PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
23935841-10	2013	RESULTS: In hMCT4-expressing oocytes, treatment with phenylglyoxal (PGO), a compound specific for arginine residues, completely abolished the transport activity of hMCT4, although this abolishment was prevented by the presence of L-lactate.	Phenylglyoxal	53-66	solute carrier family 16 member 3	Homo sapiens	12-17
23935841-10	2013	RESULTS: In hMCT4-expressing oocytes, treatment with phenylglyoxal (PGO), a compound specific for arginine residues, completely abolished the transport activity of hMCT4, although this abolishment was prevented by the presence of L-lactate.	Phenylglyoxal	53-66	solute carrier family 16 member 3	Homo sapiens	164-169
23935841-10	2013	RESULTS: In hMCT4-expressing oocytes, treatment with phenylglyoxal (PGO), a compound specific for arginine residues, completely abolished the transport activity of hMCT4, although this abolishment was prevented by the presence of L-lactate.	Phenylglyoxal	68-71	solute carrier family 16 member 3	Homo sapiens	12-17
23935841-10	2013	RESULTS: In hMCT4-expressing oocytes, treatment with phenylglyoxal (PGO), a compound specific for arginine residues, completely abolished the transport activity of hMCT4, although this abolishment was prevented by the presence of L-lactate.	Phenylglyoxal	68-71	solute carrier family 16 member 3	Homo sapiens	164-169
17042490-5	2006	The chelators also protected the SOD activity against inhibition by the arginine-specific reagent, phenylglyoxal.	Phenylglyoxal	99-112	superoxide dismutase 1	Homo sapiens	33-36
16307304-8	2005	Treatment of sulfite reductase with the arginine-modifying reagent, phenylglyoxal, inhibited both the ferredoxin-linked and methyl viologen-linked activities of the enzyme but had a significantly greater effect on the ferredoxin-dependent activity than on the reduced methyl viologen-linked activity.	Phenylglyoxal	68-81	ferredoxin	Zea mays	102-112
16307304-8	2005	Treatment of sulfite reductase with the arginine-modifying reagent, phenylglyoxal, inhibited both the ferredoxin-linked and methyl viologen-linked activities of the enzyme but had a significantly greater effect on the ferredoxin-dependent activity than on the reduced methyl viologen-linked activity.	Phenylglyoxal	68-81	ferredoxin	Zea mays	218-228
15475303-11	2004	The increase in trehalase inactivation by phenyl glyoxal in the presence of MalphaGlu agrees with the last observation.	Phenylglyoxal	42-56	trehalase	Homo sapiens	16-25
15103693-4	2004	DA, Hill coefficient 1.0, and its analogs 3-hydroxyphenethylamine and 4-hydroxyphenethylamine attenuated the effects of PG on the DAT while phenethylamine did not.	Phenylglyoxal	120-122	solute carrier family 6 member 3	Rattus norvegicus	130-133
15103693-5	2004	The tropane-based DAT inhibitors cocaine, WIN 35065-2, and WIN 35428 also attenuated the effects of PG.	Phenylglyoxal	100-102	solute carrier family 6 member 3	Rattus norvegicus	18-21
12197387-1	2002	A chemical modification of single-chain urokinase-type plasminogen activator (scu-PA) with phenylglyoxal under mild conditions resulted in the scu-PA derivatives with various numbers of the modified Arg residues.	Phenylglyoxal	91-104	plasminogen activator, urokinase	Homo sapiens	40-76
11846392-8	2002	Both PGO or 4-HNE are themselves potent inhibitors of ALDH, and their protective effect cannot be blocked by an ALDH inhibitor.	Phenylglyoxal	5-8	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	54-58
11594461-6	2001	Glucokinase activity assays show that enzyme preincubated with glucose possesses residual activity corresponding to the fraction of unmodified enzyme observed by mass spectrometry, strongly suggesting that glucokinase preincubated with glucose is specifically labeled and inactivated upon modification by phenylglyoxal.	Phenylglyoxal	305-318	glucokinase	Homo sapiens	0-11
11594461-6	2001	Glucokinase activity assays show that enzyme preincubated with glucose possesses residual activity corresponding to the fraction of unmodified enzyme observed by mass spectrometry, strongly suggesting that glucokinase preincubated with glucose is specifically labeled and inactivated upon modification by phenylglyoxal.	Phenylglyoxal	305-318	glucokinase	Homo sapiens	206-217
10774743-8	2000	This result indicates that GDH saturated with NADH or 2-oxoglutarate is still open to attack by phenylglyoxal.	Phenylglyoxal	96-109	Glu/Leu/Phe/Val dehydrogenase	Saccharolobus solfataricus	27-30
10774743-10	2000	The above results suggests that the phenylglyoxal-modified arginine residues are not located at the catalytic site and the inactivation of GDH by phenylglyoxal might be due to a steric hindrance or a conformational change affected by the interaction of the enzyme with its inhibitor.	Phenylglyoxal	36-49	Glu/Leu/Phe/Val dehydrogenase	Saccharolobus solfataricus	139-142
10774743-10	2000	The above results suggests that the phenylglyoxal-modified arginine residues are not located at the catalytic site and the inactivation of GDH by phenylglyoxal might be due to a steric hindrance or a conformational change affected by the interaction of the enzyme with its inhibitor.	Phenylglyoxal	146-159	Glu/Leu/Phe/Val dehydrogenase	Saccharolobus solfataricus	139-142
10685032-6	2000	The inhibitory effects of N-ethylmaleimide and phenylglyoxal on the LPP1-encoded enzyme were novel properties when compared with other Mg(2+)-independent lipid phosphate phosphatases from S. cerevisiae and mammalian cells.	Phenylglyoxal	47-60	phosphatidate phosphatase LPP1	Saccharomyces cerevisiae S288C	68-72
10666306-6	2000	GmGlyox I was active toward the hemithioacetal adducts formed by reacting methylglyoxal, or phenylglyoxal, with glutathione, homoglutathione, or gamma-glutamylcysteine, showing no preference for homoglutathione adducts over glutathione adducts, even though homoglutathione is the dominant thiol in soybean.	Phenylglyoxal	92-105	lactoylglutathione lyase	Glycine max	0-9
10574940-7	1999	Treatment of mitochondrial GPAT with arginine-modifying agents, phenylglyoxal and cyclohexanedione, inactivated the enzyme.	Phenylglyoxal	64-77	glycerol-3-phosphate acyltransferase, mitochondrial	Mus musculus	27-31
10510318-5	1999	In contrast, AKR1A1 reduces a broad spectrum of carbonyl-containing compounds, displaying highest specific activity for SSA, 4-carboxybenzaldehyde, 4-nitrobenzaldehyde, pyridine-3-aldehyde, pyridine-4-aldehyde, 4-hydroxynonenal, phenylglyoxal, methylglyoxal, 2,3-hexanedione, 1, 2-NQ, 16-ketoestrone and d-glucuronic acid.	Phenylglyoxal	229-242	aldo-keto reductase family 1 member A1	Homo sapiens	13-19
9608747-10	1998	Preincubation of the NAT with AcCoA provided significant protection against the inhibition of iodoacetamide and diethylpyrocarbonate, but only partial protection against the inhibition of phenylglyoxal.	Phenylglyoxal	188-201	bromodomain containing 2	Homo sapiens	21-24
9359858-8	1997	With the hemithioacetal of glutathione and phenylglyoxal, the kinetic parameters of the mutants were also of the same magnitude as those of wild-type glyoxalase I.	Phenylglyoxal	43-56	glyoxalase I	Homo sapiens	150-162
9108251-8	1997	Among the purine PRT in our possession, only schistosomal HGPRT, the only other enzyme that contains an arginine residue at the corresponding location (Arg187), was susceptible to phenylglyoxal and butane-2,3-dione.	Phenylglyoxal	180-193	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	58-63
8761469-0	1996	Involvement of an arginyl residue in the nucleotide-binding site of Ca(2+)-ATPase from sarcoplasmic reticulum as seen by reaction with phenylglyoxal.	Phenylglyoxal	135-148	dynein axonemal heavy chain 8	Homo sapiens	75-81
8761469-7	1996	The way in which ATPase inhibition depends on the presence of phenylglyoxal indicates that this process occurs in a pseudo-first-order reaction.	Phenylglyoxal	62-75	dynein axonemal heavy chain 8	Homo sapiens	17-23
8852756-1	1996	Lysine and arginine residues of pig kidney diamine oxidase (DAO) were modified with 2,4,6-trinitrobenzenesulphonic acid (TNBS), 2,3-butanedione and phenylglyoxal, respectively, using different concentrations and time periods.	Phenylglyoxal	148-161	amine oxidase copper containing 1	Sus scrofa	43-58
8852756-1	1996	Lysine and arginine residues of pig kidney diamine oxidase (DAO) were modified with 2,4,6-trinitrobenzenesulphonic acid (TNBS), 2,3-butanedione and phenylglyoxal, respectively, using different concentrations and time periods.	Phenylglyoxal	148-161	amine oxidase copper containing 1	Sus scrofa	60-63
7929602-8	1994	Three lysosomotrophic agents and the endocytosis inhibitor, phenylglyoxal, markedly reduced Fe uptake at both Tf concentrations, and it is concluded that a saturable process consistent with receptor-mediated endocytosis of Tf occurred at the lower Tf concentration, while the predominant mechanism of Fe uptake at high Tf concentrations was a second saturable process consistent with adsorptive pinocytosis.	Phenylglyoxal	60-73	transferrin	Homo sapiens	110-112
7929602-8	1994	Three lysosomotrophic agents and the endocytosis inhibitor, phenylglyoxal, markedly reduced Fe uptake at both Tf concentrations, and it is concluded that a saturable process consistent with receptor-mediated endocytosis of Tf occurred at the lower Tf concentration, while the predominant mechanism of Fe uptake at high Tf concentrations was a second saturable process consistent with adsorptive pinocytosis.	Phenylglyoxal	60-73	transferrin	Homo sapiens	223-225
7929602-8	1994	Three lysosomotrophic agents and the endocytosis inhibitor, phenylglyoxal, markedly reduced Fe uptake at both Tf concentrations, and it is concluded that a saturable process consistent with receptor-mediated endocytosis of Tf occurred at the lower Tf concentration, while the predominant mechanism of Fe uptake at high Tf concentrations was a second saturable process consistent with adsorptive pinocytosis.	Phenylglyoxal	60-73	transferrin	Homo sapiens	223-225
7929602-8	1994	Three lysosomotrophic agents and the endocytosis inhibitor, phenylglyoxal, markedly reduced Fe uptake at both Tf concentrations, and it is concluded that a saturable process consistent with receptor-mediated endocytosis of Tf occurred at the lower Tf concentration, while the predominant mechanism of Fe uptake at high Tf concentrations was a second saturable process consistent with adsorptive pinocytosis.	Phenylglyoxal	60-73	transferrin	Homo sapiens	223-225
8147915-2	1994	Modification of arginyl residues using phenylglyoxal significantly reduced activation of the NMDA receptor as measured by specific binding of [3H]MK-801 [(+)-5-methyl-10,11-dihydro-dibenzo[a,d]cyclohepten-5,10-imine].	Phenylglyoxal	39-52	glutamate ionotropic receptor NMDA type subunit 1	Sus scrofa	93-106
8135541-13	1994	Reaction of purified porcine OTCase with phenylglyoxal, an arginine-specific reagent, results in complete loss of catalytic activity.	Phenylglyoxal	41-54	ornithine transcarbamylase	Homo sapiens	29-35
8245689-1	1993	Modification of arginyl residues of Hageman factor by phenylglyoxal hydrate inhibits activation of this clotting factor in a plasma-free system, that is, in the absence of the other constituents of the contact activation system.	Phenylglyoxal	54-67	coagulation factor XII	Homo sapiens	36-50
8494891-1	1993	Modification of class III alcohol dehydrogenase (chi chi-ADH) with phenylglyoxal eliminates fatty acid activation by pentanoate and octanoate and concomitantly increases specific activity toward ethanol and 3-methylcrotyl alcohol 2-3-fold.	Phenylglyoxal	67-80	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	57-60
8486696-0	1993	Arginine residues of the globular regions of human C1q involved in the interaction with immunoglobulin G. The immunoglobulin G binding site in the globular regions of human complement subcomponent C1q has been investigated by chemical modification of histidine residues with diethylpyrocarbonate and arginine residues with phenylglyoxal and cyclohexane-1,2-dione (CHD).	Phenylglyoxal	323-336	complement C1q A chain	Homo sapiens	51-54
8486696-0	1993	Arginine residues of the globular regions of human C1q involved in the interaction with immunoglobulin G. The immunoglobulin G binding site in the globular regions of human complement subcomponent C1q has been investigated by chemical modification of histidine residues with diethylpyrocarbonate and arginine residues with phenylglyoxal and cyclohexane-1,2-dione (CHD).	Phenylglyoxal	323-336	complement C1q A chain	Homo sapiens	197-200
8356909-1	1993	Chemical modification of pig muscle aldose reductase (ALR2) with the arginine specific reagent phenylglyoxal resulted in the inactivation of the enzyme.	Phenylglyoxal	95-108	aldo-keto reductase family 1 member B	Sus scrofa	36-52
8356909-1	1993	Chemical modification of pig muscle aldose reductase (ALR2) with the arginine specific reagent phenylglyoxal resulted in the inactivation of the enzyme.	Phenylglyoxal	95-108	aldo-keto reductase family 1 member B	Sus scrofa	54-58
1323462-0	1992	Inactivation of liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase by phenylglyoxal.	Phenylglyoxal	78-91	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3	Homo sapiens	22-74
1837236-4	1991	Modification of the proteins with phenylglyoxal, an arginine-specific reagent, resulted in the loss of Type 1 IL-1 receptor binding activity.	Phenylglyoxal	34-47	interleukin 1 alpha	Homo sapiens	110-114
1837236-6	1991	Cyanogen bromide cleavage of phenylglyoxal modified IL-1 alpha and IL-1 beta, followed by sequencing of the peptides, revealed that arginine-12 in IL-1 alpha and arginine-4 in IL-1 beta, which occupy the same topology in the respective crystallographic structures, are the target of phenylglyoxal.	Phenylglyoxal	29-42	interleukin 1 alpha	Homo sapiens	52-62
1837236-6	1991	Cyanogen bromide cleavage of phenylglyoxal modified IL-1 alpha and IL-1 beta, followed by sequencing of the peptides, revealed that arginine-12 in IL-1 alpha and arginine-4 in IL-1 beta, which occupy the same topology in the respective crystallographic structures, are the target of phenylglyoxal.	Phenylglyoxal	29-42	interleukin 1 beta	Homo sapiens	67-76
1837236-6	1991	Cyanogen bromide cleavage of phenylglyoxal modified IL-1 alpha and IL-1 beta, followed by sequencing of the peptides, revealed that arginine-12 in IL-1 alpha and arginine-4 in IL-1 beta, which occupy the same topology in the respective crystallographic structures, are the target of phenylglyoxal.	Phenylglyoxal	29-42	interleukin 1 alpha	Homo sapiens	147-157
1837236-6	1991	Cyanogen bromide cleavage of phenylglyoxal modified IL-1 alpha and IL-1 beta, followed by sequencing of the peptides, revealed that arginine-12 in IL-1 alpha and arginine-4 in IL-1 beta, which occupy the same topology in the respective crystallographic structures, are the target of phenylglyoxal.	Phenylglyoxal	29-42	interleukin 1 beta	Homo sapiens	176-185
1837236-6	1991	Cyanogen bromide cleavage of phenylglyoxal modified IL-1 alpha and IL-1 beta, followed by sequencing of the peptides, revealed that arginine-12 in IL-1 alpha and arginine-4 in IL-1 beta, which occupy the same topology in the respective crystallographic structures, are the target of phenylglyoxal.	Phenylglyoxal	283-296	interleukin 1 alpha	Homo sapiens	147-157
1837236-6	1991	Cyanogen bromide cleavage of phenylglyoxal modified IL-1 alpha and IL-1 beta, followed by sequencing of the peptides, revealed that arginine-12 in IL-1 alpha and arginine-4 in IL-1 beta, which occupy the same topology in the respective crystallographic structures, are the target of phenylglyoxal.	Phenylglyoxal	283-296	interleukin 1 beta	Homo sapiens	176-185
1722124-1	1991	Chemical derivatization by phenylglyoxal (PGX) was applied to the identification of arginine in the neuropeptides dynorphin A (1-6) and substance P. The obtained products were separated on a short reversed phase C18 column and analysed on-line with the photodiode array UV technique.	Phenylglyoxal	42-45	Bardet-Biedl syndrome 9	Homo sapiens	212-215
1681807-1	1991	Reagents phenylglyoxal or 1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulfonate inactivate the enzyme prolidase, with protection conferred by the competitive inhibitor N-acetylproline.	Phenylglyoxal	9-22	peptidase D	Homo sapiens	120-129
1654780-1	1991	The reaction of the Cu,Co derivative of bovine Cu,Zn superoxide dismutase with phenylglyoxal or butanedione, which are known to inactivate the enzyme by selectively binding to Arg 141, has been studied by 1H NMR.	Phenylglyoxal	79-92	superoxide dismutase [Cu-Zn]	Bos taurus	47-73
1864444-2	1991	Porphyrinogen carboxylase from the liver of normal and hexachlorobenzene porphyric rats was subjected to chemical modification using photo-oxidation with methylene blue, diethylpyrocarbonate, butane-2,3-dione, and phenylglyoxal.	Phenylglyoxal	214-227	uroporphyrinogen decarboxylase	Rattus norvegicus	0-25
16667568-4	1990	The half-maximal inhibition was brought about by 20 millimolar PGO and 50 millimolar BD for membrane bound and 1.5 millimolar PGO and 5.0 millimolar BD for soluble PPase, respectively.	Phenylglyoxal	63-66	pyrophosphate-energized vacuolar membrane proton pump	Vigna radiata	164-169
16667568-4	1990	The half-maximal inhibition was brought about by 20 millimolar PGO and 50 millimolar BD for membrane bound and 1.5 millimolar PGO and 5.0 millimolar BD for soluble PPase, respectively.	Phenylglyoxal	126-129	pyrophosphate-energized vacuolar membrane proton pump	Vigna radiata	164-169
16667568-7	1990	The double logarithm plots of pseudo-first order rate constant versus reagent concentrations gave slopes of 0.88 (PGO) and 0.90 (BD), respectively, suggesting that the inactivation may possibly result from reaction of at least one arginyl residue at the active site of H(+)-translocating PPase.	Phenylglyoxal	114-117	pyrophosphate-energized vacuolar membrane proton pump	Vigna radiata	288-293
2327787-9	1990	Both types of P-PST activity were inhibited to similar extents by incubation with 50 microM N-ethylmaleimide or 5 mM phenylglyoxal.	Phenylglyoxal	117-130	sulfotransferase family 1A member 1	Homo sapiens	14-19
2597194-8	1989	Those three PST forms differed in sensitivity to 2,6-dichloro-4-nitrophenol (DCNP), N-ethyl maleimide (NEM), iodoacetamide (IAA) and phenylglyoxal (PG).	Phenylglyoxal	133-146	sulfotransferase family 1A member 1	Homo sapiens	12-15
2597194-8	1989	Those three PST forms differed in sensitivity to 2,6-dichloro-4-nitrophenol (DCNP), N-ethyl maleimide (NEM), iodoacetamide (IAA) and phenylglyoxal (PG).	Phenylglyoxal	148-150	sulfotransferase family 1A member 1	Homo sapiens	12-15
2597194-13	1989	Phenylglyoxal, a reagent specific for arginine residues inhibited bull testis PST and both boar phenol sulfotransferases.	Phenylglyoxal	0-13	sulfotransferase family 1A member 1	Homo sapiens	78-81
2536743-2	1989	The arginine-specific reagents phenylglyoxal, 2,3-butanedione, and 1,2-cyclohexanedione all irreversibly inhibit the enzyme with second-order rate constants of 3.42 M-1 min-1, 3.13 M-1 min-1 and 0.313 M-1 min-1, respectively.	Phenylglyoxal	31-44	CD59 molecule (CD59 blood group)	Homo sapiens	169-174
2536743-2	1989	The arginine-specific reagents phenylglyoxal, 2,3-butanedione, and 1,2-cyclohexanedione all irreversibly inhibit the enzyme with second-order rate constants of 3.42 M-1 min-1, 3.13 M-1 min-1 and 0.313 M-1 min-1, respectively.	Phenylglyoxal	31-44	CD59 molecule (CD59 blood group)	Homo sapiens	185-190
2536743-2	1989	The arginine-specific reagents phenylglyoxal, 2,3-butanedione, and 1,2-cyclohexanedione all irreversibly inhibit the enzyme with second-order rate constants of 3.42 M-1 min-1, 3.13 M-1 min-1 and 0.313 M-1 min-1, respectively.	Phenylglyoxal	31-44	CD59 molecule (CD59 blood group)	Homo sapiens	185-190
3233203-5	1988	Preincubation of bindin with fucan can almost completely protect bindin from inactivation by arginine-specific reagents, butanedione and phenylglyoxal, but only moderately slowed the inactivation by the histidine reagent diethyl pyrocarbonate.	Phenylglyoxal	137-150	bindin	Strongylocentrotus purpuratus	17-23
3233203-5	1988	Preincubation of bindin with fucan can almost completely protect bindin from inactivation by arginine-specific reagents, butanedione and phenylglyoxal, but only moderately slowed the inactivation by the histidine reagent diethyl pyrocarbonate.	Phenylglyoxal	137-150	bindin	Strongylocentrotus purpuratus	65-71
2456783-6	1988	(3) Externally applied phenylglyoxal markedly reduced INa and Igat, but many fibres were lost during or shortly after the treatment.	Phenylglyoxal	23-36	internexin neuronal intermediate filament protein alpha	Homo sapiens	54-57
2456783-6	1988	(3) Externally applied phenylglyoxal markedly reduced INa and Igat, but many fibres were lost during or shortly after the treatment.	Phenylglyoxal	23-36	IGAT	Homo sapiens	62-66
2456783-7	1988	A few min treatment with 5 mM phenylglyoxal at pH 9 reduced INa to 20% and the on-response of Igat to 69.5%.	Phenylglyoxal	30-43	internexin neuronal intermediate filament protein alpha	Homo sapiens	60-63
2456783-7	1988	A few min treatment with 5 mM phenylglyoxal at pH 9 reduced INa to 20% and the on-response of Igat to 69.5%.	Phenylglyoxal	30-43	IGAT	Homo sapiens	94-98
2456783-13	1988	(5) 5 mM phenylglyoxal, 10 mM nitrophenylglyoxal and 20 mM hydroxyphenylglyoxal shifted the steady-state inactivation curve by 10-15 mV to more negative values of membrane potential but did not affect the descending branch of the INa(E) curve.	Phenylglyoxal	9-22	internexin neuronal intermediate filament protein alpha	Homo sapiens	230-233
2847349-6	1988	Modification of arginine residues with Phenylglyoxal and 2,3,Butanedione led to loss of thrombomodulin binding affinity.	Phenylglyoxal	39-52	thrombomodulin	Homo sapiens	88-102
3366770-5	1988	DEPC, phenylglyoxal, and 2,3-butanedione inactivated the specifically mediated PAH transport, i.e. probenecid inhibitable transport with IC50 values of 160, 710, and 1780 microM, respectively.	Phenylglyoxal	6-19	phenylalanine hydroxylase	Canis lupus familiaris	79-82
3350811-1	1988	Chemical modification by phenylglyoxal was used to investigate relationships between the structure, function, and regulation of the type II calmodulin-dependent protein kinase.	Phenylglyoxal	25-38	calmodulin 1	Homo sapiens	140-150
3350811-6	1988	Inactivation of the enzyme by phenylglyoxal was dependent on the presence of Mg2+ or Ca2+/calmodulin, and further enhanced by the simultaneous addition of these effectors to the reaction.	Phenylglyoxal	30-43	calmodulin 1	Homo sapiens	90-100
2837286-3	1988	Phenylglyoxal was 10-fold more effective than pHPG in promoting the loss of CaM-stimulated activity with a second-order rate constant of 13.3 M-1 min-1.	Phenylglyoxal	0-13	CD59 molecule (CD59 blood group)	Homo sapiens	146-151
3442671-1	1987	Rat liver glycine methyltransferase is inactivated irreversibly by phenylglyoxal in potassium phosphate buffer.	Phenylglyoxal	67-80	glycine N-methyltransferase	Rattus norvegicus	10-35
3118957-6	1987	Aldose reductase was partially inactivated by phenylglyoxal, but insensitive to 2,3-butanedione.	Phenylglyoxal	46-59	aldo-keto reductase family 1 member B	Homo sapiens	0-16
3118957-10	1987	The effect of phenylglyoxal on aldose reductase may be explained by the modification of a reactive thiol or lysine rather than an arginine residue.	Phenylglyoxal	14-27	aldo-keto reductase family 1 member B	Homo sapiens	31-47
2887428-8	1987	Comparative analyses of CNBr fragments obtained from apoenzyme, holoenzyme and the 8-mercapto derivative of D-amino-acid oxidase after reaction with phenylglyoxal did not provide unequivocal identification of the essential arginine residue within the primary structure of the enzyme.	Phenylglyoxal	149-162	D-amino acid oxidase	Homo sapiens	108-128
3611085-0	1987	Chemical modification of the calmodulin-stimulated phosphatase, calcineurin, by phenylglyoxal.	Phenylglyoxal	80-93	calmodulin 1	Homo sapiens	29-39
3028261-0	1987	The interaction of anions with native and phenylglyoxal-modified human serum transferrin.	Phenylglyoxal	42-55	transferrin	Homo sapiens	77-88
3028261-12	1987	We found that phenylglyoxal-modified Fe-transferrin, with no loss of bound iron, was much more resistant to iron removal by phosphate and other competitive chelators.	Phenylglyoxal	14-27	transferrin	Homo sapiens	40-51
3522576-1	1986	The effect of the arginine-specific reagents phenylglyoxal and butanedione on the activity of neutral endopeptidase 24.11 ("enkephalinase") was determined.	Phenylglyoxal	45-58	membrane metalloendopeptidase	Homo sapiens	94-121
3530833-0	1986	Enzymatic reduction of phenylglyoxal and 2,3-butanedione, two commonly used arginine-modifying reagents, by the ketoacyl reductase domain of fatty acid synthase.	Phenylglyoxal	23-36	fatty acid synthase	Homo sapiens	141-160
3530833-1	1986	Fatty acid synthase catalyzes the reduction of one of the carbonyl groups in phenylglyoxal and 2,3-butanedione using NADPH as the reductant.	Phenylglyoxal	77-90	fatty acid synthase	Homo sapiens	0-19
2863142-4	1985	With phenylglyoxal and 2,4-pentanedione as modifiers there was a selective activation of pseudocholinesterase alone with no effect on aryl acylamidase.	Phenylglyoxal	5-18	butyrylcholinesterase	Homo sapiens	89-109
2932113-3	1985	Phenylglyoxal reacted with arginine residues of gizzard myosin in a mol ratio of two to one, phenylglyoxal to arginine as determined spectrophotometrically.	Phenylglyoxal	93-106	myosin, heavy chain 15	Gallus gallus	56-62
2932113-6	1985	The same results were obtained when the myosin was phosphorylated and then incubated with phenylglyoxal.	Phenylglyoxal	90-103	myosin, heavy chain 15	Gallus gallus	40-46
3872340-4	1985	In contrast, the pI 5.1 component of PBM IL-1 is resistant to heat denaturation and sulfhydryl reagents, although it is totally inactivated by phenylglyoxal.	Phenylglyoxal	143-156	interleukin 1 alpha	Homo sapiens	41-45
2859285-1	1985	The ATPase activity of soluble chloroplast coupling factor (CF1) was irreversibly inactivated by phenylglyoxal, an arginine reagent.	Phenylglyoxal	97-110	AT695_RS06370	Staphylococcus aureus	4-10
2857576-8	1985	Bovine brain glutamine synthetase is inactivated by phenylglyoxal and N-ethylmaleimide.	Phenylglyoxal	52-65	glutamate-ammonia ligase	Bos taurus	13-33
3925401-1	1985	Chemical modification studies on homogeneous bovine lens aldose reductase using diethylpyrocarbonate, phenylglyoxal, butanedione, N-ethylmaleimide and p-chloromercuribenzoate indicate that histidine and arginine residues located at or near the nucleotide binding site may be important in binding or orientation of the NADPH, and that NADPH oxidation with glucose requires protein thiol.	Phenylglyoxal	102-115	aldose reductase	Bos taurus	57-73
6525172-1	1984	Chemical modification of amino acid residues with phenylglyoxal, N-ethylmaleimide and diethyl pyrocarbonate indicated that at least one residue each of arginine, cysteine and histidine were essential for the activity of sheep liver serine hydroxymethyltransferase.	Phenylglyoxal	50-63	serine hydroxymethyltransferase, cytosolic	Ovis aries	232-263
6086333-8	1984	Porin-induced hemolysis was inhibited with anti-porin serum, as well as by a treatment with phenylglyoxal, which reacts with the arginine residues of proteins.	Phenylglyoxal	92-105	voltage dependent anion channel 1	Homo sapiens	0-5
6320902-3	1984	The interleukin 1 and chondrocyte-stimulating activities are destroyed by pretreatment of the material with phenylglyoxal.	Phenylglyoxal	108-121	interleukin 1 alpha	Homo sapiens	4-17
7161255-1	1982	Adrenodoxin reductase from bovine adrenocortex was inactivated by arginine specific reagents, p-hydroxyphenylglyoxal, phenylglyoxal, 2,3-butanedione, and 1,2-cyclohexanedione.	Phenylglyoxal	103-116	ferredoxin reductase	Bos taurus	0-21
7118924-0	1982	Inhibition of the binding of dexamethasone to mammary cytoplasmic glucocorticoid receptor by phenylglyoxal.	Phenylglyoxal	93-106	nuclear receptor subfamily 3 group C member 1	Homo sapiens	66-89
7118924-1	1982	We have studied the effects of phenylglyoxal and other related arginine-specific reagents on the mammary cytoplasmic glucocorticoid receptor.	Phenylglyoxal	31-44	nuclear receptor subfamily 3 group C member 1	Homo sapiens	117-140
7055581-1	1982	Glutathione reductase (NAD(P)H: oxidized-glutathione oxidoreductase, EC 1.6.4.2) from human erythrocytes as well as from other sources was inactivated irreversibly by the arginine modifying reagents 2,3-butanedione, 1,2-cyclohexanedione and phenylglyoxal.	Phenylglyoxal	241-254	glutathione-disulfide reductase	Homo sapiens	0-21
7316981-1	1981	Rat liver ATP citrate lyase was inactivated by 2, 3-butanedione and phenylglyoxal.	Phenylglyoxal	68-81	ATP citrate lyase	Rattus norvegicus	10-27
7316981-4	1981	Phenylglyoxal also decreased autophosphorylation (catalytic phosphate) of ATP citrate lyase.	Phenylglyoxal	0-13	ATP citrate lyase	Rattus norvegicus	74-91
35531-1	1979	Pig kidney aldehyde reductase is inactivated by 2,3-butanedione, phenylglyoxal, methylglyoxal, and 1,2-cyclohexanedione.	Phenylglyoxal	65-78	aldo-keto reductase family 1 member B	Sus scrofa	11-29
711738-3	1978	Treatment of free rhodanese with near-stoichiometric quantities of either iodoacetate or phenylglyoxal results in the rapid modification of the essential sulfhydryl group of Cys-247 and the consequent inactivation of the enzyme.	Phenylglyoxal	89-102	thiosulfate sulfurtransferase	Bos taurus	18-27
711738-5	1978	Inactivation of free rhodanese by phenylglyoxal in the presence of cyanide was shown to be caused by a novel reaction in which disulfide bonds are formed between Cys-247 and either Cys-254 or Cys-263.	Phenylglyoxal	34-47	thiosulfate sulfurtransferase	Bos taurus	21-30
354693-1	1978	Yeast hexokinase PII is rapidly inactivated (assayed at pH 8.0) by either butanedione in borate buffer or phenylglyoxal, reagents which are highly selective for the modification of arginyl residues.	Phenylglyoxal	106-119	hexokinase	Saccharomyces cerevisiae S288C	6-16
590939-9	1977	Pyruvate kinase from rabbit muscle is modified by phenylglyoxal in a similar manner.	Phenylglyoxal	50-63	pyruvate kinase PKLR	Oryctolagus cuniculus	0-15
323257-4	1977	If N-(phosphonacetyl)-L-aspartate is used to protect the active site, we find that phenylglyoxal causes destruction of the enzyme"s susceptibility to activation by ATP and inhibition by CTP.	Phenylglyoxal	83-96	solute carrier family 25 member 1	Homo sapiens	186-189
321441-8	1977	Extensive modification of the arginine residues by PGO occurred with RCM-derivatives of ribonuclease A and insulin B chain.	Phenylglyoxal	51-54	insulin	Homo sapiens	107-114
10962-1	1976	The reactions between yeast carboxypeptidase C and the group-specific reagents, phenylglyoxal and iodoacetamide, have been studied in detail and the reactions of residue at the active site with N-tosyl-L-phenylalanine chloromethyl ketone and diisopropyl phosphorofluoridate have been confirmed.	Phenylglyoxal	80-93	carboxypeptidase C	Saccharomyces cerevisiae S288C	28-46
30946572-4	2019	A flavin-dependent oxidase encoded by gene ro02984 was found to oxidize either mandelic acid or phenylglyoxal.	Phenylglyoxal	96-109	multicopper oxidase family protein	Rhodococcus jostii RHA1	19-26