	110-113	phenylalanine hydroxylase	Homo sapiens	142-145
30961089-1	2018	Hydrogen peroxide (H2O2)-sensitive layer-by-layer films were prepared based on combining phenyl boronic acid (PBA)-modified poly(allylamine) (PAH) with shikimic acid (SA)-modified-PAH through boronate ester bonds.	Shikimic Acid	152-165	phenylalanine hydroxylase	Homo sapiens	142-145
30961089-1	2018	Hydrogen peroxide (H2O2)-sensitive layer-by-layer films were prepared based on combining phenyl boronic acid (PBA)-modified poly(allylamine) (PAH) with shikimic acid (SA)-modified-PAH through boronate ester bonds.	Shikimic Acid	152-165	phenylalanine hydroxylase	Homo sapiens	180-183
30961089-1	2018	Hydrogen peroxide (H2O2)-sensitive layer-by-layer films were prepared based on combining phenyl boronic acid (PBA)-modified poly(allylamine) (PAH) with shikimic acid (SA)-modified-PAH through boronate ester bonds.	Shikimic Acid	167-169	phenylalanine hydroxylase	Homo sapiens	180-183
30961089-2	2018	These PBA-PAH/SA-PAH multilayer films could be prepared in aqueous solutions at pH 7.4 and 9.0 in the presence of NaCl.	Shikimic Acid	14-16	phenylalanine hydroxylase	Homo sapiens	17-20
30961089-2	2018	These PBA-PAH/SA-PAH multilayer films could be prepared in aqueous solutions at pH 7.4 and 9.0 in the presence of NaCl.	Sodium Chloride	114-118	phenylalanine hydroxylase	Homo sapiens	10-13
30961089-2	2018	These PBA-PAH/SA-PAH multilayer films could be prepared in aqueous solutions at pH 7.4 and 9.0 in the presence of NaCl.	Sodium Chloride	114-118	phenylalanine hydroxylase	Homo sapiens	17-20
30961089-3	2018	It is believed that the electrostatic repulsion between the SA-PAH and PBA-PAH was diminished and the formation of ester bonds between the SA and PBA was promoted in the presence of NaCl.	Esters	115-120	phenylalanine hydroxylase	Homo sapiens	63-66
30961089-3	2018	It is believed that the electrostatic repulsion between the SA-PAH and PBA-PAH was diminished and the formation of ester bonds between the SA and PBA was promoted in the presence of NaCl.	Shikimic Acid	60-62	phenylalanine hydroxylase	Homo sapiens	63-66
30961089-3	2018	It is believed that the electrostatic repulsion between the SA-PAH and PBA-PAH was diminished and the formation of ester bonds between the SA and PBA was promoted in the presence of NaCl.	Sodium Chloride	182-186	phenylalanine hydroxylase	Homo sapiens	63-66
30961089-3	2018	It is believed that the electrostatic repulsion between the SA-PAH and PBA-PAH was diminished and the formation of ester bonds between the SA and PBA was promoted in the presence of NaCl.	Sodium Chloride	182-186	phenylalanine hydroxylase	Homo sapiens	75-78
30961089-5	2018	In addition, SA-PAH/PBA-PAH multilayer films combined with glucose oxidase (GOx) were decomposed in the presence of glucose because GOx catalyzes the oxidation of D-glucose to generate H2O2.	Glucose	59-66	phenylalanine hydroxylase	Homo sapiens	16-19
30961089-5	2018	In addition, SA-PAH/PBA-PAH multilayer films combined with glucose oxidase (GOx) were decomposed in the presence of glucose because GOx catalyzes the oxidation of D-glucose to generate H2O2.	Glucose	59-66	phenylalanine hydroxylase	Homo sapiens	24-27
30961089-5	2018	In addition, SA-PAH/PBA-PAH multilayer films combined with glucose oxidase (GOx) were decomposed in the presence of glucose because GOx catalyzes the oxidation of D-glucose to generate H2O2.	Glucose	163-172	phenylalanine hydroxylase	Homo sapiens	16-19
30961089-5	2018	In addition, SA-PAH/PBA-PAH multilayer films combined with glucose oxidase (GOx) were decomposed in the presence of glucose because GOx catalyzes the oxidation of D-glucose to generate H2O2.	Glucose	163-172	phenylalanine hydroxylase	Homo sapiens	24-27
30961089-5	2018	In addition, SA-PAH/PBA-PAH multilayer films combined with glucose oxidase (GOx) were decomposed in the presence of glucose because GOx catalyzes the oxidation of D-glucose to generate H2O2.	Hydrogen Peroxide	185-189	phenylalanine hydroxylase	Homo sapiens	16-19
30961089-5	2018	In addition, SA-PAH/PBA-PAH multilayer films combined with glucose oxidase (GOx) were decomposed in the presence of glucose because GOx catalyzes the oxidation of D-glucose to generate H2O2.	Hydrogen Peroxide	185-189	phenylalanine hydroxylase	Homo sapiens	24-27
30961089-6	2018	The surfaces of CaCO3 microparticles were coated with PAH/GOx/(SA-PAH/PBA-PAH)5 films that absorbed insulin.	Calcium Carbonate	16-21	phenylalanine hydroxylase	Homo sapiens	54-57
30961089-6	2018	The surfaces of CaCO3 microparticles were coated with PAH/GOx/(SA-PAH/PBA-PAH)5 films that absorbed insulin.	Calcium Carbonate	16-21	phenylalanine hydroxylase	Homo sapiens	66-69
30961089-6	2018	The surfaces of CaCO3 microparticles were coated with PAH/GOx/(SA-PAH/PBA-PAH)5 films that absorbed insulin.	Calcium Carbonate	16-21	phenylalanine hydroxylase	Homo sapiens	66-69
29777816-1	2018	The genetic disorder phenylketonuria (PKU) is the inability to metabolize phenylalanine because of a lack of the enzyme phenylalanine hydroxylase.	Phenylalanine	74-87	phenylalanine hydroxylase	Homo sapiens	120-145
29653233-7	2018	The mutant PAH protein levels were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), western blot and enzyme-linked immunosorbent assay (ELISA).	Sodium Dodecyl Sulfate	49-71	phenylalanine hydroxylase	Homo sapiens	11-14
29653233-7	2018	The mutant PAH protein levels were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), western blot and enzyme-linked immunosorbent assay (ELISA).	polyacrylamide	72-86	phenylalanine hydroxylase	Homo sapiens	11-14
29653233-7	2018	The mutant PAH protein levels were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), western blot and enzyme-linked immunosorbent assay (ELISA).	Sodium Dodecyl Sulfate	108-111	phenylalanine hydroxylase	Homo sapiens	11-14
29653326-4	2018	In LE-WAFs, the Microtox EC50 was associated with biodegradation of the predominant hydrocarbons (naphthalenes, 2- to 3-ring PAH), as well as with phenol degradation products.	Hydrocarbons	84-96	phenylalanine hydroxylase	Homo sapiens	125-128
29909188-1	2018	Phenylketonuria (PKU) is a prevalent inherited metabolic disorder caused by a phenylalanine hydroxylase (PAH) or tetrahydrobiopterin (BH4) deficiency, which leads to the accumulation of phenylalanine (PHE).	Phenylalanine	78-91	phenylalanine hydroxylase	Homo sapiens	105-108
29909188-1	2018	Phenylketonuria (PKU) is a prevalent inherited metabolic disorder caused by a phenylalanine hydroxylase (PAH) or tetrahydrobiopterin (BH4) deficiency, which leads to the accumulation of phenylalanine (PHE).	Phenylalanine	201-204	phenylalanine hydroxylase	Homo sapiens	78-103
29909188-1	2018	Phenylketonuria (PKU) is a prevalent inherited metabolic disorder caused by a phenylalanine hydroxylase (PAH) or tetrahydrobiopterin (BH4) deficiency, which leads to the accumulation of phenylalanine (PHE).	Phenylalanine	201-204	phenylalanine hydroxylase	Homo sapiens	105-108
30002478-3	2018	Here we develop a H+ biotransducer that changes the pH in a mitochondrial matrix by controlling the flow of H+ between a conductive polymer of sulfonated polyaniline and solution.	Polymers	132-139	phenylalanine hydroxylase	Homo sapiens	52-54
30002478-3	2018	Here we develop a H+ biotransducer that changes the pH in a mitochondrial matrix by controlling the flow of H+ between a conductive polymer of sulfonated polyaniline and solution.	polyaniline	154-165	phenylalanine hydroxylase	Homo sapiens	52-54
30002478-4	2018	We have successfully modulated the rate of ATP synthesis in mitochondria by altering the solution pH.	Adenosine Triphosphate	43-46	phenylalanine hydroxylase	Homo sapiens	98-100
29862653-3	2018	Based on the change of fluorescence signals by the interaction with biomolecules, QD-dye conjugates are exploited as biosensors for the detection of pH, O2 , nicotinamide adenine dinucleotide (phosphate), ions, proteases, glutathione, and microRNA.	Glutathione	222-233	phenylalanine hydroxylase	Homo sapiens	149-151
29475030-3	2018	PAH adducts to plasma proteins are applied as sensitive biomarkers of PAH exposure in humans and other species, thus the presence of PAH protein adducts in Atlantic cod plasma was investigated to identify PAH protein adduct biomarker candidates of exposure to PAHs.	Polycyclic Aromatic Hydrocarbons	260-264	phenylalanine hydroxylase	Homo sapiens	0-3
29713476-12	2018	Conclusion: Our study shows the evidence of associations between some urinary PAH metabolite levels (1-hydroxyphenanthrene and 1-hydroxypyrene) and residence characteristics.	1-hydroxyphenanthrene	101-122	phenylalanine hydroxylase	Homo sapiens	78-81
29258033-4	2018	These studied sediments are highly contaminated by metals, notably copper (1445 and 835mg/kg, in the unweathered and naturally-weathered sediments, respectively), lead (760 and 1260mg/kg, respectively), zinc (2085 and 2550mg/kg, respectively), as well as by organic contaminants (PAH, PCB) and organometallics (organotins).	sediments	14-23	phenylalanine hydroxylase	Homo sapiens	280-283
29667677-4	2018	Regarding (i), in this work, we determined the lowest energy structures of PAH-ice systems for a variety of PAHs ranging from naphthalene to ovalene on three types of ice - crystalline (Ih and Ic) and amorphous (low density) - using an explicit description of the electrons and a finite-sized system.	Polycyclic Aromatic Hydrocarbons	108-112	phenylalanine hydroxylase	Homo sapiens	75-78
29667677-4	2018	Regarding (i), in this work, we determined the lowest energy structures of PAH-ice systems for a variety of PAHs ranging from naphthalene to ovalene on three types of ice - crystalline (Ih and Ic) and amorphous (low density) - using an explicit description of the electrons and a finite-sized system.	naphthalene	126-137	phenylalanine hydroxylase	Homo sapiens	75-78
29667677-4	2018	Regarding (i), in this work, we determined the lowest energy structures of PAH-ice systems for a variety of PAHs ranging from naphthalene to ovalene on three types of ice - crystalline (Ih and Ic) and amorphous (low density) - using an explicit description of the electrons and a finite-sized system.	Ovalene	141-148	phenylalanine hydroxylase	Homo sapiens	75-78
29667677-6	2018	Regarding (ii), the influence of the interaction with ice on the Vertical Ionisation Potentials (VIPs) of the series of PAHs was determined using the constrained SCC-DFTB scheme benchmarked against correlated wavefunction results for PAH-(H2O)n (n = 1-6, 13) clusters.	dftb	166-170	phenylalanine hydroxylase	Homo sapiens	120-123
29667677-6	2018	Regarding (ii), the influence of the interaction with ice on the Vertical Ionisation Potentials (VIPs) of the series of PAHs was determined using the constrained SCC-DFTB scheme benchmarked against correlated wavefunction results for PAH-(H2O)n (n = 1-6, 13) clusters.	Water	239-242	phenylalanine hydroxylase	Homo sapiens	120-123
29653686-1	2018	BACKGROUND: Phenylketonuria (PKU) is caused by phenylalanine hydroxylase (PAH) deficiency that results in phenylalanine (Phe) accumulation.	Phenylalanine	12-15	phenylalanine hydroxylase	Homo sapiens	47-72
29024459-3	2018	The fabrication procedure includes the modification of a track-etched asymmetric (conical) nanochannel with polyallylamine (PAH) by electrostatic self-assembly.	polyallylamine	108-122	phenylalanine hydroxylase	Homo sapiens	124-127
29024459-4	2018	PAH is the arcaetypical model of polyamine and it is further used to address the nanochannels with phosphate responsivity.	Polyamines	33-42	phenylalanine hydroxylase	Homo sapiens	0-3
29024459-4	2018	PAH is the arcaetypical model of polyamine and it is further used to address the nanochannels with phosphate responsivity.	Phosphates	99-108	phenylalanine hydroxylase	Homo sapiens	0-3
29730800-1	2018	To examine ambient air pollutants, specifically polycyclic aromatic hydrocarbons (PAHs), as a factor in the geographic variation of breast cancer incidence seen in the US, we conducted an ecological study involving counties throughout the US to examine breast cancer incidence in relation to PAH emissions in ambient air.	Polycyclic Aromatic Hydrocarbons	48-80	phenylalanine hydroxylase	Homo sapiens	82-85
29713476-12	2018	Conclusion: Our study shows the evidence of associations between some urinary PAH metabolite levels (1-hydroxyphenanthrene and 1-hydroxypyrene) and residence characteristics.	1-hydroxypyrene	127-142	phenylalanine hydroxylase	Homo sapiens	78-81
29149738-3	2018	However, few studies have investigated associations of PAH exposures with FeNO or eCO.	feno	74-78	phenylalanine hydroxylase	Homo sapiens	55-58
29454221-2	2018	The rate-limiting step for phenylalanine metabolism is catalyzed by phenylalanine hydroxylase (PAH) and its cofactor tetrahydrobiopterin.	Phenylalanine	27-40	phenylalanine hydroxylase	Homo sapiens	68-93
29454221-2	2018	The rate-limiting step for phenylalanine metabolism is catalyzed by phenylalanine hydroxylase (PAH) and its cofactor tetrahydrobiopterin.	Phenylalanine	27-40	phenylalanine hydroxylase	Homo sapiens	95-98
29454221-2	2018	The rate-limiting step for phenylalanine metabolism is catalyzed by phenylalanine hydroxylase (PAH) and its cofactor tetrahydrobiopterin.	sapropterin	117-136	phenylalanine hydroxylase	Homo sapiens	68-93
29454221-2	2018	The rate-limiting step for phenylalanine metabolism is catalyzed by phenylalanine hydroxylase (PAH) and its cofactor tetrahydrobiopterin.	sapropterin	117-136	phenylalanine hydroxylase	Homo sapiens	95-98
29149738-4	2018	Therefore, we aimed to quantify the associations of urinary PAH metabolites with FeNO and eCO levels, and investigate their potential effect modifiers by linear mixed models among 4133 participants from the Wuhan-Zhuhai cohort in China.	feno	81-85	phenylalanine hydroxylase	Homo sapiens	60-63
29149738-4	2018	Therefore, we aimed to quantify the associations of urinary PAH metabolites with FeNO and eCO levels, and investigate their potential effect modifiers by linear mixed models among 4133 participants from the Wuhan-Zhuhai cohort in China.	ECO	90-93	phenylalanine hydroxylase	Homo sapiens	60-63
29149738-6	2018	We found significant associations of increased urinary PAH metabolites with elevated eCO and FeNO.	ECO	85-88	phenylalanine hydroxylase	Homo sapiens	55-58
29149738-6	2018	We found significant associations of increased urinary PAH metabolites with elevated eCO and FeNO.	feno	93-97	phenylalanine hydroxylase	Homo sapiens	55-58
29149738-9	2018	Increased urinary PAH metabolites were associated with decreased FeNO among ever-smokers and elevated FeNO levels among non-smokers.	feno	65-69	phenylalanine hydroxylase	Homo sapiens	18-21
29149738-9	2018	Increased urinary PAH metabolites were associated with decreased FeNO among ever-smokers and elevated FeNO levels among non-smokers.	feno	102-106	phenylalanine hydroxylase	Homo sapiens	18-21
29101890-8	2018	The sudden increase in atmospheric PAH concentrations in the winter of 2014 may also be due to iron manufacturing.	Iron	95-99	phenylalanine hydroxylase	Homo sapiens	35-38
29510479-0	2018	Conductometric Sensor for PAH Detection with Molecularly Imprinted Polymer as Recognition Layer.	Polymers	67-74	phenylalanine hydroxylase	Homo sapiens	26-29
28968578-1	2018	Aging soot in soil under neutral aqueous condition for 30days significantly (p&lt;0.05) reduced the apparent gastrointestinal bioaccessibility (Bapp) of polycyclic aromatic hydrocarbons (PAHs) and PAH derivatives (d-PAHs) natively present in a composite fuel soot sample.	d-pahs	214-220	phenylalanine hydroxylase	Homo sapiens	187-190
28939924-2	2018	The objective of this study was to characterize PAH levels in people living near oil drilling operations in relation to fish consumption, occupation, source of water and other socio-demographic characteristics.	Water	160-165	phenylalanine hydroxylase	Homo sapiens	48-51
30652640-8	2018	The characteristic features of doxorubicine-CNT complex are high loading efficiency, pH-dependent release in acidic tumor microenviroment, enough stability in biological fluid.	Doxorubicin	31-43	phenylalanine hydroxylase	Homo sapiens	85-87
29067613-0	2018	Treatment of PAH-contaminated soil using cement-activated persulfate.	Peroxydisulfate	58-68	phenylalanine hydroxylase	Homo sapiens	13-16
28939924-3	2018	METHODS: This pilot study examined PAH exposure by measuring 1-hydroxypyrene (1-OHP) in urine samples using high-performance liquid chromatography and fluorescence detection from 75 women and men in the Ecuadorian and Peruvian Amazon living near oil drilling operations and who answered a questionnaire collecting socio-demographic, occupational and dietary information.	1-hydroxypyrene	61-76	phenylalanine hydroxylase	Homo sapiens	35-38
28939924-3	2018	METHODS: This pilot study examined PAH exposure by measuring 1-hydroxypyrene (1-OHP) in urine samples using high-performance liquid chromatography and fluorescence detection from 75 women and men in the Ecuadorian and Peruvian Amazon living near oil drilling operations and who answered a questionnaire collecting socio-demographic, occupational and dietary information.	Oxaliplatin	78-83	phenylalanine hydroxylase	Homo sapiens	35-38
30348250-4	2018	This may significantly impact the absorption of other drugs that have pH-dependent solubility, such as ketoconazole, a weak base.	Ketoconazole	103-115	phenylalanine hydroxylase	Homo sapiens	70-72
30348250-5	2018	Within this context, the purpose of this study was to demonstrate how GastroPlusTM - a physiological based software program- can be used to predict clinical pharmacokinetics of ketoconazole in a normal physiological state vs. elevated gastric pH.	Ketoconazole	177-189	phenylalanine hydroxylase	Homo sapiens	243-245
28956315-3	2018	Additionally, 15 other different variations in the PAH gene were identified, each with very low incidence, providing ground for phenotypic variability and potential response to BH4 therapy.	sapropterin	177-180	phenylalanine hydroxylase	Homo sapiens	51-54
29289134-6	2017	This model can predict the tendency of PAH dimerization as validated by pyrene dimerization experiments [H. Sabbah et al., J. Phys.	pyrene	72-78	phenylalanine hydroxylase	Homo sapiens	39-42
29174366-2	2018	HPA is known to be caused by deficiencies of the enzyme phenylalanine hydroxylase (PAH) or its cofactor tetrahydrobiopterin (BH4).	sapropterin	104-123	phenylalanine hydroxylase	Homo sapiens	83-86
33445396-0	2017	Cell Microenvironment pH Sensing in 3D Microgels Using Fluorescent Carbon Dots.	Carbon	67-73	phenylalanine hydroxylase	Homo sapiens	22-24
33445396-1	2017	We report here a 3D cell culture microgel-based system containing carbon dots capable of sensing the pH changes in the cellular microenvironment.	Carbon	66-72	phenylalanine hydroxylase	Homo sapiens	101-103
33445396-2	2017	We have utilized a simple droplet-based microfluidics methodology for encapsulating cells and fluorescent pH sensitive carbon dots in polyethylene glycol microgels.	Carbon	119-125	phenylalanine hydroxylase	Homo sapiens	106-108
33445396-2	2017	We have utilized a simple droplet-based microfluidics methodology for encapsulating cells and fluorescent pH sensitive carbon dots in polyethylene glycol microgels.	Polyethylene Glycols	134-153	phenylalanine hydroxylase	Homo sapiens	106-108
33445396-4	2017	The synthesized pH sensitive carbon dots possess green fluorescence emission, which increases as the pH is lowered from neutral to acidic.	Carbon	29-35	phenylalanine hydroxylase	Homo sapiens	16-18
33445396-4	2017	The synthesized pH sensitive carbon dots possess green fluorescence emission, which increases as the pH is lowered from neutral to acidic.	Carbon	29-35	phenylalanine hydroxylase	Homo sapiens	101-103
29208962-4	2017	Herein we present azomethine ylide homocoupling as a strategy to afford internally nitrogen-doped, non-planar PAH in solution and planar nanographene on surfaces, with central pyrazine rings.	azomethine ylide	18-34	phenylalanine hydroxylase	Homo sapiens	110-113
29208962-4	2017	Herein we present azomethine ylide homocoupling as a strategy to afford internally nitrogen-doped, non-planar PAH in solution and planar nanographene on surfaces, with central pyrazine rings.	Nitrogen	83-91	phenylalanine hydroxylase	Homo sapiens	110-113
28783518-5	2017	The PAH also exhibited high condensation activity in acidic and neutral conditions to produce silica particles.	Silicon Dioxide	94-100	phenylalanine hydroxylase	Homo sapiens	4-7
28783518-6	2017	Moreover, PAH also created the nuclei of the silica particles, and the number of nuclei could be controlled by the concentration of PAH.	Silicon Dioxide	45-51	phenylalanine hydroxylase	Homo sapiens	10-13
28783518-6	2017	Moreover, PAH also created the nuclei of the silica particles, and the number of nuclei could be controlled by the concentration of PAH.	Silicon Dioxide	45-51	phenylalanine hydroxylase	Homo sapiens	132-135
28783518-10	2017	In particular, by adjusting the PAH concentration, it was possible to obtain nearly perfect spherical-shaped silica nanoparticles with uniform sizes, which has rarely been reported.	Silicon Dioxide	109-115	phenylalanine hydroxylase	Homo sapiens	32-35
28783518-11	2017	Above all, using this paper, we can get closer to understanding the principles of silica formation using PAH as a replacement for the bioactive proteins of microorganisms.	Silicon Dioxide	82-88	phenylalanine hydroxylase	Homo sapiens	105-108
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	Phenylalanine	149-164	phenylalanine hydroxylase	Homo sapiens	79-104
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	Phenylalanine	149-164	phenylalanine hydroxylase	Homo sapiens	106-109
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	Phenylalanine	166-171	phenylalanine hydroxylase	Homo sapiens	79-104
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	Phenylalanine	166-171	phenylalanine hydroxylase	Homo sapiens	106-109
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	Tyrosine	176-186	phenylalanine hydroxylase	Homo sapiens	79-104
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	Tyrosine	176-186	phenylalanine hydroxylase	Homo sapiens	106-109
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	Tyrosine	188-193	phenylalanine hydroxylase	Homo sapiens	79-104
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	Tyrosine	188-193	phenylalanine hydroxylase	Homo sapiens	106-109
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	sapropterin	223-242	phenylalanine hydroxylase	Homo sapiens	79-104
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	sapropterin	223-242	phenylalanine hydroxylase	Homo sapiens	106-109
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	sapropterin	244-247	phenylalanine hydroxylase	Homo sapiens	79-104
28768147-1	2017	Phenylketonuria (PKU) is an autosomal recessive disorder caused by a defective phenylalanine hydroxylase (PAH), which catalyzes the hydroxylation of l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr) in presence of the cofactor tetrahydrobiopterin (BH4).	sapropterin	244-247	phenylalanine hydroxylase	Homo sapiens	106-109
28768147-2	2017	Defective PAH causes accumulation of phenylalanine, which has neurotoxic effects and leads to dermatological, behavioral, and neurocognitive problems.	Phenylalanine	37-50	phenylalanine hydroxylase	Homo sapiens	10-13
28768147-4	2017	In this study, we propose a system where a probiotic lactic acid bacteria (LAB) can be used as vehicle to express in situ an engineered human PAH.	Lactic Acid	53-64	phenylalanine hydroxylase	Homo sapiens	142-145
29114196-2	2017	Phenylketonuria (PKU), a relatively common disorder that is responsive to treatment, is an inherited autosomal recessive disorder caused by a deficiency in phenylalanine hydroxylase (PAH) or one of several enzymes mediating biosynthesis or regeneration of the PAH cofactor tetrahydrobiopterin.	sapropterin	273-292	phenylalanine hydroxylase	Homo sapiens	183-186
29108285-6	2017	We found that chronic PAH exposure saturated lung cell xenobiotic metabolic pathways, promoting intercellular reactive oxygen species production and accumulation.	Reactive Oxygen Species	110-133	phenylalanine hydroxylase	Homo sapiens	22-25
28801706-10	2017	Among the seven carcinogenic PAHs, BaP accounted for the majority of the potency and could potentially be used as a unique indicator of PAH toxicity.	benzylaminopurine	35-38	phenylalanine hydroxylase	Homo sapiens	29-32
28653649-8	2017	Our findings contribute to better understanding of structure and function of PAH mutated enzymes and optimal treatment of PKU patients carrying these mutations using BH4 supplementation.	sapropterin	166-169	phenylalanine hydroxylase	Homo sapiens	77-80
28636458-12	2017	Field decontamination using dish soap, water, and scrubbing was able to reduce PAH contamination on turnout jackets by a median of 85%.	Water	39-44	phenylalanine hydroxylase	Homo sapiens	79-82
28768147-5	2017	Engineered PAHs contain a secretion peptide, a gastrointestinal signal (GI), the human PAH, and a flexible glycine linker followed by the fluorescence protein mEGFP.	Glycine	107-114	phenylalanine hydroxylase	Homo sapiens	11-14
28500931-3	2017	An interquartile change in urinary PAH metabolite was associated with significant decrements in FEV1 and FVC for eight PAHs, 2-hydroxynapthalene, 1-, and 2-hydroxyphenanthrene, 2-, 3-, and 9-hydroxyfluorene and 3- and 4-hydroxyphenanthrene.	Polycyclic Aromatic Hydrocarbons	119-123	phenylalanine hydroxylase	Homo sapiens	35-38
28500931-3	2017	An interquartile change in urinary PAH metabolite was associated with significant decrements in FEV1 and FVC for eight PAHs, 2-hydroxynapthalene, 1-, and 2-hydroxyphenanthrene, 2-, 3-, and 9-hydroxyfluorene and 3- and 4-hydroxyphenanthrene.	2-hydroxynapthalene	125-144	phenylalanine hydroxylase	Homo sapiens	35-38
28500931-3	2017	An interquartile change in urinary PAH metabolite was associated with significant decrements in FEV1 and FVC for eight PAHs, 2-hydroxynapthalene, 1-, and 2-hydroxyphenanthrene, 2-, 3-, and 9-hydroxyfluorene and 3- and 4-hydroxyphenanthrene.	1-, and 2-hydroxyphenanthrene	146-175	phenylalanine hydroxylase	Homo sapiens	35-38
28500931-3	2017	An interquartile change in urinary PAH metabolite was associated with significant decrements in FEV1 and FVC for eight PAHs, 2-hydroxynapthalene, 1-, and 2-hydroxyphenanthrene, 2-, 3-, and 9-hydroxyfluorene and 3- and 4-hydroxyphenanthrene.	2-, 3-, and 9-hydroxyfluorene	177-206	phenylalanine hydroxylase	Homo sapiens	35-38
28500931-3	2017	An interquartile change in urinary PAH metabolite was associated with significant decrements in FEV1 and FVC for eight PAHs, 2-hydroxynapthalene, 1-, and 2-hydroxyphenanthrene, 2-, 3-, and 9-hydroxyfluorene and 3- and 4-hydroxyphenanthrene.	3- and 4-hydroxyphenanthrene	211-239	phenylalanine hydroxylase	Homo sapiens	35-38
28630284-8	2017	Using [3H]PAH as a substrate of OAT1, nalidixic acid inhibited but dantrolene, glafenine, and prazosin stimulated uptake.	Tritium	7-9	phenylalanine hydroxylase	Homo sapiens	10-13
28630284-9	2017	Nalidixic acid decreased equilibrium content of [3H]PAH, suggesting that it may possibly be exchanged by OAT1.	Nalidixic Acid	0-14	phenylalanine hydroxylase	Homo sapiens	52-55
28820526-3	2017	Silica nanoparticle monolayers of controlled coverage were formed on macroion (PAH)-modified mica.	Silicon Dioxide	0-6	phenylalanine hydroxylase	Homo sapiens	79-82
28630284-9	2017	Nalidixic acid decreased equilibrium content of [3H]PAH, suggesting that it may possibly be exchanged by OAT1.	Tritium	49-51	phenylalanine hydroxylase	Homo sapiens	52-55
28883751-4	2017	By flow cytometry experiment, after Res (5 microg/ml)+PA-H (10 microg/ml) treatment, the A549 cells showed the most apoptosic cells compared to other group treatments, and after additional treatment with Res, the apoptosic cells of both two PA concentrations were raised.	Resveratrol	204-207	phenylalanine hydroxylase	Homo sapiens	54-58
28820526-3	2017	Silica nanoparticle monolayers of controlled coverage were formed on macroion (PAH)-modified mica.	mica	93-97	phenylalanine hydroxylase	Homo sapiens	79-82
28645531-1	2017	Phenylketonuria (PKU) and less severe hyperphenylalaninemia (HPA) constitute the most common inborn error of amino acid metabolism, and is most often caused by defects in phenylalanine hydroxylase (PAH) function resulting in accumulation of Phe to neurotoxic levels.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	171-196
28656579-3	2017	Low molecular weight PAHs, such as naphthalene and phenanthrene, were generally predominant, displaying properties of PAH mixtures generated from petrogenic pollution.	naphthalene	35-46	phenylalanine hydroxylase	Homo sapiens	21-24
28656579-3	2017	Low molecular weight PAHs, such as naphthalene and phenanthrene, were generally predominant, displaying properties of PAH mixtures generated from petrogenic pollution.	phenanthrene	51-63	phenylalanine hydroxylase	Homo sapiens	21-24
27943120-7	2017	This review provides information about the occurrence of the polycyclic aromatic hydrocarbons (PAHs) and their influence on human exposure and biological effects, including PAH-derived DNA adduct formation and repair processes.	Polycyclic Aromatic Hydrocarbons	61-93	phenylalanine hydroxylase	Homo sapiens	95-98
28818881-7	2017	Selexipag reduced the risk of composite morbidity/mortality events in patients with PAH-CTD by 41% (HR 0.59; 95% CI 0.41-0.85).	selexipag	0-9	phenylalanine hydroxylase	Homo sapiens	84-87
28818881-9	2017	Adverse events were predominately prostacyclin-related and known for selexipag treatment.GRIPHON has allowed the comprehensive characterisation of patients with PAH-CTD.	Epoprostenol	34-46	phenylalanine hydroxylase	Homo sapiens	161-164
28818881-9	2017	Adverse events were predominately prostacyclin-related and known for selexipag treatment.GRIPHON has allowed the comprehensive characterisation of patients with PAH-CTD.	selexipag	69-78	phenylalanine hydroxylase	Homo sapiens	161-164
28818881-10	2017	Selexipag delayed progression of PAH and was well-tolerated among PAH-CTD patients, including those with PAH-SSc and PAH-SLE.	selexipag	0-9	phenylalanine hydroxylase	Homo sapiens	33-36
28818881-10	2017	Selexipag delayed progression of PAH and was well-tolerated among PAH-CTD patients, including those with PAH-SSc and PAH-SLE.	selexipag	0-9	phenylalanine hydroxylase	Homo sapiens	66-69
28818881-10	2017	Selexipag delayed progression of PAH and was well-tolerated among PAH-CTD patients, including those with PAH-SSc and PAH-SLE.	selexipag	0-9	phenylalanine hydroxylase	Homo sapiens	66-69
28818881-10	2017	Selexipag delayed progression of PAH and was well-tolerated among PAH-CTD patients, including those with PAH-SSc and PAH-SLE.	selexipag	0-9	phenylalanine hydroxylase	Homo sapiens	66-69
28556602-4	2017	These aryl-type radical additions to conjugated hydrocarbons via resonantly stabilized free-radical intermediates defy conventional wisdom that PAH growth is predominantly a high-temperature phenomenon and thus may represent an overlooked path to PAHs as complex as coronene and corannulene in cold regions of the interstellar medium like in the Taurus Molecular Cloud.	Hydrocarbons	48-60	phenylalanine hydroxylase	Homo sapiens	144-147
28556602-4	2017	These aryl-type radical additions to conjugated hydrocarbons via resonantly stabilized free-radical intermediates defy conventional wisdom that PAH growth is predominantly a high-temperature phenomenon and thus may represent an overlooked path to PAHs as complex as coronene and corannulene in cold regions of the interstellar medium like in the Taurus Molecular Cloud.	Polycyclic Aromatic Hydrocarbons	247-251	phenylalanine hydroxylase	Homo sapiens	144-147
28556602-4	2017	These aryl-type radical additions to conjugated hydrocarbons via resonantly stabilized free-radical intermediates defy conventional wisdom that PAH growth is predominantly a high-temperature phenomenon and thus may represent an overlooked path to PAHs as complex as coronene and corannulene in cold regions of the interstellar medium like in the Taurus Molecular Cloud.	coronene	266-274	phenylalanine hydroxylase	Homo sapiens	144-147
28556602-4	2017	These aryl-type radical additions to conjugated hydrocarbons via resonantly stabilized free-radical intermediates defy conventional wisdom that PAH growth is predominantly a high-temperature phenomenon and thus may represent an overlooked path to PAHs as complex as coronene and corannulene in cold regions of the interstellar medium like in the Taurus Molecular Cloud.	corannulene	279-290	phenylalanine hydroxylase	Homo sapiens	144-147
28767725-7	2017	To detect coldspots/hotspots unaffected by population bias, we analysed the presence of germline mutations obtained from HGMD database in the 5-nucleotide segments repeatedly occurring in genes associated with common inherited disorders, in particular, the PAH, LDLR, CFTR, F8, and F9 genes.	5-nucleotide	142-154	phenylalanine hydroxylase	Homo sapiens	257-260
28389235-2	2017	We therefore investigated the DNA methylation pattern of the phenylalanine hydroxylase (PAH) gene promoter at different phe levels, and the possibility of DNA methylation pattern changes being a biomarker of high phe exposure in diet free newborns with HPA.	Phenylalanine	61-64	phenylalanine hydroxylase	Homo sapiens	88-91
28389235-2	2017	We therefore investigated the DNA methylation pattern of the phenylalanine hydroxylase (PAH) gene promoter at different phe levels, and the possibility of DNA methylation pattern changes being a biomarker of high phe exposure in diet free newborns with HPA.	Phenylalanine	120-123	phenylalanine hydroxylase	Homo sapiens	88-91
28389235-3	2017	DESIGN AND METHODS: With a combination of methylated PCR, high resolution melting, and sequencing, the cytosine phosphodiester bond guanine (CpG) dinucleotides in the 5" untranslated region of the PAH gene were analysed 2-15days after birth using leukocyte DNA from diet free 16 newborns with HPA and 16 healthy controls.	Guanine	132-141	phenylalanine hydroxylase	Homo sapiens	197-200
28389235-3	2017	DESIGN AND METHODS: With a combination of methylated PCR, high resolution melting, and sequencing, the cytosine phosphodiester bond guanine (CpG) dinucleotides in the 5" untranslated region of the PAH gene were analysed 2-15days after birth using leukocyte DNA from diet free 16 newborns with HPA and 16 healthy controls.	cpg) dinucleotides	141-159	phenylalanine hydroxylase	Homo sapiens	197-200
28645531-1	2017	Phenylketonuria (PKU) and less severe hyperphenylalaninemia (HPA) constitute the most common inborn error of amino acid metabolism, and is most often caused by defects in phenylalanine hydroxylase (PAH) function resulting in accumulation of Phe to neurotoxic levels.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	198-201
28645531-5	2017	Here we refine this view to address how PKU-associated missense variants can perturb the equilibrium among alternate native PAH structures (resting-state PAH and activated PAH), thus shifting the tipping point of this equilibrium to a neurotoxic Phe concentration.	Phenylalanine	246-249	phenylalanine hydroxylase	Homo sapiens	124-127
28645531-5	2017	Here we refine this view to address how PKU-associated missense variants can perturb the equilibrium among alternate native PAH structures (resting-state PAH and activated PAH), thus shifting the tipping point of this equilibrium to a neurotoxic Phe concentration.	Phenylalanine	246-249	phenylalanine hydroxylase	Homo sapiens	154-157
28645531-5	2017	Here we refine this view to address how PKU-associated missense variants can perturb the equilibrium among alternate native PAH structures (resting-state PAH and activated PAH), thus shifting the tipping point of this equilibrium to a neurotoxic Phe concentration.	Phenylalanine	246-249	phenylalanine hydroxylase	Homo sapiens	154-157
28526196-2	2017	Investigations of PAH air-water exchange are mostly based on observational data obtained using complicated field sampling processes.	Water	26-31	phenylalanine hydroxylase	Homo sapiens	18-21
28593914-3	2017	BH4 is the co-factor of the enzyme phenylalanine hydroxylase (PAH) and improves PAH activity and, thus, Phe tolerance in the diet.	Phenylalanine	104-107	phenylalanine hydroxylase	Homo sapiens	35-60
28526196-3	2017	This study proposes a new approach to improve the estimation of long-term PAH air-water exchange fluxes by using a multivariate regression model to simulate hourly gaseous PAH concentrations.	Water	82-87	phenylalanine hydroxylase	Homo sapiens	74-77
28526196-3	2017	This study proposes a new approach to improve the estimation of long-term PAH air-water exchange fluxes by using a multivariate regression model to simulate hourly gaseous PAH concentrations.	Water	82-87	phenylalanine hydroxylase	Homo sapiens	172-175
28039187-4	2017	METHODS: This was a post hoc analysis of patients with CTD-PAH and SSc-PAH from AMBITION, an event-driven, double-blind trial in patients with WHO functional class II/III PAH.	beta-cyclodextrin tetradecasulfate	55-58	phenylalanine hydroxylase	Homo sapiens	59-62
28039187-11	2017	CONCLUSIONS: This post hoc subgroup analysis provides evidence that CTD-PAH and SSc-PAH patients benefit from initial ambrisentan and tadalafil combination therapy.	ambrisentan	118-129	phenylalanine hydroxylase	Homo sapiens	72-75
28039187-11	2017	CONCLUSIONS: This post hoc subgroup analysis provides evidence that CTD-PAH and SSc-PAH patients benefit from initial ambrisentan and tadalafil combination therapy.	ambrisentan	118-129	phenylalanine hydroxylase	Homo sapiens	84-87
28039187-11	2017	CONCLUSIONS: This post hoc subgroup analysis provides evidence that CTD-PAH and SSc-PAH patients benefit from initial ambrisentan and tadalafil combination therapy.	Tadalafil	134-143	phenylalanine hydroxylase	Homo sapiens	72-75
28039187-11	2017	CONCLUSIONS: This post hoc subgroup analysis provides evidence that CTD-PAH and SSc-PAH patients benefit from initial ambrisentan and tadalafil combination therapy.	Tadalafil	134-143	phenylalanine hydroxylase	Homo sapiens	84-87
28342081-5	2017	Further analysis revealed that PAH patterns in soil samples also showed some difference between secondary copper and aluminum smelter, which may be attributed to the difference in their fuel and smelting process.	Copper	106-112	phenylalanine hydroxylase	Homo sapiens	31-34
28706611-5	2017	RESULTS: Mutation analysis revealed a novel homozygous insertion of a single adenine nucleotide at position 335 in exon 3 of the PAH gene.	Adenine Nucleotides	77-95	phenylalanine hydroxylase	Homo sapiens	129-132
28540542-4	2017	Four PAH sources were identified using the positive matrix factorization model and conditional probability function, which were vehicular emissions (45%), heavy oil combustion (23%), coal and natural gas combustion (22%), and biomass combustion (10%).	heavy oil	155-164	phenylalanine hydroxylase	Homo sapiens	5-8
28680815-1	2017	Mammalian phenylalanine hydroxylase (PAH) is a key enzyme in l-phenylalanine (l-Phe) metabolism and is active as a homotetramer.	Phenylalanine	61-76	phenylalanine hydroxylase	Homo sapiens	10-35
28680815-1	2017	Mammalian phenylalanine hydroxylase (PAH) is a key enzyme in l-phenylalanine (l-Phe) metabolism and is active as a homotetramer.	Phenylalanine	61-76	phenylalanine hydroxylase	Homo sapiens	37-40
28680815-1	2017	Mammalian phenylalanine hydroxylase (PAH) is a key enzyme in l-phenylalanine (l-Phe) metabolism and is active as a homotetramer.	Phenylalanine	78-83	phenylalanine hydroxylase	Homo sapiens	10-35
28680815-1	2017	Mammalian phenylalanine hydroxylase (PAH) is a key enzyme in l-phenylalanine (l-Phe) metabolism and is active as a homotetramer.	Phenylalanine	78-83	phenylalanine hydroxylase	Homo sapiens	37-40
27940234-4	2017	After Nb immobilizing, the as-prepared Fe@RGO/PAH/Nbs showed good selectivity and high quenching ability (92% quenching) in the presence of antigen (Ag) and polyethylene glycol (PEG) modified CdTe QDs (Ag/QDs@PEG), which is a nearly 4 fold than that of the unmodified GO in same condition.	cadmium telluride	192-196	phenylalanine hydroxylase	Homo sapiens	46-49
27940234-4	2017	After Nb immobilizing, the as-prepared Fe@RGO/PAH/Nbs showed good selectivity and high quenching ability (92% quenching) in the presence of antigen (Ag) and polyethylene glycol (PEG) modified CdTe QDs (Ag/QDs@PEG), which is a nearly 4 fold than that of the unmodified GO in same condition.	Polyethylene Glycols	209-212	phenylalanine hydroxylase	Homo sapiens	46-49
27068894-4	2017	Nearly 75 % of the total polycyclic aromatic hydrocarbon (PAH) pool was represented by high molecular four-to-six-ring compounds, deriving mainly from combustion sources.	Polycyclic Aromatic Hydrocarbons	25-56	phenylalanine hydroxylase	Homo sapiens	58-61
28593914-3	2017	BH4 is the co-factor of the enzyme phenylalanine hydroxylase (PAH) and improves PAH activity and, thus, Phe tolerance in the diet.	sapropterin	0-3	phenylalanine hydroxylase	Homo sapiens	35-60
27940234-2	2017	Specifically, we prepared iron doped polyacrylic hydrazide modified reduced graphene nanocomposites (Fe@RGO/PAH) by in-situ polymerization approach and subsequent a one-pot reaction with hydrazine.	Iron	26-30	phenylalanine hydroxylase	Homo sapiens	108-111
27940234-2	2017	Specifically, we prepared iron doped polyacrylic hydrazide modified reduced graphene nanocomposites (Fe@RGO/PAH) by in-situ polymerization approach and subsequent a one-pot reaction with hydrazine.	polyacrylic hydrazide	37-58	phenylalanine hydroxylase	Homo sapiens	108-111
27940234-2	2017	Specifically, we prepared iron doped polyacrylic hydrazide modified reduced graphene nanocomposites (Fe@RGO/PAH) by in-situ polymerization approach and subsequent a one-pot reaction with hydrazine.	Graphite	76-84	phenylalanine hydroxylase	Homo sapiens	108-111
27940234-2	2017	Specifically, we prepared iron doped polyacrylic hydrazide modified reduced graphene nanocomposites (Fe@RGO/PAH) by in-situ polymerization approach and subsequent a one-pot reaction with hydrazine.	hydrazine	187-196	phenylalanine hydroxylase	Homo sapiens	108-111
27940234-3	2017	The resulting Fe@RGO/PAH nanocomposites displayed low nonspecific adsorption to analytes (11% quenching caused by nonspecific adsorption) due to electrostatic, energetic and steric effect of the nanocomposites.	Iron	14-16	phenylalanine hydroxylase	Homo sapiens	21-24
27940234-4	2017	After Nb immobilizing, the as-prepared Fe@RGO/PAH/Nbs showed good selectivity and high quenching ability (92% quenching) in the presence of antigen (Ag) and polyethylene glycol (PEG) modified CdTe QDs (Ag/QDs@PEG), which is a nearly 4 fold than that of the unmodified GO in same condition.	Polyethylene Glycols	157-176	phenylalanine hydroxylase	Homo sapiens	46-49
27940234-4	2017	After Nb immobilizing, the as-prepared Fe@RGO/PAH/Nbs showed good selectivity and high quenching ability (92% quenching) in the presence of antigen (Ag) and polyethylene glycol (PEG) modified CdTe QDs (Ag/QDs@PEG), which is a nearly 4 fold than that of the unmodified GO in same condition.	Polyethylene Glycols	178-181	phenylalanine hydroxylase	Homo sapiens	46-49
28342081-5	2017	Further analysis revealed that PAH patterns in soil samples also showed some difference between secondary copper and aluminum smelter, which may be attributed to the difference in their fuel and smelting process.	Aluminum	117-125	phenylalanine hydroxylase	Homo sapiens	31-34
28342081-6	2017	PAH patterns and diagnostic ratios indicated that biomass burning may be also an important source of PAHs in the surrounding soil in addition to the emissions from the plants investigated.	Polycyclic Aromatic Hydrocarbons	101-105	phenylalanine hydroxylase	Homo sapiens	0-3
28175985-3	2017	Hence, we investigated associations (1) between PAH exposure and IgE levels and asthma in children and (2) between PAH exposure and the oxidative stress marker 8OHdG potentially involved in disease pathogenesis stratifying by (3) sex-based differences.	8-ohdg	160-165	phenylalanine hydroxylase	Homo sapiens	115-118
28175985-5	2017	Urine biomarker of PAH exposure (1-OHP levels) was measured by UPLC-MS/MS and a marker of oxidative stress (8OHdG) was measured by ELISA.	Oxaliplatin	33-38	phenylalanine hydroxylase	Homo sapiens	19-22
28175985-8	2017	A mediation analysis was conducted to evaluate whether the risk of increased IgE and asthma related to PAH exposure is explained by 8OHdG changes.	8-ohdg	132-137	phenylalanine hydroxylase	Homo sapiens	103-106
28175985-13	2017	It is estimated that 35% of the effect of PAH exposure on asthma is mediated by 8OHdG levels.	8-ohdg	80-85	phenylalanine hydroxylase	Homo sapiens	42-45
27925506-0	2017	Aliphatic and polycyclic aromatic hydrocarbons (PAHs) in soils of the northwest Qinling Mountains: Patterns, potential risk and an appraisal of the PAH ratios to infer their source.	Polycyclic Aromatic Hydrocarbons	14-46	phenylalanine hydroxylase	Homo sapiens	48-51
28274234-1	2017	BACKGROUND: Sapropterin dihydrochloride, a synthetic formulation of BH4, the cofactor for phenylalanine hydroxylase (PAH, EC 1.14.16.1), was initially approved in Europe only for patients &gt;=4 years with BH4-responsive phenylketonuria.	sapropterin	12-39	phenylalanine hydroxylase	Homo sapiens	90-115
28007386-3	2017	In general, the PAH levels of the water samples from Chabahar Bay were higher in postmonsoon than in premonsoon (p&lt;0.05).	Water	34-39	phenylalanine hydroxylase	Homo sapiens	16-19
28065424-3	2017	Biomonitoring of hydroxylated PAH (OH-PAH) metabolites in urine provides an integrated measure of exposure to PAHs via multiple routes and has been used to characterize exposure to PAHs in humans.	Polycyclic Aromatic Hydrocarbons	110-114	phenylalanine hydroxylase	Homo sapiens	30-33
28065424-3	2017	Biomonitoring of hydroxylated PAH (OH-PAH) metabolites in urine provides an integrated measure of exposure to PAHs via multiple routes and has been used to characterize exposure to PAHs in humans.	Polycyclic Aromatic Hydrocarbons	110-114	phenylalanine hydroxylase	Homo sapiens	38-41
28065424-3	2017	Biomonitoring of hydroxylated PAH (OH-PAH) metabolites in urine provides an integrated measure of exposure to PAHs via multiple routes and has been used to characterize exposure to PAHs in humans.	Polycyclic Aromatic Hydrocarbons	181-185	phenylalanine hydroxylase	Homo sapiens	30-33
28065424-3	2017	Biomonitoring of hydroxylated PAH (OH-PAH) metabolites in urine provides an integrated measure of exposure to PAHs via multiple routes and has been used to characterize exposure to PAHs in humans.	Polycyclic Aromatic Hydrocarbons	181-185	phenylalanine hydroxylase	Homo sapiens	38-41
28077210-2	2017	Here, we analyzed 16 PAH occurrences in water, suspended particulate matter (SPM), and sediment monthly for a year in the Maozhou River mainstream (Shenzhen, South China).	Water	40-45	phenylalanine hydroxylase	Homo sapiens	21-24
28077210-3	2017	Monthly rainfall positively correlated with both total PAH concentrations in filtered water (water PAHs) and SPM.	Water	86-91	phenylalanine hydroxylase	Homo sapiens	55-58
28274234-1	2017	BACKGROUND: Sapropterin dihydrochloride, a synthetic formulation of BH4, the cofactor for phenylalanine hydroxylase (PAH, EC 1.14.16.1), was initially approved in Europe only for patients &gt;=4 years with BH4-responsive phenylketonuria.	sapropterin	68-71	phenylalanine hydroxylase	Homo sapiens	90-115
28182360-1	2017	BACKGROUND: Deficiency of phenylalanine hydroxylase (PAH) enzyme and elevation of phenylalanine in body fluids cause phenylketonuria (PKU).	Phenylalanine	26-39	phenylalanine hydroxylase	Homo sapiens	53-56
27816287-5	2017	Based on both the results of a principal component analysis (PCA) and the PAH ratios, the main sources of the PAHs in soils were determined to be the combustion of coal and petroleum.	Polycyclic Aromatic Hydrocarbons	110-114	phenylalanine hydroxylase	Homo sapiens	74-77
27933233-3	2016	An important way of enhancing the rate of PAH desorption is to compost crude oil sludge by incorporating commercial surfactants, thereby making them available for microbial degradation.	Oils	77-80	phenylalanine hydroxylase	Homo sapiens	42-45
28174686-0	2017	PKU mutation p.G46S prevents the stereospecific binding of l-phenylalanine to the dimer of human phenylalanine hydroxylase regulatory domain.	Phenylalanine	59-74	phenylalanine hydroxylase	Homo sapiens	97-122
28174686-1	2017	Mammalian phenylalanine hydroxylase (PAH) has a potential allosteric regulatory binding site for l-phenylalanine (l-Phe), in addition to its catalytic site.	Phenylalanine	97-112	phenylalanine hydroxylase	Homo sapiens	10-35
28174686-1	2017	Mammalian phenylalanine hydroxylase (PAH) has a potential allosteric regulatory binding site for l-phenylalanine (l-Phe), in addition to its catalytic site.	Phenylalanine	97-112	phenylalanine hydroxylase	Homo sapiens	37-40
28174686-1	2017	Mammalian phenylalanine hydroxylase (PAH) has a potential allosteric regulatory binding site for l-phenylalanine (l-Phe), in addition to its catalytic site.	Phenylalanine	114-119	phenylalanine hydroxylase	Homo sapiens	10-35
28174686-1	2017	Mammalian phenylalanine hydroxylase (PAH) has a potential allosteric regulatory binding site for l-phenylalanine (l-Phe), in addition to its catalytic site.	Phenylalanine	114-119	phenylalanine hydroxylase	Homo sapiens	37-40
27886187-8	2016	The decreased CPSI expression in CHD-PAH patients may reveal a mechanism related to endogenous nitric oxide and the decrease of CFHR2 protein may demonstrate the deficiency of the immune system and coagulation mechanism.	Nitric Oxide	95-107	phenylalanine hydroxylase	Homo sapiens	37-40
27450342-3	2016	Further kinetic analysis reveals that the oxidation of individual PAH in the biphasic tar/water system follows the first-order kinetics, and individual PAH oxidation rate is primary determined by the mass transfer coefficients, tar/water interfacial areas, the aqueous solubility of individual PAH and its concentration in coal tar.	Water	90-95	phenylalanine hydroxylase	Homo sapiens	66-69
27450342-3	2016	Further kinetic analysis reveals that the oxidation of individual PAH in the biphasic tar/water system follows the first-order kinetics, and individual PAH oxidation rate is primary determined by the mass transfer coefficients, tar/water interfacial areas, the aqueous solubility of individual PAH and its concentration in coal tar.	Water	232-237	phenylalanine hydroxylase	Homo sapiens	66-69
27450342-3	2016	Further kinetic analysis reveals that the oxidation of individual PAH in the biphasic tar/water system follows the first-order kinetics, and individual PAH oxidation rate is primary determined by the mass transfer coefficients, tar/water interfacial areas, the aqueous solubility of individual PAH and its concentration in coal tar.	Water	232-237	phenylalanine hydroxylase	Homo sapiens	152-155
27450342-3	2016	Further kinetic analysis reveals that the oxidation of individual PAH in the biphasic tar/water system follows the first-order kinetics, and individual PAH oxidation rate is primary determined by the mass transfer coefficients, tar/water interfacial areas, the aqueous solubility of individual PAH and its concentration in coal tar.	Water	232-237	phenylalanine hydroxylase	Homo sapiens	152-155
20301677-0	1993	Phenylalanine Hydroxylase Deficiency CLINICAL CHARACTERISTICS: Phenylalanine hydroxylase (PAH) deficiency results in intolerance to the dietary intake of the essential amino acid phenylalanine and produces a spectrum of disorders.	essential amino acid phenylalanine	158-192	phenylalanine hydroxylase	Homo sapiens	63-88
20301677-0	1993	Phenylalanine Hydroxylase Deficiency CLINICAL CHARACTERISTICS: Phenylalanine hydroxylase (PAH) deficiency results in intolerance to the dietary intake of the essential amino acid phenylalanine and produces a spectrum of disorders.	essential amino acid phenylalanine	158-192	phenylalanine hydroxylase	Homo sapiens	90-93
29291362-1	2017	Phenylketonuria (PKU) is the autosomal recessive deficiency of phenylalanine hydroxylase resulting in the accumulation of phenylalanine (Phe) in blood and in the brain.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	63-88
27262414-0	2016	Relationship between the water-exchangeable fraction of PAH and the organic matter composition of sediments.	Water	25-30	phenylalanine hydroxylase	Homo sapiens	56-59
27262414-3	2016	Simultaneously, the water-exchangeable fraction of the sorbed PAH defined as the amount of PAH freely exchanged between the water and the sediment (by opposition to the PAH harshly sorbed to the sediments particles) was determined using a passive sampler methodology recently developed.	Water	20-25	phenylalanine hydroxylase	Homo sapiens	62-65
27262414-3	2016	Simultaneously, the water-exchangeable fraction of the sorbed PAH defined as the amount of PAH freely exchanged between the water and the sediment (by opposition to the PAH harshly sorbed to the sediments particles) was determined using a passive sampler methodology recently developed.	Water	20-25	phenylalanine hydroxylase	Homo sapiens	91-94
27262414-3	2016	Simultaneously, the water-exchangeable fraction of the sorbed PAH defined as the amount of PAH freely exchanged between the water and the sediment (by opposition to the PAH harshly sorbed to the sediments particles) was determined using a passive sampler methodology recently developed.	Water	20-25	phenylalanine hydroxylase	Homo sapiens	91-94
27262414-3	2016	Simultaneously, the water-exchangeable fraction of the sorbed PAH defined as the amount of PAH freely exchanged between the water and the sediment (by opposition to the PAH harshly sorbed to the sediments particles) was determined using a passive sampler methodology recently developed.	Water	124-129	phenylalanine hydroxylase	Homo sapiens	62-65
27262414-3	2016	Simultaneously, the water-exchangeable fraction of the sorbed PAH defined as the amount of PAH freely exchanged between the water and the sediment (by opposition to the PAH harshly sorbed to the sediments particles) was determined using a passive sampler methodology recently developed.	Water	124-129	phenylalanine hydroxylase	Homo sapiens	91-94
27262414-3	2016	Simultaneously, the water-exchangeable fraction of the sorbed PAH defined as the amount of PAH freely exchanged between the water and the sediment (by opposition to the PAH harshly sorbed to the sediments particles) was determined using a passive sampler methodology recently developed.	Water	124-129	phenylalanine hydroxylase	Homo sapiens	91-94
27262414-5	2016	Hence, the present study provides the distribution coefficients of PAH between the water and 4 different OM fractions combusted at a specific temperature range.	Water	83-88	phenylalanine hydroxylase	Homo sapiens	67-70
27669419-2	2016	The N-hydroxycinnamide moiety is identified as critical for potent and tetrahydrobiopterin-competitive inhibition of phenylalanine hydroxylase leading to increases in phenylalanine and decreases in tyrosine levels.	n-hydroxycinnamide	4-22	phenylalanine hydroxylase	Homo sapiens	117-142
27669419-2	2016	The N-hydroxycinnamide moiety is identified as critical for potent and tetrahydrobiopterin-competitive inhibition of phenylalanine hydroxylase leading to increases in phenylalanine and decreases in tyrosine levels.	sapropterin	71-90	phenylalanine hydroxylase	Homo sapiens	117-142
27669419-2	2016	The N-hydroxycinnamide moiety is identified as critical for potent and tetrahydrobiopterin-competitive inhibition of phenylalanine hydroxylase leading to increases in phenylalanine and decreases in tyrosine levels.	Tyrosine	198-206	phenylalanine hydroxylase	Homo sapiens	117-142
27266337-2	2016	Four hydroxy metabolites of known and suspected carcinogenic PAHs (benzo[a]pyrene (B[a]P), benz[a]anthracene (B[a]A), and chrysene (CRY)) were selected as suitable biomarkers of PAH exposure and associated risks to human health.	Benzo(a)pyrene	67-81	phenylalanine hydroxylase	Homo sapiens	61-64
27255324-5	2016	Symmetric and dissymmetric Gemini surfactants have opposite effect on the aspect of removing of PAH attributing to their solubilization and sorption behavior in soil-water system.	Water	166-171	phenylalanine hydroxylase	Homo sapiens	96-99
27452439-3	2016	We hypothesized that exposure of human fetoplacental endothelial cells (ECs) to the PAH benzo[a]yrene (BaP) would result in up-regulation of cyclooxygenase-2 (PTGS2) and preferential production of vasoconstrictive prostanoids via activation of the aryl hydrocarbon receptor (AHR) pathway.	benzylaminopurine	103-106	phenylalanine hydroxylase	Homo sapiens	84-87
27452439-3	2016	We hypothesized that exposure of human fetoplacental endothelial cells (ECs) to the PAH benzo[a]yrene (BaP) would result in up-regulation of cyclooxygenase-2 (PTGS2) and preferential production of vasoconstrictive prostanoids via activation of the aryl hydrocarbon receptor (AHR) pathway.	Prostaglandins	214-225	phenylalanine hydroxylase	Homo sapiens	84-87
27196671-5	2016	We then exposed cells to either binary mixtures of the highly genotoxic benzo[a]pyrene (B[a]P) with each PAH or complex mixtures of all studied PAHs mimicking by real emissions including combustion of wood, cigarette smoke, and atmospheres of garage, silicon factory and urban environments.	Benzo(a)pyrene	72-86	phenylalanine hydroxylase	Homo sapiens	105-108
27037876-0	2016	Assessing the relation between anthropogenic pressure and PAH concentrations in surface water in the Seine River basin using multivariate analysis.	Water	88-93	phenylalanine hydroxylase	Homo sapiens	58-61
27212712-4	2016	We recorded by action spectroscopy the relative intensities of photo-fragmentation and photo-ionization for a set of eight PAH cations ranging in size from 14 to 24 carbon atoms, with different structures.	Carbon	165-171	phenylalanine hydroxylase	Homo sapiens	123-126
26962957-1	2016	Phenylketonuria (PKU) is an autosomal recessive metabolic disorder due to mutations in the phenylalanine hydroxylase (PAH) gene, which converts phenylalanine (PHE) to tyrosine.	Phenylalanine	91-104	phenylalanine hydroxylase	Homo sapiens	118-121
26962957-1	2016	Phenylketonuria (PKU) is an autosomal recessive metabolic disorder due to mutations in the phenylalanine hydroxylase (PAH) gene, which converts phenylalanine (PHE) to tyrosine.	Phenylalanine	159-162	phenylalanine hydroxylase	Homo sapiens	91-116
26962957-1	2016	Phenylketonuria (PKU) is an autosomal recessive metabolic disorder due to mutations in the phenylalanine hydroxylase (PAH) gene, which converts phenylalanine (PHE) to tyrosine.	Phenylalanine	159-162	phenylalanine hydroxylase	Homo sapiens	118-121
26962957-1	2016	Phenylketonuria (PKU) is an autosomal recessive metabolic disorder due to mutations in the phenylalanine hydroxylase (PAH) gene, which converts phenylalanine (PHE) to tyrosine.	Tyrosine	167-175	phenylalanine hydroxylase	Homo sapiens	91-116
26962957-1	2016	Phenylketonuria (PKU) is an autosomal recessive metabolic disorder due to mutations in the phenylalanine hydroxylase (PAH) gene, which converts phenylalanine (PHE) to tyrosine.	Tyrosine	167-175	phenylalanine hydroxylase	Homo sapiens	118-121
27145334-1	2016	Mammalian phenylalanine hydroxylase (PheH) is an allosteric enzyme that catalyzes the first step in the catabolism of the amino acid phenylalanine.	amino acid phenylalanine	122-146	phenylalanine hydroxylase	Homo sapiens	10-35
27145334-1	2016	Mammalian phenylalanine hydroxylase (PheH) is an allosteric enzyme that catalyzes the first step in the catabolism of the amino acid phenylalanine.	amino acid phenylalanine	122-146	phenylalanine hydroxylase	Homo sapiens	37-41
27145334-8	2016	Together, these results support a model for allostery in PheH in which phenylalanine stabilizes the dimerization of the regulatory domains and exposes the active site for substrate binding and other structural changes needed for activity.	Phenylalanine	71-84	phenylalanine hydroxylase	Homo sapiens	57-61
26122564-3	2016	Accumulation of PAH degraders was particularly high in the SML, where PAHs accumulated.	Polycyclic Aromatic Hydrocarbons	70-74	phenylalanine hydroxylase	Homo sapiens	16-19
26883219-1	2016	Phenylalanine hydroxylase (PAH) deficiency is an inherited metabolic disorder requiring life-long restriction of dietary protein and phenylalanine-free medical food.	Phenylalanine	133-146	phenylalanine hydroxylase	Homo sapiens	0-25
27049649-1	2016	The multi-domain enzyme phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of dietary I-phenylalanine (Phe) to I-tyrosine.	i-phenylalanine	95-110	phenylalanine hydroxylase	Homo sapiens	24-49
27049649-1	2016	The multi-domain enzyme phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of dietary I-phenylalanine (Phe) to I-tyrosine.	i-phenylalanine	95-110	phenylalanine hydroxylase	Homo sapiens	51-54
27049649-1	2016	The multi-domain enzyme phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of dietary I-phenylalanine (Phe) to I-tyrosine.	Phenylalanine	112-115	phenylalanine hydroxylase	Homo sapiens	24-49
27049649-1	2016	The multi-domain enzyme phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of dietary I-phenylalanine (Phe) to I-tyrosine.	Phenylalanine	112-115	phenylalanine hydroxylase	Homo sapiens	51-54
27049649-1	2016	The multi-domain enzyme phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of dietary I-phenylalanine (Phe) to I-tyrosine.	i-tyrosine	120-130	phenylalanine hydroxylase	Homo sapiens	24-49
27049649-1	2016	The multi-domain enzyme phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of dietary I-phenylalanine (Phe) to I-tyrosine.	i-tyrosine	120-130	phenylalanine hydroxylase	Homo sapiens	51-54
27049649-3	2016	Phe is the substrate for the PAH active site, but also an allosteric ligand that increases enzyme activity.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	29-32
27049649-4	2016	Phe has been proposed to bind, in addition to the catalytic domain, a site at the PAH N-terminal regulatory domain (PAH-RD), to activate the enzyme via an unclear mechanism.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	82-85
27049649-4	2016	Phe has been proposed to bind, in addition to the catalytic domain, a site at the PAH N-terminal regulatory domain (PAH-RD), to activate the enzyme via an unclear mechanism.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	116-119
27049649-5	2016	Here we report the crystal structure of human PAH-RD bound with Phe at 1.8 A resolution, revealing a homodimer of ACT folds with Phe bound at the dimer interface.	Phenylalanine	64-67	phenylalanine hydroxylase	Homo sapiens	46-49
27049649-5	2016	Here we report the crystal structure of human PAH-RD bound with Phe at 1.8 A resolution, revealing a homodimer of ACT folds with Phe bound at the dimer interface.	Phenylalanine	129-132	phenylalanine hydroxylase	Homo sapiens	46-49
27049649-6	2016	This work delivers the structural evidence to support previous solution studies that a binding site exists in the RD for Phe, and that Phe binding results in dimerization of PAH-RD.	Phenylalanine	121-124	phenylalanine hydroxylase	Homo sapiens	174-177
27049649-6	2016	This work delivers the structural evidence to support previous solution studies that a binding site exists in the RD for Phe, and that Phe binding results in dimerization of PAH-RD.	Phenylalanine	135-138	phenylalanine hydroxylase	Homo sapiens	174-177
27049649-7	2016	Consistent with our structural observation, a disease-associated PAH mutant impaired in Phe binding disrupts the monomer:dimer equilibrium of PAH-RD.	Phenylalanine	88-91	phenylalanine hydroxylase	Homo sapiens	65-68
27049649-7	2016	Consistent with our structural observation, a disease-associated PAH mutant impaired in Phe binding disrupts the monomer:dimer equilibrium of PAH-RD.	Phenylalanine	88-91	phenylalanine hydroxylase	Homo sapiens	142-145
27049649-8	2016	Our data therefore support an emerging model of PAH allosteric regulation, whereby Phe binds to PAH-RD and mediates the dimerization of regulatory modules that would bring about conformational changes to activate the enzyme.	Phenylalanine	83-86	phenylalanine hydroxylase	Homo sapiens	48-51
27049649-8	2016	Our data therefore support an emerging model of PAH allosteric regulation, whereby Phe binds to PAH-RD and mediates the dimerization of regulatory modules that would bring about conformational changes to activate the enzyme.	Phenylalanine	83-86	phenylalanine hydroxylase	Homo sapiens	96-99
26803807-4	2016	PAH variant proteins were transiently co-transfected in COS-7 cells.	carbonyl sulfide	56-59	phenylalanine hydroxylase	Homo sapiens	0-3
26697808-3	2016	Initially, silicone cord sorption efficacy was determined by assessing sorption kinetics using PAH-spiked sand (phenanthrene, pyrene and benzo[a]pyrene; 10-1000mgkg(-1)).	Silicones	11-19	phenylalanine hydroxylase	Homo sapiens	95-98
26490935-0	2016	Polycyclic aromatic hydrocarbons (PAHs) at traffic and urban background sites of northern Greece: source apportionment of ambient PAH levels and PAH-induced lung cancer risk.	Polycyclic Aromatic Hydrocarbons	0-32	phenylalanine hydroxylase	Homo sapiens	34-37
26490935-0	2016	Polycyclic aromatic hydrocarbons (PAHs) at traffic and urban background sites of northern Greece: source apportionment of ambient PAH levels and PAH-induced lung cancer risk.	Polycyclic Aromatic Hydrocarbons	0-32	phenylalanine hydroxylase	Homo sapiens	130-133
26547031-0	2016	Modeling the adsorption of PAH mixture in silica nanopores by molecular dynamic simulation combined with machine learning.	Silicon Dioxide	42-48	phenylalanine hydroxylase	Homo sapiens	27-30
26697808-4	2016	Irrespective of PAH and concentration, &gt;95% of the initial PAH mass partitioned into the silicone cord within 12h although rates were lower at higher concentration and with increasing hydrophobicity.	Silicones	92-100	phenylalanine hydroxylase	Homo sapiens	62-65
26490935-0	2016	Polycyclic aromatic hydrocarbons (PAHs) at traffic and urban background sites of northern Greece: source apportionment of ambient PAH levels and PAH-induced lung cancer risk.	Polycyclic Aromatic Hydrocarbons	34-38	phenylalanine hydroxylase	Homo sapiens	130-133
26479306-0	2016	Towards the identification of the allosteric Phe-binding site in phenylalanine hydroxylase.	Phenylalanine	45-48	phenylalanine hydroxylase	Homo sapiens	65-90
26599600-2	2016	The layer-by-layer assembled poly(allylamine hydrochloride)/poly(acrylic acid) (PAH/PAA) network is used as the model material.	polyallylamine	29-59	phenylalanine hydroxylase	Homo sapiens	80-83
26599600-2	2016	The layer-by-layer assembled poly(allylamine hydrochloride)/poly(acrylic acid) (PAH/PAA) network is used as the model material.	carbopol 940	60-78	phenylalanine hydroxylase	Homo sapiens	80-83
26599600-6	2016	Second, ionic cross-links can break and self-re-form, and this mechanism dominates force relaxation of PAH/PAA under a constant indentation depth.	carbopol 940	107-110	phenylalanine hydroxylase	Homo sapiens	103-106
27014574-1	2016	BACKGROUND: Phenylketonuria (PKU) is characterized by phenylalanine (Phe) accumulation to toxic levels due to the low activity of phenylalanine-hydroxylase.	Phenylalanine	54-67	phenylalanine hydroxylase	Homo sapiens	130-155
27014574-1	2016	BACKGROUND: Phenylketonuria (PKU) is characterized by phenylalanine (Phe) accumulation to toxic levels due to the low activity of phenylalanine-hydroxylase.	Phenylalanine	12-15	phenylalanine hydroxylase	Homo sapiens	130-155
26573838-1	2016	The adsorption behavior of pyrene on corncob was studied to provide a theoretical basis for the possible use of this material as an immobilized carrier for improving the bioremediation of PAH-contaminated soil.	pyrene	27-33	phenylalanine hydroxylase	Homo sapiens	188-191
26953246-6	2016	Supplementation with the cofactor BH4 exerts a multifactorial response in PAH, where one of the main mechanisms for the induced increase in PAH activity in BH4- responsive PKU patients appears to be a pharmacological chaperone effect.	sapropterin	34-37	phenylalanine hydroxylase	Homo sapiens	74-77
26953246-6	2016	Supplementation with the cofactor BH4 exerts a multifactorial response in PAH, where one of the main mechanisms for the induced increase in PAH activity in BH4- responsive PKU patients appears to be a pharmacological chaperone effect.	sapropterin	34-37	phenylalanine hydroxylase	Homo sapiens	140-143
26953246-6	2016	Supplementation with the cofactor BH4 exerts a multifactorial response in PAH, where one of the main mechanisms for the induced increase in PAH activity in BH4- responsive PKU patients appears to be a pharmacological chaperone effect.	sapropterin	156-159	phenylalanine hydroxylase	Homo sapiens	74-77
26953246-6	2016	Supplementation with the cofactor BH4 exerts a multifactorial response in PAH, where one of the main mechanisms for the induced increase in PAH activity in BH4- responsive PKU patients appears to be a pharmacological chaperone effect.	sapropterin	156-159	phenylalanine hydroxylase	Homo sapiens	140-143
26479306-2	2016	PAH, a tetrameric enzyme, is highly regulated and displays positive cooperativity for its substrate, Phe.	Phenylalanine	101-104	phenylalanine hydroxylase	Homo sapiens	0-3
26602133-3	2016	The most common cause of PKU is deficiency of the enzyme phenylalanine hydroxylase that converts phenylalanine to tyrosine.	Tyrosine	114-122	phenylalanine hydroxylase	Homo sapiens	57-82
26602133-5	2016	Less commonly, it can result from defects in the synthesis or regeneration of tetrahydrobiopterin (BH4), an essential cofactor for the enzyme phenylalanine hydroxylase.	sapropterin	78-97	phenylalanine hydroxylase	Homo sapiens	142-167
26602133-5	2016	Less commonly, it can result from defects in the synthesis or regeneration of tetrahydrobiopterin (BH4), an essential cofactor for the enzyme phenylalanine hydroxylase.	sapropterin	99-102	phenylalanine hydroxylase	Homo sapiens	142-167
26530167-2	2016	Benzo(a)pyrene (B(a)P), a representative PAH compound is released into the environment from automobile exhausts, industrial emissions, and considerable intake of B(a)P is also expected in people who are smokers and barbecued red meat eaters.	Benzo(a)pyrene	0-14	phenylalanine hydroxylase	Homo sapiens	41-44
26530167-2	2016	Benzo(a)pyrene (B(a)P), a representative PAH compound is released into the environment from automobile exhausts, industrial emissions, and considerable intake of B(a)P is also expected in people who are smokers and barbecued red meat eaters.	Benzo(a)pyrene	16-21	phenylalanine hydroxylase	Homo sapiens	41-44
26530167-2	2016	Benzo(a)pyrene (B(a)P), a representative PAH compound is released into the environment from automobile exhausts, industrial emissions, and considerable intake of B(a)P is also expected in people who are smokers and barbecued red meat eaters.	Benzo(a)pyrene	162-167	phenylalanine hydroxylase	Homo sapiens	41-44
26691207-7	2016	Also during the casting moulds with molten metal, they emit pyrolysis gases containing many different compounds, often dangerous from the BTEX and PAH group, which has adverse impacts on the environment and workers.	Metals	43-48	phenylalanine hydroxylase	Homo sapiens	147-150
26517941-0	2015	Evaluation of the boundary condition influence on PAH concentrations in the water column during the sediment dredging of a port.	Water	76-81	phenylalanine hydroxylase	Homo sapiens	50-53
26517941-3	2015	The results showed relatively low background PAH concentrations in the water column and confirmed the dredging as the primary rising factor of concentrations in the water column, but also showed a complex scenario in which the different environmental and dredging factors forced the concentrations at different levels and moments.	Water	71-76	phenylalanine hydroxylase	Homo sapiens	45-48
26666653-5	2015	METHODS: A total of 364 French patients among which, 9 % had mild hyperphenylalaninemia, 17.7 % mild phenylketonuria and 73.1 % classical phenylketonuria, benefited from a 24-hour BH4-loading test and had the PAH gene sequenced and analyzed by Multiplex Ligation Probe Amplification.	sapropterin	180-183	phenylalanine hydroxylase	Homo sapiens	209-212
26370630-2	2015	Prior to admission, his PAH had been successfully managed with the use of tadalafil, ambrisentan and inhaled Tyvaso.	Tadalafil	74-83	phenylalanine hydroxylase	Homo sapiens	24-27
26241318-4	2015	These solution properties are consistent with the regulatory mechanisms of the two enzymes, in that phenylalanine hydroxylase is activated by phenylalanine binding to an allosteric site, while tyrosine hydroxylase is regulated by binding of catecholamines in the active site.	Catecholamines	241-255	phenylalanine hydroxylase	Homo sapiens	100-125
26322415-1	2015	BACKGROUND: A growing body of research has suggested that tetrahydrobiopterin (BH4) responsive phenotype can be predicted by the phenylalanine hydroxylase (PAH) genotype in patients with phenylketonuria (PKU), but data concerning the association between genotype and BH4 responsiveness are scarce in China.	sapropterin	58-77	phenylalanine hydroxylase	Homo sapiens	129-154
26322415-1	2015	BACKGROUND: A growing body of research has suggested that tetrahydrobiopterin (BH4) responsive phenotype can be predicted by the phenylalanine hydroxylase (PAH) genotype in patients with phenylketonuria (PKU), but data concerning the association between genotype and BH4 responsiveness are scarce in China.	sapropterin	58-77	phenylalanine hydroxylase	Homo sapiens	156-159
26322415-1	2015	BACKGROUND: A growing body of research has suggested that tetrahydrobiopterin (BH4) responsive phenotype can be predicted by the phenylalanine hydroxylase (PAH) genotype in patients with phenylketonuria (PKU), but data concerning the association between genotype and BH4 responsiveness are scarce in China.	sapropterin	79-82	phenylalanine hydroxylase	Homo sapiens	129-154
26322415-1	2015	BACKGROUND: A growing body of research has suggested that tetrahydrobiopterin (BH4) responsive phenotype can be predicted by the phenylalanine hydroxylase (PAH) genotype in patients with phenylketonuria (PKU), but data concerning the association between genotype and BH4 responsiveness are scarce in China.	sapropterin	79-82	phenylalanine hydroxylase	Homo sapiens	156-159
26322415-1	2015	BACKGROUND: A growing body of research has suggested that tetrahydrobiopterin (BH4) responsive phenotype can be predicted by the phenylalanine hydroxylase (PAH) genotype in patients with phenylketonuria (PKU), but data concerning the association between genotype and BH4 responsiveness are scarce in China.	sapropterin	267-270	phenylalanine hydroxylase	Homo sapiens	129-154
26322415-1	2015	BACKGROUND: A growing body of research has suggested that tetrahydrobiopterin (BH4) responsive phenotype can be predicted by the phenylalanine hydroxylase (PAH) genotype in patients with phenylketonuria (PKU), but data concerning the association between genotype and BH4 responsiveness are scarce in China.	sapropterin	267-270	phenylalanine hydroxylase	Homo sapiens	156-159
25894915-12	2015	This study identified one novel PAH variant-c.699C&gt;G-and and tries to show a genotype-phenotype relationship also regarding BH4-responsiveness.	sapropterin	127-130	phenylalanine hydroxylase	Homo sapiens	32-35
26370630-2	2015	Prior to admission, his PAH had been successfully managed with the use of tadalafil, ambrisentan and inhaled Tyvaso.	ambrisentan	85-96	phenylalanine hydroxylase	Homo sapiens	24-27
26370630-2	2015	Prior to admission, his PAH had been successfully managed with the use of tadalafil, ambrisentan and inhaled Tyvaso.	treprostinil	109-115	phenylalanine hydroxylase	Homo sapiens	24-27
25600323-3	2015	The urinary metabolites 1-hydroxypyrene, 1-,2-,3-,4- and 9-hydroxyphenanthrene and 3-hydroxybenzo[a]pyrene were selected as indicators of PAH exposure.	1-hydroxypyrene	24-39	phenylalanine hydroxylase	Homo sapiens	138-141
26701937-1	2015	Sapropterin enhances phenylalanine hydroxylase activity, thus lowering blood phenylalanine (Phe) concentration while increasing protein tolerance in sapropterin-responsive patients.	sapropterin	0-11	phenylalanine hydroxylase	Homo sapiens	21-46
26962606-5	2015	Health Canada has approved eight treatment options covering four different classes of drugs for PAH, World Health Organization (WHO) Group 1: Prostanoids (epoprostenol, treprostinil).	Prostaglandins	142-153	phenylalanine hydroxylase	Homo sapiens	96-99
26962606-12	2015	The objective of this review was to evaluate the beneficial and harmful effects of macitentan (Opsumit) as monotherapy or in combination with other drugs for the treatment of PAH patients (WHO Group 1) of WHO FC II or III.	macitentan	83-93	phenylalanine hydroxylase	Homo sapiens	175-178
26962606-12	2015	The objective of this review was to evaluate the beneficial and harmful effects of macitentan (Opsumit) as monotherapy or in combination with other drugs for the treatment of PAH patients (WHO Group 1) of WHO FC II or III.	macitentan	95-102	phenylalanine hydroxylase	Homo sapiens	175-178
25772555-4	2015	When associated with silica sand, PAHs were released at relatively low temperatures (&lt;300  C) close to corresponding boiling point, whereas for the PAH/bentonite mixture, PAHs were desorbed at much higher temperatures; they were also present in much lower abundance and were associated with mono-aromatic compounds.	Silicon Dioxide	21-27	phenylalanine hydroxylase	Homo sapiens	34-37
25772555-5	2015	With bentonite, the PAH abundances decreased and the mono-aromatics increased with the increasing PAH molecular weight.	Bentonite	5-14	phenylalanine hydroxylase	Homo sapiens	20-23
25772555-5	2015	With bentonite, the PAH abundances decreased and the mono-aromatics increased with the increasing PAH molecular weight.	Bentonite	5-14	phenylalanine hydroxylase	Homo sapiens	98-101
25772555-6	2015	These results indicated a clear PAH retention by the bentonite due to polymerization, followed by a thermal cracking at higher temperatures.	Bentonite	53-62	phenylalanine hydroxylase	Homo sapiens	32-35
25882749-6	2015	We further explored possible relationships between mutations in the PAH gene, BH4 responsiveness and growth outcome.	sapropterin	78-81	phenylalanine hydroxylase	Homo sapiens	68-71
26363863-2	2015	The main cause is due to a mutation in the gene that codes the phenylalanine hydroxylase that catalyses the reaction that converts phenylalanine into tyrosine.	Tyrosine	150-158	phenylalanine hydroxylase	Homo sapiens	63-88
26151110-1	2015	The adhesive characteristics of poly(allylamine hydrochloride) (PAH)/hyaluronic acid (HA) self-assemblies were investigated using contact adhesion testing.	polyallylamine	32-62	phenylalanine hydroxylase	Homo sapiens	64-67
26351554-1	2015	OBJECTIVES: Phenylketonuria (PKU) is a genetic inborn error of phenylalanine (Phe) metabolism resulting from insufficiency in the hepatic enzyme, phenylalanine hydroxylase (PAH), which leads to elevated levels of Phe in the blood.	Phenylalanine	12-15	phenylalanine hydroxylase	Homo sapiens	146-171
26351554-1	2015	OBJECTIVES: Phenylketonuria (PKU) is a genetic inborn error of phenylalanine (Phe) metabolism resulting from insufficiency in the hepatic enzyme, phenylalanine hydroxylase (PAH), which leads to elevated levels of Phe in the blood.	Phenylalanine	12-15	phenylalanine hydroxylase	Homo sapiens	173-176
26351554-1	2015	OBJECTIVES: Phenylketonuria (PKU) is a genetic inborn error of phenylalanine (Phe) metabolism resulting from insufficiency in the hepatic enzyme, phenylalanine hydroxylase (PAH), which leads to elevated levels of Phe in the blood.	Phenylalanine	78-81	phenylalanine hydroxylase	Homo sapiens	146-171
25990285-1	2015	The toxicities of polycyclic aromatic hydrocarbons (PAHs) have been extensively explored due to their carcinogenic and mutagenic potency; however, little is known about the metabolic responses to chronic environmental PAH exposure among the general population.	Polycyclic Aromatic Hydrocarbons	18-50	phenylalanine hydroxylase	Homo sapiens	52-55
25990285-6	2015	1-Hydroxyphenanthrene and dodecadienylcarnitine have potential as sensitive and reliable biomarkers for PAH exposure and its metabolic outcomes, respectively, in the general population.	1-hydroxyphenanthrene	0-21	phenylalanine hydroxylase	Homo sapiens	104-107
25990285-6	2015	1-Hydroxyphenanthrene and dodecadienylcarnitine have potential as sensitive and reliable biomarkers for PAH exposure and its metabolic outcomes, respectively, in the general population.	dodecadienylcarnitine	26-47	phenylalanine hydroxylase	Homo sapiens	104-107
25943030-1	2015	BACKGROUND: Phenylketonuria (PKU) is an autosomal recessive disorder caused by deficiency of hepatic phenylalanine hydroxylase (PAH) leading to increased levels of phenylalanine in the plasma.	Phenylalanine	101-114	phenylalanine hydroxylase	Homo sapiens	128-131
25943030-3	2015	1-(13)C-phenylalanine, a stable isotope can be used to examine phenylalanine metabolism, as the conversion of phenylalanine to tyrosine occurs in vivo via PAH and subsequently releases the carboxyl labeled (13)C as (13)CO2 in breath.	1-(13)c-phenylalanine	0-21	phenylalanine hydroxylase	Homo sapiens	155-158
25943030-3	2015	1-(13)C-phenylalanine, a stable isotope can be used to examine phenylalanine metabolism, as the conversion of phenylalanine to tyrosine occurs in vivo via PAH and subsequently releases the carboxyl labeled (13)C as (13)CO2 in breath.	Phenylalanine	8-21	phenylalanine hydroxylase	Homo sapiens	155-158
25943030-3	2015	1-(13)C-phenylalanine, a stable isotope can be used to examine phenylalanine metabolism, as the conversion of phenylalanine to tyrosine occurs in vivo via PAH and subsequently releases the carboxyl labeled (13)C as (13)CO2 in breath.	Phenylalanine	63-76	phenylalanine hydroxylase	Homo sapiens	155-158
25943030-3	2015	1-(13)C-phenylalanine, a stable isotope can be used to examine phenylalanine metabolism, as the conversion of phenylalanine to tyrosine occurs in vivo via PAH and subsequently releases the carboxyl labeled (13)C as (13)CO2 in breath.	Tyrosine	127-135	phenylalanine hydroxylase	Homo sapiens	155-158
25943030-3	2015	1-(13)C-phenylalanine, a stable isotope can be used to examine phenylalanine metabolism, as the conversion of phenylalanine to tyrosine occurs in vivo via PAH and subsequently releases the carboxyl labeled (13)C as (13)CO2 in breath.	Carbon-13	2-7	phenylalanine hydroxylase	Homo sapiens	155-158
25943030-12	2015	Following sapropterin supplementation for a week, production of (13)CO2 significantly increased in five children with a subsequent decline in blood phenylalanine levels, suggesting improved PAH activity.	sapropterin	10-21	phenylalanine hydroxylase	Homo sapiens	190-193
26000544-1	2015	Phenylketonuria (PKU) is an autosomal recessive disorder of phenylalanine (Phe) metabolism characterized by deficient activity of the hepatic enzyme, phenylalanine hydroxylase.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	150-175
26701937-1	2015	Sapropterin enhances phenylalanine hydroxylase activity, thus lowering blood phenylalanine (Phe) concentration while increasing protein tolerance in sapropterin-responsive patients.	Phenylalanine	92-95	phenylalanine hydroxylase	Homo sapiens	21-46
25557939-5	2015	H2O2 and Fenton-like treatments presented low efficiency to degrade PAH in the soil presenting poor PAH availability, however, the PAH degradation rates were improved with the pre-heating.	Hydrogen Peroxide	0-4	phenylalanine hydroxylase	Homo sapiens	68-71
25557939-5	2015	H2O2 and Fenton-like treatments presented low efficiency to degrade PAH in the soil presenting poor PAH availability, however, the PAH degradation rates were improved with the pre-heating.	Hydrogen Peroxide	0-4	phenylalanine hydroxylase	Homo sapiens	100-103
25557939-5	2015	H2O2 and Fenton-like treatments presented low efficiency to degrade PAH in the soil presenting poor PAH availability, however, the PAH degradation rates were improved with the pre-heating.	Hydrogen Peroxide	0-4	phenylalanine hydroxylase	Homo sapiens	100-103
25557939-6	2015	Consequently H2O2-based treatments (including Fenton-like) are highly sensitive to contaminant availability and seem to be valid methods to estimate the available PAH fraction in contaminated soils.	Hydrogen Peroxide	13-17	phenylalanine hydroxylase	Homo sapiens	163-166
25660215-4	2015	Sapropterin dihydrochloride is a synthetic form of tetrahydrobiopterin, the cofactor of phenylalanine hydroxylase that in pharmacological doses can stabilize and increase residual enzyme activity in some patients with PKU.	sapropterin	0-27	phenylalanine hydroxylase	Homo sapiens	88-113
25726095-2	2015	BH4 responsiveness in phenylalanine hydroxylase (PAH)-deficient patients introduced a new diagnostic aspect for this test.	sapropterin	0-3	phenylalanine hydroxylase	Homo sapiens	22-47
25686536-0	2015	The power of power: electrokinetic control of PAH interactions with exfoliated graphite.	Graphite	79-87	phenylalanine hydroxylase	Homo sapiens	46-49
25692665-0	2015	Kinetics of silver nanoparticle deposition at PAH monolayers: reference QCM results.	Silver	12-18	phenylalanine hydroxylase	Homo sapiens	46-49
25692665-1	2015	The deposition kinetics of silver nanoparticles on Au/SiO2 /PAH substrate was studied under in situ conditions using the QCM method and the ex situ SEM imaging.	Silver	27-33	phenylalanine hydroxylase	Homo sapiens	60-63
25764397-1	2015	Tetrahydrobiopterin (BH4) is a co-factor required for catalytic activity of nitric oxide synthase (NOS) and amino acid-monooxygenases, including phenylalanine hydroxylase.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	145-170
25764397-1	2015	Tetrahydrobiopterin (BH4) is a co-factor required for catalytic activity of nitric oxide synthase (NOS) and amino acid-monooxygenases, including phenylalanine hydroxylase.	sapropterin	21-24	phenylalanine hydroxylase	Homo sapiens	145-170
25644325-2	2015	In this paper, we report on a novel architecture comprising electrospun polyamide 6/poly(allylamine hydrochloride) (PA6/PAH) nanofibers functionalized with multiwalled carbon nanotubes, used to detect the neurotransmitter dopamine (DA).	nylon 6	72-83	phenylalanine hydroxylase	Homo sapiens	116-123
25644325-2	2015	In this paper, we report on a novel architecture comprising electrospun polyamide 6/poly(allylamine hydrochloride) (PA6/PAH) nanofibers functionalized with multiwalled carbon nanotubes, used to detect the neurotransmitter dopamine (DA).	polyallylamine	84-114	phenylalanine hydroxylase	Homo sapiens	116-123
25644325-2	2015	In this paper, we report on a novel architecture comprising electrospun polyamide 6/poly(allylamine hydrochloride) (PA6/PAH) nanofibers functionalized with multiwalled carbon nanotubes, used to detect the neurotransmitter dopamine (DA).	Dopamine	222-230	phenylalanine hydroxylase	Homo sapiens	116-123
25644325-2	2015	In this paper, we report on a novel architecture comprising electrospun polyamide 6/poly(allylamine hydrochloride) (PA6/PAH) nanofibers functionalized with multiwalled carbon nanotubes, used to detect the neurotransmitter dopamine (DA).	Dopamine	232-234	phenylalanine hydroxylase	Homo sapiens	116-123
25577565-8	2015	Among classic responders, 12 (60%) had IPAH and 8 (40%) had connective tissue disease-associated PAH (CTD-PAH); however, only responders with IPAH had improved survival compared with non-responders (p = 0.02).	beta-cyclodextrin tetradecasulfate	102-105	phenylalanine hydroxylase	Homo sapiens	97-100
25660215-4	2015	Sapropterin dihydrochloride is a synthetic form of tetrahydrobiopterin, the cofactor of phenylalanine hydroxylase that in pharmacological doses can stabilize and increase residual enzyme activity in some patients with PKU.	sapropterin	51-70	phenylalanine hydroxylase	Homo sapiens	88-113
25453233-1	2014	Phenylalanine hydroxylase (PheH), a liver enzyme that catalyzes the hydroxylation of excess phenylalanine in the diet to tyrosine, is activated by phenylalanine.	Phenylalanine	92-105	phenylalanine hydroxylase	Homo sapiens	0-25
25458282-2	2015	In this work, polyelectrolyte complexes (PECs) were formed by adding polyacrylic acid (PAA) or 4-O-methylglucuronoxylan (Xyl) on poly(allylamine hydrochloride) (PAH) solutions, at different ionic strength and neutral pH.	4-O-methyl glucuronoxylan	95-119	phenylalanine hydroxylase	Homo sapiens	161-164
25458282-2	2015	In this work, polyelectrolyte complexes (PECs) were formed by adding polyacrylic acid (PAA) or 4-O-methylglucuronoxylan (Xyl) on poly(allylamine hydrochloride) (PAH) solutions, at different ionic strength and neutral pH.	Xylose	121-124	phenylalanine hydroxylase	Homo sapiens	161-164
25458282-2	2015	In this work, polyelectrolyte complexes (PECs) were formed by adding polyacrylic acid (PAA) or 4-O-methylglucuronoxylan (Xyl) on poly(allylamine hydrochloride) (PAH) solutions, at different ionic strength and neutral pH.	polyallylamine	129-159	phenylalanine hydroxylase	Homo sapiens	161-164
25458282-5	2015	Adsorption studies on silica surfaces, performed by Quartz Crystal Microbalance with Dissipation (QCM-D) showed that PAA/PAH adsorbed complexes layers were rigid, while the corresponding Xyl/PAH layers were viscoelastic.	Silicon Dioxide	22-28	phenylalanine hydroxylase	Homo sapiens	117-124
25458282-5	2015	Adsorption studies on silica surfaces, performed by Quartz Crystal Microbalance with Dissipation (QCM-D) showed that PAA/PAH adsorbed complexes layers were rigid, while the corresponding Xyl/PAH layers were viscoelastic.	Silicon Dioxide	22-28	phenylalanine hydroxylase	Homo sapiens	121-124
25790516-4	2015	The emissions inventory revealed that PAH emissions to water were almost entirely attributable to the cokemaking process, with emissions factors ranging from 20 to 55 mg/tonne of coke.	Water	55-60	phenylalanine hydroxylase	Homo sapiens	38-41
25467057-2	2015	Treatment includes restriction of dietary phenylalanine, and in some individuals, supplementation with the PAH cofactor, tetrahydrobiopterin (sapropterin dihydrochloride).	sapropterin	121-140	phenylalanine hydroxylase	Homo sapiens	107-110
25467057-2	2015	Treatment includes restriction of dietary phenylalanine, and in some individuals, supplementation with the PAH cofactor, tetrahydrobiopterin (sapropterin dihydrochloride).	sapropterin	142-169	phenylalanine hydroxylase	Homo sapiens	107-110
25569307-1	2015	Gel-like coacervates that adhere to both hydrophilic and hydrophobic substrates under water have recently been prepared by ionically cross-linking poly(allylamine) (PAH) with pyrophosphate (PPi) and tripolyphosphate (TPP).	Water	86-91	phenylalanine hydroxylase	Homo sapiens	165-168
25569307-1	2015	Gel-like coacervates that adhere to both hydrophilic and hydrophobic substrates under water have recently been prepared by ionically cross-linking poly(allylamine) (PAH) with pyrophosphate (PPi) and tripolyphosphate (TPP).	polyallylamine	147-163	phenylalanine hydroxylase	Homo sapiens	165-168
25569307-1	2015	Gel-like coacervates that adhere to both hydrophilic and hydrophobic substrates under water have recently been prepared by ionically cross-linking poly(allylamine) (PAH) with pyrophosphate (PPi) and tripolyphosphate (TPP).	diphosphoric acid	175-188	phenylalanine hydroxylase	Homo sapiens	165-168
25569307-1	2015	Gel-like coacervates that adhere to both hydrophilic and hydrophobic substrates under water have recently been prepared by ionically cross-linking poly(allylamine) (PAH) with pyrophosphate (PPi) and tripolyphosphate (TPP).	triphosphoric acid	199-215	phenylalanine hydroxylase	Homo sapiens	165-168
25569307-1	2015	Gel-like coacervates that adhere to both hydrophilic and hydrophobic substrates under water have recently been prepared by ionically cross-linking poly(allylamine) (PAH) with pyrophosphate (PPi) and tripolyphosphate (TPP).	triphosphoric acid	217-220	phenylalanine hydroxylase	Homo sapiens	165-168
25569307-3	2015	To further analyze their stimulus-responsive properties, we have investigated the pH and ionic strength effects on the formation, rheology and adhesion of PAH/PPi and PAH/TPP complexes.	ppi	159-162	phenylalanine hydroxylase	Homo sapiens	155-158
25569307-3	2015	To further analyze their stimulus-responsive properties, we have investigated the pH and ionic strength effects on the formation, rheology and adhesion of PAH/PPi and PAH/TPP complexes.	triphosphoric acid	171-174	phenylalanine hydroxylase	Homo sapiens	167-170
25569307-8	2015	Additionally, the sensitivity of PAH/PPi and PAH/TPP complexes to ionic strength was demonstrated as a potential route to injectable adhesive design (where spontaneous adhesive formation was triggered via injection of low-viscosity, colloidal PAH/TPP dispersions into phosphate buffered saline).	triphosphoric acid	247-250	phenylalanine hydroxylase	Homo sapiens	33-36
25569307-8	2015	Additionally, the sensitivity of PAH/PPi and PAH/TPP complexes to ionic strength was demonstrated as a potential route to injectable adhesive design (where spontaneous adhesive formation was triggered via injection of low-viscosity, colloidal PAH/TPP dispersions into phosphate buffered saline).	triphosphoric acid	247-250	phenylalanine hydroxylase	Homo sapiens	45-48
25569307-8	2015	Additionally, the sensitivity of PAH/PPi and PAH/TPP complexes to ionic strength was demonstrated as a potential route to injectable adhesive design (where spontaneous adhesive formation was triggered via injection of low-viscosity, colloidal PAH/TPP dispersions into phosphate buffered saline).	triphosphoric acid	247-250	phenylalanine hydroxylase	Homo sapiens	45-48
25569307-8	2015	Additionally, the sensitivity of PAH/PPi and PAH/TPP complexes to ionic strength was demonstrated as a potential route to injectable adhesive design (where spontaneous adhesive formation was triggered via injection of low-viscosity, colloidal PAH/TPP dispersions into phosphate buffered saline).	Phosphate-Buffered Saline	268-293	phenylalanine hydroxylase	Homo sapiens	33-36
25569307-8	2015	Additionally, the sensitivity of PAH/PPi and PAH/TPP complexes to ionic strength was demonstrated as a potential route to injectable adhesive design (where spontaneous adhesive formation was triggered via injection of low-viscosity, colloidal PAH/TPP dispersions into phosphate buffered saline).	Phosphate-Buffered Saline	268-293	phenylalanine hydroxylase	Homo sapiens	45-48
25569307-8	2015	Additionally, the sensitivity of PAH/PPi and PAH/TPP complexes to ionic strength was demonstrated as a potential route to injectable adhesive design (where spontaneous adhesive formation was triggered via injection of low-viscosity, colloidal PAH/TPP dispersions into phosphate buffered saline).	Phosphate-Buffered Saline	268-293	phenylalanine hydroxylase	Homo sapiens	45-48
25338975-1	2015	BACKGROUND AND OBJECTIVES: Untreated phenylketonuria (PKU), a hereditary metabolic disorder caused by a genetic mutation in phenylalanine hydroxylase (PAH), is characterized by elevated blood phenylalanine (Phe) and severe neurologic disease.	Phenylalanine	207-210	phenylalanine hydroxylase	Homo sapiens	124-149
25338975-1	2015	BACKGROUND AND OBJECTIVES: Untreated phenylketonuria (PKU), a hereditary metabolic disorder caused by a genetic mutation in phenylalanine hydroxylase (PAH), is characterized by elevated blood phenylalanine (Phe) and severe neurologic disease.	Phenylalanine	207-210	phenylalanine hydroxylase	Homo sapiens	151-154
25338975-2	2015	Sapropterin dihydrochloride, a synthetic preparation of naturally occurring PAH cofactor tetrahydrobiopterin (BH4), activates residual PAH in a subset of patients, resulting in decreased blood Phe and increased Phe tolerance.	sapropterin	0-27	phenylalanine hydroxylase	Homo sapiens	76-79
25338975-2	2015	Sapropterin dihydrochloride, a synthetic preparation of naturally occurring PAH cofactor tetrahydrobiopterin (BH4), activates residual PAH in a subset of patients, resulting in decreased blood Phe and increased Phe tolerance.	sapropterin	0-27	phenylalanine hydroxylase	Homo sapiens	135-138
25338975-2	2015	Sapropterin dihydrochloride, a synthetic preparation of naturally occurring PAH cofactor tetrahydrobiopterin (BH4), activates residual PAH in a subset of patients, resulting in decreased blood Phe and increased Phe tolerance.	sapropterin	89-108	phenylalanine hydroxylase	Homo sapiens	76-79
25338975-2	2015	Sapropterin dihydrochloride, a synthetic preparation of naturally occurring PAH cofactor tetrahydrobiopterin (BH4), activates residual PAH in a subset of patients, resulting in decreased blood Phe and increased Phe tolerance.	sapropterin	89-108	phenylalanine hydroxylase	Homo sapiens	135-138
25338975-2	2015	Sapropterin dihydrochloride, a synthetic preparation of naturally occurring PAH cofactor tetrahydrobiopterin (BH4), activates residual PAH in a subset of patients, resulting in decreased blood Phe and increased Phe tolerance.	sapropterin	110-113	phenylalanine hydroxylase	Homo sapiens	76-79
25338975-2	2015	Sapropterin dihydrochloride, a synthetic preparation of naturally occurring PAH cofactor tetrahydrobiopterin (BH4), activates residual PAH in a subset of patients, resulting in decreased blood Phe and increased Phe tolerance.	sapropterin	110-113	phenylalanine hydroxylase	Homo sapiens	135-138
25338975-2	2015	Sapropterin dihydrochloride, a synthetic preparation of naturally occurring PAH cofactor tetrahydrobiopterin (BH4), activates residual PAH in a subset of patients, resulting in decreased blood Phe and increased Phe tolerance.	Phenylalanine	211-214	phenylalanine hydroxylase	Homo sapiens	135-138
24628256-0	2015	In silico thermodynamics stability change analysis involved in BH4 responsive mutations in phenylalanine hydroxylase: QM/MM and MD simulations analysis.	sapropterin	63-66	phenylalanine hydroxylase	Homo sapiens	91-116
24628256-1	2015	The mammalian tetrahydrobiopterin (BH4)-dependent phenylalanine hydroxylases (PAH), involved in important metabolic pathways of phenylalanine, belong to non-heme iron-containing aromatic acid hydroxylases" enzyme (AAH) family.	sapropterin	14-33	phenylalanine hydroxylase	Homo sapiens	78-81
24628256-1	2015	The mammalian tetrahydrobiopterin (BH4)-dependent phenylalanine hydroxylases (PAH), involved in important metabolic pathways of phenylalanine, belong to non-heme iron-containing aromatic acid hydroxylases" enzyme (AAH) family.	sapropterin	35-38	phenylalanine hydroxylase	Homo sapiens	78-81
24628256-1	2015	The mammalian tetrahydrobiopterin (BH4)-dependent phenylalanine hydroxylases (PAH), involved in important metabolic pathways of phenylalanine, belong to non-heme iron-containing aromatic acid hydroxylases" enzyme (AAH) family.	Phenylalanine	50-63	phenylalanine hydroxylase	Homo sapiens	78-81
25614310-1	2015	Phenylketonuria (PKU) is caused by a deficiency or inactivity of the enzyme phenylalanine hydroxylase that converts phenylalanine (Phe) to tyrosine (Tyr).	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	76-101
25614310-1	2015	Phenylketonuria (PKU) is caused by a deficiency or inactivity of the enzyme phenylalanine hydroxylase that converts phenylalanine (Phe) to tyrosine (Tyr).	Tyrosine	139-147	phenylalanine hydroxylase	Homo sapiens	76-101
25614310-1	2015	Phenylketonuria (PKU) is caused by a deficiency or inactivity of the enzyme phenylalanine hydroxylase that converts phenylalanine (Phe) to tyrosine (Tyr).	Tyrosine	149-152	phenylalanine hydroxylase	Homo sapiens	76-101
25453233-1	2014	Phenylalanine hydroxylase (PheH), a liver enzyme that catalyzes the hydroxylation of excess phenylalanine in the diet to tyrosine, is activated by phenylalanine.	Phenylalanine	92-105	phenylalanine hydroxylase	Homo sapiens	27-31
25453233-1	2014	Phenylalanine hydroxylase (PheH), a liver enzyme that catalyzes the hydroxylation of excess phenylalanine in the diet to tyrosine, is activated by phenylalanine.	Tyrosine	121-129	phenylalanine hydroxylase	Homo sapiens	0-25
25453233-1	2014	Phenylalanine hydroxylase (PheH), a liver enzyme that catalyzes the hydroxylation of excess phenylalanine in the diet to tyrosine, is activated by phenylalanine.	Tyrosine	121-129	phenylalanine hydroxylase	Homo sapiens	27-31
25453233-1	2014	Phenylalanine hydroxylase (PheH), a liver enzyme that catalyzes the hydroxylation of excess phenylalanine in the diet to tyrosine, is activated by phenylalanine.	Phenylalanine	147-160	phenylalanine hydroxylase	Homo sapiens	0-25
25453233-1	2014	Phenylalanine hydroxylase (PheH), a liver enzyme that catalyzes the hydroxylation of excess phenylalanine in the diet to tyrosine, is activated by phenylalanine.	Phenylalanine	147-160	phenylalanine hydroxylase	Homo sapiens	27-31
25453233-9	2014	Both results establish that activation of PheH by phenylalanine does not require binding of the amino acid in the active site.	Phenylalanine	50-63	phenylalanine hydroxylase	Homo sapiens	42-46
25268819-4	2014	As the charge density of PAH chain depends on the pH of the polyelectrolyte solution, PEC particles exhibit distinct behaviors under salt addition depending on the pH of the continuous phase.	Salts	133-137	phenylalanine hydroxylase	Homo sapiens	25-28
25268819-6	2014	Conversely, at pH=10 where PAH is only partially charged, the addition of salt drives a progressive disentanglement of the two polyelectrolytes, as revealed by both viscosimetric and spectroscopic measurements.	Salts	74-78	phenylalanine hydroxylase	Homo sapiens	27-30
25465954-0	2014	Role of goethite during air-oxidation of PAH-contaminated soils.	goethite	8-16	phenylalanine hydroxylase	Homo sapiens	41-44
25465954-1	2014	The impact of goethite on air-oxidation of PAH-contaminated soils was studied through two sets of experiments.	goethite	14-22	phenylalanine hydroxylase	Homo sapiens	43-46
25465954-4	2014	The decrease in EOM and PAH contents, and the oxygenated-PAC production observed during EOM oxidation, were enhanced by the presence of goethite.	goethite	136-144	phenylalanine hydroxylase	Homo sapiens	24-27
25693375-3	2014	The total concentrations of 16 PAH ranged from 81.5-8019 ng   L(-1) in underground river, 288.7-15,200 ng   L(-1) in karst springs, and 128.4-2,442 ng   L(-1) in surface water.	Water	170-175	phenylalanine hydroxylase	Homo sapiens	31-34
25223838-1	2014	OBJECTIVE: To assess the safety and efficacy of tetrahydrobiopterin therapy with sapropterin to treat tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency in children aged &lt;4 years compared with those aged &gt;=4 years.	sapropterin	48-67	phenylalanine hydroxylase	Homo sapiens	139-164
25223838-1	2014	OBJECTIVE: To assess the safety and efficacy of tetrahydrobiopterin therapy with sapropterin to treat tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency in children aged &lt;4 years compared with those aged &gt;=4 years.	sapropterin	48-67	phenylalanine hydroxylase	Homo sapiens	166-169
25223838-1	2014	OBJECTIVE: To assess the safety and efficacy of tetrahydrobiopterin therapy with sapropterin to treat tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency in children aged &lt;4 years compared with those aged &gt;=4 years.	sapropterin	81-92	phenylalanine hydroxylase	Homo sapiens	139-164
25223838-1	2014	OBJECTIVE: To assess the safety and efficacy of tetrahydrobiopterin therapy with sapropterin to treat tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency in children aged &lt;4 years compared with those aged &gt;=4 years.	sapropterin	102-121	phenylalanine hydroxylase	Homo sapiens	139-164
25223838-1	2014	OBJECTIVE: To assess the safety and efficacy of tetrahydrobiopterin therapy with sapropterin to treat tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency in children aged &lt;4 years compared with those aged &gt;=4 years.	sapropterin	102-121	phenylalanine hydroxylase	Homo sapiens	166-169
25223838-1	2014	OBJECTIVE: To assess the safety and efficacy of tetrahydrobiopterin therapy with sapropterin to treat tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency in children aged &lt;4 years compared with those aged &gt;=4 years.	sapropterin	123-126	phenylalanine hydroxylase	Homo sapiens	139-164
25223838-1	2014	OBJECTIVE: To assess the safety and efficacy of tetrahydrobiopterin therapy with sapropterin to treat tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency in children aged &lt;4 years compared with those aged &gt;=4 years.	sapropterin	123-126	phenylalanine hydroxylase	Homo sapiens	166-169
25299136-0	2014	Phenylalanine binding is linked to dimerization of the regulatory domain of phenylalanine hydroxylase.	Phenylalanine	0-13	phenylalanine hydroxylase	Homo sapiens	76-101
25046852-6	2014	The estimates were based on benzo[a]pyrene equivalent (BaPeq) total PAH concentrations calculated using toxic equivalency factors.	bapeq	55-60	phenylalanine hydroxylase	Homo sapiens	68-71
25693375-8	2014	The levels of ecological risk were generally moderately polluted and heavily polluted according to all detected PAH compounds in the water.	Water	133-138	phenylalanine hydroxylase	Homo sapiens	112-115
24488205-1	2014	Phenylketonuria (PKU) is a disorder caused by a deficiency in phenylalanine hydroxylase activity, which converts phenylalanine (Phe) to tyrosine, leading to hyperphenylalaninemia (HPA) with accumulation of Phe in tissues of patients.	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	62-87
25228517-7	2014	In turn, mutations of the ATP7A and PAH genes, regulating intracellular copper concentration and activity of phenylalanine hydroxylase, lead to Menkes syndrome and phenylketonuria.	Copper	72-78	phenylalanine hydroxylase	Homo sapiens	109-134
24488205-1	2014	Phenylketonuria (PKU) is a disorder caused by a deficiency in phenylalanine hydroxylase activity, which converts phenylalanine (Phe) to tyrosine, leading to hyperphenylalaninemia (HPA) with accumulation of Phe in tissues of patients.	Tyrosine	136-144	phenylalanine hydroxylase	Homo sapiens	62-87
24488205-1	2014	Phenylketonuria (PKU) is a disorder caused by a deficiency in phenylalanine hydroxylase activity, which converts phenylalanine (Phe) to tyrosine, leading to hyperphenylalaninemia (HPA) with accumulation of Phe in tissues of patients.	Phenylalanine	128-131	phenylalanine hydroxylase	Homo sapiens	62-87
24769260-2	2014	Benzo[a]pyrene (B[a]P) is the prototypical carcinogenic PAH, and dibenzo[def,p]chrysene (DBC) is a less prevalent, but highly potent transplacental carcinogenic PAH.	Benzo(a)pyrene	0-14	phenylalanine hydroxylase	Homo sapiens	56-59
25101170-0	2014	Synthesis, modification and graft polymerization of magnetic nano particles for PAH removal in contaminated water.	Water	108-113	phenylalanine hydroxylase	Homo sapiens	80-83
24743000-1	2014	BACKGROUND: Phenylketonuria is an inherited disease caused by impaired activity of phenylalanine hydroxylase, the enzyme that converts phenylalanine to tyrosine, leading to accumulation of phenylalanine and subsequent neurocognitive dysfunction.	Tyrosine	152-160	phenylalanine hydroxylase	Homo sapiens	83-108
24743000-1	2014	BACKGROUND: Phenylketonuria is an inherited disease caused by impaired activity of phenylalanine hydroxylase, the enzyme that converts phenylalanine to tyrosine, leading to accumulation of phenylalanine and subsequent neurocognitive dysfunction.	Phenylalanine	135-148	phenylalanine hydroxylase	Homo sapiens	83-108
24936877-0	2014	Engineering bacterial phenylalanine 4-hydroxylase for microbial synthesis of human neurotransmitter precursor 5-hydroxytryptophan.	5-Hydroxytryptophan	110-129	phenylalanine hydroxylase	Homo sapiens	22-49
24910181-4	2014	Spatial distribution maps revealed that PAH levels were higher in the coastal areas of the Caspian Sea where oil related activities have been common since 1800"s.	Oils	109-112	phenylalanine hydroxylase	Homo sapiens	40-43
24769260-2	2014	Benzo[a]pyrene (B[a]P) is the prototypical carcinogenic PAH, and dibenzo[def,p]chrysene (DBC) is a less prevalent, but highly potent transplacental carcinogenic PAH.	dibenzo(a,l)pyrene	65-87	phenylalanine hydroxylase	Homo sapiens	161-164
24769260-2	2014	Benzo[a]pyrene (B[a]P) is the prototypical carcinogenic PAH, and dibenzo[def,p]chrysene (DBC) is a less prevalent, but highly potent transplacental carcinogenic PAH.	dibenzo(a,l)pyrene	89-92	phenylalanine hydroxylase	Homo sapiens	161-164
24356981-0	2014	Community structure and PAH ring-hydroxylating dioxygenase genes of a marine pyrene-degrading microbial consortium.	pyrene	77-83	phenylalanine hydroxylase	Homo sapiens	24-27
25003100-1	2014	BACKGROUND: Phenylketonuria (PKU) is caused by the inherited defect of the phenylalanine hydroxylase enzyme, which converts phenylalanine (Phe) into tyrosine (Tyr).	Phenylalanine	12-15	phenylalanine hydroxylase	Homo sapiens	75-100
25003100-1	2014	BACKGROUND: Phenylketonuria (PKU) is caused by the inherited defect of the phenylalanine hydroxylase enzyme, which converts phenylalanine (Phe) into tyrosine (Tyr).	Tyrosine	149-157	phenylalanine hydroxylase	Homo sapiens	75-100
25003100-1	2014	BACKGROUND: Phenylketonuria (PKU) is caused by the inherited defect of the phenylalanine hydroxylase enzyme, which converts phenylalanine (Phe) into tyrosine (Tyr).	Tyrosine	159-162	phenylalanine hydroxylase	Homo sapiens	75-100
24636414-6	2014	We show that the sorption selectivity characteristics can have a significant impact on the fluorescence sensor response of [Zn2(bdc)2(dpNDI)]n towards environmentally important hydrocarbons based contaminants (i.e., BTEX, PAH).	[zn2(bdc)2(dpndi)]n	123-142	phenylalanine hydroxylase	Homo sapiens	222-225
24775069-6	2014	PAH levels in the Coquina tissues were highly variable, perhaps indicative of the heterogeneous distribution of oil and tar on the beaches and exposure to tar particles.	Oils	112-115	phenylalanine hydroxylase	Homo sapiens	0-3
24775069-7	2014	Overall, PAH levels decreased continuously in both sand and Coquina tissues, reaching limits of detection within one and two years respectively after oil landed on Florida Panhandle beaches.	Oils	150-153	phenylalanine hydroxylase	Homo sapiens	9-12
24713088-6	2014	In the PheH reaction, the transient formation of the 4a-hydroxypterin product was readily detected; tandem mass spectrometry confirmed attachment of the oxygen to C(4a).	4a-hydroxypterin	53-69	phenylalanine hydroxylase	Homo sapiens	7-11
24713088-6	2014	In the PheH reaction, the transient formation of the 4a-hydroxypterin product was readily detected; tandem mass spectrometry confirmed attachment of the oxygen to C(4a).	Oxygen	153-159	phenylalanine hydroxylase	Homo sapiens	7-11
24717604-0	2014	[Treatment with imatinib for refractory PAH].	Imatinib Mesylate	16-24	phenylalanine hydroxylase	Homo sapiens	40-43
26835324-6	2014	The only alternative therapy currently approved is the supplementation of BH4, the requisite co-factor of PAH, in the orally-available form of sapropterin dihydrochloride.	sapropterin	74-77	phenylalanine hydroxylase	Homo sapiens	106-109
26835324-6	2014	The only alternative therapy currently approved is the supplementation of BH4, the requisite co-factor of PAH, in the orally-available form of sapropterin dihydrochloride.	sapropterin	143-170	phenylalanine hydroxylase	Homo sapiens	106-109
24595755-3	2014	The degradation of phenanthrene (chosen as a model of PAH) by persulfate in freshly contaminated soil microcosms was studied to assess its impact on the biodegradation process and on soil properties.	phenanthrene	19-31	phenylalanine hydroxylase	Homo sapiens	54-57
24595755-3	2014	The degradation of phenanthrene (chosen as a model of PAH) by persulfate in freshly contaminated soil microcosms was studied to assess its impact on the biodegradation process and on soil properties.	Peroxydisulfate	62-72	phenylalanine hydroxylase	Homo sapiens	54-57
24385074-10	2014	Pharmacotherapy for phenylalanine hydroxylase deficiency is in early stages with one approved medication (sapropterin, a derivative of the natural cofactor of phenylalanine hydroxylase) and others under development.	sapropterin	106-117	phenylalanine hydroxylase	Homo sapiens	20-45
24270708-6	2014	We demonstrate that deuterium atoms adsorbed on graphite can react with adsorbed PAH molecules, forming superhydrogenated PAH species.	Deuterium	20-29	phenylalanine hydroxylase	Homo sapiens	81-84
24270708-6	2014	We demonstrate that deuterium atoms adsorbed on graphite can react with adsorbed PAH molecules, forming superhydrogenated PAH species.	Deuterium	20-29	phenylalanine hydroxylase	Homo sapiens	122-125
24270708-6	2014	We demonstrate that deuterium atoms adsorbed on graphite can react with adsorbed PAH molecules, forming superhydrogenated PAH species.	Graphite	48-56	phenylalanine hydroxylase	Homo sapiens	81-84
24270708-6	2014	We demonstrate that deuterium atoms adsorbed on graphite can react with adsorbed PAH molecules, forming superhydrogenated PAH species.	Graphite	48-56	phenylalanine hydroxylase	Homo sapiens	122-125
24270708-8	2014	We suggest that further reactive processes may be responsible for part of this deuterium loss, indicating that PAHs adsorbed on hydrogenated carbonaceous grains in warm interstellar environments may serve as a route to release H2 as well as forming superhydrogenated PAH species.	Deuterium	79-88	phenylalanine hydroxylase	Homo sapiens	111-114
24270708-8	2014	We suggest that further reactive processes may be responsible for part of this deuterium loss, indicating that PAHs adsorbed on hydrogenated carbonaceous grains in warm interstellar environments may serve as a route to release H2 as well as forming superhydrogenated PAH species.	Hydrogen	227-229	phenylalanine hydroxylase	Homo sapiens	111-114
24239815-8	2014	CONCLUSIONS: Both 1-OHP and 1-OHPG can be used to assess the relatively low PAH levels to which the general population is exposed.	Oxaliplatin	18-23	phenylalanine hydroxylase	Homo sapiens	76-79
23972323-1	2014	Forest fires are known as an important natural source of polycyclic aromatic hydrocarbons (PAHs), but time trends of PAH levels and patterns in various environmental compartments after forest fires have not been thoroughly studied yet.	Polycyclic Aromatic Hydrocarbons	57-89	phenylalanine hydroxylase	Homo sapiens	91-94
24510568-2	2014	METHODS: For 55 patients whose blood Phe concentration was over 2.0 mg/dL, potential mutations in 13 exons and flanking sequences of the PAH gene were detected by PCR and DNA sequencing.	Phenylalanine	37-40	phenylalanine hydroxylase	Homo sapiens	137-140
24844894-2	2014	The total PAH concentrations (sum of the concentrations of 17 individual PAH compounds) in water samples ranged from 67 to 96 ng L(-1), which were predominated by two- and three-ring PAHs.	Water	91-96	phenylalanine hydroxylase	Homo sapiens	10-13
24844894-2	2014	The total PAH concentrations (sum of the concentrations of 17 individual PAH compounds) in water samples ranged from 67 to 96 ng L(-1), which were predominated by two- and three-ring PAHs.	Water	91-96	phenylalanine hydroxylase	Homo sapiens	73-76
24844894-2	2014	The total PAH concentrations (sum of the concentrations of 17 individual PAH compounds) in water samples ranged from 67 to 96 ng L(-1), which were predominated by two- and three-ring PAHs.	Polycyclic Aromatic Hydrocarbons	183-187	phenylalanine hydroxylase	Homo sapiens	10-13
24844894-8	2014	A selected number of concentration ratios of specific PAH compounds reflected a pattern of pyrogenic input as a major source of PAHs.	Polycyclic Aromatic Hydrocarbons	128-132	phenylalanine hydroxylase	Homo sapiens	54-57
24368688-5	2014	A number of patients have been previously tested for their response to dietary supplementation of tetrahydrobiopterin (BH4), the cofactor of PAH.	sapropterin	98-117	phenylalanine hydroxylase	Homo sapiens	141-144
24368688-5	2014	A number of patients have been previously tested for their response to dietary supplementation of tetrahydrobiopterin (BH4), the cofactor of PAH.	sapropterin	119-122	phenylalanine hydroxylase	Homo sapiens	141-144
24367237-0	2014	Benchscale Assessment of the Efficacy of a Reactive Core Mat to Isolate PAH-spiked Aquatic Sediments.	methylallyl trisulfide	57-60	phenylalanine hydroxylase	Homo sapiens	72-75
25563006-3	2014	In case where PKU patient is responsive to tetrahydrobiopterin treatment, sapropterin restores the impaired activity of the enzyme phenylalanine hydroxylase, resulting in the stimulation of normal Phe metabolism and thereby enhancing patient tolerance to natural products.	sapropterin	74-85	phenylalanine hydroxylase	Homo sapiens	131-156
25563006-3	2014	In case where PKU patient is responsive to tetrahydrobiopterin treatment, sapropterin restores the impaired activity of the enzyme phenylalanine hydroxylase, resulting in the stimulation of normal Phe metabolism and thereby enhancing patient tolerance to natural products.	Phenylalanine	197-200	phenylalanine hydroxylase	Homo sapiens	131-156
24465804-2	2014	Inflammation, increasingly implicated in schizophrenia, can impair the function of the enzyme Phenylalanine hydroxylase (PAH; which catalyzes the conversion of phenylalanine to tyrosine) and thus lead to elevated phenylalanine levels and reduced tyrosine levels.	Phenylalanine	160-173	phenylalanine hydroxylase	Homo sapiens	94-119
24465804-2	2014	Inflammation, increasingly implicated in schizophrenia, can impair the function of the enzyme Phenylalanine hydroxylase (PAH; which catalyzes the conversion of phenylalanine to tyrosine) and thus lead to elevated phenylalanine levels and reduced tyrosine levels.	Phenylalanine	160-173	phenylalanine hydroxylase	Homo sapiens	121-124
24465804-2	2014	Inflammation, increasingly implicated in schizophrenia, can impair the function of the enzyme Phenylalanine hydroxylase (PAH; which catalyzes the conversion of phenylalanine to tyrosine) and thus lead to elevated phenylalanine levels and reduced tyrosine levels.	Tyrosine	177-185	phenylalanine hydroxylase	Homo sapiens	94-119
24465804-2	2014	Inflammation, increasingly implicated in schizophrenia, can impair the function of the enzyme Phenylalanine hydroxylase (PAH; which catalyzes the conversion of phenylalanine to tyrosine) and thus lead to elevated phenylalanine levels and reduced tyrosine levels.	Tyrosine	177-185	phenylalanine hydroxylase	Homo sapiens	121-124
24465804-2	2014	Inflammation, increasingly implicated in schizophrenia, can impair the function of the enzyme Phenylalanine hydroxylase (PAH; which catalyzes the conversion of phenylalanine to tyrosine) and thus lead to elevated phenylalanine levels and reduced tyrosine levels.	Phenylalanine	213-226	phenylalanine hydroxylase	Homo sapiens	94-119
24465804-2	2014	Inflammation, increasingly implicated in schizophrenia, can impair the function of the enzyme Phenylalanine hydroxylase (PAH; which catalyzes the conversion of phenylalanine to tyrosine) and thus lead to elevated phenylalanine levels and reduced tyrosine levels.	Phenylalanine	213-226	phenylalanine hydroxylase	Homo sapiens	121-124
24465804-2	2014	Inflammation, increasingly implicated in schizophrenia, can impair the function of the enzyme Phenylalanine hydroxylase (PAH; which catalyzes the conversion of phenylalanine to tyrosine) and thus lead to elevated phenylalanine levels and reduced tyrosine levels.	Tyrosine	246-254	phenylalanine hydroxylase	Homo sapiens	94-119
24465804-2	2014	Inflammation, increasingly implicated in schizophrenia, can impair the function of the enzyme Phenylalanine hydroxylase (PAH; which catalyzes the conversion of phenylalanine to tyrosine) and thus lead to elevated phenylalanine levels and reduced tyrosine levels.	Tyrosine	246-254	phenylalanine hydroxylase	Homo sapiens	121-124
24326190-12	2014	The negative effects of the PAH addition on the microbial nitrogen cycle were in six out of eight cases best correlated to the amount of alkylated bioavailable PAH in the sediments, and thus microbial nitrogen cycle is a possible good indicator for assessing PAH-induced stress.	Nitrogen	58-66	phenylalanine hydroxylase	Homo sapiens	28-31
24326190-12	2014	The negative effects of the PAH addition on the microbial nitrogen cycle were in six out of eight cases best correlated to the amount of alkylated bioavailable PAH in the sediments, and thus microbial nitrogen cycle is a possible good indicator for assessing PAH-induced stress.	Nitrogen	58-66	phenylalanine hydroxylase	Homo sapiens	160-163
24326190-12	2014	The negative effects of the PAH addition on the microbial nitrogen cycle were in six out of eight cases best correlated to the amount of alkylated bioavailable PAH in the sediments, and thus microbial nitrogen cycle is a possible good indicator for assessing PAH-induced stress.	Nitrogen	58-66	phenylalanine hydroxylase	Homo sapiens	160-163
24326190-12	2014	The negative effects of the PAH addition on the microbial nitrogen cycle were in six out of eight cases best correlated to the amount of alkylated bioavailable PAH in the sediments, and thus microbial nitrogen cycle is a possible good indicator for assessing PAH-induced stress.	Nitrogen	201-209	phenylalanine hydroxylase	Homo sapiens	28-31
25302382-2	2014	The process occurs via atomic hydrogen addition reactions leading to the formation of super-hydrogenated PAH species, followed by molecular hydrogen forming abstraction reactions.	Hydrogen	30-38	phenylalanine hydroxylase	Homo sapiens	105-108
25302382-2	2014	The process occurs via atomic hydrogen addition reactions leading to the formation of super-hydrogenated PAH species, followed by molecular hydrogen forming abstraction reactions.	Hydrogen	92-100	phenylalanine hydroxylase	Homo sapiens	105-108
25302382-3	2014	Here, we combine quadrupole mass spectrometry data with kinetic simulations to follow the addition of deuterium atoms to the PAH molecule coronene.	Deuterium	102-111	phenylalanine hydroxylase	Homo sapiens	125-128
25302382-3	2014	Here, we combine quadrupole mass spectrometry data with kinetic simulations to follow the addition of deuterium atoms to the PAH molecule coronene.	coronene	138-146	phenylalanine hydroxylase	Homo sapiens	125-128
24660059-3	2014	In other cells, activation of GCH-I leads to the formation of 5,6,7,8-tetrahydrobiopterin (BH4), the necessary cofactor of amino acid hydroxylases like phenylalanine 4-hydroxylase (PAH).	sapropterin	62-89	phenylalanine hydroxylase	Homo sapiens	152-179
24660059-3	2014	In other cells, activation of GCH-I leads to the formation of 5,6,7,8-tetrahydrobiopterin (BH4), the necessary cofactor of amino acid hydroxylases like phenylalanine 4-hydroxylase (PAH).	sapropterin	91-94	phenylalanine hydroxylase	Homo sapiens	152-179
24190797-0	2014	Influence of PAH Genotype on Sapropterin Response in PKU: Results of a Single-Center Cohort Study.	sapropterin	29-40	phenylalanine hydroxylase	Homo sapiens	13-16
24190797-1	2014	OBJECTIVE: Identifying phenylalanine hydroxylase (PAH) mutations associated with sapropterin response in phenylketonuria (PKU) would be an advantageous means to determine clinical benefit to sapropterin therapy.	sapropterin	81-92	phenylalanine hydroxylase	Homo sapiens	23-48
24190797-1	2014	OBJECTIVE: Identifying phenylalanine hydroxylase (PAH) mutations associated with sapropterin response in phenylketonuria (PKU) would be an advantageous means to determine clinical benefit to sapropterin therapy.	sapropterin	81-92	phenylalanine hydroxylase	Homo sapiens	50-53
24190797-1	2014	OBJECTIVE: Identifying phenylalanine hydroxylase (PAH) mutations associated with sapropterin response in phenylketonuria (PKU) would be an advantageous means to determine clinical benefit to sapropterin therapy.	sapropterin	191-202	phenylalanine hydroxylase	Homo sapiens	23-48
24190797-1	2014	OBJECTIVE: Identifying phenylalanine hydroxylase (PAH) mutations associated with sapropterin response in phenylketonuria (PKU) would be an advantageous means to determine clinical benefit to sapropterin therapy.	sapropterin	191-202	phenylalanine hydroxylase	Homo sapiens	50-53
24239815-8	2014	CONCLUSIONS: Both 1-OHP and 1-OHPG can be used to assess the relatively low PAH levels to which the general population is exposed.	1-ohpg	28-34	phenylalanine hydroxylase	Homo sapiens	76-79
23792259-3	2013	METHODS: Phenylalanine hydroxylase (PAH) gene mutations have been analyzed by direct DNA sequencing in 30 HPA patients (Phe levels ranging from 2 to 6mg/dL) from Southern Italy who were identified in a neonatal screening program and a genotype-phenotype correlation was performed.	Phenylalanine	9-12	phenylalanine hydroxylase	Homo sapiens	36-39
24244510-1	2013	Phenylalanine hydroxylase (PAH) catalyzes the conversion of L-Phe to L-Tyr.	Phenylalanine	60-65	phenylalanine hydroxylase	Homo sapiens	0-25
24171660-6	2013	For PAH/citrate, the film growth rate reaches a plateau value when the spraying rate of citrate is increased while that of PAH is maintained constant, whereas when the spraying rate of citrate is maintained constant and that of PAH is increased, a behavior similar to that of PAH/CD-S is observed.	Citric Acid	8-15	phenylalanine hydroxylase	Homo sapiens	4-7
24171660-6	2013	For PAH/citrate, the film growth rate reaches a plateau value when the spraying rate of citrate is increased while that of PAH is maintained constant, whereas when the spraying rate of citrate is maintained constant and that of PAH is increased, a behavior similar to that of PAH/CD-S is observed.	Citric Acid	8-15	phenylalanine hydroxylase	Homo sapiens	123-126
24171660-6	2013	For PAH/citrate, the film growth rate reaches a plateau value when the spraying rate of citrate is increased while that of PAH is maintained constant, whereas when the spraying rate of citrate is maintained constant and that of PAH is increased, a behavior similar to that of PAH/CD-S is observed.	Citric Acid	8-15	phenylalanine hydroxylase	Homo sapiens	123-126
24171660-6	2013	For PAH/citrate, the film growth rate reaches a plateau value when the spraying rate of citrate is increased while that of PAH is maintained constant, whereas when the spraying rate of citrate is maintained constant and that of PAH is increased, a behavior similar to that of PAH/CD-S is observed.	Citric Acid	8-15	phenylalanine hydroxylase	Homo sapiens	123-126
24171660-6	2013	For PAH/citrate, the film growth rate reaches a plateau value when the spraying rate of citrate is increased while that of PAH is maintained constant, whereas when the spraying rate of citrate is maintained constant and that of PAH is increased, a behavior similar to that of PAH/CD-S is observed.	Citric Acid	88-95	phenylalanine hydroxylase	Homo sapiens	4-7
24171660-7	2013	The composition of PAH/CD-S sprayed films determined by X-ray photoelectron spectroscopy is independent of the spraying rate ratio of the two constituents and corresponds to one allylamine for one sulfate group.	Allylamine	178-188	phenylalanine hydroxylase	Homo sapiens	19-22
24171660-7	2013	The composition of PAH/CD-S sprayed films determined by X-ray photoelectron spectroscopy is independent of the spraying rate ratio of the two constituents and corresponds to one allylamine for one sulfate group.	Sulfates	197-204	phenylalanine hydroxylase	Homo sapiens	19-22
24171660-8	2013	For PAH/citrate, by increasing the PAH/citrate spraying rate ratio, the carboxylic/nitrogen ratio in the film increases and tends to 1.	Citric Acid	8-15	phenylalanine hydroxylase	Homo sapiens	4-7
24171660-8	2013	For PAH/citrate, by increasing the PAH/citrate spraying rate ratio, the carboxylic/nitrogen ratio in the film increases and tends to 1.	Citric Acid	8-15	phenylalanine hydroxylase	Homo sapiens	35-38
24171660-8	2013	For PAH/citrate, by increasing the PAH/citrate spraying rate ratio, the carboxylic/nitrogen ratio in the film increases and tends to 1.	Citric Acid	39-46	phenylalanine hydroxylase	Homo sapiens	4-7
24171660-8	2013	For PAH/citrate, by increasing the PAH/citrate spraying rate ratio, the carboxylic/nitrogen ratio in the film increases and tends to 1.	Citric Acid	39-46	phenylalanine hydroxylase	Homo sapiens	35-38
24171660-8	2013	For PAH/citrate, by increasing the PAH/citrate spraying rate ratio, the carboxylic/nitrogen ratio in the film increases and tends to 1.	Nitrogen	83-91	phenylalanine hydroxylase	Homo sapiens	4-7
24171660-8	2013	For PAH/citrate, by increasing the PAH/citrate spraying rate ratio, the carboxylic/nitrogen ratio in the film increases and tends to 1.	Nitrogen	83-91	phenylalanine hydroxylase	Homo sapiens	35-38
24171660-12	2013	A model based on strong (respectively weak) interactions between PAH and CD-S (respectively citrate) is proposed to explain these features.	Citric Acid	92-99	phenylalanine hydroxylase	Homo sapiens	65-68
24244510-1	2013	Phenylalanine hydroxylase (PAH) catalyzes the conversion of L-Phe to L-Tyr.	Phenylalanine	60-65	phenylalanine hydroxylase	Homo sapiens	27-30
24244510-1	2013	Phenylalanine hydroxylase (PAH) catalyzes the conversion of L-Phe to L-Tyr.	Tyrosine	69-74	phenylalanine hydroxylase	Homo sapiens	0-25
24244510-1	2013	Phenylalanine hydroxylase (PAH) catalyzes the conversion of L-Phe to L-Tyr.	Tyrosine	69-74	phenylalanine hydroxylase	Homo sapiens	27-30
24244510-4	2013	In particular, PAH displays positive cooperativity for L-Phe, which is proposed to bind the enzyme on an allosteric site in the N-terminal regulatory domain (RD), also classified as an ACT domain.	Phenylalanine	55-60	phenylalanine hydroxylase	Homo sapiens	15-18
23972908-3	2013	PAHs (Polycyclic Aromatic Hydrocarbons) levels in the range of 29.4-64.2 ng g(-1) (dry weight) indicated that PAH contamination level classified as low along the Aegean coast.	Polycyclic Aromatic Hydrocarbons	6-38	phenylalanine hydroxylase	Homo sapiens	0-3
24219191-8	2013	A logistic regression model with state fixed-effects was then fit to examine the association between facility characteristics and the likelihood of having higher-than-expected rates of PAH (O-E &gt; 0).	oleoyl-estrone	190-193	phenylalanine hydroxylase	Homo sapiens	185-188
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	polyallylamine	133-147	phenylalanine hydroxylase	Homo sapiens	55-58
23532445-0	2013	In vitro read-through of phenylalanine hydroxylase (PAH) nonsense mutations using aminoglycosides: a potential therapy for phenylketonuria.	Aminoglycosides	82-97	phenylalanine hydroxylase	Homo sapiens	25-50
23532445-0	2013	In vitro read-through of phenylalanine hydroxylase (PAH) nonsense mutations using aminoglycosides: a potential therapy for phenylketonuria.	Aminoglycosides	82-97	phenylalanine hydroxylase	Homo sapiens	52-55
23532445-7	2013	Gentamicin and G-418 induced read-through of nonsense PAH mutations in HEK293 cells.	Gentamicins	0-10	phenylalanine hydroxylase	Homo sapiens	54-57
23532445-7	2013	Gentamicin and G-418 induced read-through of nonsense PAH mutations in HEK293 cells.	antibiotic G 418	15-20	phenylalanine hydroxylase	Homo sapiens	54-57
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	pei	46-49	phenylalanine hydroxylase	Homo sapiens	55-58
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	polyallylamine	133-147	phenylalanine hydroxylase	Homo sapiens	75-78
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	pei	46-49	phenylalanine hydroxylase	Homo sapiens	75-78
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	pei	62-65	phenylalanine hydroxylase	Homo sapiens	55-58
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	hexacyanoferrate II	264-280	phenylalanine hydroxylase	Homo sapiens	55-58
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	Prostaglandins A	51-54	phenylalanine hydroxylase	Homo sapiens	55-58
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	hexacyanoferrate II	264-280	phenylalanine hydroxylase	Homo sapiens	75-78
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	Prostaglandins A	51-54	phenylalanine hydroxylase	Homo sapiens	75-78
23274807-0	2013	Temporal variation and spatial distribution of PAH in water of Three Gorges Reservoir during the complete impoundment period.	Water	54-59	phenylalanine hydroxylase	Homo sapiens	47-50
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	aziridine	89-106	phenylalanine hydroxylase	Homo sapiens	55-58
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	aziridine	89-106	phenylalanine hydroxylase	Homo sapiens	75-78
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	Polyglutamic Acid	108-128	phenylalanine hydroxylase	Homo sapiens	55-58
23999654-3	2013	In this investigation the Donnan potential of PEI-(PGA-PAH)n (PEI, PGA and PAH stand for polyethyleneimine, poly-L-glutamic acid and polyallylamine) films will be determined as a function of the number of deposition steps and the concentration of the redox probe, hexacyanoferrate anions, for films made from 10 layer pairs.	Polyglutamic Acid	108-128	phenylalanine hydroxylase	Homo sapiens	75-78
23850629-4	2013	By combining the CEPBET bioaccessibility test with an infinite sink, the removal of PAH from spiked solutions was monitored.	cepbet	17-23	phenylalanine hydroxylase	Homo sapiens	84-87
23274807-2	2013	PAH concentrations in water of TGR in the period of completely impounding water were 15-381 ng L(-1).	Water	22-27	phenylalanine hydroxylase	Homo sapiens	0-3
23274807-2	2013	PAH concentrations in water of TGR in the period of completely impounding water were 15-381 ng L(-1).	Water	74-79	phenylalanine hydroxylase	Homo sapiens	0-3
23274807-5	2013	An obvious decrease of PAH concentration was observed after 175-m water impounding in 2011 in TGR.	Water	66-71	phenylalanine hydroxylase	Homo sapiens	23-26
23274807-7	2013	Passive sampling method has been successfully applied in the investigation of trace PAH in water of TGR and proved to be a useful and efficient tool for the management and sustainable development of the big reservoir.	Water	91-96	phenylalanine hydroxylase	Homo sapiens	84-87
23898865-1	2013	BACKGROUND: Phenylalanine hydroxylase (PAH) is the enzyme that metabolizes phenylalanine, an essential amino acid required for catecholamine synthesis.	Phenylalanine	75-88	phenylalanine hydroxylase	Homo sapiens	12-37
23860686-1	2013	Phenylalanine hydroxylase (PAH) is a non-heme iron enzyme that catalyzes oxidation of phenylalanine to tyrosine, a reaction that must be kept under tight regulatory control.	Iron	46-50	phenylalanine hydroxylase	Homo sapiens	0-25
23860686-1	2013	Phenylalanine hydroxylase (PAH) is a non-heme iron enzyme that catalyzes oxidation of phenylalanine to tyrosine, a reaction that must be kept under tight regulatory control.	Iron	46-50	phenylalanine hydroxylase	Homo sapiens	27-30
23860686-1	2013	Phenylalanine hydroxylase (PAH) is a non-heme iron enzyme that catalyzes oxidation of phenylalanine to tyrosine, a reaction that must be kept under tight regulatory control.	Phenylalanine	86-99	phenylalanine hydroxylase	Homo sapiens	0-25
23860686-1	2013	Phenylalanine hydroxylase (PAH) is a non-heme iron enzyme that catalyzes oxidation of phenylalanine to tyrosine, a reaction that must be kept under tight regulatory control.	Phenylalanine	86-99	phenylalanine hydroxylase	Homo sapiens	27-30
23860686-1	2013	Phenylalanine hydroxylase (PAH) is a non-heme iron enzyme that catalyzes oxidation of phenylalanine to tyrosine, a reaction that must be kept under tight regulatory control.	Tyrosine	103-111	phenylalanine hydroxylase	Homo sapiens	0-25
23860686-1	2013	Phenylalanine hydroxylase (PAH) is a non-heme iron enzyme that catalyzes oxidation of phenylalanine to tyrosine, a reaction that must be kept under tight regulatory control.	Tyrosine	103-111	phenylalanine hydroxylase	Homo sapiens	27-30
23860686-4	2013	In an attempt to crystallographically characterize substrate binding by PAH from Chromobacterium violaceum, a single-domain monomeric enzyme, electron density for phenylalanine was observed at a distal site 15.7 A from the active site.	Phenylalanine	163-176	phenylalanine hydroxylase	Homo sapiens	72-75
24251098-1	2013	Phenylalanine hydroxylase from Legionella pneumophila (lpPAH) has a major functional role in the synthesis of the pigment pyomelanin, which is a potential virulence factor.	pyomelanin	122-132	phenylalanine hydroxylase	Homo sapiens	0-25
23940767-1	2013	Phenylketonuria (PKU), an autosomal recessive disorder of amino acid metabolism caused by mutations in the phenylalanine hydroxylase (PAH) gene, leads to childhood mental retardation by exposing neurons to cytotoxic levels of phenylalanine (Phe).	Phenylalanine	107-120	phenylalanine hydroxylase	Homo sapiens	134-137
23940767-1	2013	Phenylketonuria (PKU), an autosomal recessive disorder of amino acid metabolism caused by mutations in the phenylalanine hydroxylase (PAH) gene, leads to childhood mental retardation by exposing neurons to cytotoxic levels of phenylalanine (Phe).	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	107-132
23940767-1	2013	Phenylketonuria (PKU), an autosomal recessive disorder of amino acid metabolism caused by mutations in the phenylalanine hydroxylase (PAH) gene, leads to childhood mental retardation by exposing neurons to cytotoxic levels of phenylalanine (Phe).	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	134-137
23771645-1	2013	Phenylketonuria is an inherited disorder of metabolism of the amino acid phenylalanine caused by a deficit of the enzyme phenylalanine hydroxylase.	amino acid phenylalanine	62-86	phenylalanine hydroxylase	Homo sapiens	121-146
23898865-1	2013	BACKGROUND: Phenylalanine hydroxylase (PAH) is the enzyme that metabolizes phenylalanine, an essential amino acid required for catecholamine synthesis.	Phenylalanine	75-88	phenylalanine hydroxylase	Homo sapiens	39-42
23898865-1	2013	BACKGROUND: Phenylalanine hydroxylase (PAH) is the enzyme that metabolizes phenylalanine, an essential amino acid required for catecholamine synthesis.	Amino Acids, Essential	93-113	phenylalanine hydroxylase	Homo sapiens	12-37
23898865-1	2013	BACKGROUND: Phenylalanine hydroxylase (PAH) is the enzyme that metabolizes phenylalanine, an essential amino acid required for catecholamine synthesis.	Amino Acids, Essential	93-113	phenylalanine hydroxylase	Homo sapiens	39-42
23898865-1	2013	BACKGROUND: Phenylalanine hydroxylase (PAH) is the enzyme that metabolizes phenylalanine, an essential amino acid required for catecholamine synthesis.	Catecholamines	127-140	phenylalanine hydroxylase	Homo sapiens	12-37
23898865-1	2013	BACKGROUND: Phenylalanine hydroxylase (PAH) is the enzyme that metabolizes phenylalanine, an essential amino acid required for catecholamine synthesis.	Catecholamines	127-140	phenylalanine hydroxylase	Homo sapiens	39-42
23537590-1	2013	The enzyme phenylalanine hydroxylase catalyzes the hydroxylation of excess phenylalanine in the liver to tyrosine.	Tyrosine	105-113	phenylalanine hydroxylase	Homo sapiens	11-36
23325502-9	2013	PAH dissipation through water leaching was limited and did not present a significant risk for the environment.	Water	24-29	phenylalanine hydroxylase	Homo sapiens	0-3
23325502-10	2013	This PAH water concentration appeared however as a good indicator of overall dissipation rate, thereby illustrating the importance of pollutant availability in predicting its degradation potential.	Water	9-14	phenylalanine hydroxylase	Homo sapiens	5-8
23072726-3	2013	Diminished conversion of phenylalanine (Phen) to tyrosine (Tyr), the primary amino acid precursor of DA, has been associated with inflammation, and may reflect decreased activity of the enzyme phenylalanine-hydroxylase (PAH).	Phenylalanine	25-38	phenylalanine hydroxylase	Homo sapiens	193-218
23072726-3	2013	Diminished conversion of phenylalanine (Phen) to tyrosine (Tyr), the primary amino acid precursor of DA, has been associated with inflammation, and may reflect decreased activity of the enzyme phenylalanine-hydroxylase (PAH).	Phenylalanine	40-44	phenylalanine hydroxylase	Homo sapiens	193-218
23072726-3	2013	Diminished conversion of phenylalanine (Phen) to tyrosine (Tyr), the primary amino acid precursor of DA, has been associated with inflammation, and may reflect decreased activity of the enzyme phenylalanine-hydroxylase (PAH).	Tyrosine	49-57	phenylalanine hydroxylase	Homo sapiens	193-218
23072726-3	2013	Diminished conversion of phenylalanine (Phen) to tyrosine (Tyr), the primary amino acid precursor of DA, has been associated with inflammation, and may reflect decreased activity of the enzyme phenylalanine-hydroxylase (PAH).	Tyrosine	59-62	phenylalanine hydroxylase	Homo sapiens	193-218
23072726-3	2013	Diminished conversion of phenylalanine (Phen) to tyrosine (Tyr), the primary amino acid precursor of DA, has been associated with inflammation, and may reflect decreased activity of the enzyme phenylalanine-hydroxylase (PAH).	Dopamine	101-103	phenylalanine hydroxylase	Homo sapiens	193-218
23529398-3	2013	The extent of damage to organisms from PAH exposure is dependent on numerous factors including degree and type of PAH exposure, nature of the environment contaminated (i.e. terrestrial or aquatic), the ability of an organism to relocate to pristine environments, type and sensitivity of organism to specific hydrocarbon fractions and ability of the organism to metabolise different PAH fractions.	Hydrocarbons	308-319	phenylalanine hydroxylase	Homo sapiens	39-42
23559577-1	2013	In about 20%-30% of phenylketonuria (PKU) patients (all phenotypes of PAH deficiency), Phe levels may be controlled through phenylalanine hydroxylase cofactor tetrahydrobiopterin therapy.	Phenylalanine	87-90	phenylalanine hydroxylase	Homo sapiens	124-149
23559577-1	2013	In about 20%-30% of phenylketonuria (PKU) patients (all phenotypes of PAH deficiency), Phe levels may be controlled through phenylalanine hydroxylase cofactor tetrahydrobiopterin therapy.	sapropterin	159-178	phenylalanine hydroxylase	Homo sapiens	124-149
23523934-0	2013	Induction of ATP synthase beta by H2O2 induces melanogenesis by activating PAH and cAMP/CREB/MITF signaling in melanoma cells.	Hydrogen Peroxide	34-38	phenylalanine hydroxylase	Homo sapiens	75-78
23523934-7	2013	In summary, H2O2 may induce melanogenesis via the upregulation of PAH and activation of cAMP/p-CREB/MITF signaling by increasing intracellular cAMP levels through the induction of ATP5B.	Hydrogen Peroxide	12-16	phenylalanine hydroxylase	Homo sapiens	66-69
23730366-1	2013	BACKGROUND: The aim is to correlate pulmonary arterial (PA) remodeling estimated by PA fibrosis in PA hypertension (PAH) with clinical follow-up.	Protactinium	56-58	phenylalanine hydroxylase	Homo sapiens	116-119
23582045-0	2013	PAH fluxes to Siskiwit revisted: trends in fluxes and sources of pyrogenic PAH and perylene constrained via radiocarbon analysis.	Perylene	83-91	phenylalanine hydroxylase	Homo sapiens	0-3
23523120-0	2013	Water concentrations of PAH, PCB and OCP by using semipermeable membrane devices and sediments.	Water	0-5	phenylalanine hydroxylase	Homo sapiens	24-27
23782930-8	2013	CONCLUSION: This study reveals the high pyrene (PAH) exposure of the Kinshasa population.	pyrene	40-46	phenylalanine hydroxylase	Homo sapiens	48-51
23782930-9	2013	However, more work, with a rigorous design in the exposed population (monitoring of air concentrations and identifying other sources of pyrene -PAH exposure), is needed to establish further documentation.	pyrene	136-142	phenylalanine hydroxylase	Homo sapiens	144-147
23552227-6	2013	The influence of the PAH chain length (polymers containing on average 150 and 700 monomers were examined) on the protonation equilibrium of PAH could not be observed.	Polymers	39-47	phenylalanine hydroxylase	Homo sapiens	140-143
23425894-6	2013	RESULTS: During flushing, PAH levels frequently exceeded drinking water quality standards; after flushing, these levels dropped rapidly.	Water	66-71	phenylalanine hydroxylase	Homo sapiens	26-29
23425894-7	2013	After the repair of cast iron water mains, PAH levels exceeded the drinking water standards for up to 40 days in some locations.	iron water	25-35	phenylalanine hydroxylase	Homo sapiens	43-46
23425894-8	2013	CONCLUSIONS: The estimated margin of exposure for PAH exposure through drinking water was &gt; 10,000 for all 120 measurement locations, which suggests that PAH exposure through drinking water is of low concern for consumer health.	Water	80-85	phenylalanine hydroxylase	Homo sapiens	50-53
23425894-8	2013	CONCLUSIONS: The estimated margin of exposure for PAH exposure through drinking water was &gt; 10,000 for all 120 measurement locations, which suggests that PAH exposure through drinking water is of low concern for consumer health.	Water	80-85	phenylalanine hydroxylase	Homo sapiens	157-160
23425894-8	2013	CONCLUSIONS: The estimated margin of exposure for PAH exposure through drinking water was &gt; 10,000 for all 120 measurement locations, which suggests that PAH exposure through drinking water is of low concern for consumer health.	Water	187-192	phenylalanine hydroxylase	Homo sapiens	50-53
23425894-8	2013	CONCLUSIONS: The estimated margin of exposure for PAH exposure through drinking water was &gt; 10,000 for all 120 measurement locations, which suggests that PAH exposure through drinking water is of low concern for consumer health.	Water	187-192	phenylalanine hydroxylase	Homo sapiens	157-160
23425894-9	2013	However, factors that differ among water systems, such as the use of chlorination for disinfection, may influence PAH levels in other locations.	Water	35-40	phenylalanine hydroxylase	Homo sapiens	114-117
23480348-1	2013	Polyallylamine (PAH) functionalized Pd icosahedra are synthesized through a simple, one-pot, seedless and hydrothermal growth method.	polyallylamine	0-14	phenylalanine hydroxylase	Homo sapiens	16-19
23480348-1	2013	Polyallylamine (PAH) functionalized Pd icosahedra are synthesized through a simple, one-pot, seedless and hydrothermal growth method.	pd icosahedra	36-49	phenylalanine hydroxylase	Homo sapiens	16-19
23480348-3	2013	The strong interaction between PAH and Pd atom sharply changes the electronic structure of Pd atom in the Pd icosahedra.	Palladium	39-41	phenylalanine hydroxylase	Homo sapiens	31-34
23480348-3	2013	The strong interaction between PAH and Pd atom sharply changes the electronic structure of Pd atom in the Pd icosahedra.	Palladium	91-93	phenylalanine hydroxylase	Homo sapiens	31-34
23480348-3	2013	The strong interaction between PAH and Pd atom sharply changes the electronic structure of Pd atom in the Pd icosahedra.	icosahedra	109-119	phenylalanine hydroxylase	Homo sapiens	31-34
23480348-4	2013	The protective function of PAH layers and enhanced antietching capability of Pd atom are responsible for the formation of the Pd icosahedra.	pd icosahedra	126-139	phenylalanine hydroxylase	Homo sapiens	27-30
23480348-5	2013	Very importantly, the as-prepared PAH functionalized Pd icosahedra exhibit superior electrocatalytic activity and ethanol tolerant ability toward the oxygen reduction reaction (ORR) compared to the commercially available Pt black in alkaline media.	pd icosahedra	53-66	phenylalanine hydroxylase	Homo sapiens	34-37
23480348-5	2013	Very importantly, the as-prepared PAH functionalized Pd icosahedra exhibit superior electrocatalytic activity and ethanol tolerant ability toward the oxygen reduction reaction (ORR) compared to the commercially available Pt black in alkaline media.	Ethanol	114-121	phenylalanine hydroxylase	Homo sapiens	34-37
23480348-5	2013	Very importantly, the as-prepared PAH functionalized Pd icosahedra exhibit superior electrocatalytic activity and ethanol tolerant ability toward the oxygen reduction reaction (ORR) compared to the commercially available Pt black in alkaline media.	Oxygen	150-156	phenylalanine hydroxylase	Homo sapiens	34-37
23457044-1	2013	Mammalian phenylalanine hydroxylase (PAH) catalyzes the rate-limiting step in the phenylalanine catabolism, consuming about 75% of the phenylalanine input from the diet and protein catabolism under physiological conditions.	Phenylalanine	10-23	phenylalanine hydroxylase	Homo sapiens	37-40
23425894-0	2013	Health implications of PAH release from coated cast iron drinking water distribution systems in The Netherlands.	Iron	52-56	phenylalanine hydroxylase	Homo sapiens	23-26
23425894-0	2013	Health implications of PAH release from coated cast iron drinking water distribution systems in The Netherlands.	Water	66-71	phenylalanine hydroxylase	Homo sapiens	23-26
23376598-2	2013	The highest PAH concentrations recovered in foodstuffs corresponded to the following contributors: chrysene (25.7%), benzo[b]fluoranthene (15.0%) and benz[a]anthracene (9.0%) whereas the lowest concentrations were those of dibenz[a,h]anthracene, 5 methylchrysene and dibenzo[a,h]pyrene (below 2.0%).	chrysene	99-107	phenylalanine hydroxylase	Homo sapiens	12-15
23376598-2	2013	The highest PAH concentrations recovered in foodstuffs corresponded to the following contributors: chrysene (25.7%), benzo[b]fluoranthene (15.0%) and benz[a]anthracene (9.0%) whereas the lowest concentrations were those of dibenz[a,h]anthracene, 5 methylchrysene and dibenzo[a,h]pyrene (below 2.0%).	benzo(b)fluoranthene	117-137	phenylalanine hydroxylase	Homo sapiens	12-15
23376598-2	2013	The highest PAH concentrations recovered in foodstuffs corresponded to the following contributors: chrysene (25.7%), benzo[b]fluoranthene (15.0%) and benz[a]anthracene (9.0%) whereas the lowest concentrations were those of dibenz[a,h]anthracene, 5 methylchrysene and dibenzo[a,h]pyrene (below 2.0%).	anthracene	157-167	phenylalanine hydroxylase	Homo sapiens	12-15
23376598-2	2013	The highest PAH concentrations recovered in foodstuffs corresponded to the following contributors: chrysene (25.7%), benzo[b]fluoranthene (15.0%) and benz[a]anthracene (9.0%) whereas the lowest concentrations were those of dibenz[a,h]anthracene, 5 methylchrysene and dibenzo[a,h]pyrene (below 2.0%).	1,2,5,6-dibenzanthracene	223-244	phenylalanine hydroxylase	Homo sapiens	12-15
23376598-2	2013	The highest PAH concentrations recovered in foodstuffs corresponded to the following contributors: chrysene (25.7%), benzo[b]fluoranthene (15.0%) and benz[a]anthracene (9.0%) whereas the lowest concentrations were those of dibenz[a,h]anthracene, 5 methylchrysene and dibenzo[a,h]pyrene (below 2.0%).	6-methylchrysene	248-262	phenylalanine hydroxylase	Homo sapiens	12-15
23376598-2	2013	The highest PAH concentrations recovered in foodstuffs corresponded to the following contributors: chrysene (25.7%), benzo[b]fluoranthene (15.0%) and benz[a]anthracene (9.0%) whereas the lowest concentrations were those of dibenz[a,h]anthracene, 5 methylchrysene and dibenzo[a,h]pyrene (below 2.0%).	dibenzo(a,h)pyrene	267-285	phenylalanine hydroxylase	Homo sapiens	12-15
23457044-1	2013	Mammalian phenylalanine hydroxylase (PAH) catalyzes the rate-limiting step in the phenylalanine catabolism, consuming about 75% of the phenylalanine input from the diet and protein catabolism under physiological conditions.	Phenylalanine	82-95	phenylalanine hydroxylase	Homo sapiens	10-35
23457044-1	2013	Mammalian phenylalanine hydroxylase (PAH) catalyzes the rate-limiting step in the phenylalanine catabolism, consuming about 75% of the phenylalanine input from the diet and protein catabolism under physiological conditions.	Phenylalanine	82-95	phenylalanine hydroxylase	Homo sapiens	37-40
23457044-5	2013	Importantly, there has also been an increased number of studies on the structure and function of PAH from bacteria and lower eukaryote organisms, revealing an additional anabolic role of the enzyme in the synthesis of melanin-like pigments.	Melanins	218-225	phenylalanine hydroxylase	Homo sapiens	97-100
23457044-6	2013	In this review, we discuss these recent studies, which contribute to define the evolutionary adaptation of the PAH structure and function leading to sophisticated regulation for effective catabolic processing of phenylalanine in mammalian organisms.	Phenylalanine	212-225	phenylalanine hydroxylase	Homo sapiens	111-114
23260251-4	2013	Individual PAH flux ranged from 627 ng m(-2) d(-1) volatilization of phenanthrene during the rainy season with storm-water discharges raising dissolved phase concentration, to 67 ng m(-2) d(-1) absorption of fluoranthene during high wind speed periods.	phenanthrene	69-81	phenylalanine hydroxylase	Homo sapiens	11-14
23295026-4	2013	In this paper, optimized mats of ZnO nanofibers with an average fiber diameter of 60 nm are shown to be highly effective in the photocatalytic degradation of the PAH dyes--naphthalene and anthracene.	Zinc Oxide	33-36	phenylalanine hydroxylase	Homo sapiens	162-165
23295026-4	2013	In this paper, optimized mats of ZnO nanofibers with an average fiber diameter of 60 nm are shown to be highly effective in the photocatalytic degradation of the PAH dyes--naphthalene and anthracene.	naphthalene	172-183	phenylalanine hydroxylase	Homo sapiens	162-165
23295026-4	2013	In this paper, optimized mats of ZnO nanofibers with an average fiber diameter of 60 nm are shown to be highly effective in the photocatalytic degradation of the PAH dyes--naphthalene and anthracene.	anthracene	188-198	phenylalanine hydroxylase	Homo sapiens	162-165
23436109-1	2013	INTRODUCTION: Pharmacological levels of the phenylalanine hydroxylase enzyme cofactor, tetrahydrobiopterin (BH4), reduce plasma phenylalanine levels in some patients with phenylketonuria (PKU), providing the first pharmacological therapy for PKU.	sapropterin	87-106	phenylalanine hydroxylase	Homo sapiens	44-69
23436109-1	2013	INTRODUCTION: Pharmacological levels of the phenylalanine hydroxylase enzyme cofactor, tetrahydrobiopterin (BH4), reduce plasma phenylalanine levels in some patients with phenylketonuria (PKU), providing the first pharmacological therapy for PKU.	sapropterin	108-111	phenylalanine hydroxylase	Homo sapiens	44-69
23260251-4	2013	Individual PAH flux ranged from 627 ng m(-2) d(-1) volatilization of phenanthrene during the rainy season with storm-water discharges raising dissolved phase concentration, to 67 ng m(-2) d(-1) absorption of fluoranthene during high wind speed periods.	fluoranthene	208-220	phenylalanine hydroxylase	Homo sapiens	11-14
23260251-5	2013	Due to PAH annual fluxes through air-water exchange, Kenting seawater is a source of low molecular weight PAHs and a reservoir of high molecular weight PAHs.	Water	37-42	phenylalanine hydroxylase	Homo sapiens	7-10
23837345-2	2013	Pyrene was continuously the most abundant PAH, whereas anthracene was the PAH with the lowest concentrations.	pyrene	0-6	phenylalanine hydroxylase	Homo sapiens	42-45
23837345-2	2013	Pyrene was continuously the most abundant PAH, whereas anthracene was the PAH with the lowest concentrations.	anthracene	55-65	phenylalanine hydroxylase	Homo sapiens	74-77
23634439-1	2013	6R l-erythro-5,6,7,8-tetrahydrobiopterin (BH4) is an essential cofactor for several enzymes including phenylalanine hydroxylase and the nitric oxide synthases (NOS).	sapropterin	0-40	phenylalanine hydroxylase	Homo sapiens	102-127
23375473-2	2013	In these patients hepatic phenylalanine hydroxylase system is compromised due to subnormal tetrahydrobiopterin (BH(4)) levels and hydroxylation of phenylalanine (Phe) to tyrosine (Tyr) is reduced with elevated Phe/Tyr ratio 1-2 h after oral Phe administration (100 mg/kg bw) administration.	sapropterin	91-110	phenylalanine hydroxylase	Homo sapiens	26-51
23375473-2	2013	In these patients hepatic phenylalanine hydroxylase system is compromised due to subnormal tetrahydrobiopterin (BH(4)) levels and hydroxylation of phenylalanine (Phe) to tyrosine (Tyr) is reduced with elevated Phe/Tyr ratio 1-2 h after oral Phe administration (100 mg/kg bw) administration.	Phenylalanine	162-165	phenylalanine hydroxylase	Homo sapiens	26-51
23375473-2	2013	In these patients hepatic phenylalanine hydroxylase system is compromised due to subnormal tetrahydrobiopterin (BH(4)) levels and hydroxylation of phenylalanine (Phe) to tyrosine (Tyr) is reduced with elevated Phe/Tyr ratio 1-2 h after oral Phe administration (100 mg/kg bw) administration.	Tyrosine	170-178	phenylalanine hydroxylase	Homo sapiens	26-51
23375473-2	2013	In these patients hepatic phenylalanine hydroxylase system is compromised due to subnormal tetrahydrobiopterin (BH(4)) levels and hydroxylation of phenylalanine (Phe) to tyrosine (Tyr) is reduced with elevated Phe/Tyr ratio 1-2 h after oral Phe administration (100 mg/kg bw) administration.	Tyrosine	180-183	phenylalanine hydroxylase	Homo sapiens	26-51
23375473-2	2013	In these patients hepatic phenylalanine hydroxylase system is compromised due to subnormal tetrahydrobiopterin (BH(4)) levels and hydroxylation of phenylalanine (Phe) to tyrosine (Tyr) is reduced with elevated Phe/Tyr ratio 1-2 h after oral Phe administration (100 mg/kg bw) administration.	Phenylalanine	210-213	phenylalanine hydroxylase	Homo sapiens	26-51
23375473-2	2013	In these patients hepatic phenylalanine hydroxylase system is compromised due to subnormal tetrahydrobiopterin (BH(4)) levels and hydroxylation of phenylalanine (Phe) to tyrosine (Tyr) is reduced with elevated Phe/Tyr ratio 1-2 h after oral Phe administration (100 mg/kg bw) administration.	Tyrosine	214-217	phenylalanine hydroxylase	Homo sapiens	26-51
23375473-2	2013	In these patients hepatic phenylalanine hydroxylase system is compromised due to subnormal tetrahydrobiopterin (BH(4)) levels and hydroxylation of phenylalanine (Phe) to tyrosine (Tyr) is reduced with elevated Phe/Tyr ratio 1-2 h after oral Phe administration (100 mg/kg bw) administration.	Phenylalanine	210-213	phenylalanine hydroxylase	Homo sapiens	26-51
23634439-1	2013	6R l-erythro-5,6,7,8-tetrahydrobiopterin (BH4) is an essential cofactor for several enzymes including phenylalanine hydroxylase and the nitric oxide synthases (NOS).	sapropterin	42-45	phenylalanine hydroxylase	Homo sapiens	102-127
23317152-1	2013	Membranes composed of multilayer poly(4-styrenesulfonate) (PSS)/protonated poly(allylamine) (PAH) films on porous alumina supports exhibit high monovalent/divalent cation selectivities.	polyallylamine	75-91	phenylalanine hydroxylase	Homo sapiens	93-96
23368961-1	2013	The aromatic amino acid hydroxylases tyrosine hydroxylase (TyrH) and phenylalanine hydroxylase (PheH) have essentially identical active sites; however, PheH is nearly incapable of hydroxylating tyrosine, while TyrH can readily hydroxylate both tyrosine and phenylalanine.	Tyrosine	37-45	phenylalanine hydroxylase	Homo sapiens	96-100
23368961-1	2013	The aromatic amino acid hydroxylases tyrosine hydroxylase (TyrH) and phenylalanine hydroxylase (PheH) have essentially identical active sites; however, PheH is nearly incapable of hydroxylating tyrosine, while TyrH can readily hydroxylate both tyrosine and phenylalanine.	Tyrosine	37-45	phenylalanine hydroxylase	Homo sapiens	152-156
23368961-1	2013	The aromatic amino acid hydroxylases tyrosine hydroxylase (TyrH) and phenylalanine hydroxylase (PheH) have essentially identical active sites; however, PheH is nearly incapable of hydroxylating tyrosine, while TyrH can readily hydroxylate both tyrosine and phenylalanine.	Tyrosine	194-202	phenylalanine hydroxylase	Homo sapiens	69-94
23368961-1	2013	The aromatic amino acid hydroxylases tyrosine hydroxylase (TyrH) and phenylalanine hydroxylase (PheH) have essentially identical active sites; however, PheH is nearly incapable of hydroxylating tyrosine, while TyrH can readily hydroxylate both tyrosine and phenylalanine.	Tyrosine	194-202	phenylalanine hydroxylase	Homo sapiens	152-156
23368961-1	2013	The aromatic amino acid hydroxylases tyrosine hydroxylase (TyrH) and phenylalanine hydroxylase (PheH) have essentially identical active sites; however, PheH is nearly incapable of hydroxylating tyrosine, while TyrH can readily hydroxylate both tyrosine and phenylalanine.	Phenylalanine	69-82	phenylalanine hydroxylase	Homo sapiens	96-100
23368961-1	2013	The aromatic amino acid hydroxylases tyrosine hydroxylase (TyrH) and phenylalanine hydroxylase (PheH) have essentially identical active sites; however, PheH is nearly incapable of hydroxylating tyrosine, while TyrH can readily hydroxylate both tyrosine and phenylalanine.	Phenylalanine	69-82	phenylalanine hydroxylase	Homo sapiens	152-156
23327364-1	2013	Phenylalanine hydroxylase (PheH) catalyzes the key step in the catabolism of dietary phenylalanine, its hydroxylation to tyrosine using tetrahydrobiopterin (BH(4)) and O(2).	Phenylalanine	85-98	phenylalanine hydroxylase	Homo sapiens	0-25
23327364-1	2013	Phenylalanine hydroxylase (PheH) catalyzes the key step in the catabolism of dietary phenylalanine, its hydroxylation to tyrosine using tetrahydrobiopterin (BH(4)) and O(2).	Phenylalanine	85-98	phenylalanine hydroxylase	Homo sapiens	27-31
23327364-1	2013	Phenylalanine hydroxylase (PheH) catalyzes the key step in the catabolism of dietary phenylalanine, its hydroxylation to tyrosine using tetrahydrobiopterin (BH(4)) and O(2).	Tyrosine	121-129	phenylalanine hydroxylase	Homo sapiens	0-25
23327364-1	2013	Phenylalanine hydroxylase (PheH) catalyzes the key step in the catabolism of dietary phenylalanine, its hydroxylation to tyrosine using tetrahydrobiopterin (BH(4)) and O(2).	Tyrosine	121-129	phenylalanine hydroxylase	Homo sapiens	27-31
23327364-1	2013	Phenylalanine hydroxylase (PheH) catalyzes the key step in the catabolism of dietary phenylalanine, its hydroxylation to tyrosine using tetrahydrobiopterin (BH(4)) and O(2).	sapropterin	136-155	phenylalanine hydroxylase	Homo sapiens	0-25
23327364-1	2013	Phenylalanine hydroxylase (PheH) catalyzes the key step in the catabolism of dietary phenylalanine, its hydroxylation to tyrosine using tetrahydrobiopterin (BH(4)) and O(2).	sapropterin	136-155	phenylalanine hydroxylase	Homo sapiens	27-31
23317152-1	2013	Membranes composed of multilayer poly(4-styrenesulfonate) (PSS)/protonated poly(allylamine) (PAH) films on porous alumina supports exhibit high monovalent/divalent cation selectivities.	Aluminum Oxide	114-121	phenylalanine hydroxylase	Homo sapiens	93-96
23317152-4	2013	Under MgCl(2) concentration gradients across either (PSS/PAH)(4)- or (PSS/PAH)(4)PSS-coated alumina, transmembrane potentials indicate Mg(2+) transference numbers approaching 0.	Aluminum Oxide	92-99	phenylalanine hydroxylase	Homo sapiens	74-77
24350308-3	2013	The selection of patients eligible for BH4-therapy by means of genotyping of the PAH gene mutations may be recommended as a complementary approach.	sapropterin	39-42	phenylalanine hydroxylase	Homo sapiens	81-84
23141842-8	2013	The bioavailable fraction of PAH was inversely correlated to the number of benzene rings and the octanol-water partition coefficient.	Benzene	75-82	phenylalanine hydroxylase	Homo sapiens	29-32
23141842-8	2013	The bioavailable fraction of PAH was inversely correlated to the number of benzene rings and the octanol-water partition coefficient.	Octanols	97-104	phenylalanine hydroxylase	Homo sapiens	29-32
23141842-8	2013	The bioavailable fraction of PAH was inversely correlated to the number of benzene rings and the octanol-water partition coefficient.	Water	105-110	phenylalanine hydroxylase	Homo sapiens	29-32
24350308-9	2013	Analysis of the published data shows similar percentage of the "BH4-responsive" variants of a PAH gene in patients from other countries of Eastern Europe.	sapropterin	64-67	phenylalanine hydroxylase	Homo sapiens	94-97
23176388-11	2013	CONCLUSIONS: iPAH, hPAH and aPAH were characterized by increased levels of EMP and of small PMP, a new class of PMP which seems to be differentially produced than large PMP.	pmp	92-95	phenylalanine hydroxylase	Homo sapiens	19-23
23010059-1	2013	Stable hollow microcapsules composed of sodium carboxymethyl cellulose (CMC) and poly (allylamine hydrochloride) (PAH) were produced by layer-by-layer adsorption of polyelectrolytes onto CaCO(3) microparticles.	polyallylamine	81-112	phenylalanine hydroxylase	Homo sapiens	114-117
23176388-11	2013	CONCLUSIONS: iPAH, hPAH and aPAH were characterized by increased levels of EMP and of small PMP, a new class of PMP which seems to be differentially produced than large PMP.	pmp	112-115	phenylalanine hydroxylase	Homo sapiens	19-23
23176388-11	2013	CONCLUSIONS: iPAH, hPAH and aPAH were characterized by increased levels of EMP and of small PMP, a new class of PMP which seems to be differentially produced than large PMP.	pmp	112-115	phenylalanine hydroxylase	Homo sapiens	19-23
22805987-7	2013	Mixed-effects models were used to evaluate the associations between air or food PAH concentrations and urine 1-OHPG concentrations.	1-ohpg	109-115	phenylalanine hydroxylase	Homo sapiens	80-83
23485234-7	2013	Total PAH level did not change with the addition of 5% DEA and only 10% decreased with 5% TiO2 addition.	titanium dioxide	90-94	phenylalanine hydroxylase	Homo sapiens	6-9
23485234-8	2013	PAH removal ratios were 8% and 32% when DEA (20%) and TiO2 (20%) were added, respectively.	diethylamine	40-43	phenylalanine hydroxylase	Homo sapiens	0-3
23485234-8	2013	PAH removal ratios were 8% and 32% when DEA (20%) and TiO2 (20%) were added, respectively.	titanium dioxide	54-58	phenylalanine hydroxylase	Homo sapiens	0-3
23081889-0	2012	A boron-containing PAH as a substructure of boron-doped graphene.	Boron	2-7	phenylalanine hydroxylase	Homo sapiens	19-22
23430494-1	2013	Phenylketonuria (PKU) is an autosomal recessive inherited metabolic disorder caused by a complete or near-complete deficiency of the liver enzyme phenylalanine hydroxylase (PAH), which converts the amino acid phenylalanine to tyrosine, leading to the increase of blood and tissue concentration of phenylalanine to toxic levels.	amino acid phenylalanine	198-222	phenylalanine hydroxylase	Homo sapiens	173-176
23430494-1	2013	Phenylketonuria (PKU) is an autosomal recessive inherited metabolic disorder caused by a complete or near-complete deficiency of the liver enzyme phenylalanine hydroxylase (PAH), which converts the amino acid phenylalanine to tyrosine, leading to the increase of blood and tissue concentration of phenylalanine to toxic levels.	Tyrosine	226-234	phenylalanine hydroxylase	Homo sapiens	173-176
23430494-1	2013	Phenylketonuria (PKU) is an autosomal recessive inherited metabolic disorder caused by a complete or near-complete deficiency of the liver enzyme phenylalanine hydroxylase (PAH), which converts the amino acid phenylalanine to tyrosine, leading to the increase of blood and tissue concentration of phenylalanine to toxic levels.	Phenylalanine	146-159	phenylalanine hydroxylase	Homo sapiens	173-176
23484001-9	2013	This decreased the damage of PAHs to hydrogen bonds in double-stranded DNA by isolating DNA molecules from PAHs and consequently enhanced the transformation efficiency of DNA exposed to PAH contaminants.	Hydrogen	37-45	phenylalanine hydroxylase	Homo sapiens	29-32
23170945-6	2012	Blending the weak polyanion poly(acrylic acid), PAA, with the strong polyanion poly(styrene sulfonate), PSS, to layer alternately with the polycation poly(allyamine hydrochloride), PAH, is shown to be a viable method to achieve intermediate free volume characteristics in these LbL films.	carbopol 940	48-51	phenylalanine hydroxylase	Homo sapiens	181-184
23081889-0	2012	A boron-containing PAH as a substructure of boron-doped graphene.	Boron	44-49	phenylalanine hydroxylase	Homo sapiens	19-22
23081889-0	2012	A boron-containing PAH as a substructure of boron-doped graphene.	Graphite	56-64	phenylalanine hydroxylase	Homo sapiens	19-22
22527117-4	2012	Total PAH concentrations in indoor dust samples showed a better correlation to black carbon compared to total organic carbon contents.	Carbon	85-91	phenylalanine hydroxylase	Homo sapiens	6-9
23087908-10	2012	Total PAH concentrations in wood dust varied greatly (0.24-7.95 ppm) with the lowest being in MDF dust and the highest in wood melamine dust.	melamine	127-135	phenylalanine hydroxylase	Homo sapiens	6-9
22477023-1	2012	Phenylketonuria is a recessive autosomal disorder that is caused by a deficiency in the activity of phenylalanine-4-hydroxylase, which converts phenylalanine to tyrosine, leading to the accumulation of phenylalanine and its metabolites phenyllactic acid, phenylacetic acid, and phenylpyruvic acid in the blood and tissues of patients.	Tyrosine	161-169	phenylalanine hydroxylase	Homo sapiens	100-127
22477023-1	2012	Phenylketonuria is a recessive autosomal disorder that is caused by a deficiency in the activity of phenylalanine-4-hydroxylase, which converts phenylalanine to tyrosine, leading to the accumulation of phenylalanine and its metabolites phenyllactic acid, phenylacetic acid, and phenylpyruvic acid in the blood and tissues of patients.	Phenylalanine	144-157	phenylalanine hydroxylase	Homo sapiens	100-127
22477023-1	2012	Phenylketonuria is a recessive autosomal disorder that is caused by a deficiency in the activity of phenylalanine-4-hydroxylase, which converts phenylalanine to tyrosine, leading to the accumulation of phenylalanine and its metabolites phenyllactic acid, phenylacetic acid, and phenylpyruvic acid in the blood and tissues of patients.	3-phenyllactic acid	236-253	phenylalanine hydroxylase	Homo sapiens	100-127
22477023-1	2012	Phenylketonuria is a recessive autosomal disorder that is caused by a deficiency in the activity of phenylalanine-4-hydroxylase, which converts phenylalanine to tyrosine, leading to the accumulation of phenylalanine and its metabolites phenyllactic acid, phenylacetic acid, and phenylpyruvic acid in the blood and tissues of patients.	phenylacetic acid	255-272	phenylalanine hydroxylase	Homo sapiens	100-127
22477023-1	2012	Phenylketonuria is a recessive autosomal disorder that is caused by a deficiency in the activity of phenylalanine-4-hydroxylase, which converts phenylalanine to tyrosine, leading to the accumulation of phenylalanine and its metabolites phenyllactic acid, phenylacetic acid, and phenylpyruvic acid in the blood and tissues of patients.	phenylpyruvic acid	278-296	phenylalanine hydroxylase	Homo sapiens	100-127
23092998-2	2012	The objectives of the present study were: (1) to establish the levels and spatial distribution of polycyclic aromatic hydrocarbons (PAHs) in soil across the Xiamen metropolis, (2) to evaluate the extent to which PAH concentrations were elevated in the high urbanization area (HUA) of the island and how these compared with those in the low urbanization area (LUA) of the mainland, and (3) to evaluate the PAH hazard based upon their Carcinogenic Potential (CP), defined as toxicity equivalence of  PAHs.	Polycyclic Aromatic Hydrocarbons	98-130	phenylalanine hydroxylase	Homo sapiens	132-135
23225039-2	2012	METHODS: Thirteen exons and flanking introns of PAH gene in 102 patients with high blood phenylalanine levels (Phe &gt; 120 umol/L) at initial diagnosis were amplified with polymerase chain reaction and analyzed with single strand conformation polymorphism (SSCP), denaturing high performance liquid chromatography (DHPLC) and DNA sequencing.	Phenylalanine	89-102	phenylalanine hydroxylase	Homo sapiens	48-51
23225039-2	2012	METHODS: Thirteen exons and flanking introns of PAH gene in 102 patients with high blood phenylalanine levels (Phe &gt; 120 umol/L) at initial diagnosis were amplified with polymerase chain reaction and analyzed with single strand conformation polymorphism (SSCP), denaturing high performance liquid chromatography (DHPLC) and DNA sequencing.	Phenylalanine	111-114	phenylalanine hydroxylase	Homo sapiens	48-51
23089061-0	2012	Using slow-release permanganate candles to remediate PAH-contaminated water.	Water	70-75	phenylalanine hydroxylase	Homo sapiens	53-56
23089061-6	2012	Results showed most of the 16 PAHs tested were degraded within 2-4 h. Using (14)C-labled phenanthrene and benzo(a)pyrene, we demonstrated that the wax matrix of the candle initially adsorbs the PAH, but then releases the PAH back into solution as transformed, more water soluble products.	Polycyclic Aromatic Hydrocarbons	30-34	phenylalanine hydroxylase	Homo sapiens	194-197
23089061-6	2012	Results showed most of the 16 PAHs tested were degraded within 2-4 h. Using (14)C-labled phenanthrene and benzo(a)pyrene, we demonstrated that the wax matrix of the candle initially adsorbs the PAH, but then releases the PAH back into solution as transformed, more water soluble products.	phenanthrene	89-101	phenylalanine hydroxylase	Homo sapiens	30-33
23089061-6	2012	Results showed most of the 16 PAHs tested were degraded within 2-4 h. Using (14)C-labled phenanthrene and benzo(a)pyrene, we demonstrated that the wax matrix of the candle initially adsorbs the PAH, but then releases the PAH back into solution as transformed, more water soluble products.	phenanthrene	89-101	phenylalanine hydroxylase	Homo sapiens	194-197
23089061-6	2012	Results showed most of the 16 PAHs tested were degraded within 2-4 h. Using (14)C-labled phenanthrene and benzo(a)pyrene, we demonstrated that the wax matrix of the candle initially adsorbs the PAH, but then releases the PAH back into solution as transformed, more water soluble products.	Benzo(a)pyrene	106-120	phenylalanine hydroxylase	Homo sapiens	30-33
23089061-6	2012	Results showed most of the 16 PAHs tested were degraded within 2-4 h. Using (14)C-labled phenanthrene and benzo(a)pyrene, we demonstrated that the wax matrix of the candle initially adsorbs the PAH, but then releases the PAH back into solution as transformed, more water soluble products.	Benzo(a)pyrene	106-120	phenylalanine hydroxylase	Homo sapiens	194-197
23089061-6	2012	Results showed most of the 16 PAHs tested were degraded within 2-4 h. Using (14)C-labled phenanthrene and benzo(a)pyrene, we demonstrated that the wax matrix of the candle initially adsorbs the PAH, but then releases the PAH back into solution as transformed, more water soluble products.	Water	265-270	phenylalanine hydroxylase	Homo sapiens	30-33
23089061-6	2012	Results showed most of the 16 PAHs tested were degraded within 2-4 h. Using (14)C-labled phenanthrene and benzo(a)pyrene, we demonstrated that the wax matrix of the candle initially adsorbs the PAH, but then releases the PAH back into solution as transformed, more water soluble products.	Water	265-270	phenylalanine hydroxylase	Homo sapiens	194-197
22869394-3	2012	The following PAH were found in bioavailable form: acenaphthylene, acenaphthene, fluorene, phenanthrene, anthracene, fluoranthene, pyrene, with C(free) varying between 2.38 and 62.35 ng/L.	acenaphthylene	51-65	phenylalanine hydroxylase	Homo sapiens	14-17
22869394-3	2012	The following PAH were found in bioavailable form: acenaphthylene, acenaphthene, fluorene, phenanthrene, anthracene, fluoranthene, pyrene, with C(free) varying between 2.38 and 62.35 ng/L.	acenaphthene	67-79	phenylalanine hydroxylase	Homo sapiens	14-17
22869394-3	2012	The following PAH were found in bioavailable form: acenaphthylene, acenaphthene, fluorene, phenanthrene, anthracene, fluoranthene, pyrene, with C(free) varying between 2.38 and 62.35 ng/L.	fluorene	81-89	phenylalanine hydroxylase	Homo sapiens	14-17
22869394-3	2012	The following PAH were found in bioavailable form: acenaphthylene, acenaphthene, fluorene, phenanthrene, anthracene, fluoranthene, pyrene, with C(free) varying between 2.38 and 62.35 ng/L.	phenanthrene	91-103	phenylalanine hydroxylase	Homo sapiens	14-17
22869394-3	2012	The following PAH were found in bioavailable form: acenaphthylene, acenaphthene, fluorene, phenanthrene, anthracene, fluoranthene, pyrene, with C(free) varying between 2.38 and 62.35 ng/L.	anthracene	105-115	phenylalanine hydroxylase	Homo sapiens	14-17
22869394-3	2012	The following PAH were found in bioavailable form: acenaphthylene, acenaphthene, fluorene, phenanthrene, anthracene, fluoranthene, pyrene, with C(free) varying between 2.38 and 62.35 ng/L.	fluoranthene	117-129	phenylalanine hydroxylase	Homo sapiens	14-17
22869394-3	2012	The following PAH were found in bioavailable form: acenaphthylene, acenaphthene, fluorene, phenanthrene, anthracene, fluoranthene, pyrene, with C(free) varying between 2.38 and 62.35 ng/L.	pyrene	131-137	phenylalanine hydroxylase	Homo sapiens	14-17
22527117-4	2012	Total PAH concentrations in indoor dust samples showed a better correlation to black carbon compared to total organic carbon contents.	Carbon	118-124	phenylalanine hydroxylase	Homo sapiens	6-9
22300847-2	2012	Activity of in vitro expressed mutant PAH may predict the patient"s phenotype and response to tetrahydrobiopterin (BH(4)), the cofactor of PAH.	sapropterin	94-113	phenylalanine hydroxylase	Homo sapiens	38-41
22838646-1	2012	A simple nanocarrier coated with chitosan and the pH-responsive charge-reversible polymer, PAH-Cit, was constructed using layer-by-layer assembly to deliver siRNA.	Polymers	82-89	phenylalanine hydroxylase	Homo sapiens	91-94
22838646-3	2012	Charge-reversible PAH-Cit and polyethylenimine (PEI) were sequentially deposited onto the surface of AuNP-CS through electrostatic interaction, forming a PEI/PAH-Cit/AuNP-CS shell/core structure.	Polyethyleneimine	30-46	phenylalanine hydroxylase	Homo sapiens	158-161
22838646-3	2012	Charge-reversible PAH-Cit and polyethylenimine (PEI) were sequentially deposited onto the surface of AuNP-CS through electrostatic interaction, forming a PEI/PAH-Cit/AuNP-CS shell/core structure.	Polyethyleneimine	48-51	phenylalanine hydroxylase	Homo sapiens	18-21
22838646-3	2012	Charge-reversible PAH-Cit and polyethylenimine (PEI) were sequentially deposited onto the surface of AuNP-CS through electrostatic interaction, forming a PEI/PAH-Cit/AuNP-CS shell/core structure.	Polyethyleneimine	48-51	phenylalanine hydroxylase	Homo sapiens	158-161
22838646-3	2012	Charge-reversible PAH-Cit and polyethylenimine (PEI) were sequentially deposited onto the surface of AuNP-CS through electrostatic interaction, forming a PEI/PAH-Cit/AuNP-CS shell/core structure.	aunp-cs	101-108	phenylalanine hydroxylase	Homo sapiens	18-21
22838646-3	2012	Charge-reversible PAH-Cit and polyethylenimine (PEI) were sequentially deposited onto the surface of AuNP-CS through electrostatic interaction, forming a PEI/PAH-Cit/AuNP-CS shell/core structure.	aunp-cs	101-108	phenylalanine hydroxylase	Homo sapiens	158-161
22838646-3	2012	Charge-reversible PAH-Cit and polyethylenimine (PEI) were sequentially deposited onto the surface of AuNP-CS through electrostatic interaction, forming a PEI/PAH-Cit/AuNP-CS shell/core structure.	Polyethyleneimine	154-157	phenylalanine hydroxylase	Homo sapiens	18-21
22838646-3	2012	Charge-reversible PAH-Cit and polyethylenimine (PEI) were sequentially deposited onto the surface of AuNP-CS through electrostatic interaction, forming a PEI/PAH-Cit/AuNP-CS shell/core structure.	Polyethyleneimine	154-157	phenylalanine hydroxylase	Homo sapiens	158-161
22838646-3	2012	Charge-reversible PAH-Cit and polyethylenimine (PEI) were sequentially deposited onto the surface of AuNP-CS through electrostatic interaction, forming a PEI/PAH-Cit/AuNP-CS shell/core structure.	aunp-cs	166-173	phenylalanine hydroxylase	Homo sapiens	18-21
22838646-3	2012	Charge-reversible PAH-Cit and polyethylenimine (PEI) were sequentially deposited onto the surface of AuNP-CS through electrostatic interaction, forming a PEI/PAH-Cit/AuNP-CS shell/core structure.	aunp-cs	166-173	phenylalanine hydroxylase	Homo sapiens	158-161
22838646-6	2012	An in vitro release profile demonstrated an efficient siRNA release (79%) from siRNA/PEI/PAH-Cit/AuNP-CS at pH 5.5, suggesting a pH-induced charge-reversing action of PAH-Cit.	aunp-cs	97-104	phenylalanine hydroxylase	Homo sapiens	89-92
22838646-6	2012	An in vitro release profile demonstrated an efficient siRNA release (79%) from siRNA/PEI/PAH-Cit/AuNP-CS at pH 5.5, suggesting a pH-induced charge-reversing action of PAH-Cit.	aunp-cs	97-104	phenylalanine hydroxylase	Homo sapiens	167-170
23716935-9	2012	All of the detected mutations in this study are related to CpG dinucleotides in the PAH gene sequence.	cytidylyl-3'-5'-guanosine	59-76	phenylalanine hydroxylase	Homo sapiens	84-87
22841515-0	2012	Utility of phenylalanine hydroxylase genotype for tetrahydrobiopterin responsiveness classification in patients with phenylketonuria.	sapropterin	50-69	phenylalanine hydroxylase	Homo sapiens	11-36
23478721-1	2012	The phenylalanine hydroxylase (PAH) in the liver hydroxylates phenylalanine from the diet.	Phenylalanine	4-17	phenylalanine hydroxylase	Homo sapiens	31-34
22027505-7	2012	Para-aminohippuric acid (PAH) significantly reduced the intracellular accumulation of AAI in rOAT1-transfected HEK293 cells.	p-Aminohippuric Acid	0-23	phenylalanine hydroxylase	Homo sapiens	25-28
22027505-7	2012	Para-aminohippuric acid (PAH) significantly reduced the intracellular accumulation of AAI in rOAT1-transfected HEK293 cells.	aai	86-89	phenylalanine hydroxylase	Homo sapiens	25-28
22373643-6	2012	(31)P-MRS-derived cerebral pH was first measured in rodents during chronic intoxication with 3-nitropropionic acid (3NP).	3-nitropropionic acid	93-114	phenylalanine hydroxylase	Homo sapiens	27-29
22373643-6	2012	(31)P-MRS-derived cerebral pH was first measured in rodents during chronic intoxication with 3-nitropropionic acid (3NP).	3-nitropropionic acid	116-119	phenylalanine hydroxylase	Homo sapiens	27-29
22373643-8	2012	Furthermore, pH changes correlated with the 3NP-induced inhibition of succinate dehydrogenase and preceded striatum lesions.	3-nitropropionic acid	44-47	phenylalanine hydroxylase	Homo sapiens	13-15
22373643-8	2012	Furthermore, pH changes correlated with the 3NP-induced inhibition of succinate dehydrogenase and preceded striatum lesions.	Succinic Acid	70-79	phenylalanine hydroxylase	Homo sapiens	13-15
22155355-0	2012	Simultaneous determination of nicotine and PAH metabolites in human hair specimen: a potential methodology to assess tobacco smoke contribution in PAH exposure.	Nicotine	30-38	phenylalanine hydroxylase	Homo sapiens	147-150
22409540-0	2012	gammaH2AX, pChk1, and Wip1 as potential markers of persistent DNA damage derived from dibenzo[a,l]pyrene and PAH-containing extracts from contaminated soils.	gammah2ax	0-9	phenylalanine hydroxylase	Homo sapiens	109-112
22409540-6	2012	Signaling in HepG2 cells exposed to soil PAH extracts corresponding to 1 muM benzo[a]pyrene was similar to that of 0.1 muM dibenzo[a,l]pyrene, a highly carcinogenic PAH known to produce persistent DNA damage.	Benzo(a)pyrene	77-91	phenylalanine hydroxylase	Homo sapiens	41-44
22409540-6	2012	Signaling in HepG2 cells exposed to soil PAH extracts corresponding to 1 muM benzo[a]pyrene was similar to that of 0.1 muM dibenzo[a,l]pyrene, a highly carcinogenic PAH known to produce persistent DNA damage.	dibenzo(a,l)pyrene	123-141	phenylalanine hydroxylase	Homo sapiens	165-168
22429107-0	2012	Reduction of PAH and soot precursors in benzene flames by addition of ethanol.	Benzene	40-47	phenylalanine hydroxylase	Homo sapiens	13-16
22429107-0	2012	Reduction of PAH and soot precursors in benzene flames by addition of ethanol.	Ethanol	70-77	phenylalanine hydroxylase	Homo sapiens	13-16
22429107-5	2012	The effects of oxygenate addition to the benzene base flame were seen to result in interesting differences, especially regarding trends to form PAH.	Benzene	41-48	phenylalanine hydroxylase	Homo sapiens	144-147
22429107-6	2012	The modeling results indicated that the concentration of acetylene and propargyl radicals, the main PAH precursors, as well as the PAH amounts were lower in the flame of the ethanol-benzene fuel mixture than in the pure benzene flame and that all of the formed PAHs were issued from the phenyl radical.	Ethanol	174-181	phenylalanine hydroxylase	Homo sapiens	100-103
22429107-6	2012	The modeling results indicated that the concentration of acetylene and propargyl radicals, the main PAH precursors, as well as the PAH amounts were lower in the flame of the ethanol-benzene fuel mixture than in the pure benzene flame and that all of the formed PAHs were issued from the phenyl radical.	Ethanol	174-181	phenylalanine hydroxylase	Homo sapiens	131-134
22429107-6	2012	The modeling results indicated that the concentration of acetylene and propargyl radicals, the main PAH precursors, as well as the PAH amounts were lower in the flame of the ethanol-benzene fuel mixture than in the pure benzene flame and that all of the formed PAHs were issued from the phenyl radical.	Benzene	182-189	phenylalanine hydroxylase	Homo sapiens	100-103
22429107-6	2012	The modeling results indicated that the concentration of acetylene and propargyl radicals, the main PAH precursors, as well as the PAH amounts were lower in the flame of the ethanol-benzene fuel mixture than in the pure benzene flame and that all of the formed PAHs were issued from the phenyl radical.	Benzene	182-189	phenylalanine hydroxylase	Homo sapiens	131-134
22429107-6	2012	The modeling results indicated that the concentration of acetylene and propargyl radicals, the main PAH precursors, as well as the PAH amounts were lower in the flame of the ethanol-benzene fuel mixture than in the pure benzene flame and that all of the formed PAHs were issued from the phenyl radical.	Polycyclic Aromatic Hydrocarbons	261-265	phenylalanine hydroxylase	Homo sapiens	131-134
22429107-6	2012	The modeling results indicated that the concentration of acetylene and propargyl radicals, the main PAH precursors, as well as the PAH amounts were lower in the flame of the ethanol-benzene fuel mixture than in the pure benzene flame and that all of the formed PAHs were issued from the phenyl radical.	acetophenone	287-301	phenylalanine hydroxylase	Homo sapiens	131-134
22429107-7	2012	Finally, the modeling results provided evidence that the PAH reduction was a result of simply replacing "sooting" benzene with "nonsooting" ethanol without influencing the combustion chemistry of the benzene.	Benzene	114-121	phenylalanine hydroxylase	Homo sapiens	57-60
22429107-7	2012	Finally, the modeling results provided evidence that the PAH reduction was a result of simply replacing "sooting" benzene with "nonsooting" ethanol without influencing the combustion chemistry of the benzene.	Ethanol	140-147	phenylalanine hydroxylase	Homo sapiens	57-60
22429107-7	2012	Finally, the modeling results provided evidence that the PAH reduction was a result of simply replacing "sooting" benzene with "nonsooting" ethanol without influencing the combustion chemistry of the benzene.	Benzene	200-207	phenylalanine hydroxylase	Homo sapiens	57-60
22300847-2	2012	Activity of in vitro expressed mutant PAH may predict the patient"s phenotype and response to tetrahydrobiopterin (BH(4)), the cofactor of PAH.	sapropterin	94-113	phenylalanine hydroxylase	Homo sapiens	139-142
22300847-3	2012	METHODS: A robust LC-ESI-MSMS PAH assay for the quantification of phenylalanine and tyrosine was developed.	Phenylalanine	66-79	phenylalanine hydroxylase	Homo sapiens	30-33
22300847-3	2012	METHODS: A robust LC-ESI-MSMS PAH assay for the quantification of phenylalanine and tyrosine was developed.	Tyrosine	84-92	phenylalanine hydroxylase	Homo sapiens	30-33
22300847-5	2012	RESULTS: The PAH assay was linear for phenylalanine and tyrosine (r(2)&gt;=0.99), with a detection limit of 105 nmol/L for Phe and 398 nmol/L for Tyr.	Phenylalanine	38-51	phenylalanine hydroxylase	Homo sapiens	13-16
22300847-5	2012	RESULTS: The PAH assay was linear for phenylalanine and tyrosine (r(2)&gt;=0.99), with a detection limit of 105 nmol/L for Phe and 398 nmol/L for Tyr.	Tyrosine	56-64	phenylalanine hydroxylase	Homo sapiens	13-16
22300847-5	2012	RESULTS: The PAH assay was linear for phenylalanine and tyrosine (r(2)&gt;=0.99), with a detection limit of 105 nmol/L for Phe and 398 nmol/L for Tyr.	r(2)&gt	66-73	phenylalanine hydroxylase	Homo sapiens	13-16
22300847-5	2012	RESULTS: The PAH assay was linear for phenylalanine and tyrosine (r(2)&gt;=0.99), with a detection limit of 105 nmol/L for Phe and 398 nmol/L for Tyr.	Phenylalanine	123-126	phenylalanine hydroxylase	Homo sapiens	13-16
22300847-5	2012	RESULTS: The PAH assay was linear for phenylalanine and tyrosine (r(2)&gt;=0.99), with a detection limit of 105 nmol/L for Phe and 398 nmol/L for Tyr.	Tyrosine	146-149	phenylalanine hydroxylase	Homo sapiens	13-16
22300847-8	2012	Compared to the wild-type enzyme, the highest PAH activity at standard conditions (1 mmol/L L-Phe; 200 mumol/L BH(4)) was found for the mutant p.Y417C (76%), followed by p.E390G (54%), p.R261Q (43%), p.I65T (33%), p.E280A (15%), p.R158Q (5%), and p.R408W (2%).	Phenylalanine	92-97	phenylalanine hydroxylase	Homo sapiens	46-49
22005392-1	2012	The liver enzyme phenylalanine hydroxylase is responsible for conversion of excess phenylalanine in the diet to tyrosine.	Tyrosine	112-120	phenylalanine hydroxylase	Homo sapiens	17-42
22005392-2	2012	Phenylalanine hydroxylase is activated by phenylalanine; this activation is inhibited by the physiological reducing substrate tetrahydrobiopterin.	Phenylalanine	42-55	phenylalanine hydroxylase	Homo sapiens	0-25
22005392-2	2012	Phenylalanine hydroxylase is activated by phenylalanine; this activation is inhibited by the physiological reducing substrate tetrahydrobiopterin.	sapropterin	126-145	phenylalanine hydroxylase	Homo sapiens	0-25
22178226-1	2012	Because of the relatively high human oral exposure to polycyclic aromatic hydrocarbons (PAHs) compared to the inhalation exposure, the known carcinogenicity of this type of compounds and the limited data from oral studies available with polycyclic aromatic hydrocarbons, an oral carcinogenicity study was performed using benzo[a]pyrene (B[a]P) as a PAH representative.	Polycyclic Aromatic Hydrocarbons	54-86	phenylalanine hydroxylase	Homo sapiens	88-91
22433455-7	2012	On univariate analysis, the baseline variables associated with a poor outcome were related to pulmonary arterial hypertension associated with connective tissue disease (CDT-PAH), New York Heart Association (NYHA) functional class, 6-min walk test and right atrial pressure.	1,5,9-cyclododecatriene	169-172	phenylalanine hydroxylase	Homo sapiens	173-176
22112818-1	2012	UNLABELLED: Sapropterin dihydrochloride, a synthetic tetrahydrobiopterin (BH4), works as a chaperone of phenylalanine hydroxylase (PAH) in phenylketonuria (PKU) to facilitate and stabilize folding of PAH into its most active conformation.	sapropterin	12-39	phenylalanine hydroxylase	Homo sapiens	104-129
22112818-1	2012	UNLABELLED: Sapropterin dihydrochloride, a synthetic tetrahydrobiopterin (BH4), works as a chaperone of phenylalanine hydroxylase (PAH) in phenylketonuria (PKU) to facilitate and stabilize folding of PAH into its most active conformation.	sapropterin	12-39	phenylalanine hydroxylase	Homo sapiens	131-134
22112818-1	2012	UNLABELLED: Sapropterin dihydrochloride, a synthetic tetrahydrobiopterin (BH4), works as a chaperone of phenylalanine hydroxylase (PAH) in phenylketonuria (PKU) to facilitate and stabilize folding of PAH into its most active conformation.	sapropterin	12-39	phenylalanine hydroxylase	Homo sapiens	200-203
22112818-1	2012	UNLABELLED: Sapropterin dihydrochloride, a synthetic tetrahydrobiopterin (BH4), works as a chaperone of phenylalanine hydroxylase (PAH) in phenylketonuria (PKU) to facilitate and stabilize folding of PAH into its most active conformation.	sapropterin	53-72	phenylalanine hydroxylase	Homo sapiens	104-129
22112818-1	2012	UNLABELLED: Sapropterin dihydrochloride, a synthetic tetrahydrobiopterin (BH4), works as a chaperone of phenylalanine hydroxylase (PAH) in phenylketonuria (PKU) to facilitate and stabilize folding of PAH into its most active conformation.	sapropterin	53-72	phenylalanine hydroxylase	Homo sapiens	131-134
22112818-1	2012	UNLABELLED: Sapropterin dihydrochloride, a synthetic tetrahydrobiopterin (BH4), works as a chaperone of phenylalanine hydroxylase (PAH) in phenylketonuria (PKU) to facilitate and stabilize folding of PAH into its most active conformation.	sapropterin	53-72	phenylalanine hydroxylase	Homo sapiens	200-203
22112818-1	2012	UNLABELLED: Sapropterin dihydrochloride, a synthetic tetrahydrobiopterin (BH4), works as a chaperone of phenylalanine hydroxylase (PAH) in phenylketonuria (PKU) to facilitate and stabilize folding of PAH into its most active conformation.	sapropterin	74-77	phenylalanine hydroxylase	Homo sapiens	104-129
22112818-1	2012	UNLABELLED: Sapropterin dihydrochloride, a synthetic tetrahydrobiopterin (BH4), works as a chaperone of phenylalanine hydroxylase (PAH) in phenylketonuria (PKU) to facilitate and stabilize folding of PAH into its most active conformation.	sapropterin	74-77	phenylalanine hydroxylase	Homo sapiens	131-134
22112818-1	2012	UNLABELLED: Sapropterin dihydrochloride, a synthetic tetrahydrobiopterin (BH4), works as a chaperone of phenylalanine hydroxylase (PAH) in phenylketonuria (PKU) to facilitate and stabilize folding of PAH into its most active conformation.	sapropterin	74-77	phenylalanine hydroxylase	Homo sapiens	200-203
22112818-9	2012	The p.R408W mutation, in which substitution of straight chain arginine with bulky aromatic amine, tryptophan, at the crux of a strategic hinge site activating folding of PAH, amino acid sequence 408, was strongly associated with non-response (21/29 patients non-responsive, 12/17 genotypes non-responsive).	Arginine	62-70	phenylalanine hydroxylase	Homo sapiens	170-173
22112818-9	2012	The p.R408W mutation, in which substitution of straight chain arginine with bulky aromatic amine, tryptophan, at the crux of a strategic hinge site activating folding of PAH, amino acid sequence 408, was strongly associated with non-response (21/29 patients non-responsive, 12/17 genotypes non-responsive).	aromatic amine	82-96	phenylalanine hydroxylase	Homo sapiens	170-173
22112818-9	2012	The p.R408W mutation, in which substitution of straight chain arginine with bulky aromatic amine, tryptophan, at the crux of a strategic hinge site activating folding of PAH, amino acid sequence 408, was strongly associated with non-response (21/29 patients non-responsive, 12/17 genotypes non-responsive).	Tryptophan	98-108	phenylalanine hydroxylase	Homo sapiens	170-173
22433455-8	2012	On multivariate analysis only CDT-PAH and NYHA functional class remained independently associated with poor survival.	1,5,9-cyclododecatriene	30-33	phenylalanine hydroxylase	Homo sapiens	34-37
22455670-13	2012	Comparisons of the concentrations of creatinine-corrected hydroxy-PAH to those reported in other studies indicate that exposure of public transport drivers to PAH could be similar.	Creatinine	37-47	phenylalanine hydroxylase	Homo sapiens	66-69
21839840-1	2011	Phenylalanine hydroxylase (PAH) is an important metabolic enzyme of aromatic amino acids, which is responsible for the irreversible oxidation of phenylalanine to tyrosine.	Amino Acids, Aromatic	68-88	phenylalanine hydroxylase	Homo sapiens	0-25
22371403-6	2012	The signal molecule cAMP regulates MITF, TYR, THI, GTP-cyclohydroxylase I (GTP-CHI) transcription and phenylalanine hydroxylase (PAH) phosphorylation at Ser16 by protein kinase A (PKA).	Cyclic AMP	20-24	phenylalanine hydroxylase	Homo sapiens	102-127
22455670-2	2012	In this study, we assessed the influence of traffic on levels of hydroxy polycyclic aromatic hydrocarbons (OH-PAHs) in commercial bus drivers in Trujillo, Peru, by measuring the within-shift changes in the urinary whole weight and creatinine-corrected concentrations of the PAH metabolites.	hydroxy polycyclic aromatic hydrocarbons	65-105	phenylalanine hydroxylase	Homo sapiens	110-113
21839840-1	2011	Phenylalanine hydroxylase (PAH) is an important metabolic enzyme of aromatic amino acids, which is responsible for the irreversible oxidation of phenylalanine to tyrosine.	Phenylalanine	145-158	phenylalanine hydroxylase	Homo sapiens	0-25
21839840-1	2011	Phenylalanine hydroxylase (PAH) is an important metabolic enzyme of aromatic amino acids, which is responsible for the irreversible oxidation of phenylalanine to tyrosine.	Tyrosine	162-170	phenylalanine hydroxylase	Homo sapiens	0-25
21839840-8	2011	These results indicated collectively that CfPAH, as a homologue of phenylalanine hydroxylase in scallop C. farreri, could be induced by cytokine and involved in the immunomodulation of scallops by supplying the starting material tyrosine for the synthesis of melanin and catecholamines.	Tyrosine	229-237	phenylalanine hydroxylase	Homo sapiens	67-92
21839840-8	2011	These results indicated collectively that CfPAH, as a homologue of phenylalanine hydroxylase in scallop C. farreri, could be induced by cytokine and involved in the immunomodulation of scallops by supplying the starting material tyrosine for the synthesis of melanin and catecholamines.	Melanins	259-266	phenylalanine hydroxylase	Homo sapiens	67-92
21839840-8	2011	These results indicated collectively that CfPAH, as a homologue of phenylalanine hydroxylase in scallop C. farreri, could be induced by cytokine and involved in the immunomodulation of scallops by supplying the starting material tyrosine for the synthesis of melanin and catecholamines.	Catecholamines	271-285	phenylalanine hydroxylase	Homo sapiens	67-92
22052564-0	2011	Core/shell Fe3O4 @SiO2 nanoparticles modified with PAH as a vector for EGFP plasmid DNA delivery into HeLa cells.	ferryl iron	11-16	phenylalanine hydroxylase	Homo sapiens	51-54
21889157-4	2011	The zeta potential of mica modified by the adsorption of cationic polyelectrolytes: PEI and PAH was also determined using the streaming potential measurements.	mica	22-26	phenylalanine hydroxylase	Homo sapiens	92-95
21889157-10	2011	It was also demonstrated that for higher ionic strengths, the maximum coverage of particle monolayers on PAH modified mica exceeded 0.39.	mica	118-122	phenylalanine hydroxylase	Homo sapiens	105-108
22052564-0	2011	Core/shell Fe3O4 @SiO2 nanoparticles modified with PAH as a vector for EGFP plasmid DNA delivery into HeLa cells.	Silicon Dioxide	18-22	phenylalanine hydroxylase	Homo sapiens	51-54
22052564-1	2011	Novel stable core/shell Fe(3)O(4)@SiO(2)/PAH nanoparticles are synthesized using 15 nm Fe(3)O(4) as the template that is modified with PAH.	fe(3)o(4)@	24-34	phenylalanine hydroxylase	Homo sapiens	135-138
22052564-1	2011	Novel stable core/shell Fe(3)O(4)@SiO(2)/PAH nanoparticles are synthesized using 15 nm Fe(3)O(4) as the template that is modified with PAH.	Silicon Dioxide	34-40	phenylalanine hydroxylase	Homo sapiens	135-138
22052564-1	2011	Novel stable core/shell Fe(3)O(4)@SiO(2)/PAH nanoparticles are synthesized using 15 nm Fe(3)O(4) as the template that is modified with PAH.	fe(3)o(4)	24-33	phenylalanine hydroxylase	Homo sapiens	41-44
22052564-1	2011	Novel stable core/shell Fe(3)O(4)@SiO(2)/PAH nanoparticles are synthesized using 15 nm Fe(3)O(4) as the template that is modified with PAH.	fe(3)o(4)	24-33	phenylalanine hydroxylase	Homo sapiens	135-138
22052564-3	2011	An electrophoretic assay suggests that the Fe(3)O(4)@SiO(2)/PAH nanoparticles protect the plasmid DNA from serum and DNase I degradation.	fe(3)o(4)@	43-53	phenylalanine hydroxylase	Homo sapiens	60-63
22052564-3	2011	An electrophoretic assay suggests that the Fe(3)O(4)@SiO(2)/PAH nanoparticles protect the plasmid DNA from serum and DNase I degradation.	Silicon Dioxide	53-59	phenylalanine hydroxylase	Homo sapiens	60-63
21820508-10	2011	Moreover, using confocal microscopy with the number and brightness technique, we studied the effect of BH4 addition directly in living human cells expressing wild-type PAH or p.A403V, a mild mutant associated with BH4 responsiveness in vivo.	sapropterin	103-106	phenylalanine hydroxylase	Homo sapiens	168-171
22616346-3	2011	Here we present a case of PCD with recurrent respiratory tract infections, bronchiectasis and severe PAH, who responded to treatment with Oxygen, IV broad spectrum antibiotics and oral sildenafil.	Oxygen	138-144	phenylalanine hydroxylase	Homo sapiens	101-104
22616346-3	2011	Here we present a case of PCD with recurrent respiratory tract infections, bronchiectasis and severe PAH, who responded to treatment with Oxygen, IV broad spectrum antibiotics and oral sildenafil.	Sildenafil Citrate	185-195	phenylalanine hydroxylase	Homo sapiens	101-104
21527427-5	2011	Experiments in eukaryotic cells revealed that the availability of the active PAH enzyme depends on the phenylalanine-to-BH(4) ratio.	Phenylalanine	103-116	phenylalanine hydroxylase	Homo sapiens	77-80
21764083-2	2011	The sediment PAH concentrations of thirty-nine 2-6 ring PAHs ranged from 13.5 to 22,600 ng/g.	Polycyclic Aromatic Hydrocarbons	56-60	phenylalanine hydroxylase	Homo sapiens	13-16
21764083-6	2011	Molecular indices based on ratios of selected PAH concentrations were used to differentiate PAHs from pyrogenic and petrogenic and mixed origins.	Polycyclic Aromatic Hydrocarbons	92-96	phenylalanine hydroxylase	Homo sapiens	46-49
21646032-1	2011	BACKGROUND: Phenylketonuria (PKU) results from impaired breakdown of phenylalanine (Phe) due to deficient phenylalanine hydroxylase (PAH) activity.	Phenylalanine	12-15	phenylalanine hydroxylase	Homo sapiens	133-136
21646032-2	2011	Sapropterin dihydrochloride (sapropterin, Kuvan ) is the only US- and EU-approved pharmaceutical version of naturally occurring 6R-BH(4), the cofactor required for PAH activity.	sapropterin	0-27	phenylalanine hydroxylase	Homo sapiens	164-167
21646032-2	2011	Sapropterin dihydrochloride (sapropterin, Kuvan ) is the only US- and EU-approved pharmaceutical version of naturally occurring 6R-BH(4), the cofactor required for PAH activity.	sapropterin	29-40	phenylalanine hydroxylase	Homo sapiens	164-167
21646032-2	2011	Sapropterin dihydrochloride (sapropterin, Kuvan ) is the only US- and EU-approved pharmaceutical version of naturally occurring 6R-BH(4), the cofactor required for PAH activity.	sapropterin	42-47	phenylalanine hydroxylase	Homo sapiens	164-167
21646032-2	2011	Sapropterin dihydrochloride (sapropterin, Kuvan ) is the only US- and EU-approved pharmaceutical version of naturally occurring 6R-BH(4), the cofactor required for PAH activity.	6r-bh	128-133	phenylalanine hydroxylase	Homo sapiens	164-167
21646032-3	2011	Sapropterin enhances residual PAH activity in sapropterin-responsive PKU patients and, in conjunction with dietary management, helps reduce blood Phe concentrations for optimal control.	sapropterin	0-11	phenylalanine hydroxylase	Homo sapiens	30-33
21524783-8	2011	Two PAH source indicators, including Ant/(Ant+Phe) and Fl/(Fl+Py), indicates that PAHs sources in the RI stream sediments are most likely of petroleum origin, while PAHs in the UR and AG stream sediments most likely came from combustion activities.	Polycyclic Aromatic Hydrocarbons	82-86	phenylalanine hydroxylase	Homo sapiens	4-7
22052564-4	2011	A cell viability assay shows that the Fe(3)O(4)@SiO(2)/PAH nanoparticles exhibit a low cytotoxicity toward endothelial cells.	fe(3)o(4)@	38-48	phenylalanine hydroxylase	Homo sapiens	55-58
22052564-4	2011	A cell viability assay shows that the Fe(3)O(4)@SiO(2)/PAH nanoparticles exhibit a low cytotoxicity toward endothelial cells.	Silicon Dioxide	48-54	phenylalanine hydroxylase	Homo sapiens	55-58
22052564-6	2011	Thus, Fe(3)O(4)@SiO(2)/PAH nanoparticles are biocompatible and suitable for nonviral delivery, and may find applications in cancer therapy.	fe(3)o(4)@	6-16	phenylalanine hydroxylase	Homo sapiens	23-26
22052564-6	2011	Thus, Fe(3)O(4)@SiO(2)/PAH nanoparticles are biocompatible and suitable for nonviral delivery, and may find applications in cancer therapy.	Silicon Dioxide	16-22	phenylalanine hydroxylase	Homo sapiens	23-26
21870859-7	2011	By depositing four bilayers [GOD/PAH](4) on the CdSe/ZnS electrode, a fast-responding sensor for the concentration range of 0.1-5 mM glucose can be prepared.	cdse	48-52	phenylalanine hydroxylase	Homo sapiens	33-39
21870859-7	2011	By depositing four bilayers [GOD/PAH](4) on the CdSe/ZnS electrode, a fast-responding sensor for the concentration range of 0.1-5 mM glucose can be prepared.	Zinc	53-56	phenylalanine hydroxylase	Homo sapiens	33-39
21870859-7	2011	By depositing four bilayers [GOD/PAH](4) on the CdSe/ZnS electrode, a fast-responding sensor for the concentration range of 0.1-5 mM glucose can be prepared.	Glucose	133-140	phenylalanine hydroxylase	Homo sapiens	33-39
21621181-7	2011	Results are discussed, obtained for cationic polyelectrolytes (PEI, PAH) and fibrinogen adsorbing on mica, interpreted quantitatively in terms of the theoretical approach postulating a heterogeneous 3D charge distribution.	mica	101-105	phenylalanine hydroxylase	Homo sapiens	68-71
22400275-1	2011	The silica-based multilayer films exhibiting both self-cleaning property and antireflection in the visible and near infrared regions have been deposited onto glass substrate by layer-by-layer deposition of PAH/PAA polyelectrolyte bilayers, followed by sequential deposition of PAH/SiO2 nanocomposite layers to create the nanoporous structure in the film, and finally treating with fluorosilane.	Silicon Dioxide	4-10	phenylalanine hydroxylase	Homo sapiens	206-209
22400275-1	2011	The silica-based multilayer films exhibiting both self-cleaning property and antireflection in the visible and near infrared regions have been deposited onto glass substrate by layer-by-layer deposition of PAH/PAA polyelectrolyte bilayers, followed by sequential deposition of PAH/SiO2 nanocomposite layers to create the nanoporous structure in the film, and finally treating with fluorosilane.	Silicon Dioxide	4-10	phenylalanine hydroxylase	Homo sapiens	277-280
22400275-3	2011	Scanning electron microscopy and atomic force microscopy analysis revealed that a highly nanoporous structure was obtained from the more deposition of loosely agglomerated SiO2 nanoparticles which increased with the increased cycle of PAH/SiO2 deposition.	Silicon Dioxide	172-176	phenylalanine hydroxylase	Homo sapiens	235-238
21761884-1	2011	In this work, two synthetic polyelectrolytes, PSS and PAH, are employed as strong adsorbed surfactants to disperse and stabilize neodymium oxide nanoparticles.	Polyelectrolytes	28-44	phenylalanine hydroxylase	Homo sapiens	54-57
21761884-1	2011	In this work, two synthetic polyelectrolytes, PSS and PAH, are employed as strong adsorbed surfactants to disperse and stabilize neodymium oxide nanoparticles.	neodymium oxide	129-144	phenylalanine hydroxylase	Homo sapiens	54-57
21785767-8	2011	The study of PAH distribution between the fine and coarse fraction at the urban site revealed that on average around 80% of total PAHs were associated with fine particles.	Polycyclic Aromatic Hydrocarbons	130-134	phenylalanine hydroxylase	Homo sapiens	13-16
21725549-1	2011	Monitoring of high-molecular weight polycyclic aromatic hydrocarbons (HMW-PAH) via simple and cost effective methods still remains a challenge.	Polycyclic Aromatic Hydrocarbons	36-68	phenylalanine hydroxylase	Homo sapiens	74-77
21834273-6	2011	RESULTS: We estimated that PAH exposure as measured by benzo[a]pyrene (BaP) can explain a significant part of the excess risk but not fully (Odd Ratio (OR)   3 as compared to an observed OR = 8 for smoky coal users versus smokeless coal users).	Benzo(a)pyrene	55-69	phenylalanine hydroxylase	Homo sapiens	27-30
21659675-3	2011	The mutation causes a variable [corrected] dysfunction in PAH, that metabolizes phenylalanine (Phe) to tyrosine (Tyr) with the cofactor tetrahydrobiopterin (BH4).	Phenylalanine	80-93	phenylalanine hydroxylase	Homo sapiens	58-61
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	ammonium ferrous sulfate	39-47	phenylalanine hydroxylase	Homo sapiens	0-25
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	ammonium ferrous sulfate	39-47	phenylalanine hydroxylase	Homo sapiens	27-31
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	aromatic amino acid l-phenylalanine	101-136	phenylalanine hydroxylase	Homo sapiens	0-25
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	aromatic amino acid l-phenylalanine	101-136	phenylalanine hydroxylase	Homo sapiens	27-31
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	Phenylalanine	138-143	phenylalanine hydroxylase	Homo sapiens	0-25
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	Phenylalanine	138-143	phenylalanine hydroxylase	Homo sapiens	27-31
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	Tyrosine	148-158	phenylalanine hydroxylase	Homo sapiens	0-25
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	Tyrosine	148-158	phenylalanine hydroxylase	Homo sapiens	27-31
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	Tyrosine	160-165	phenylalanine hydroxylase	Homo sapiens	0-25
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	Tyrosine	160-165	phenylalanine hydroxylase	Homo sapiens	27-31
21568264-4	2011	Through addition of an eight-hour colon compartment to PBET and use of a carbohydrate-rich fed-state medium we demonstrated that colon-extended PBET (CE-PBET) increased assessments of soil-bound PAH bioaccessibility by up to 50% in laboratory soils and a factor of 4 in field soils.	Carbohydrates	73-85	phenylalanine hydroxylase	Homo sapiens	195-198
21568264-5	2011	We attribute this increased bioaccessibility to a combination of the additional extraction time and the presence of carbohydrates in the colon compartment, both of which favor PAH desorption from soil.	Carbohydrates	116-129	phenylalanine hydroxylase	Homo sapiens	176-179
21487017-9	2011	This has similarities to the disease phenylketonuria, which arises from mutation in the enzyme phenylalanine hydroxylase or from a decrease in the supply of its cofactor tetrahydrobiopterin (BH4).	sapropterin	170-189	phenylalanine hydroxylase	Homo sapiens	95-120
21632310-5	2011	Benzo[b]fluoranthene, dibenz[a,h]anthracene, benzo[a]pyrene, and dibenzo[a,l]pyrene were the most carcinogenic PAH species evaluated.	benzo(b)fluoranthene	0-20	phenylalanine hydroxylase	Homo sapiens	111-114
21632310-5	2011	Benzo[b]fluoranthene, dibenz[a,h]anthracene, benzo[a]pyrene, and dibenzo[a,l]pyrene were the most carcinogenic PAH species evaluated.	1,2,5,6-dibenzanthracene	22-43	phenylalanine hydroxylase	Homo sapiens	111-114
21632310-5	2011	Benzo[b]fluoranthene, dibenz[a,h]anthracene, benzo[a]pyrene, and dibenzo[a,l]pyrene were the most carcinogenic PAH species evaluated.	Benzo(a)pyrene	45-59	phenylalanine hydroxylase	Homo sapiens	111-114
21632310-5	2011	Benzo[b]fluoranthene, dibenz[a,h]anthracene, benzo[a]pyrene, and dibenzo[a,l]pyrene were the most carcinogenic PAH species evaluated.	dibenzo(a,l)pyrene	65-83	phenylalanine hydroxylase	Homo sapiens	111-114
21659675-3	2011	The mutation causes a variable [corrected] dysfunction in PAH, that metabolizes phenylalanine (Phe) to tyrosine (Tyr) with the cofactor tetrahydrobiopterin (BH4).	Phenylalanine	95-98	phenylalanine hydroxylase	Homo sapiens	58-61
21659675-3	2011	The mutation causes a variable [corrected] dysfunction in PAH, that metabolizes phenylalanine (Phe) to tyrosine (Tyr) with the cofactor tetrahydrobiopterin (BH4).	Tyrosine	103-111	phenylalanine hydroxylase	Homo sapiens	58-61
21659675-3	2011	The mutation causes a variable [corrected] dysfunction in PAH, that metabolizes phenylalanine (Phe) to tyrosine (Tyr) with the cofactor tetrahydrobiopterin (BH4).	Tyrosine	113-116	phenylalanine hydroxylase	Homo sapiens	58-61
21659675-3	2011	The mutation causes a variable [corrected] dysfunction in PAH, that metabolizes phenylalanine (Phe) to tyrosine (Tyr) with the cofactor tetrahydrobiopterin (BH4).	sapropterin	136-155	phenylalanine hydroxylase	Homo sapiens	58-61
21659675-3	2011	The mutation causes a variable [corrected] dysfunction in PAH, that metabolizes phenylalanine (Phe) to tyrosine (Tyr) with the cofactor tetrahydrobiopterin (BH4).	sapropterin	157-160	phenylalanine hydroxylase	Homo sapiens	58-61
20961044-7	2011	In comparison with common major metabolites, PAH transformations produced various types of potentially toxic intermediates, including epoxide, quinone, phenols, aldehydes, and phthalates.	Epoxy Compounds	134-141	phenylalanine hydroxylase	Homo sapiens	45-48
21431140-4	2011	These photochemical products most likely form, after hydrogen bonding between C(24)H(12) and H(2)O, through ionization of the PAH and subsequent reactivity with water upon irradiation.	Hydrogen	53-61	phenylalanine hydroxylase	Homo sapiens	126-129
21431140-4	2011	These photochemical products most likely form, after hydrogen bonding between C(24)H(12) and H(2)O, through ionization of the PAH and subsequent reactivity with water upon irradiation.	Carbon	78-79	phenylalanine hydroxylase	Homo sapiens	126-129
21431140-4	2011	These photochemical products most likely form, after hydrogen bonding between C(24)H(12) and H(2)O, through ionization of the PAH and subsequent reactivity with water upon irradiation.	Water	93-98	phenylalanine hydroxylase	Homo sapiens	126-129
21431140-4	2011	These photochemical products most likely form, after hydrogen bonding between C(24)H(12) and H(2)O, through ionization of the PAH and subsequent reactivity with water upon irradiation.	Water	161-166	phenylalanine hydroxylase	Homo sapiens	126-129
22007406-1	2011	Abstract In the present paper, a technique of laser-induced fluorescence(LIF)for direct assay of polycyclic aromatic hydrocarbons(PAH) in soil was put forward.	Polycyclic Aromatic Hydrocarbons	97-129	phenylalanine hydroxylase	Homo sapiens	130-133
20961044-7	2011	In comparison with common major metabolites, PAH transformations produced various types of potentially toxic intermediates, including epoxide, quinone, phenols, aldehydes, and phthalates.	quinone	143-150	phenylalanine hydroxylase	Homo sapiens	45-48
20961044-7	2011	In comparison with common major metabolites, PAH transformations produced various types of potentially toxic intermediates, including epoxide, quinone, phenols, aldehydes, and phthalates.	Phenols	152-159	phenylalanine hydroxylase	Homo sapiens	45-48
20961044-7	2011	In comparison with common major metabolites, PAH transformations produced various types of potentially toxic intermediates, including epoxide, quinone, phenols, aldehydes, and phthalates.	Aldehydes	161-170	phenylalanine hydroxylase	Homo sapiens	45-48
20961044-7	2011	In comparison with common major metabolites, PAH transformations produced various types of potentially toxic intermediates, including epoxide, quinone, phenols, aldehydes, and phthalates.	phthalic acid	176-186	phenylalanine hydroxylase	Homo sapiens	45-48
20680698-0	2011	PAH desorption from sediments with different contents of organic carbon from wastewater receiving rivers.	Carbon	65-71	phenylalanine hydroxylase	Homo sapiens	0-3
21216643-1	2011	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase gene (PAH) with consequent elevation of blood phenylalanine (Phe), reduction in tyrosine (Tyr) and elevation of Phe/Tyr ratio (P/T).	Phenylalanine	52-65	phenylalanine hydroxylase	Homo sapiens	84-87
21216643-1	2011	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase gene (PAH) with consequent elevation of blood phenylalanine (Phe), reduction in tyrosine (Tyr) and elevation of Phe/Tyr ratio (P/T).	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	52-77
21216643-1	2011	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase gene (PAH) with consequent elevation of blood phenylalanine (Phe), reduction in tyrosine (Tyr) and elevation of Phe/Tyr ratio (P/T).	Phenylalanine	0-3	phenylalanine hydroxylase	Homo sapiens	84-87
21216643-1	2011	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase gene (PAH) with consequent elevation of blood phenylalanine (Phe), reduction in tyrosine (Tyr) and elevation of Phe/Tyr ratio (P/T).	Tyrosine	158-166	phenylalanine hydroxylase	Homo sapiens	52-77
21216643-1	2011	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase gene (PAH) with consequent elevation of blood phenylalanine (Phe), reduction in tyrosine (Tyr) and elevation of Phe/Tyr ratio (P/T).	Tyrosine	158-166	phenylalanine hydroxylase	Homo sapiens	84-87
21216643-1	2011	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase gene (PAH) with consequent elevation of blood phenylalanine (Phe), reduction in tyrosine (Tyr) and elevation of Phe/Tyr ratio (P/T).	Tyrosine	168-171	phenylalanine hydroxylase	Homo sapiens	52-77
21216643-1	2011	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase gene (PAH) with consequent elevation of blood phenylalanine (Phe), reduction in tyrosine (Tyr) and elevation of Phe/Tyr ratio (P/T).	Tyrosine	168-171	phenylalanine hydroxylase	Homo sapiens	84-87
21216643-1	2011	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase gene (PAH) with consequent elevation of blood phenylalanine (Phe), reduction in tyrosine (Tyr) and elevation of Phe/Tyr ratio (P/T).	Phenylalanine	139-142	phenylalanine hydroxylase	Homo sapiens	52-77
21216643-1	2011	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase gene (PAH) with consequent elevation of blood phenylalanine (Phe), reduction in tyrosine (Tyr) and elevation of Phe/Tyr ratio (P/T).	Phenylalanine	139-142	phenylalanine hydroxylase	Homo sapiens	84-87
21216643-1	2011	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase gene (PAH) with consequent elevation of blood phenylalanine (Phe), reduction in tyrosine (Tyr) and elevation of Phe/Tyr ratio (P/T).	Tyrosine	194-197	phenylalanine hydroxylase	Homo sapiens	52-77
21216643-1	2011	Phenylketonuria (PKU) is caused by mutations in the phenylalanine hydroxylase gene (PAH) with consequent elevation of blood phenylalanine (Phe), reduction in tyrosine (Tyr) and elevation of Phe/Tyr ratio (P/T).	Tyrosine	194-197	phenylalanine hydroxylase	Homo sapiens	84-87
21351297-3	2011	A model for this structure was obtained in a previous study of water-ligand dissociation from the hexacoordinate model complex of the X-ray crystal structure of the catalytic domain of phenylalanine hydroxylase in complex with the cofactor (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) (PAH-Fe(II)-BH(4)).	pah-fe(ii)-bh	292-305	phenylalanine hydroxylase	Homo sapiens	185-210
21351297-3	2011	A model for this structure was obtained in a previous study of water-ligand dissociation from the hexacoordinate model complex of the X-ray crystal structure of the catalytic domain of phenylalanine hydroxylase in complex with the cofactor (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) (PAH-Fe(II)-BH(4)).	Water	63-68	phenylalanine hydroxylase	Homo sapiens	185-210
21351297-3	2011	A model for this structure was obtained in a previous study of water-ligand dissociation from the hexacoordinate model complex of the X-ray crystal structure of the catalytic domain of phenylalanine hydroxylase in complex with the cofactor (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)) (PAH-Fe(II)-BH(4)).	-l-erythro-5,6,7,8-tetrahydrobiopterin	244-282	phenylalanine hydroxylase	Homo sapiens	185-210
21216057-2	2011	A novel passive air sampler was designed and tested for measuring the vertical concentration profile of 4 low molecular weight PAHs in gaseous phase (PAH(LMW4)) in near soil surface air.	Polycyclic Aromatic Hydrocarbons	127-131	phenylalanine hydroxylase	Homo sapiens	150-158
21111795-7	2011	Another structural N-PAH variant, 1,7-phenanthroline, downregulated ATRA-mediated response at most of tested ATRA concentrations and exposure times.	1,7-phenanthroline	34-52	phenylalanine hydroxylase	Homo sapiens	21-24
21111795-7	2011	Another structural N-PAH variant, 1,7-phenanthroline, downregulated ATRA-mediated response at most of tested ATRA concentrations and exposure times.	Tretinoin	68-72	phenylalanine hydroxylase	Homo sapiens	21-24
21111795-8	2011	Interesting concentration-dependent biphasic effects (i.e. downregulation with subsequent up-regulation to control levels) were observed at co-exposures of ATRA and parent PAH phenanthrene.	phenanthrene	176-188	phenylalanine hydroxylase	Homo sapiens	172-175
20300832-2	2011	The PAH mixture in the soils is mainly of low molecular weight compounds, with naphthalene (21.4%) and phenanthrene (21.8%) being dominant.	naphthalene	79-90	phenylalanine hydroxylase	Homo sapiens	4-7
20300832-2	2011	The PAH mixture in the soils is mainly of low molecular weight compounds, with naphthalene (21.4%) and phenanthrene (21.8%) being dominant.	phenanthrene	103-115	phenylalanine hydroxylase	Homo sapiens	4-7
20937381-0	2011	Phenylketonuria as a protein misfolding disease: The mutation pG46S in phenylalanine hydroxylase promotes self-association and fibril formation.	pg46s	62-67	phenylalanine hydroxylase	Homo sapiens	71-96
21147011-0	2011	Molecular genetics and impact of residual in vitro phenylalanine hydroxylase activity on tetrahydrobiopterin responsiveness in Turkish PKU population.	sapropterin	89-108	phenylalanine hydroxylase	Homo sapiens	51-76
20937381-1	2011	The missense mutation pG46S in the regulatory (R) domain of human phenylalanine hydroxylase (hPAH), associated with a severe form of phenylketonuria, generates a misfolded protein which is rapidly degraded on expression in HEK293 cells.	pg46s	22-27	phenylalanine hydroxylase	Homo sapiens	66-91
21714627-8	2011	Urinary 2-naphthol levels correlated with the levels of PAH species, including pyrene, benzo[k]fluoranthene, benezo[g,h,i]pyrene, naphthalene, phenanthrene, anthracene, indeno[1,2,3-cd]pyrene, benzo[k]fluoranthene, and total PAHs.	2-naphthol	8-18	phenylalanine hydroxylase	Homo sapiens	56-59
20971365-7	2010	Tetrahydrobiopterin stimulates phenylalanine hydroxylase activity in about 20% of patients, and in those patients serves as a useful adjunct to the phenylalanine-restricted diet because it increases phenylalanine tolerance and allows some dietary freedom.	sapropterin	0-19	phenylalanine hydroxylase	Homo sapiens	31-56
21871828-5	2011	The natural cofactor of human PAH, (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)), has already been approved for oral treatment of HPA, giving a positive response in mild forms of the disease showing considerable residual enzymatic activity.	sapropterin	35-77	phenylalanine hydroxylase	Homo sapiens	30-33
20832169-5	2010	The removal efficiencies gradually improved during the SS-SBR operation, achieving at the end of the study rather constant removal rates above 80% for both 3-rings PAHs (fluorene and anthracene) and 4-ring PAHs (pyrene and crysene) for an inlet total PAH concentration of 70 mg/kg as dry weight (dw).	fluorene	170-178	phenylalanine hydroxylase	Homo sapiens	164-167
20843538-2	2010	Total PAH ( (28)PAH) concentrations in the dichloromethane-soluble fraction ("binder"), comprising 5-10% of pavement mass, were as high as 200,000 mgkg(-1) (10,000 mgkg(-1) in binder+aggregate).	Methylene Chloride	43-58	phenylalanine hydroxylase	Homo sapiens	6-9
20973527-0	2010	Ozone oxidation of surface-adsorbed polycyclic aromatic hydrocarbons: role of PAH-surface interaction.	Ozone	0-5	phenylalanine hydroxylase	Homo sapiens	78-81
20973527-0	2010	Ozone oxidation of surface-adsorbed polycyclic aromatic hydrocarbons: role of PAH-surface interaction.	Polycyclic Aromatic Hydrocarbons	36-68	phenylalanine hydroxylase	Homo sapiens	78-81
20973527-3	2010	We examine the effects of the PAH-substrate interaction on the oxidation of surface-adsorbed anthracene, pyrene, and benzo[a]pyrene by ozone (O(3)) using density functional theory.	anthracene	93-103	phenylalanine hydroxylase	Homo sapiens	30-33
20973527-3	2010	We examine the effects of the PAH-substrate interaction on the oxidation of surface-adsorbed anthracene, pyrene, and benzo[a]pyrene by ozone (O(3)) using density functional theory.	pyrene	105-111	phenylalanine hydroxylase	Homo sapiens	30-33
20973527-3	2010	We examine the effects of the PAH-substrate interaction on the oxidation of surface-adsorbed anthracene, pyrene, and benzo[a]pyrene by ozone (O(3)) using density functional theory.	Benzo(a)pyrene	117-131	phenylalanine hydroxylase	Homo sapiens	30-33
21620420-4	2011	Both EL-FAME and DGGE demonstrated a marked shift in microbial community, in all the PAH level treatments, afterwards, with increases in the number of fatty acid degraders, the relative abundance of fatty acid biomarkers for gram-negative bacteria and a decrease in species diversity.	Fatty Acids	151-161	phenylalanine hydroxylase	Homo sapiens	85-88
21620420-4	2011	Both EL-FAME and DGGE demonstrated a marked shift in microbial community, in all the PAH level treatments, afterwards, with increases in the number of fatty acid degraders, the relative abundance of fatty acid biomarkers for gram-negative bacteria and a decrease in species diversity.	Fatty Acids	199-209	phenylalanine hydroxylase	Homo sapiens	85-88
21112613-3	2010	Other PAH sources considered included several coal- and vehicle-related sources, wood combustion, and fuel-oil combustion.	Oils	107-110	phenylalanine hydroxylase	Homo sapiens	6-9
20217238-1	2010	Treatment with tetrahydrobiopterin (BH4), the natural cofactor of phenylalanine hydroxylase (PAH), can reduce blood phenylalanine (Phe) levels in patients with BH4-responsive phenylketonuria (PKU).	sapropterin	15-34	phenylalanine hydroxylase	Homo sapiens	66-91
20217238-1	2010	Treatment with tetrahydrobiopterin (BH4), the natural cofactor of phenylalanine hydroxylase (PAH), can reduce blood phenylalanine (Phe) levels in patients with BH4-responsive phenylketonuria (PKU).	sapropterin	36-39	phenylalanine hydroxylase	Homo sapiens	66-91
20217238-1	2010	Treatment with tetrahydrobiopterin (BH4), the natural cofactor of phenylalanine hydroxylase (PAH), can reduce blood phenylalanine (Phe) levels in patients with BH4-responsive phenylketonuria (PKU).	Phenylalanine	131-134	phenylalanine hydroxylase	Homo sapiens	66-91
20480196-1	2010	Phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of L-Phe to L-Tyr.	Phenylalanine	63-68	phenylalanine hydroxylase	Homo sapiens	0-25
20480196-1	2010	Phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of L-Phe to L-Tyr.	Phenylalanine	63-68	phenylalanine hydroxylase	Homo sapiens	27-30
20480196-1	2010	Phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of L-Phe to L-Tyr.	Tyrosine	72-77	phenylalanine hydroxylase	Homo sapiens	0-25
20480196-1	2010	Phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of L-Phe to L-Tyr.	Tyrosine	72-77	phenylalanine hydroxylase	Homo sapiens	27-30
20480196-2	2010	Dysfunctional PAH results in phenylketonuria and mammalian PAH is therefore highly regulated and displays positive cooperativity for L-Phe (Hill coefficient (h)=2).	Phenylalanine	133-138	phenylalanine hydroxylase	Homo sapiens	14-17
20480196-2	2010	Dysfunctional PAH results in phenylketonuria and mammalian PAH is therefore highly regulated and displays positive cooperativity for L-Phe (Hill coefficient (h)=2).	Phenylalanine	133-138	phenylalanine hydroxylase	Homo sapiens	59-62
20480196-3	2010	L-Phe does not bind to the regulatory ACT domain in full-length tetrameric human PAH and cooperativity is elicited by homotropic binding to the catalytic site (Thorolfsson et al.	Phenylalanine	0-5	phenylalanine hydroxylase	Homo sapiens	81-84
20480196-5	2010	PAH from Caenorhabditis elegans (cePAH) is devoid of cooperativity for L-Phe (h=0.9), and, as shown in this work, structural analysis reveal an additional L-Phe binding site at the regulatory domain of full-length cePAH.	Phenylalanine	71-76	phenylalanine hydroxylase	Homo sapiens	0-3
20480196-5	2010	PAH from Caenorhabditis elegans (cePAH) is devoid of cooperativity for L-Phe (h=0.9), and, as shown in this work, structural analysis reveal an additional L-Phe binding site at the regulatory domain of full-length cePAH.	Phenylalanine	155-160	phenylalanine hydroxylase	Homo sapiens	0-3
20480196-11	2010	Our results support that the acquisition of positive cooperativity in mammalian forms of PAH is accompanied by a closure of the regulatory L: -Phe binding site.	Phenylalanine	143-146	phenylalanine hydroxylase	Homo sapiens	89-92
21553452-1	2010	INTRODUCTION: Phenylketonuria is a genetic disorder of metabolism of amino acid phenylalanine, which results in the absence of phenylalanine hydroxylase, an enzyme that catalyzes the conversion of phenylalanine into tyrosine.	amino acid phenylalanine	69-93	phenylalanine hydroxylase	Homo sapiens	127-152
21553452-1	2010	INTRODUCTION: Phenylketonuria is a genetic disorder of metabolism of amino acid phenylalanine, which results in the absence of phenylalanine hydroxylase, an enzyme that catalyzes the conversion of phenylalanine into tyrosine.	Phenylalanine	80-93	phenylalanine hydroxylase	Homo sapiens	127-152
21553452-1	2010	INTRODUCTION: Phenylketonuria is a genetic disorder of metabolism of amino acid phenylalanine, which results in the absence of phenylalanine hydroxylase, an enzyme that catalyzes the conversion of phenylalanine into tyrosine.	Tyrosine	216-224	phenylalanine hydroxylase	Homo sapiens	127-152
19937396-4	2010	In this study, we investigated the effect of different polyol compounds, e.g. glycerol, mannitol and PEG-6000 on the in vitro stability of purified hPAH produced in a heterologous prokaryotic expression system.	Glycerol	78-86	phenylalanine hydroxylase	Homo sapiens	148-152
20667834-2	2010	PAH is complexly regulated by its substrate L-Phenylalanine and its natural cofactor 6R-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)).	Phenylalanine	44-59	phenylalanine hydroxylase	Homo sapiens	0-3
20667834-2	2010	PAH is complexly regulated by its substrate L-Phenylalanine and its natural cofactor 6R-L-erythro-5,6,7,8-tetrahydrobiopterin (BH(4)).	sapropterin	85-125	phenylalanine hydroxylase	Homo sapiens	0-3
20667834-6	2010	Current standard PAH activity assays are either indirect (NADH) or discontinuous due to substrate and product separation before detection.	NAD	58-62	phenylalanine hydroxylase	Homo sapiens	17-20
19937396-4	2010	In this study, we investigated the effect of different polyol compounds, e.g. glycerol, mannitol and PEG-6000 on the in vitro stability of purified hPAH produced in a heterologous prokaryotic expression system.	Mannitol	88-96	phenylalanine hydroxylase	Homo sapiens	148-152
19937396-4	2010	In this study, we investigated the effect of different polyol compounds, e.g. glycerol, mannitol and PEG-6000 on the in vitro stability of purified hPAH produced in a heterologous prokaryotic expression system.	Polyethylene Glycol 6000	101-109	phenylalanine hydroxylase	Homo sapiens	148-152
22475869-1	2010	Phenylketonuria (PKU) is caused by deficient activity of the enzyme phenylalanine hydroxylase, needed to convert the essential amino acid (AA) phenylalanine (phe) to tyrosine.	essential amino acid (aa) phenylalanine	117-156	phenylalanine hydroxylase	Homo sapiens	68-93
20630638-0	2010	Spatial uncoupling of biodegradation, soil respiration, and PAH concentration in a creosote contaminated soil.	Creosote	83-91	phenylalanine hydroxylase	Homo sapiens	60-63
20720592-2	2010	Owing to mutations in the gene encoding the enzyme phenylalanine hydroxylase, the essential amino acid phenylalanine cannot be hydroxylated to tyrosine and blood and tissue concentrations of phenylalanine increase.	essential amino acid phenylalanine	82-116	phenylalanine hydroxylase	Homo sapiens	51-76
20720592-2	2010	Owing to mutations in the gene encoding the enzyme phenylalanine hydroxylase, the essential amino acid phenylalanine cannot be hydroxylated to tyrosine and blood and tissue concentrations of phenylalanine increase.	Tyrosine	143-151	phenylalanine hydroxylase	Homo sapiens	51-76
20714359-2	2010	PKU is caused by an inherited deficiency of the enzyme phenylalanine hydroxylase (PAH), and the pathophysiology of the disorder is related to chronic accumulation of the free amino acid phenylalanine in tissues.	Phenylalanine	55-68	phenylalanine hydroxylase	Homo sapiens	82-85
20714359-5	2010	Sapropterin dihydrochloride is a synthetic version of tetrahydrobiopterin, the naturally occurring pterin cofactor that is required for PAH-mediated phenylalanine hydroxylation.	sapropterin	0-27	phenylalanine hydroxylase	Homo sapiens	136-139
20714359-5	2010	Sapropterin dihydrochloride is a synthetic version of tetrahydrobiopterin, the naturally occurring pterin cofactor that is required for PAH-mediated phenylalanine hydroxylation.	sapropterin	54-73	phenylalanine hydroxylase	Homo sapiens	136-139
20714359-5	2010	Sapropterin dihydrochloride is a synthetic version of tetrahydrobiopterin, the naturally occurring pterin cofactor that is required for PAH-mediated phenylalanine hydroxylation.	Pterins	5-11	phenylalanine hydroxylase	Homo sapiens	136-139
20714359-5	2010	Sapropterin dihydrochloride is a synthetic version of tetrahydrobiopterin, the naturally occurring pterin cofactor that is required for PAH-mediated phenylalanine hydroxylation.	Phenylalanine	149-162	phenylalanine hydroxylase	Homo sapiens	136-139
20492352-1	2010	Phenylalanine hydroxylase (PAH), tyrosine hydroxylase (TH) and the tryptophan hydroxylases (TPH1 and TPH2) are structurally and functionally related enzymes that share a number of ligands, such as amino acid substrates, pterin cofactors and inhibitors.	Pterins	220-226	phenylalanine hydroxylase	Homo sapiens	0-25
20492352-1	2010	Phenylalanine hydroxylase (PAH), tyrosine hydroxylase (TH) and the tryptophan hydroxylases (TPH1 and TPH2) are structurally and functionally related enzymes that share a number of ligands, such as amino acid substrates, pterin cofactors and inhibitors.	Pterins	220-226	phenylalanine hydroxylase	Homo sapiens	27-30
30780801-2	2010	It is essential for the conversion of phenylalanine (Phe) by phenylalanine-4-hydroxylase (PAH) to tyrosine.	Phenylalanine	38-51	phenylalanine hydroxylase	Homo sapiens	61-88
30780801-2	2010	It is essential for the conversion of phenylalanine (Phe) by phenylalanine-4-hydroxylase (PAH) to tyrosine.	Phenylalanine	53-56	phenylalanine hydroxylase	Homo sapiens	61-88
30780801-2	2010	It is essential for the conversion of phenylalanine (Phe) by phenylalanine-4-hydroxylase (PAH) to tyrosine.	Tyrosine	98-106	phenylalanine hydroxylase	Homo sapiens	61-88
22475869-1	2010	Phenylketonuria (PKU) is caused by deficient activity of the enzyme phenylalanine hydroxylase, needed to convert the essential amino acid (AA) phenylalanine (phe) to tyrosine.	Tyrosine	166-174	phenylalanine hydroxylase	Homo sapiens	68-93
23056707-1	2010	OBJECTIVE: Phenylalanine hydroxylase or its cofactor, tetrahydrobiopterin (BH(4)), deficiency causes accumulation of phenylalanine in body fluids and central nervous system.	sapropterin	54-73	phenylalanine hydroxylase	Homo sapiens	11-36
23056707-1	2010	OBJECTIVE: Phenylalanine hydroxylase or its cofactor, tetrahydrobiopterin (BH(4)), deficiency causes accumulation of phenylalanine in body fluids and central nervous system.	Phenylalanine	117-130	phenylalanine hydroxylase	Homo sapiens	11-36