PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24361276-1 2014 Tyrosine hydroxylase (TyrH) catalyzes the hydroxylation of tyrosine to form 3,4-dihydroxyphenylalanine in the biosynthesis of the catecholamine neurotransmitters. Dihydroxyphenylalanine 76-102 tyrosine hydroxylase Rattus norvegicus 0-20 24361276-1 2014 Tyrosine hydroxylase (TyrH) catalyzes the hydroxylation of tyrosine to form 3,4-dihydroxyphenylalanine in the biosynthesis of the catecholamine neurotransmitters. Dihydroxyphenylalanine 76-102 tyrosine hydroxylase Rattus norvegicus 22-26 22294150-0 2012 Design of a single AAV vector for coexpression of TH and GCH1 to establish continuous DOPA synthesis in a rat model of Parkinson"s disease. Dihydroxyphenylalanine 86-90 tyrosine hydroxylase Rattus norvegicus 50-52 22294150-2 2012 So far, all studies have utilized a mix of two monocistronic vectors expressing either of the two genes, tyrosine hydroxylase (TH) and GTP cyclohydrolase-1 (GCH1), needed for DOPA production. Dihydroxyphenylalanine 175-179 tyrosine hydroxylase Rattus norvegicus 105-125 22294150-2 2012 So far, all studies have utilized a mix of two monocistronic vectors expressing either of the two genes, tyrosine hydroxylase (TH) and GTP cyclohydrolase-1 (GCH1), needed for DOPA production. Dihydroxyphenylalanine 175-179 tyrosine hydroxylase Rattus norvegicus 127-129 19686242-6 2009 We show that increasing the availability of 5,6,7,8-tetrahydro-l-biopterin (BH4) in the same cellular compartment as the TH enzyme resulted in better efficiency in DOPA synthesis, most likely by hindering inactivation of the enzyme and increasing its stability. Dihydroxyphenylalanine 164-168 tyrosine hydroxylase Rattus norvegicus 121-123 19686242-2 2009 Recombinant adeno-associated viral (rAAV) vector in particular has been utilized for continuous l-3,4 dihydroxyphenylalanine (DOPA) delivery by expressing the tyrosine hydroxylase (TH) and GTP cyclohydrolase 1 (GCH1) genes which are necessary and sufficient for efficient synthesis of DOPA from dietary tyrosine. Dihydroxyphenylalanine 126-130 tyrosine hydroxylase Rattus norvegicus 159-179 19686242-2 2009 Recombinant adeno-associated viral (rAAV) vector in particular has been utilized for continuous l-3,4 dihydroxyphenylalanine (DOPA) delivery by expressing the tyrosine hydroxylase (TH) and GTP cyclohydrolase 1 (GCH1) genes which are necessary and sufficient for efficient synthesis of DOPA from dietary tyrosine. Dihydroxyphenylalanine 126-130 tyrosine hydroxylase Rattus norvegicus 181-183 19686242-2 2009 Recombinant adeno-associated viral (rAAV) vector in particular has been utilized for continuous l-3,4 dihydroxyphenylalanine (DOPA) delivery by expressing the tyrosine hydroxylase (TH) and GTP cyclohydrolase 1 (GCH1) genes which are necessary and sufficient for efficient synthesis of DOPA from dietary tyrosine. Dihydroxyphenylalanine 285-289 tyrosine hydroxylase Rattus norvegicus 159-179 19686242-2 2009 Recombinant adeno-associated viral (rAAV) vector in particular has been utilized for continuous l-3,4 dihydroxyphenylalanine (DOPA) delivery by expressing the tyrosine hydroxylase (TH) and GTP cyclohydrolase 1 (GCH1) genes which are necessary and sufficient for efficient synthesis of DOPA from dietary tyrosine. Dihydroxyphenylalanine 285-289 tyrosine hydroxylase Rattus norvegicus 181-183 19686242-3 2009 The present study was designed to determine the optimal stoichiometric relationship between TH and GCH1 genes for ectopic DOPA production and the cellular machinery involved in its synthesis, storage, and metabolism. Dihydroxyphenylalanine 122-126 tyrosine hydroxylase Rattus norvegicus 92-94 17010321-8 2006 Decreased DOPA synthesis, despite increased levels of TH protein, may reflect the inhibitory effect of increased DA binding to TH protein or decreased concentrations of cofactor tetrahydrobiopterin. Dihydroxyphenylalanine 10-14 tyrosine hydroxylase Rattus norvegicus 127-129 18096660-4 2008 TH activity was determined from the rate of 3,4-dihydroxyphenylalanine (DOPA) accumulation. Dihydroxyphenylalanine 44-70 tyrosine hydroxylase Rattus norvegicus 0-2 18096660-4 2008 TH activity was determined from the rate of 3,4-dihydroxyphenylalanine (DOPA) accumulation. Dihydroxyphenylalanine 72-76 tyrosine hydroxylase Rattus norvegicus 0-2 11207812-6 2001 In addition, the dopamine D(2) receptor agonist reduced both basal and forskolin-stimulated activity of TH, measured as 3,4-dihydroxyphenylalanine (DOPA) accumulation. Dihydroxyphenylalanine 120-146 tyrosine hydroxylase Rattus norvegicus 104-106 11207812-6 2001 In addition, the dopamine D(2) receptor agonist reduced both basal and forskolin-stimulated activity of TH, measured as 3,4-dihydroxyphenylalanine (DOPA) accumulation. Dihydroxyphenylalanine 148-152 tyrosine hydroxylase Rattus norvegicus 104-106 8577397-4 1995 On the contrary, 1 mM 2,9-Me2NH+ rapidly reduced 3,4-dihydroxyphenylalanine production to 10% of the basal level only during its perfusion, indicating direct inhibition of TH activity. Dihydroxyphenylalanine 49-75 tyrosine hydroxylase Rattus norvegicus 172-174 8798695-2 1996 Tyrosine hydroxylase is an iron-containing monooxygenase that uses a tetrahydropterin to catalyze the hydroxylation of tyrosine to dihydroxyphenylalanine in catecholamine biosynthesis. Dihydroxyphenylalanine 131-153 tyrosine hydroxylase Rattus norvegicus 0-20 10479065-4 1999 Tyrosine hydroxylase activity was evaluated biochemically, by measuring the in vivo accumulation of dihydroxyphenylalanine (DOPA) in the presence of a DOPA-decarboxylase inhibitor. Dihydroxyphenylalanine 100-122 tyrosine hydroxylase Rattus norvegicus 0-20 10479065-4 1999 Tyrosine hydroxylase activity was evaluated biochemically, by measuring the in vivo accumulation of dihydroxyphenylalanine (DOPA) in the presence of a DOPA-decarboxylase inhibitor. Dihydroxyphenylalanine 124-128 tyrosine hydroxylase Rattus norvegicus 0-20 21554649-5 1992 The rate of DOPA accumulation, determined by measuring DOPA levels in the stalk-median eminence by high-performance liquid chromatography with electrochemical detection was used as a measure of tyrosine hydroxylase (TH) catalytic activity. Dihydroxyphenylalanine 12-16 tyrosine hydroxylase Rattus norvegicus 194-214 7906722-2 1994 TH activity (determined by 3,4-dihydroxyphenylalanine accumulation in the median eminence after blockade of decarboxylase with NSD 1055) showed a dose-dependent increase within 2 h of incubation of the hypothalamic slices with PRL. Dihydroxyphenylalanine 27-53 tyrosine hydroxylase Rattus norvegicus 0-2 7909929-3 1994 In an attempt to understand the effect of NPY on TH activities, an in vitro assay is carried out using chromatographic analysis of 3,4-dihydroxyphenylalanine (DOPA) formation from tyrosine. Dihydroxyphenylalanine 131-157 tyrosine hydroxylase Rattus norvegicus 49-51 7909929-3 1994 In an attempt to understand the effect of NPY on TH activities, an in vitro assay is carried out using chromatographic analysis of 3,4-dihydroxyphenylalanine (DOPA) formation from tyrosine. Dihydroxyphenylalanine 159-163 tyrosine hydroxylase Rattus norvegicus 49-51 7909929-4 1994 NPY (40-120 pmol/ml) produced a dose-dependent depression of DOPA formation catalysed by the adrenal TH of rats. Dihydroxyphenylalanine 61-65 tyrosine hydroxylase Rattus norvegicus 101-103 7901391-4 1993 The in situ molar activity of TH was expressed as the moles of DOPA accumulating in the tissue per mole of TH per hour. Dihydroxyphenylalanine 63-67 tyrosine hydroxylase Rattus norvegicus 30-32 7922603-4 1994 DOPA disappeared completely after inhibition of TH by alpha-methyl-p-tyrosine, showing that it reflects TH activity. Dihydroxyphenylalanine 0-4 tyrosine hydroxylase Rattus norvegicus 48-50 7922603-4 1994 DOPA disappeared completely after inhibition of TH by alpha-methyl-p-tyrosine, showing that it reflects TH activity. Dihydroxyphenylalanine 0-4 tyrosine hydroxylase Rattus norvegicus 104-106 21554649-5 1992 The rate of DOPA accumulation, determined by measuring DOPA levels in the stalk-median eminence by high-performance liquid chromatography with electrochemical detection was used as a measure of tyrosine hydroxylase (TH) catalytic activity. Dihydroxyphenylalanine 12-16 tyrosine hydroxylase Rattus norvegicus 216-218 1686424-2 1991 The catalytic activity of TH in the stalk-median eminence was also investigated using the in vitro accumulation of 3,4 dihydroxyphenylalanine (DOPA) after inhibiting aromatic amino acid decarboxylase activity. Dihydroxyphenylalanine 115-141 tyrosine hydroxylase Rattus norvegicus 26-28 1686424-2 1991 The catalytic activity of TH in the stalk-median eminence was also investigated using the in vitro accumulation of 3,4 dihydroxyphenylalanine (DOPA) after inhibiting aromatic amino acid decarboxylase activity. Dihydroxyphenylalanine 143-147 tyrosine hydroxylase Rattus norvegicus 26-28 1677330-4 1991 The in situ activity of TH was calculated using the rate of accumulation of dihydroxyphenylalanine after pharmacological inhibition of dihydroxyphenylalanine decarboxylase activity. Dihydroxyphenylalanine 76-98 tyrosine hydroxylase Rattus norvegicus 24-26 1980722-7 1990 The catalytic activity of TH, as determined by in vitro DOPA accumulation in the stalk-median eminence, was 3-fold greater in females than males. Dihydroxyphenylalanine 56-60 tyrosine hydroxylase Rattus norvegicus 26-28 1970292-5 1990 Inhibitors of TH activity caused a dose-dependent reduction in DOPA secretion. Dihydroxyphenylalanine 63-67 tyrosine hydroxylase Rattus norvegicus 14-16 2899310-5 1988 These results suggest that MPP+ acutely inhibits the phosphorylation of TH to decrease cellular DOPA formation. Dihydroxyphenylalanine 96-100 tyrosine hydroxylase Rattus norvegicus 72-74 2565217-6 1989 The in situ activity of tyrosine hydroxylase (TH; expressed as moles of DOPA per mol TH/h) in the ME was 178 +/- 16.5 in estradiol-progesterone-treated intact rats, but was 27 +/- 2.4, 52 +/- 4.2, and 35 +/- 2.5 in animals treated with the solvent vehicle, estradiol, and progesterone, respectively. Dihydroxyphenylalanine 72-76 tyrosine hydroxylase Rattus norvegicus 24-44 6125950-5 1982 Tyrosine hydroxylase activity, determined by the accumulation of DOPA after NSD-1015, was significantly reduced in the median eminence of BL+ANOS (p less than 0.05). Dihydroxyphenylalanine 65-69 tyrosine hydroxylase Rattus norvegicus 0-20 2885075-2 1987 3,4-Dihydroxyphenylalanine (DOPA) formed by TH was measured using high-performance liquid chromatography (HPLC). Dihydroxyphenylalanine 0-26 tyrosine hydroxylase Rattus norvegicus 44-46 2885075-2 1987 3,4-Dihydroxyphenylalanine (DOPA) formed by TH was measured using high-performance liquid chromatography (HPLC). Dihydroxyphenylalanine 28-32 tyrosine hydroxylase Rattus norvegicus 44-46 2866821-1 1985 Intravitreal injection of tetrahydrobiopterin (BH4), the cofactor for tyrosine hydroxylase (TH), increases 3,4-dihydroxyphenylalanine (DOPA) accumulation in retinas of dark-adapted rats, as does exposure to light. Dihydroxyphenylalanine 107-133 tyrosine hydroxylase Rattus norvegicus 70-90 2866821-1 1985 Intravitreal injection of tetrahydrobiopterin (BH4), the cofactor for tyrosine hydroxylase (TH), increases 3,4-dihydroxyphenylalanine (DOPA) accumulation in retinas of dark-adapted rats, as does exposure to light. Dihydroxyphenylalanine 107-133 tyrosine hydroxylase Rattus norvegicus 92-94 2866821-1 1985 Intravitreal injection of tetrahydrobiopterin (BH4), the cofactor for tyrosine hydroxylase (TH), increases 3,4-dihydroxyphenylalanine (DOPA) accumulation in retinas of dark-adapted rats, as does exposure to light. Dihydroxyphenylalanine 135-139 tyrosine hydroxylase Rattus norvegicus 70-90 2866821-1 1985 Intravitreal injection of tetrahydrobiopterin (BH4), the cofactor for tyrosine hydroxylase (TH), increases 3,4-dihydroxyphenylalanine (DOPA) accumulation in retinas of dark-adapted rats, as does exposure to light. Dihydroxyphenylalanine 135-139 tyrosine hydroxylase Rattus norvegicus 92-94 3929190-1 1985 Pargyline, an inhibitor of monoamine oxidase (MAO), prevented 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced inhibition of dihydroxyphenylalanine (DOPA) production by tyrosine hydroxylase (TH) system in rat striatal tissue slices. Dihydroxyphenylalanine 136-158 tyrosine hydroxylase Rattus norvegicus 180-200 3929190-1 1985 Pargyline, an inhibitor of monoamine oxidase (MAO), prevented 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced inhibition of dihydroxyphenylalanine (DOPA) production by tyrosine hydroxylase (TH) system in rat striatal tissue slices. Dihydroxyphenylalanine 136-158 tyrosine hydroxylase Rattus norvegicus 202-204 6145756-10 1984 The activation of TH presumably underlies the increase in DOPA synthesis produced by these agents. Dihydroxyphenylalanine 58-62 tyrosine hydroxylase Rattus norvegicus 18-20 6127400-1 1982 The activity of tyrosine 3-monooxygenase in rat superior cervical ganglia in vitro was measured by monitoring their rate of dopa production. Dihydroxyphenylalanine 124-128 tyrosine hydroxylase Rattus norvegicus 16-40 6109760-1 1981 Tyrosine hydroxylase, the rate-limiting enzyme in catecholamine biosynthesis, catalyzes the conversion of tyrosine to DOPA, Cyclic AMP-dependent protein phosphorylation conditions alter tyrosine hydroxylase activity in rat striatal homogenates. Dihydroxyphenylalanine 118-122 tyrosine hydroxylase Rattus norvegicus 0-20 6112040-3 1981 Tyrosine hydroxylase activity in adrenals removed from non-stressed rats following pentobarbital anesthesia was found to be 12.9 +/- 1.0 nmol DOPA formed x mg protein-1. Dihydroxyphenylalanine 142-146 tyrosine hydroxylase Rattus norvegicus 0-20 6109760-1 1981 Tyrosine hydroxylase, the rate-limiting enzyme in catecholamine biosynthesis, catalyzes the conversion of tyrosine to DOPA, Cyclic AMP-dependent protein phosphorylation conditions alter tyrosine hydroxylase activity in rat striatal homogenates. Dihydroxyphenylalanine 118-122 tyrosine hydroxylase Rattus norvegicus 186-206 32778969-4 2020 In this study, we investigated whether NT5DC2 could regulate the catalytic activity of TH, which converts tyrosine to DOPA, because the phosphorylation level of TH, controlled by protein kinases and phosphatases, is well known to regulate its catalytic activity. Dihydroxyphenylalanine 118-122 tyrosine hydroxylase Rattus norvegicus 87-89 32778969-4 2020 In this study, we investigated whether NT5DC2 could regulate the catalytic activity of TH, which converts tyrosine to DOPA, because the phosphorylation level of TH, controlled by protein kinases and phosphatases, is well known to regulate its catalytic activity. Dihydroxyphenylalanine 118-122 tyrosine hydroxylase Rattus norvegicus 161-163 32778969-5 2020 The down-regulation of NT5DC2 by siRNA increased mainly DOPA synthesis by TH in PC12D cells, although this down-regulation tended to increase the conversion of DOPA to DA by aromatic L-amino acid decarboxylase. Dihydroxyphenylalanine 56-60 tyrosine hydroxylase Rattus norvegicus 74-76 32778969-6 2020 The increased DOPA synthesis should be attributed to the catalytic activity of TH controlled by its phosphorylation, because Western blot analysis revealed that the down-regulation of NT5DC2 tended to increase the level of TH phosphorylated at its Ser residues, but not that of the TH protein. Dihydroxyphenylalanine 14-18 tyrosine hydroxylase Rattus norvegicus 79-81 32778969-6 2020 The increased DOPA synthesis should be attributed to the catalytic activity of TH controlled by its phosphorylation, because Western blot analysis revealed that the down-regulation of NT5DC2 tended to increase the level of TH phosphorylated at its Ser residues, but not that of the TH protein. Dihydroxyphenylalanine 14-18 tyrosine hydroxylase Rattus norvegicus 223-225 32778969-6 2020 The increased DOPA synthesis should be attributed to the catalytic activity of TH controlled by its phosphorylation, because Western blot analysis revealed that the down-regulation of NT5DC2 tended to increase the level of TH phosphorylated at its Ser residues, but not that of the TH protein. Dihydroxyphenylalanine 14-18 tyrosine hydroxylase Rattus norvegicus 223-225 32778969-9 2020 Collectively, our results indicate that NT5DC2 could work to inhibit the DOPA synthesis by decreasing the phosphorylation of TH at its Ser40. Dihydroxyphenylalanine 73-77 tyrosine hydroxylase Rattus norvegicus 125-127 41406-2 1979 Tyrosine hydroxylase and tryptophan hydroxylase activity was studied in different brain regions (hemispheres, striatum, midbrain and brainstem in vivo by measuring the accumulation of dihydroxyphenylalanine (Dopa) and 5-hydroxytryptophan (5-HTP) respectively, after inhibition of aromatic L-amino acid decarobyxlase with NSD 1015. Dihydroxyphenylalanine 184-206 tyrosine hydroxylase Rattus norvegicus 0-20