PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9172156-1 1997 Previous studies have demonstrated that the synergistic interaction of acidic fibroblast growth factor (aFGF) and a number of co-activator molecules (dopamine, TPA, IBMX/forskolin) can induce the novel expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in non-TH-expressing neurons. Catecholamines 220-233 tyrosine hydroxylase Homo sapiens 254-274 9172156-1 1997 Previous studies have demonstrated that the synergistic interaction of acidic fibroblast growth factor (aFGF) and a number of co-activator molecules (dopamine, TPA, IBMX/forskolin) can induce the novel expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in non-TH-expressing neurons. Catecholamines 220-233 tyrosine hydroxylase Homo sapiens 276-278 9172156-1 1997 Previous studies have demonstrated that the synergistic interaction of acidic fibroblast growth factor (aFGF) and a number of co-activator molecules (dopamine, TPA, IBMX/forskolin) can induce the novel expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in non-TH-expressing neurons. Catecholamines 220-233 tyrosine hydroxylase Homo sapiens 287-289 8723206-4 1996 The study of a key enzyme in the synthesis of catecholamines, tyrosine hydroxylase (TH), has provided clues about these adaptive responses. Catecholamines 46-60 tyrosine hydroxylase Homo sapiens 62-82 8990146-4 1997 All three cell types in the composite tumor and all chromaffin cells in both nodular and nonnodular areas of the remaining medulla were strongly immunoreactive for tyrosine hydroxylase, the rate-limiting enzyme in catecholamine synthesis. Catecholamines 214-227 tyrosine hydroxylase Homo sapiens 164-184 8912950-2 1996 In an attempt to identify the involved genes, several linkage and association studies have focused on the gene coding for tyrosine hydroxylase, the rate-limiting enzyme in catecholamine synthesis. Catecholamines 172-185 tyrosine hydroxylase Homo sapiens 122-142 8767166-7 1996 It has been proposed that immature beta cells could express tyrosine hydroxylase, the first enzyme of the catecholamine biosynthetic pathway, but additional markers are needed to further characterize these immature cells. Catecholamines 106-119 tyrosine hydroxylase Homo sapiens 60-80 8723206-4 1996 The study of a key enzyme in the synthesis of catecholamines, tyrosine hydroxylase (TH), has provided clues about these adaptive responses. Catecholamines 46-60 tyrosine hydroxylase Homo sapiens 84-86 7559551-1 1995 We reported recently that the gene that encodes tyrosine hydroxylase (TH), the rate-limiting enzyme in the biosynthesis of catecholamines, is regulated by hypoxia in the dopaminergic cells of the mammalian carotid body (Czyzyk-Krzeska, M. F., Bayliss, D. A., Lawson, E. E. & Millhorn, D. E. (1992) J. Neurochem. Catecholamines 123-137 tyrosine hydroxylase Homo sapiens 48-68 9182249-1 1996 Catecholamine biosynthesis is regulated by tyrosine hydroxylase (TH) requiring tetrahydrobiopterin (BH4) as the cofactor. Catecholamines 0-13 tyrosine hydroxylase Homo sapiens 43-63 9182249-1 1996 Catecholamine biosynthesis is regulated by tyrosine hydroxylase (TH) requiring tetrahydrobiopterin (BH4) as the cofactor. Catecholamines 0-13 tyrosine hydroxylase Homo sapiens 65-67 8771559-2 1996 PACAP induced dose-and time-dependent increases in mRNAs for the catecholamine synthesizing enzymes, tyrosine hydroxylase (TH) and dopamine beta-hydroxylase (DBH), with maximal 6- and 4-fold increases occurring at 8-16 h, respectively. Catecholamines 65-78 tyrosine hydroxylase Homo sapiens 101-121 8771559-2 1996 PACAP induced dose-and time-dependent increases in mRNAs for the catecholamine synthesizing enzymes, tyrosine hydroxylase (TH) and dopamine beta-hydroxylase (DBH), with maximal 6- and 4-fold increases occurring at 8-16 h, respectively. Catecholamines 65-78 tyrosine hydroxylase Homo sapiens 123-125 8984738-4 1996 The study of a key enzyme in the synthesis of catecholamines, tyrosine hydroxylase (TH), has provided clues about these adaptive responses. Catecholamines 46-60 tyrosine hydroxylase Homo sapiens 62-82 8984738-4 1996 The study of a key enzyme in the synthesis of catecholamines, tyrosine hydroxylase (TH), has provided clues about these adaptive responses. Catecholamines 46-60 tyrosine hydroxylase Homo sapiens 84-86 8699193-5 1996 Occasional neurons with immunoreactivity to the catecholamine-synthesizing enzyme, tyrosine hydroxylase, were also observed. Catecholamines 48-61 tyrosine hydroxylase Homo sapiens 83-103 7559551-1 1995 We reported recently that the gene that encodes tyrosine hydroxylase (TH), the rate-limiting enzyme in the biosynthesis of catecholamines, is regulated by hypoxia in the dopaminergic cells of the mammalian carotid body (Czyzyk-Krzeska, M. F., Bayliss, D. A., Lawson, E. E. & Millhorn, D. E. (1992) J. Neurochem. Catecholamines 123-137 tyrosine hydroxylase Homo sapiens 70-72 7790865-1 1995 Cell type-specific expression of the catecholamine synthetic enzyme, tyrosine hydroxylase (TH), appears to be mediated in part by cis-acting elements located at the 3" end of the human gene. Catecholamines 37-50 tyrosine hydroxylase Homo sapiens 69-89 7790865-1 1995 Cell type-specific expression of the catecholamine synthetic enzyme, tyrosine hydroxylase (TH), appears to be mediated in part by cis-acting elements located at the 3" end of the human gene. Catecholamines 37-50 tyrosine hydroxylase Homo sapiens 91-93 7551967-0 1995 Association of polymorphic VNTR region in the first intron of the human TH gene with disturbances of the catecholamine pathway in schizophrenia. Catecholamines 105-118 tyrosine hydroxylase Homo sapiens 72-74 7551967-4 1995 These results suggest that the polymorphic intron 1 of the human TH gene may be associated with disturbances of the catecholamine pathway in schizophrenia. Catecholamines 116-129 tyrosine hydroxylase Homo sapiens 65-67 7743482-2 1995 The feasibility and clinical value of using the reverse transcriptase-(RT) polymerase chain reaction (PCR) to amplify mRNA for tyrosine hydroxylase (TH), the first enzyme of catecholamine synthesis, was evaluated to detect neuroblastoma cells in patient samples. Catecholamines 174-187 tyrosine hydroxylase Homo sapiens 127-147 7743482-2 1995 The feasibility and clinical value of using the reverse transcriptase-(RT) polymerase chain reaction (PCR) to amplify mRNA for tyrosine hydroxylase (TH), the first enzyme of catecholamine synthesis, was evaluated to detect neuroblastoma cells in patient samples. Catecholamines 174-187 tyrosine hydroxylase Homo sapiens 149-151 7602797-4 1995 As a first step toward understanding the molecular mechanisms by which catecholamine synthesis is controlled in the tumor, we measured the levels of mRNA coding for the catecholamine synthesizing enzyme, tyrosine hydroxylase (TH) and catecholamines in 6 pheochromocytomas and 2 normal adrenal glands. Catecholamines 71-84 tyrosine hydroxylase Homo sapiens 204-224 7602797-6 1995 There was a close correlation between the TH mRNA level and the catecholamines content in the tumors. Catecholamines 64-78 tyrosine hydroxylase Homo sapiens 42-44 7602797-9 1995 These findings indicate that catecholamine overproduction in pheochromocytomas is mediated by the overexpression of genes coding for catecholamines synthesizing enzymes, TH, DBH, and AADC. Catecholamines 29-42 tyrosine hydroxylase Homo sapiens 170-172 7602797-9 1995 These findings indicate that catecholamine overproduction in pheochromocytomas is mediated by the overexpression of genes coding for catecholamines synthesizing enzymes, TH, DBH, and AADC. Catecholamines 133-147 tyrosine hydroxylase Homo sapiens 170-172 7545067-1 1995 Previous studies demonstrated that the cooperative interaction of acidic fibroblast growth factor (aFGF) and a partner molecule could induce the novel expression of the catecholamine (CA) biosynthetic enzyme, tyrosine hydroxylase (TH) in striatal neurons [Du and Iacovitti, J. Catecholamines 169-182 tyrosine hydroxylase Homo sapiens 209-229 7545067-1 1995 Previous studies demonstrated that the cooperative interaction of acidic fibroblast growth factor (aFGF) and a partner molecule could induce the novel expression of the catecholamine (CA) biosynthetic enzyme, tyrosine hydroxylase (TH) in striatal neurons [Du and Iacovitti, J. Catecholamines 169-182 tyrosine hydroxylase Homo sapiens 231-233 7527848-1 1994 Substances found in the soluble extract of muscle can alter the differentiative fate of certain brain neurons in culture by triggering novel expression of the gene for the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) (Iacovitti et al., 1989; Iacovitt, 1991). Catecholamines 172-185 tyrosine hydroxylase Homo sapiens 206-226 7735898-2 1995 In addition, dopamine beta-hydroxylase (DBH) and tyrosine hydroxylase (TH), two enzymes involved in catecholamine synthesis, were localized immunohistochemically to delineate hepatic sympathetic nerve fibres. Catecholamines 100-113 tyrosine hydroxylase Homo sapiens 71-73 7527848-1 1994 Substances found in the soluble extract of muscle can alter the differentiative fate of certain brain neurons in culture by triggering novel expression of the gene for the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) (Iacovitti et al., 1989; Iacovitt, 1991). Catecholamines 172-185 tyrosine hydroxylase Homo sapiens 228-230 7912958-4 1994 The increase in catecholamine metabolite levels could be due to stimulation of tyrosine hydroxylase (TH) activity in the catecholaminergic systems of this region. Catecholamines 16-29 tyrosine hydroxylase Homo sapiens 79-99 7719703-1 1994 Tyrosine hydroxylase (TH) is the key enzyme in the synthesis of catecholamines and may therefore be of aetiological relevance in the development of psychiatric illness. Catecholamines 64-78 tyrosine hydroxylase Homo sapiens 0-20 7719703-1 1994 Tyrosine hydroxylase (TH) is the key enzyme in the synthesis of catecholamines and may therefore be of aetiological relevance in the development of psychiatric illness. Catecholamines 64-78 tyrosine hydroxylase Homo sapiens 22-24 7804822-1 1994 In humans, the RNA for tyrosine hydroxylase (TH), the rate-limiting enzyme in the synthesis of catecholamines, can undergo alternative splicing to produce four different types of mRNA. Catecholamines 95-109 tyrosine hydroxylase Homo sapiens 23-43 7804822-1 1994 In humans, the RNA for tyrosine hydroxylase (TH), the rate-limiting enzyme in the synthesis of catecholamines, can undergo alternative splicing to produce four different types of mRNA. Catecholamines 95-109 tyrosine hydroxylase Homo sapiens 45-47 7912958-4 1994 The increase in catecholamine metabolite levels could be due to stimulation of tyrosine hydroxylase (TH) activity in the catecholaminergic systems of this region. Catecholamines 16-29 tyrosine hydroxylase Homo sapiens 101-103 7523477-1 1994 The intracellular localization of tyrosine hydroxylase (TH), which is the rate limiting enzyme in catecholamine (CA) biosynthesis, and its activity in various adrenal and other neuroendocrine tumors was studied. Catecholamines 98-111 tyrosine hydroxylase Homo sapiens 34-54 7523477-0 1994 Tyrosine hydroxylase indicates cell differentiation of catecholamine biosynthesis in neuroendocrine tumors. Catecholamines 55-68 tyrosine hydroxylase Homo sapiens 0-20 7523477-1 1994 The intracellular localization of tyrosine hydroxylase (TH), which is the rate limiting enzyme in catecholamine (CA) biosynthesis, and its activity in various adrenal and other neuroendocrine tumors was studied. Catecholamines 98-111 tyrosine hydroxylase Homo sapiens 56-58 1377728-7 1992 An immunohistochemical examination using the avidin-biotin procedure revealed that many SRF cells (estimated 57% of all SRF cells) were immunoreactive for tyrosine hydroxylase (TH, a marker of catecholamine cells). Catecholamines 193-206 tyrosine hydroxylase Homo sapiens 177-179 8093477-3 1993 This study examined the distribution of fibers, terminals, and cell bodies that are immunoreactive for tyrosine hydroxylase (TH) (the rate-limiting enzyme in the synthesis of catecholamines) in song-control nuclei of adult males and females and juvenile males. Catecholamines 175-189 tyrosine hydroxylase Homo sapiens 103-123 8093477-3 1993 This study examined the distribution of fibers, terminals, and cell bodies that are immunoreactive for tyrosine hydroxylase (TH) (the rate-limiting enzyme in the synthesis of catecholamines) in song-control nuclei of adult males and females and juvenile males. Catecholamines 175-189 tyrosine hydroxylase Homo sapiens 125-127 7909954-1 1993 The present study was undertaken to determine if gene expression for tyrosine hydroxylase (TH), the rate limiting enzyme in the biosynthesis of catecholamines, is regulated in the carotid body, sympathetic ganglia and adrenal medulla by hypoxia. Catecholamines 144-158 tyrosine hydroxylase Homo sapiens 69-89 7909954-1 1993 The present study was undertaken to determine if gene expression for tyrosine hydroxylase (TH), the rate limiting enzyme in the biosynthesis of catecholamines, is regulated in the carotid body, sympathetic ganglia and adrenal medulla by hypoxia. Catecholamines 144-158 tyrosine hydroxylase Homo sapiens 91-93 7909954-5 1993 Our results show that TH gene expression is regulated by hypoxia in the carotid body but not in other peripheral catecholamine synthesizing tissue and that the regulatory mechanism is intrinsic to type I cells. Catecholamines 113-126 tyrosine hydroxylase Homo sapiens 22-24 1355073-2 1992 Alterations in dopaminergic and noradrenergic neurotransmission have been implicated in the pathogenesis of this disease, and tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of these two catecholamines. Catecholamines 210-224 tyrosine hydroxylase Homo sapiens 126-146 1355073-2 1992 Alterations in dopaminergic and noradrenergic neurotransmission have been implicated in the pathogenesis of this disease, and tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of these two catecholamines. Catecholamines 210-224 tyrosine hydroxylase Homo sapiens 148-150 19912803-1 1991 Tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine biosynthesis, has been reported to be present in interneurons in human cerebral cortex. Catecholamines 55-68 tyrosine hydroxylase Homo sapiens 0-20 1353277-7 1992 TH is a rate-limiting enzyme of catecholamine biosynthesis and deficiency of TH is an important feature of extra-adrenal non-functioning phaeochromocytomas. Catecholamines 32-45 tyrosine hydroxylase Homo sapiens 0-2 19912803-1 1991 Tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine biosynthesis, has been reported to be present in interneurons in human cerebral cortex. Catecholamines 55-68 tyrosine hydroxylase Homo sapiens 22-24 1673911-2 1991 Tyrosine hydroxylase (TH) is the first and rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 67-80 tyrosine hydroxylase Homo sapiens 0-20 1673911-2 1991 Tyrosine hydroxylase (TH) is the first and rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 67-80 tyrosine hydroxylase Homo sapiens 22-24 1975102-3 1990 The tyrosine hydroxylase gene encodes the rate-limiting enzyme in the synthesis of catecholamines and might be a candidate for causing the manic-depressive phenotype. Catecholamines 83-97 tyrosine hydroxylase Homo sapiens 4-24 1977891-1 1990 The expression of the catecholamine biosynthetic enzyme, tyrosine hydroxylase (TH), is confined to several different types of neuroendocrine cells. Catecholamines 22-35 tyrosine hydroxylase Homo sapiens 57-77 1977891-1 1990 The expression of the catecholamine biosynthetic enzyme, tyrosine hydroxylase (TH), is confined to several different types of neuroendocrine cells. Catecholamines 22-35 tyrosine hydroxylase Homo sapiens 79-81 1980840-1 1990 We have examined the soma diameters and distribution of catecholaminergic (CA) cells in human retinae, by using an antibody to tyrosine hydroxylase (TH), the rate limiting enzyme in the production of catecholamines. Catecholamines 200-214 tyrosine hydroxylase Homo sapiens 127-147 1969278-7 1990 Perhaps TH-positive, catecholamine-negative neurons are more common than previously held or alternatively, TH expression in non-catecholamine neurons is induced by perturbations such as grafting brain tissue. Catecholamines 128-141 tyrosine hydroxylase Homo sapiens 107-109 1968265-0 1990 Tyrosine hydroxylase and enkephalin in nuclei of the solitary tracts: co-existence and convergent synaptic input to catecholamine neurons. Catecholamines 116-129 tyrosine hydroxylase Homo sapiens 0-20 20504631-1 1990 Phosphorylation of tyrosine hydroxylase, the rate-limiting enzyme, by a variety of protein kinases provides multiple mechanisms for the regulation of catecholamine synthesis. Catecholamines 150-163 tyrosine hydroxylase Homo sapiens 19-39 2573869-1 1989 A population of neurons situated in the human cerebral neocortex contains mRNA coding for tyrosine hydroxylase, the key enzyme for catecholamine biosynthesis. Catecholamines 131-144 tyrosine hydroxylase Homo sapiens 90-110 35013193-1 2022 Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the biosynthesis of dopamine (DA) and other catecholamines, and its dysfunction leads to DA deficiency and parkinsonisms. Catecholamines 106-120 tyrosine hydroxylase Homo sapiens 0-20 35013193-1 2022 Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the biosynthesis of dopamine (DA) and other catecholamines, and its dysfunction leads to DA deficiency and parkinsonisms. Catecholamines 106-120 tyrosine hydroxylase Homo sapiens 22-24 35013193-2 2022 Inhibition by catecholamines and reactivation by S40 phosphorylation are key regulatory mechanisms of TH activity and conformational stability. Catecholamines 14-28 tyrosine hydroxylase Homo sapiens 102-104 2575455-2 1989 Tyrosine hydroxylase (TH) is a rate-limiting enzyme for catecholamine biosynthesis, and it is a pterin-requiring monooxygenase. Catecholamines 56-69 tyrosine hydroxylase Homo sapiens 0-20 2575455-2 1989 Tyrosine hydroxylase (TH) is a rate-limiting enzyme for catecholamine biosynthesis, and it is a pterin-requiring monooxygenase. Catecholamines 56-69 tyrosine hydroxylase Homo sapiens 22-24 2887082-2 1987 An immunohistochemical study on tyrosine hydroxylase (TH), a rate-limiting enzyme in the catecholamine synthesizing pathway, was made on three craniocervical region paragangliomas, two of which showed metastases to the cervical lymph nodes. Catecholamines 89-102 tyrosine hydroxylase Homo sapiens 32-52 2905105-1 1988 In two groups of silver foxes--i.e. selected by the domestic type of behaviour and aggressive ones--studies have been made on the activity of the key enzyme in biosynthesis of catecholamines--i.e. tyrosine hydroxylase from the brain. Catecholamines 176-190 tyrosine hydroxylase Homo sapiens 197-217 2902075-1 1988 Tyrosine hydroxylase (TH) is a rate-limiting enzyme for catecholamine biosynthesis. Catecholamines 56-69 tyrosine hydroxylase Homo sapiens 0-20 2902075-1 1988 Tyrosine hydroxylase (TH) is a rate-limiting enzyme for catecholamine biosynthesis. Catecholamines 56-69 tyrosine hydroxylase Homo sapiens 22-24 2898127-1 1988 The gene for the catecholamine biosynthetic enzyme, tyrosine hydroxylase (TH), has been previously mapped to human chromosome 11 p15.5 in the vicinity of the loci for insulin (INS) and for the oncogene Harvey Ras 1 (HRAS). Catecholamines 17-30 tyrosine hydroxylase Homo sapiens 52-72 2898127-1 1988 The gene for the catecholamine biosynthetic enzyme, tyrosine hydroxylase (TH), has been previously mapped to human chromosome 11 p15.5 in the vicinity of the loci for insulin (INS) and for the oncogene Harvey Ras 1 (HRAS). Catecholamines 17-30 tyrosine hydroxylase Homo sapiens 74-76 2903607-2 1988 An esthesioneuroblastoma in a 16-year-old male was studied ultrastructurally and immunohistochemically, using antiserum against tyrosine hydroxylase (TH), a rate-limiting enzyme in the catecholamine-synthesizing pathway. Catecholamines 185-198 tyrosine hydroxylase Homo sapiens 128-148 2903607-2 1988 An esthesioneuroblastoma in a 16-year-old male was studied ultrastructurally and immunohistochemically, using antiserum against tyrosine hydroxylase (TH), a rate-limiting enzyme in the catecholamine-synthesizing pathway. Catecholamines 185-198 tyrosine hydroxylase Homo sapiens 150-152 2887168-1 1987 Tyrosine hydroxylase, the rate-limiting enzyme in the biosynthesis of catecholamines, was reversibly inactivated by incubation with antipain, which is known as a microbial protease inhibitor. Catecholamines 70-84 tyrosine hydroxylase Homo sapiens 0-20 2882428-2 1987 Tyrosine hydroxylase (TH) is the first enzyme in the pathway of catecholamine synthesis. Catecholamines 64-77 tyrosine hydroxylase Homo sapiens 0-20 2882428-2 1987 Tyrosine hydroxylase (TH) is the first enzyme in the pathway of catecholamine synthesis. Catecholamines 64-77 tyrosine hydroxylase Homo sapiens 22-24 2567605-1 1989 A parietal lobe ganglioglioma in a 61-year-old male was investigated ultrastructurally and immunohistochemically, using antiserum against tyrosine hydroxylase (TH), a rate-limiting enzyme of the catecholamine (CA)-synthesizing pathway. Catecholamines 195-208 tyrosine hydroxylase Homo sapiens 138-158 2567605-1 1989 A parietal lobe ganglioglioma in a 61-year-old male was investigated ultrastructurally and immunohistochemically, using antiserum against tyrosine hydroxylase (TH), a rate-limiting enzyme of the catecholamine (CA)-synthesizing pathway. Catecholamines 195-208 tyrosine hydroxylase Homo sapiens 160-162 2566138-1 1989 We carried out an immunohistochemical study of the Auerbach"s and Meissner"s plexuses of the human alimentary tract, using antiserum against tyrosine hydroxylase (TH), a rate-limiting enzyme of the catecholamine-synthesizing pathway. Catecholamines 198-211 tyrosine hydroxylase Homo sapiens 141-161 2566138-1 1989 We carried out an immunohistochemical study of the Auerbach"s and Meissner"s plexuses of the human alimentary tract, using antiserum against tyrosine hydroxylase (TH), a rate-limiting enzyme of the catecholamine-synthesizing pathway. Catecholamines 198-211 tyrosine hydroxylase Homo sapiens 163-165 2563268-0 1989 Catecholamine innervation of the human cerebral cortex as revealed by comparative immunohistochemistry of tyrosine hydroxylase and dopamine-beta-hydroxylase. Catecholamines 0-13 tyrosine hydroxylase Homo sapiens 106-126 2906039-1 1988 Tyrosine hydroxylase (TH) is the rate-limiting enzyme for catecholamine biosynthesis and a candidate gene for manic-depressive illness. Catecholamines 58-71 tyrosine hydroxylase Homo sapiens 0-20 2906039-1 1988 Tyrosine hydroxylase (TH) is the rate-limiting enzyme for catecholamine biosynthesis and a candidate gene for manic-depressive illness. Catecholamines 58-71 tyrosine hydroxylase Homo sapiens 22-24 2887276-1 1987 A parietal lobe ganglioglioma in a 2-year-old girl was investigated ultrastructurally and immunohistochemically, using antiserum against tyrosine hydroxylase (TH), a rate-limiting enzyme of the catecholamine (CA)-synthesizing pathway. Catecholamines 194-207 tyrosine hydroxylase Homo sapiens 137-157 2887276-1 1987 A parietal lobe ganglioglioma in a 2-year-old girl was investigated ultrastructurally and immunohistochemically, using antiserum against tyrosine hydroxylase (TH), a rate-limiting enzyme of the catecholamine (CA)-synthesizing pathway. Catecholamines 194-207 tyrosine hydroxylase Homo sapiens 159-161 2879374-0 1986 Correlation between tyrosine hydroxylase immunoreactive cells in tumors and urinary catecholamine output in neuroblastoma patients. Catecholamines 84-97 tyrosine hydroxylase Homo sapiens 20-40 2879374-2 1986 Although no correlations could be found between the immunoreactive pattern and the site of origin or the staging of the tumor, a positive relationship between the urinary catecholamine output and the density of TH-immunoreactive cells could be established. Catecholamines 171-184 tyrosine hydroxylase Homo sapiens 211-213 2876427-1 1986 Tyrosine hydroxylase [TyrOHase; L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2], an essential enzyme in the synthesis of catecholamines, is expressed normally by neurons in the brainstem but not by those in mature neocortex. Catecholamines 160-174 tyrosine hydroxylase Homo sapiens 0-20 2876427-1 1986 Tyrosine hydroxylase [TyrOHase; L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2], an essential enzyme in the synthesis of catecholamines, is expressed normally by neurons in the brainstem but not by those in mature neocortex. Catecholamines 160-174 tyrosine hydroxylase Homo sapiens 22-30 2875048-2 1986 Biochemical assays examined the neurotransmitter synthesizing enzymes tyrosine hydroxylase (TOH) for catecholamines and choline acetyltransferase (CAT) for acetylcholine. Catecholamines 101-115 tyrosine hydroxylase Homo sapiens 92-95 2871556-1 1986 Tyrosine hydroxylase [TyrOHase; tyrosine 3-monooxygenase; L-tyrosine,tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2] and phenylethanolamine N-methyltransferase, EC 2.1.1.28) are involved in catecholamine biosynthesis and are considered soluble proteins. Catecholamines 217-230 tyrosine hydroxylase Homo sapiens 32-56 2894459-2 1987 In view of the catecholamine hypothesis of this disorder, the gene encoding tyrosine hydroxylase (TH) the limiting enzyme in catecholamines is a good candidate to investigate. Catecholamines 15-28 tyrosine hydroxylase Homo sapiens 76-96 2894459-2 1987 In view of the catecholamine hypothesis of this disorder, the gene encoding tyrosine hydroxylase (TH) the limiting enzyme in catecholamines is a good candidate to investigate. Catecholamines 125-139 tyrosine hydroxylase Homo sapiens 76-96 2879289-1 1987 Tyrosine hydroxylase [TyrOHase, tyrosine 3-monooxygenase, L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (2-hydroxylating), EC 1.14.16.2] is the rate-limiting enzyme in the synthetic pathway of catecholamines and is expressed by neurons containing dopamine, norepinephrine, and epinephrine. Catecholamines 201-215 tyrosine hydroxylase Homo sapiens 32-56 2878337-1 1986 A rapid, simple and sensitive assay has been developed for tyrosine-3-monooxygenase, the enzyme catalyzing the rate-limiting step in catecholamine biosynthesis. Catecholamines 133-146 tyrosine hydroxylase Homo sapiens 59-83 2887082-2 1987 An immunohistochemical study on tyrosine hydroxylase (TH), a rate-limiting enzyme in the catecholamine synthesizing pathway, was made on three craniocervical region paragangliomas, two of which showed metastases to the cervical lymph nodes. Catecholamines 89-102 tyrosine hydroxylase Homo sapiens 54-56 2887082-7 1987 Application of the TH immunohistochemistry to further cases appears important for the better understanding of this neoplasm, a catecholamine-producing tumor. Catecholamines 127-140 tyrosine hydroxylase Homo sapiens 19-21 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 tyrosine hydroxylase Homo sapiens 36-56 2870726-0 1986 [Topography of the catecholamine neurons in the brain stem of the human fetus: an immunohistochemical study using antibodies to tyrosine hydroxylase]. Catecholamines 19-32 tyrosine hydroxylase Homo sapiens 128-148 2870726-1 1986 Immunohistochemistry using antibodies to tyrosine hydroxylase (TH), a rate-limiting enzyme which catalyzes the initial step in the catecholamine synthesizing pathway, has been widely accepted as one of the methods for identification of catecholamine neurons in the nervous system. Catecholamines 131-144 tyrosine hydroxylase Homo sapiens 41-61 2870726-1 1986 Immunohistochemistry using antibodies to tyrosine hydroxylase (TH), a rate-limiting enzyme which catalyzes the initial step in the catecholamine synthesizing pathway, has been widely accepted as one of the methods for identification of catecholamine neurons in the nervous system. Catecholamines 131-144 tyrosine hydroxylase Homo sapiens 63-65 2870726-1 1986 Immunohistochemistry using antibodies to tyrosine hydroxylase (TH), a rate-limiting enzyme which catalyzes the initial step in the catecholamine synthesizing pathway, has been widely accepted as one of the methods for identification of catecholamine neurons in the nervous system. Catecholamines 236-249 tyrosine hydroxylase Homo sapiens 41-61 2870726-1 1986 Immunohistochemistry using antibodies to tyrosine hydroxylase (TH), a rate-limiting enzyme which catalyzes the initial step in the catecholamine synthesizing pathway, has been widely accepted as one of the methods for identification of catecholamine neurons in the nervous system. Catecholamines 236-249 tyrosine hydroxylase Homo sapiens 63-65 2867555-1 1985 We found that the catecholamine biosynthetic enzymes, tyrosine hydroxylase, dopamine B-hydroxylase and phenylethanolamine N-methyltransferase share similar protein domains in their primary structures, and therefore are coded for by a single gene or a family of genes. Catecholamines 18-31 tyrosine hydroxylase Homo sapiens 54-74 2863177-1 1985 We found that the catecholamine biosynthetic enzymes tyrosine hydroxylase (TH) (EC 1.14.16.2), dopamine beta-hydroxylase (EC 1.14.17.1), and phenylethanolamine N-methyltransferase (EC 2.1.1.28) share similar protein domains in their primary structures and that they share common gene coding sequences. Catecholamines 18-31 tyrosine hydroxylase Homo sapiens 53-73 2863177-1 1985 We found that the catecholamine biosynthetic enzymes tyrosine hydroxylase (TH) (EC 1.14.16.2), dopamine beta-hydroxylase (EC 1.14.17.1), and phenylethanolamine N-methyltransferase (EC 2.1.1.28) share similar protein domains in their primary structures and that they share common gene coding sequences. Catecholamines 18-31 tyrosine hydroxylase Homo sapiens 75-77 6151589-3 1984 In catecholamine neurons, stained positively with the antisera to TH, specific immunoreactions were found in the LBs. Catecholamines 3-16 tyrosine hydroxylase Homo sapiens 66-68 6151589-7 1984 In catecholamine neurons in which LBs frequently occurred, TH enzyme protein might play an important part in the productions of LBs. Catecholamines 3-16 tyrosine hydroxylase Homo sapiens 59-61 6146657-1 1984 The systems responsible for phosphorylating tyrosine hydroxylase, the rate-limiting enzyme of catecholamine biosynthesis, were investigated in situ in adrenal medullary cells made permeable to solutes of up to 1,000 dalton by exposure to brief intense electric fields. Catecholamines 94-107 tyrosine hydroxylase Homo sapiens 44-64 6152375-1 1984 We found that catecholamine biosynthetic enzymes, tyrosine hydroxylase, dopamine B-hydroxylase and phenylethanolamine N-methyl-transferase share similar protein domains in their primary structures, and therefore are coded for by a single gene or a family of genes. Catecholamines 14-27 tyrosine hydroxylase Homo sapiens 50-70 6137760-1 1983 Tyrosine hydroxylase is considered to be the rate-limiting enzyme in the synthesis of catecholamines in both the central and peripheral nervous system. Catecholamines 86-100 tyrosine hydroxylase Homo sapiens 0-20 6141853-1 1984 We postulate that the catecholamine synthesizing enzyme, tyrosine hydroxylase (TH), dopamine B-hydroxylase (DBH) and phenylethanolamine N-methyltransferase (PNMT) are coded for by similar gene coding sequence(s). Catecholamines 22-35 tyrosine hydroxylase Homo sapiens 57-77 6136012-1 1983 Using a specific antibody to the catecholamine (CA) synthesizing enzyme, tyrosine hydroxylase (TH), in combination with the avidin-biotin-peroxidase complex method, we have found evidence for the existence of a new CA-containing cell group extending from the orbitofrontal cortex through the olfactory and pyriform cortices in the brain of two species of monkey. Catecholamines 33-46 tyrosine hydroxylase Homo sapiens 73-93 6136012-1 1983 Using a specific antibody to the catecholamine (CA) synthesizing enzyme, tyrosine hydroxylase (TH), in combination with the avidin-biotin-peroxidase complex method, we have found evidence for the existence of a new CA-containing cell group extending from the orbitofrontal cortex through the olfactory and pyriform cortices in the brain of two species of monkey. Catecholamines 33-46 tyrosine hydroxylase Homo sapiens 95-97 6132348-0 1983 Human brainstem catecholamine neuronal anatomy as indicated by immunocytochemistry with antibodies to tyrosine hydroxylase. Catecholamines 16-29 tyrosine hydroxylase Homo sapiens 102-122 239788-0 1975 Studies on tyrosine hydroxylase in neuroblastoma in relation to urinary levels of catecholamine metabolites. Catecholamines 82-95 tyrosine hydroxylase Homo sapiens 11-31 6111380-1 1981 Monoclonal antibodies were produced against tyrosine hydroxylase (TH), the enzyme catalyzing the rate limiting step in catecholamine neurotransmitter synthesis. Catecholamines 119-132 tyrosine hydroxylase Homo sapiens 44-64 6111380-1 1981 Monoclonal antibodies were produced against tyrosine hydroxylase (TH), the enzyme catalyzing the rate limiting step in catecholamine neurotransmitter synthesis. Catecholamines 119-132 tyrosine hydroxylase Homo sapiens 66-68 6249456-4 1980 Tyrosine hydroxylase is needed for the conversion of tyrosine to dopamine (DA) and norpinephrine (NE); altering the level of this enzyme could affect catecholamine (CA) turnover. Catecholamines 150-163 tyrosine hydroxylase Homo sapiens 0-20 6104663-0 1980 Tyrosine 3-monooxygenase regulates catecholamine synthesis in pheochromocytoma cells. Catecholamines 35-48 tyrosine hydroxylase Homo sapiens 0-24 6104663-9 1980 These results provide direct evidence that tyrosine 3-monooxygenase regulates catecholamine synthesis in pheochromocytoma cells and that incubation with 56 mM K+ or with cholera toxin causes the activation of this enzyme in these cells. Catecholamines 78-91 tyrosine hydroxylase Homo sapiens 43-67 4402349-0 1972 Tyrosine hydroxylase in human adrenal and pheochromocytoma: localization, kinetics, and catecholamine inhibition. Catecholamines 88-101 tyrosine hydroxylase Homo sapiens 0-20 32668278-5 2020 Tyrosine hydroxylase (TH) was expressed in >90% of adrenal, abdominal, and thoracic PGLs but only in 37% of head and neck PGLs reflecting their variable catecholamine synthesis. Catecholamines 153-166 tyrosine hydroxylase Homo sapiens 0-20 33309753-1 2021 Tyrosine hydroxylase (TH) catalyses the (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)-dependent conversion of l-tyrosine to L-3,4-dihydroxyphenylalanine (l-Dopa), which is the rate-limiting step in the synthesis of dopamine and other catecholamine neurotransmitters and hormones. Catecholamines 237-250 tyrosine hydroxylase Homo sapiens 0-20 33309753-1 2021 Tyrosine hydroxylase (TH) catalyses the (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)-dependent conversion of l-tyrosine to L-3,4-dihydroxyphenylalanine (l-Dopa), which is the rate-limiting step in the synthesis of dopamine and other catecholamine neurotransmitters and hormones. Catecholamines 237-250 tyrosine hydroxylase Homo sapiens 22-24 33992806-1 2022 Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in catecholamine (CA) biosynthesis pathway making TH a molecular target for controlling CA production, specifically dopamine. Catecholamines 62-75 tyrosine hydroxylase Homo sapiens 0-20 33992806-1 2022 Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in catecholamine (CA) biosynthesis pathway making TH a molecular target for controlling CA production, specifically dopamine. Catecholamines 62-75 tyrosine hydroxylase Homo sapiens 22-24 33992806-1 2022 Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in catecholamine (CA) biosynthesis pathway making TH a molecular target for controlling CA production, specifically dopamine. Catecholamines 62-75 tyrosine hydroxylase Homo sapiens 109-111 33437193-2 2021 Tyrosine hydroxylase (TH) and phenylethanolamine N-methyltransferase (PNMT) are two of the main enzymes of catecholamines (CA) synthesis. Catecholamines 107-121 tyrosine hydroxylase Homo sapiens 0-20 33437193-2 2021 Tyrosine hydroxylase (TH) and phenylethanolamine N-methyltransferase (PNMT) are two of the main enzymes of catecholamines (CA) synthesis. Catecholamines 107-121 tyrosine hydroxylase Homo sapiens 22-24 32668278-5 2020 Tyrosine hydroxylase (TH) was expressed in >90% of adrenal, abdominal, and thoracic PGLs but only in 37% of head and neck PGLs reflecting their variable catecholamine synthesis. Catecholamines 153-166 tyrosine hydroxylase Homo sapiens 22-24 33654949-12 2019 Since TH is not exclusively expressed on sympathetic fibers, but also in a number of catecholamine-producing cells, a prerequisite for automated determination of fiber densities is to reliably distinguish between cells and fibers. Catecholamines 85-98 tyrosine hydroxylase Homo sapiens 6-8 31529487-2 2020 Tyrosine hydroxylase (TH), a key enzyme of catecholamine synthesis, is regulated by multiple neuronal signaling pathways through phosphorylation at serine 19 (Ser19), serine 31 (Ser31) and serine 40 (Ser40) located in the flexible, far N-terminal region of the regulatory domain. Catecholamines 43-56 tyrosine hydroxylase Homo sapiens 0-20 31529487-2 2020 Tyrosine hydroxylase (TH), a key enzyme of catecholamine synthesis, is regulated by multiple neuronal signaling pathways through phosphorylation at serine 19 (Ser19), serine 31 (Ser31) and serine 40 (Ser40) located in the flexible, far N-terminal region of the regulatory domain. Catecholamines 43-56 tyrosine hydroxylase Homo sapiens 22-24 31035382-9 2019 Correlations with PPGL tissue data led us to conclude that catecholamine biosynthesis under hypoxia is mainly mediated through increased phosphorylation of TH, regulated as a short-term response (24-48 h) by HIF1alpha. Catecholamines 59-72 tyrosine hydroxylase Homo sapiens 156-158 31419477-2 2019 TH converts tyrosine into L-DOPA, which is the direct precursor of catecholamine biosynthesis. Catecholamines 67-80 tyrosine hydroxylase Homo sapiens 0-2 30714137-1 2019 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamines dopamine, noradrenaline and adrenaline. Catecholamines 78-92 tyrosine hydroxylase Homo sapiens 0-20 30714137-1 2019 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamines dopamine, noradrenaline and adrenaline. Catecholamines 78-92 tyrosine hydroxylase Homo sapiens 22-24 29995172-3 2019 Tyrosine hydroxylase (TH), tetrahydrobiopterin (BH4)-dependent and iron-containing monooxygenase, catalyzes the conversion of L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA), which is the initial and rate-limiting step in the biosynthesis of catecholamines (DA, noradrenaline, and adrenaline). Catecholamines 246-260 tyrosine hydroxylase Homo sapiens 0-20 29995172-3 2019 Tyrosine hydroxylase (TH), tetrahydrobiopterin (BH4)-dependent and iron-containing monooxygenase, catalyzes the conversion of L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA), which is the initial and rate-limiting step in the biosynthesis of catecholamines (DA, noradrenaline, and adrenaline). Catecholamines 246-260 tyrosine hydroxylase Homo sapiens 22-24 29995172-4 2019 PD affects specifically TH-containing catecholamine neurons. Catecholamines 38-51 tyrosine hydroxylase Homo sapiens 24-26 30361782-1 2019 Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of catecholamines and has been connected to aggravated progression of periodontal disease under chronic stress. Catecholamines 79-93 tyrosine hydroxylase Homo sapiens 0-20 30361782-1 2019 Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of catecholamines and has been connected to aggravated progression of periodontal disease under chronic stress. Catecholamines 79-93 tyrosine hydroxylase Homo sapiens 22-24 27389777-1 2017 Tyrosine hydroxylase (TH), a rate-limiting step in catecholamine synthesis in which its activity influences Alzheimer disease, Parkinson disease, and IQ of schizophrenia patients, has been studied for a long time. Catecholamines 51-64 tyrosine hydroxylase Homo sapiens 0-20 30411798-1 2019 Tyrosine hydroxylase (TH) is a multi-domain, homo-oligomeric enzyme that catalyses the rate-limiting step of catecholamine neurotransmitter biosynthesis. Catecholamines 109-122 tyrosine hydroxylase Homo sapiens 0-20 30411798-1 2019 Tyrosine hydroxylase (TH) is a multi-domain, homo-oligomeric enzyme that catalyses the rate-limiting step of catecholamine neurotransmitter biosynthesis. Catecholamines 109-122 tyrosine hydroxylase Homo sapiens 22-24 29331395-4 2018 Given that the loss of dopamine, and its rate-limiting enzyme tyrosine hydroxylase (TH) occurs in PD, the expression and accompanying post-translational changes in TH during PD progression could yield insight into the disruption of cellular signalling occurring in the CNS, and also in peripheral tissues wherein catecholamine function plays a role. Catecholamines 313-326 tyrosine hydroxylase Homo sapiens 84-86 29331395-4 2018 Given that the loss of dopamine, and its rate-limiting enzyme tyrosine hydroxylase (TH) occurs in PD, the expression and accompanying post-translational changes in TH during PD progression could yield insight into the disruption of cellular signalling occurring in the CNS, and also in peripheral tissues wherein catecholamine function plays a role. Catecholamines 313-326 tyrosine hydroxylase Homo sapiens 164-166 29404959-1 2018 Tyrosine hydroxylase (Th) encodes the rate-limiting enzyme in catecholamine biosynthesis, and the regulation of its transcription is critical for the specification and maintenance of catecholaminergic neuron phenotypes. Catecholamines 62-75 tyrosine hydroxylase Homo sapiens 0-20 29404959-1 2018 Tyrosine hydroxylase (Th) encodes the rate-limiting enzyme in catecholamine biosynthesis, and the regulation of its transcription is critical for the specification and maintenance of catecholaminergic neuron phenotypes. Catecholamines 62-75 tyrosine hydroxylase Homo sapiens 22-24 27389777-1 2017 Tyrosine hydroxylase (TH), a rate-limiting step in catecholamine synthesis in which its activity influences Alzheimer disease, Parkinson disease, and IQ of schizophrenia patients, has been studied for a long time. Catecholamines 51-64 tyrosine hydroxylase Homo sapiens 22-24 27491309-1 2016 Tyrosine hydroxylase (TH), which was discovered at the National Institutes of Health (NIH) in 1964, is a tetrahydrobiopterin (BH4)-requiring monooxygenase that catalyzes the first and rate-limiting step in the biosynthesis of catecholamines (CAs), such as dopamine, noradrenaline, and adrenaline. Catecholamines 226-240 tyrosine hydroxylase Homo sapiens 0-20 28275384-2 2016 Tyrosine hydroxylase (TH), a rate-limiting enzyme in the synthesis of catecholamine, has been highlighted because genetic variations of TH could alter the activity of the sympathetic nervous system activity and subsequently contribute to the pathogenesis of hypertension. Catecholamines 70-83 tyrosine hydroxylase Homo sapiens 0-20 28275384-2 2016 Tyrosine hydroxylase (TH), a rate-limiting enzyme in the synthesis of catecholamine, has been highlighted because genetic variations of TH could alter the activity of the sympathetic nervous system activity and subsequently contribute to the pathogenesis of hypertension. Catecholamines 70-83 tyrosine hydroxylase Homo sapiens 22-24 28275384-2 2016 Tyrosine hydroxylase (TH), a rate-limiting enzyme in the synthesis of catecholamine, has been highlighted because genetic variations of TH could alter the activity of the sympathetic nervous system activity and subsequently contribute to the pathogenesis of hypertension. Catecholamines 70-83 tyrosine hydroxylase Homo sapiens 136-138 27491309-1 2016 Tyrosine hydroxylase (TH), which was discovered at the National Institutes of Health (NIH) in 1964, is a tetrahydrobiopterin (BH4)-requiring monooxygenase that catalyzes the first and rate-limiting step in the biosynthesis of catecholamines (CAs), such as dopamine, noradrenaline, and adrenaline. Catecholamines 226-240 tyrosine hydroxylase Homo sapiens 22-24 26869038-4 2016 Catecholamine synthesis depends on the rate-limiting enzyme, tyrosine hydroxylase, whose expression is associated with working memory and the response to chronic stress. Catecholamines 0-13 tyrosine hydroxylase Homo sapiens 61-81 27626030-3 2016 Nicotine also induces tyrosine hydroxylase (TH) gene expression, leading to increased synthesis of catecholamines. Catecholamines 99-113 tyrosine hydroxylase Homo sapiens 22-42 27626030-3 2016 Nicotine also induces tyrosine hydroxylase (TH) gene expression, leading to increased synthesis of catecholamines. Catecholamines 99-113 tyrosine hydroxylase Homo sapiens 44-46 27462005-1 2016 Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the biosynthesis of catecholamine neurotransmitters. Catecholamines 82-95 tyrosine hydroxylase Homo sapiens 0-20 27462005-1 2016 Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the biosynthesis of catecholamine neurotransmitters. Catecholamines 82-95 tyrosine hydroxylase Homo sapiens 22-24 27133786-6 2016 Under chronic unpredictable stress, the adrenergic nervous system was markedly activated, as the expression of tyrosine hydroxylase, the rate-limiting enzyme in catecholamine biosynthesis, in bone marrow and colonic epithelium was enhanced, especially in the myenteric ganglia. Catecholamines 161-174 tyrosine hydroxylase Homo sapiens 111-131 27689101-6 2016 To achieve this goal we have evaluated in vivo three partial sequences of the promoter for human tyrosine hydroxylase, the rate limiting enzyme in catecholamine synthesis. Catecholamines 147-160 tyrosine hydroxylase Homo sapiens 97-117 26647061-3 2016 We studied immunohistochemically the expression of tyrosine hydroxylase (TH, first limiting enzyme for catecholamine synthesis) in LC neurons of 15 autopsied infants (brains collected from the Greek Brain Bank) in relation to the neuropathological changes of acute or chronic HII of the neonatal brain. Catecholamines 103-116 tyrosine hydroxylase Homo sapiens 51-71 28525692-2 2016 The majority of the principal ganglionic sympathetic neurons is noradrenergic and expresses tyrosine hydroxylase (TH), i.e., a key enzyme in catecholamine synthesis. Catecholamines 141-154 tyrosine hydroxylase Homo sapiens 92-112 26647061-3 2016 We studied immunohistochemically the expression of tyrosine hydroxylase (TH, first limiting enzyme for catecholamine synthesis) in LC neurons of 15 autopsied infants (brains collected from the Greek Brain Bank) in relation to the neuropathological changes of acute or chronic HII of the neonatal brain. Catecholamines 103-116 tyrosine hydroxylase Homo sapiens 73-75 26284527-3 2015 Tyrosine hydroxylase catalyzes the rate-limiting step in the catecholamine biosynthesis and is linked to several common neurological disorders such as Parkinson"s and schizophrenia. Catecholamines 61-74 tyrosine hydroxylase Homo sapiens 0-20 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 tyrosine hydroxylase Homo sapiens 193-213 25946206-2 2015 Several reports have shown that adrenal glucocorticoids (GC) play an important regulatory role on the genes encoding the main enzymes involved in catecholamine (CAT) synthesis i.e. tyrosine hydroxylase (TH), dopamine beta-hydroxylase (DBH) and phenylethanolamine N-methyltransferase (PNMT). Catecholamines 146-159 tyrosine hydroxylase Homo sapiens 181-201 25960279-2 2015 We have performed a screening of 10,000 compounds searching for pharmacological chaperones of tyrosine hydroxylase (TH), the tetrahydrobiopterin (BH4)-dependent enzyme that catalyzes the rate-limiting step in the synthesis of catecholamines. Catecholamines 226-240 tyrosine hydroxylase Homo sapiens 94-114 25960279-2 2015 We have performed a screening of 10,000 compounds searching for pharmacological chaperones of tyrosine hydroxylase (TH), the tetrahydrobiopterin (BH4)-dependent enzyme that catalyzes the rate-limiting step in the synthesis of catecholamines. Catecholamines 226-240 tyrosine hydroxylase Homo sapiens 116-118 26024204-1 2015 Tyrosine hydroxylase is a mononuclear non-heme iron monooxygenase found in the central nervous system that catalyzes the hydroxylation of tyrosine to yield L-3,4-dihydroxyphenylalanine, the rate-limiting step in the biosynthesis of catecholamine neurotransmitters. Catecholamines 232-245 tyrosine hydroxylase Homo sapiens 0-20 25946206-2 2015 Several reports have shown that adrenal glucocorticoids (GC) play an important regulatory role on the genes encoding the main enzymes involved in catecholamine (CAT) synthesis i.e. tyrosine hydroxylase (TH), dopamine beta-hydroxylase (DBH) and phenylethanolamine N-methyltransferase (PNMT). Catecholamines 146-159 tyrosine hydroxylase Homo sapiens 203-205 24283218-2 2013 In addition, tyrosine hydroxylase, the rate-limiting enzyme for the synthesis of catecholamines, is expressed in 8-10% of dorsal root ganglia (DRG) neurons, suggesting that dopamine may be released in the dorsal root ganglia. Catecholamines 81-95 tyrosine hydroxylase Homo sapiens 13-33 25677368-4 2015 Therefore, our aim was to demonstrate the presence of catecholamine-synthesizing enzymes, i.e. tyrosine hydroxylase (TH), aromatic L-amino acid decarboxylase (AADC) and dopamine beta-hydroxylase (DBH) in HNPGL tissue. Catecholamines 54-67 tyrosine hydroxylase Homo sapiens 95-115 25677368-4 2015 Therefore, our aim was to demonstrate the presence of catecholamine-synthesizing enzymes, i.e. tyrosine hydroxylase (TH), aromatic L-amino acid decarboxylase (AADC) and dopamine beta-hydroxylase (DBH) in HNPGL tissue. Catecholamines 54-67 tyrosine hydroxylase Homo sapiens 117-119 24535440-6 2014 Consistent with these data, mRNAs coding for catecholamine synthesizing enzymes, i.e. tyrosine hydroxylase (TH), aromatic l-amino acid decarboxylase, and dopamine-beta-hydroxylase were detected by RT-PCR in cultured endothelial cells from SMA. Catecholamines 45-58 tyrosine hydroxylase Homo sapiens 86-106 24535440-6 2014 Consistent with these data, mRNAs coding for catecholamine synthesizing enzymes, i.e. tyrosine hydroxylase (TH), aromatic l-amino acid decarboxylase, and dopamine-beta-hydroxylase were detected by RT-PCR in cultured endothelial cells from SMA. Catecholamines 45-58 tyrosine hydroxylase Homo sapiens 108-110 24417771-2 2014 Tyrosine hydroxylase (TH) is the rate-limiting enzyme for the biosynthesis of catecholamine, including dopamine and noradrenaline. Catecholamines 78-91 tyrosine hydroxylase Homo sapiens 0-20 24417771-2 2014 Tyrosine hydroxylase (TH) is the rate-limiting enzyme for the biosynthesis of catecholamine, including dopamine and noradrenaline. Catecholamines 78-91 tyrosine hydroxylase Homo sapiens 22-24 24417771-9 2014 CONCLUSIONS: The present data suggest that the biosynthesis of catecholamine by the action of TH should be deeply involved in decreased intellectual ability in patients with schizophrenia. Catecholamines 63-76 tyrosine hydroxylase Homo sapiens 94-96 24055376-1 2014 Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of catecholamine neurotransmitters, and a reduction in TH activity is associated with several neurological diseases. Catecholamines 79-92 tyrosine hydroxylase Homo sapiens 0-20 24055376-1 2014 Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of catecholamine neurotransmitters, and a reduction in TH activity is associated with several neurological diseases. Catecholamines 79-92 tyrosine hydroxylase Homo sapiens 22-24 25230230-4 2014 This reaction is considered as rate-limiting step in the biosynthesis of catecholamines, dopamine, norepinephrine and epinephrine, which has made TH an important target for drug development. Catecholamines 73-87 tyrosine hydroxylase Homo sapiens 146-148 23647001-0 2013 The role of tetrahydrobiopterin and catecholamines in the developmental regulation of tyrosine hydroxylase level in the brain. Catecholamines 36-50 tyrosine hydroxylase Homo sapiens 86-106 23647001-7 2013 Our data demonstrate that BH4 and catecholamines are required for the post-natal augmentation of TH protein in the brain, and suggest that BH4 availability in early post-natal period is critical for the developmental regulation of TH protein level. Catecholamines 34-48 tyrosine hydroxylase Homo sapiens 97-99 23647001-7 2013 Our data demonstrate that BH4 and catecholamines are required for the post-natal augmentation of TH protein in the brain, and suggest that BH4 availability in early post-natal period is critical for the developmental regulation of TH protein level. Catecholamines 34-48 tyrosine hydroxylase Homo sapiens 231-233 23946762-2 2013 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 57-70 tyrosine hydroxylase Homo sapiens 0-20 23946762-2 2013 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 57-70 tyrosine hydroxylase Homo sapiens 22-24 23537934-1 2013 Tyrosine hydroxylase (TH) catalyses the rate-limiting step in the biosynthesis of catecholamines. Catecholamines 82-96 tyrosine hydroxylase Homo sapiens 0-20 23537934-1 2013 Tyrosine hydroxylase (TH) catalyses the rate-limiting step in the biosynthesis of catecholamines. Catecholamines 82-96 tyrosine hydroxylase Homo sapiens 22-24 23537934-3 2013 Because of its key regulatory role in central and peripheral catecholamine synthesis, TH is associated with the pathogenesis of several neurological and psychiatric diseases, including Parkinson"s disease, dystonia, schizophrenia, affective disorders, and cardiovascular diseases. Catecholamines 61-74 tyrosine hydroxylase Homo sapiens 86-88 23621023-1 2013 Tyrosine hydroxylase, the rate-limiting enzyme of catecholamine biosysthesis, is predominantly expressed in several cell groups within the brain, including the dopaminergic neurons of the substantia nigra and ventral tegmental area. Catecholamines 50-63 tyrosine hydroxylase Homo sapiens 0-20 23481708-3 2013 We studied the expression of tyrosine hydroxylase (TH), the first and rate-limiting enzyme in catecholamine synthesis, in substantia nigra, and ventral tegmental area of 18 neonates in relation to the age and severity/duration of hypoxic injury estimated by neuropathological criteria. Catecholamines 94-107 tyrosine hydroxylase Homo sapiens 29-49 23481708-3 2013 We studied the expression of tyrosine hydroxylase (TH), the first and rate-limiting enzyme in catecholamine synthesis, in substantia nigra, and ventral tegmental area of 18 neonates in relation to the age and severity/duration of hypoxic injury estimated by neuropathological criteria. Catecholamines 94-107 tyrosine hydroxylase Homo sapiens 51-53 22925890-2 2012 Since tyrosine hydroxylase is the rate-limiting step in catecholamine synthesis, an effect of ascorbate to increase tyrosine hydroxylase protein could contribute to its ability to increase or sustain catecholamine synthesis. Catecholamines 56-69 tyrosine hydroxylase Homo sapiens 6-26 23246742-1 2013 AIMS: Tyrosine hydroxylase (TH) and GTP cyclohydrolase I (GCH) are the rate-limiting enzymes for the biosynthesis of catecholamines and tetrahydrobiopterin (BH4), respectively. Catecholamines 117-131 tyrosine hydroxylase Homo sapiens 6-26 23246742-1 2013 AIMS: Tyrosine hydroxylase (TH) and GTP cyclohydrolase I (GCH) are the rate-limiting enzymes for the biosynthesis of catecholamines and tetrahydrobiopterin (BH4), respectively. Catecholamines 117-131 tyrosine hydroxylase Homo sapiens 28-30 23069677-6 2013 Tyrosine hydroxylase (TH) is the rate-limiting enzyme for the synthesis of catecholamines; and the TH level was used to assess by inference, NE output. Catecholamines 75-89 tyrosine hydroxylase Homo sapiens 0-20 23069677-6 2013 Tyrosine hydroxylase (TH) is the rate-limiting enzyme for the synthesis of catecholamines; and the TH level was used to assess by inference, NE output. Catecholamines 75-89 tyrosine hydroxylase Homo sapiens 22-24 24054137-1 2013 Tyrosine hydroxylase (TH), the rate-limiting enzyme in the biosynthesis of catecholamines, is a key protein involved in the pathogenesis of neurodegenerative diseases such as Parkinson"s disease. Catecholamines 75-89 tyrosine hydroxylase Homo sapiens 0-20 24054137-1 2013 Tyrosine hydroxylase (TH), the rate-limiting enzyme in the biosynthesis of catecholamines, is a key protein involved in the pathogenesis of neurodegenerative diseases such as Parkinson"s disease. Catecholamines 75-89 tyrosine hydroxylase Homo sapiens 22-24 24054138-1 2013 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline, and adrenaline. Catecholamines 81-95 tyrosine hydroxylase Homo sapiens 0-20 24054138-1 2013 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline, and adrenaline. Catecholamines 81-95 tyrosine hydroxylase Homo sapiens 22-24 24054138-2 2013 In response to short-term stimuli, TH activity is regulated by feedback inhibition by the catecholamines and relief of that inhibition by phosphorylation. Catecholamines 90-104 tyrosine hydroxylase Homo sapiens 35-37 22925890-2 2012 Since tyrosine hydroxylase is the rate-limiting step in catecholamine synthesis, an effect of ascorbate to increase tyrosine hydroxylase protein could contribute to its ability to increase or sustain catecholamine synthesis. Catecholamines 200-213 tyrosine hydroxylase Homo sapiens 116-136 23080186-3 2012 Tyrosine hydroxylase (TH) is the rate-limiting enzyme for catecholamine synthesis. Catecholamines 58-71 tyrosine hydroxylase Homo sapiens 0-20 22483310-3 2012 Tyrosine hydroxylase (TH) is an important neuronal enzyme that, in the presence of tetrahydrobiopterin, catalyzes the initial and rate-limiting step in the biosynthesis of the catecholamine neurotransmitters dopamine (DA) and norepinephrine, and is frequently used as a marker of DAergic neuronal loss in animal models of PD. Catecholamines 176-189 tyrosine hydroxylase Homo sapiens 0-20 22483310-3 2012 Tyrosine hydroxylase (TH) is an important neuronal enzyme that, in the presence of tetrahydrobiopterin, catalyzes the initial and rate-limiting step in the biosynthesis of the catecholamine neurotransmitters dopamine (DA) and norepinephrine, and is frequently used as a marker of DAergic neuronal loss in animal models of PD. Catecholamines 176-189 tyrosine hydroxylase Homo sapiens 22-24 22483314-1 2012 Tyrosine hydroxylase (TH) is the rate limiting step in the biosynthesis of dopamine and other catecholamines. Catecholamines 94-108 tyrosine hydroxylase Homo sapiens 0-20 22483314-1 2012 Tyrosine hydroxylase (TH) is the rate limiting step in the biosynthesis of dopamine and other catecholamines. Catecholamines 94-108 tyrosine hydroxylase Homo sapiens 22-24 22483316-1 2012 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in brain catecholamine biosynthesis, and tetrahydrobiopterin is its cofactor. Catecholamines 63-76 tyrosine hydroxylase Homo sapiens 0-20 22483316-1 2012 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in brain catecholamine biosynthesis, and tetrahydrobiopterin is its cofactor. Catecholamines 63-76 tyrosine hydroxylase Homo sapiens 22-24 22583429-0 2012 Molecular docking study of catecholamines and [4-(propan-2-yl) phenyl]carbamic acid with tyrosine hydroxylase. Catecholamines 27-41 tyrosine hydroxylase Homo sapiens 89-109 22583429-2 2012 As the classical disease-related motor symptoms are associated with the loss of dopamine-generating cells within the substantia nigra, tyrosine hydroxylase (TH), the rate-limiting enzyme in the synthesis of catecholamines has become an important target in the development of Parkinson"s disease drug candidates, with the focus to augment TH levels or its activity. Catecholamines 207-221 tyrosine hydroxylase Homo sapiens 135-155 22583429-2 2012 As the classical disease-related motor symptoms are associated with the loss of dopamine-generating cells within the substantia nigra, tyrosine hydroxylase (TH), the rate-limiting enzyme in the synthesis of catecholamines has become an important target in the development of Parkinson"s disease drug candidates, with the focus to augment TH levels or its activity. Catecholamines 207-221 tyrosine hydroxylase Homo sapiens 157-159 22583429-3 2012 By contrast, TH inhibitors are of relevance in the treatment of conditions associated with catecholamine over-production, as occurs in pheochromocytomas. Catecholamines 91-104 tyrosine hydroxylase Homo sapiens 13-15 22583429-4 2012 To aid characterizing new drug candidates, a molecular docking study of catecholamines and a novel hypothetical compound [4-(propan-2-yl) phenyl]carbamic acid (PPCA) with TH is described. Catecholamines 72-86 tyrosine hydroxylase Homo sapiens 171-173 22583429-7 2012 Our results corroborated a "hexa interacting amino acids unit" located in this deep narrow groove crucial to the interaction of PPCA and the studied catecholamines with TH, whereby the "His361-His336 dyad" was found to be even more crucial to these binding interactions. Catecholamines 149-163 tyrosine hydroxylase Homo sapiens 169-171 23080186-3 2012 Tyrosine hydroxylase (TH) is the rate-limiting enzyme for catecholamine synthesis. Catecholamines 58-71 tyrosine hydroxylase Homo sapiens 22-24 23080186-4 2012 Several studies have examined the effects of hypoxia on catecholamines by focusing on the regulation of TH. Catecholamines 56-70 tyrosine hydroxylase Homo sapiens 104-106 22001923-1 2011 Tyrosine hydroxylase (TH) is the first and rate-limiting enzyme in the biosynthesis of catecholamines, and its expression is regulated in a developmental stage- and cell type-specific manner. Catecholamines 87-101 tyrosine hydroxylase Homo sapiens 0-20 21803145-1 2011 The activity of tyrosine hydroxylase (TH, EC 1.14.16.2) gene and protein determines the catecholamine level, which, in turn, is crucial for the organism homeostasis. Catecholamines 88-101 tyrosine hydroxylase Homo sapiens 16-36 21803145-1 2011 The activity of tyrosine hydroxylase (TH, EC 1.14.16.2) gene and protein determines the catecholamine level, which, in turn, is crucial for the organism homeostasis. Catecholamines 88-101 tyrosine hydroxylase Homo sapiens 38-40 22913142-1 2012 The distribution of tyrosine hydroxylase (TH), a key enzyme of catecholamine synthesis, was studied immunocytochemically in the neurons of substantia nigra in the human brain (n=7), and localization of neuromelanin in these cells was determined. Catecholamines 63-76 tyrosine hydroxylase Homo sapiens 20-40 22913142-1 2012 The distribution of tyrosine hydroxylase (TH), a key enzyme of catecholamine synthesis, was studied immunocytochemically in the neurons of substantia nigra in the human brain (n=7), and localization of neuromelanin in these cells was determined. Catecholamines 63-76 tyrosine hydroxylase Homo sapiens 42-44 22001923-1 2011 Tyrosine hydroxylase (TH) is the first and rate-limiting enzyme in the biosynthesis of catecholamines, and its expression is regulated in a developmental stage- and cell type-specific manner. Catecholamines 87-101 tyrosine hydroxylase Homo sapiens 22-24 21907185-6 2011 The expression of catecholamine-synthesizing enzymes including tyrosine hydroxylase (TH) and dopamine beta hydroxylase (DBH) were analyzed on mRNA and protein levels. Catecholamines 18-31 tyrosine hydroxylase Homo sapiens 63-83 21907185-6 2011 The expression of catecholamine-synthesizing enzymes including tyrosine hydroxylase (TH) and dopamine beta hydroxylase (DBH) were analyzed on mRNA and protein levels. Catecholamines 18-31 tyrosine hydroxylase Homo sapiens 85-87 21302933-1 2011 Phosphorylation of Ser40 in the regulatory domain of tyrosine hydroxylase activates the enzyme by increasing the rate constant for dissociation of inhibitory catecholamines from the active site by 3 orders of magnitude. Catecholamines 158-172 tyrosine hydroxylase Homo sapiens 53-73 21176768-1 2011 Tyrosine hydroxylase is the rate-limiting enzyme of catecholamine biosynthesis; it uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to DOPA. Catecholamines 52-65 tyrosine hydroxylase Homo sapiens 0-20 19396395-0 2009 Role of N-terminus of tyrosine hydroxylase in the biosynthesis of catecholamines. Catecholamines 66-80 tyrosine hydroxylase Homo sapiens 22-42 20838244-1 2010 The purpose of this study was to determine whether the increased expression of tyrosine hydroxylase (TH), the first and limiting enzyme in catecholamine synthesis in vasopressin (VP) neurons of the human neonate, represents a primary developmental phenomenon or reflects a secondary phenomenon related to the activation of VP systems due to perinatal hypoxia. Catecholamines 139-152 tyrosine hydroxylase Homo sapiens 79-99 20838244-1 2010 The purpose of this study was to determine whether the increased expression of tyrosine hydroxylase (TH), the first and limiting enzyme in catecholamine synthesis in vasopressin (VP) neurons of the human neonate, represents a primary developmental phenomenon or reflects a secondary phenomenon related to the activation of VP systems due to perinatal hypoxia. Catecholamines 139-152 tyrosine hydroxylase Homo sapiens 101-103 20124442-1 2010 BACKGROUND: Tyrosine hydroxylase (TH) is the rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 69-82 tyrosine hydroxylase Homo sapiens 12-32 20124442-1 2010 BACKGROUND: Tyrosine hydroxylase (TH) is the rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 69-82 tyrosine hydroxylase Homo sapiens 34-36 21087208-1 2011 TH (tyrosine hydroxylase) is the rate-limiting enzyme in the synthesis of catecholamines. Catecholamines 74-88 tyrosine hydroxylase Homo sapiens 4-24 19958792-3 2010 Tyrosine hydroxylase (TH) is the initial and rate-limiting enzyme in the biosynthesis of catecholamines such as dopamine and norepinephrine, which are deeply involved in human mental functions and behaviors. Catecholamines 89-103 tyrosine hydroxylase Homo sapiens 0-20 19958792-3 2010 Tyrosine hydroxylase (TH) is the initial and rate-limiting enzyme in the biosynthesis of catecholamines such as dopamine and norepinephrine, which are deeply involved in human mental functions and behaviors. Catecholamines 89-103 tyrosine hydroxylase Homo sapiens 22-24 19958792-4 2010 It has recently been reported that the C-824T single nucleotide polymorphism in the promoter region of the TH gene (rs10770141) affects promoter activity of the TH gene and urinary catecholamine levels. Catecholamines 181-194 tyrosine hydroxylase Homo sapiens 107-109 19801645-1 2009 Tyrosine hydroxylase (TH), the rate-limiting enzyme in the synthesis of catecholamines, is activated by phosphorylation-dependent binding to 14-3-3 proteins. Catecholamines 72-86 tyrosine hydroxylase Homo sapiens 0-20 19801645-1 2009 Tyrosine hydroxylase (TH), the rate-limiting enzyme in the synthesis of catecholamines, is activated by phosphorylation-dependent binding to 14-3-3 proteins. Catecholamines 72-86 tyrosine hydroxylase Homo sapiens 22-24 19396395-1 2009 Tyrosine hydroxylase (TH) catalyzes the conversion of L: -tyrosine to L: -dopa, which is the initial and rate-limiting step in the biosynthesis of catecholamines [CA; dopamine (DA), noradrenaline, and adrenaline], and plays a central role in the neurotransmission and hormonal actions of CA. Catecholamines 147-161 tyrosine hydroxylase Homo sapiens 0-20 19396395-1 2009 Tyrosine hydroxylase (TH) catalyzes the conversion of L: -tyrosine to L: -dopa, which is the initial and rate-limiting step in the biosynthesis of catecholamines [CA; dopamine (DA), noradrenaline, and adrenaline], and plays a central role in the neurotransmission and hormonal actions of CA. Catecholamines 147-161 tyrosine hydroxylase Homo sapiens 22-24 19591812-1 2009 Tyrosine hydroxylase, the rate-limiting enzyme in catecholamine synthesis, is known to contain naturally occurring genetic variation in it"s promoter region that associates with a number of neuropsychological disorders. Catecholamines 50-63 tyrosine hydroxylase Homo sapiens 0-20 18513370-1 2008 Tyrosine hydroxylase (TH), the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline and adrenaline, is regulated acutely by feedback inhibition by the catecholamines and relief of this inhibition by phosphorylation of serine 40 (Ser40). Catecholamines 79-93 tyrosine hydroxylase Homo sapiens 0-20 19671753-2 2009 One important marker for NB is the expression of tyrosine hydroxylase (TH), the first-step enzyme of catecholamine biosynthesis. Catecholamines 101-114 tyrosine hydroxylase Homo sapiens 49-69 19671753-2 2009 One important marker for NB is the expression of tyrosine hydroxylase (TH), the first-step enzyme of catecholamine biosynthesis. Catecholamines 101-114 tyrosine hydroxylase Homo sapiens 71-73 18208403-1 2008 The TH (tyrosine hydroxylase) gene encodes the rate-limiting enzyme of catecholamine biosynthesis, and is involved in the pathogenesis of hypertension, but the relationship of its variants with hypertension has not been extensively studied. Catecholamines 71-84 tyrosine hydroxylase Homo sapiens 8-28 18534229-2 2008 TH01, a tetrameric short tandem repeat marker in the tyrosine hydroxylase gene, regulates gene expression and catecholamine production. Catecholamines 110-123 tyrosine hydroxylase Homo sapiens 53-73 18513370-1 2008 Tyrosine hydroxylase (TH), the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline and adrenaline, is regulated acutely by feedback inhibition by the catecholamines and relief of this inhibition by phosphorylation of serine 40 (Ser40). Catecholamines 79-93 tyrosine hydroxylase Homo sapiens 22-24 18513370-1 2008 Tyrosine hydroxylase (TH), the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline and adrenaline, is regulated acutely by feedback inhibition by the catecholamines and relief of this inhibition by phosphorylation of serine 40 (Ser40). Catecholamines 185-199 tyrosine hydroxylase Homo sapiens 0-20 18513370-1 2008 Tyrosine hydroxylase (TH), the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline and adrenaline, is regulated acutely by feedback inhibition by the catecholamines and relief of this inhibition by phosphorylation of serine 40 (Ser40). Catecholamines 185-199 tyrosine hydroxylase Homo sapiens 22-24 18419768-1 2008 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of catecholamine neurotransmitters. Catecholamines 74-87 tyrosine hydroxylase Homo sapiens 0-20 18419768-1 2008 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of catecholamine neurotransmitters. Catecholamines 74-87 tyrosine hydroxylase Homo sapiens 22-24 18639636-4 2008 ATP increases phosphorylation of tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis, at Ser31 with a potency similar to that for ERK1/2 phosphorylation, the kinase responsible for TH phosphorylation at this site. Catecholamines 88-101 tyrosine hydroxylase Homo sapiens 33-53 18639636-4 2008 ATP increases phosphorylation of tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis, at Ser31 with a potency similar to that for ERK1/2 phosphorylation, the kinase responsible for TH phosphorylation at this site. Catecholamines 88-101 tyrosine hydroxylase Homo sapiens 55-57 18181650-1 2008 Tyrosine hydroxylase (TH) catalyzes the first step in the biosynthesis of catecholamines. Catecholamines 74-88 tyrosine hydroxylase Homo sapiens 0-20 18447638-5 2008 Furthermore, we showed enrichment of USSCs expressing tyrosine hydroxylase (TH), an enzyme specific for dopaminergic neurons and other catecholamine-producing neurons, accompanied by induction of Nurr1, a factor regulating dopaminergic neurogenesis. Catecholamines 135-148 tyrosine hydroxylase Homo sapiens 54-74 18447638-5 2008 Furthermore, we showed enrichment of USSCs expressing tyrosine hydroxylase (TH), an enzyme specific for dopaminergic neurons and other catecholamine-producing neurons, accompanied by induction of Nurr1, a factor regulating dopaminergic neurogenesis. Catecholamines 135-148 tyrosine hydroxylase Homo sapiens 76-78 18181650-1 2008 Tyrosine hydroxylase (TH) catalyzes the first step in the biosynthesis of catecholamines. Catecholamines 74-88 tyrosine hydroxylase Homo sapiens 22-24 18096443-1 2008 The human zinc finger protein 191 (ZNF191) is a Kruppel-like protein and can specifically interact with the widespread TCAT motif which constitutes the HUMTH01 microsatellite in the tyrosine hydroxylase (TH) gene (encoding the rate-limiting enzyme in the synthesis of catecholamines). Catecholamines 268-282 tyrosine hydroxylase Homo sapiens 182-202 18096443-1 2008 The human zinc finger protein 191 (ZNF191) is a Kruppel-like protein and can specifically interact with the widespread TCAT motif which constitutes the HUMTH01 microsatellite in the tyrosine hydroxylase (TH) gene (encoding the rate-limiting enzyme in the synthesis of catecholamines). Catecholamines 268-282 tyrosine hydroxylase Homo sapiens 155-157 18183302-7 2008 This region contains several genes which have previously been associated with the function of dopaminergic neurons, including the gene for tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine biosynthesis, IGF2, and CDKN1C, which cooperates with Nurr1 in directing the differentiation of dopaminergic neurons. Catecholamines 194-207 tyrosine hydroxylase Homo sapiens 139-159 17900529-1 2007 Tyrosine hydroxylase is the rate-limiting enzyme in catecholamine biosynthesis, and its N-terminus plays a critical role in the intracellular stability of the enzyme. Catecholamines 52-65 tyrosine hydroxylase Homo sapiens 0-20 17959316-9 2007 The present data indicate that the cerebellum does represent a target of methamphetamine, which produces specific and fine alterations of the catecholamine system involving synthesis, amount, and compartmentalization of TH as well as increased noradrenaline levels. Catecholamines 142-155 tyrosine hydroxylase Homo sapiens 220-222 17698732-16 2007 Catecholamine secretion is influenced by genetic variation in the adrenergic pathway encoding catecholamine synthesis, especially at the classically rate-limiting step, TH. Catecholamines 94-107 tyrosine hydroxylase Homo sapiens 169-171 17698732-0 2007 Tyrosine hydroxylase, the rate-limiting enzyme in catecholamine biosynthesis: discovery of common human genetic variants governing transcription, autonomic activity, and blood pressure in vivo. Catecholamines 50-63 tyrosine hydroxylase Homo sapiens 0-20 17698732-1 2007 BACKGROUND: Tyrosine hydroxylase (TH) is the rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 69-82 tyrosine hydroxylase Homo sapiens 12-32 17698732-1 2007 BACKGROUND: Tyrosine hydroxylase (TH) is the rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 69-82 tyrosine hydroxylase Homo sapiens 34-36 17698732-11 2007 In the TH promoter, significant associations were found for urinary catecholamine excretion and for blood pressure response to stress. Catecholamines 68-81 tyrosine hydroxylase Homo sapiens 7-9 17698732-16 2007 Catecholamine secretion is influenced by genetic variation in the adrenergic pathway encoding catecholamine synthesis, especially at the classically rate-limiting step, TH. Catecholamines 0-13 tyrosine hydroxylase Homo sapiens 169-171 17514580-1 2007 This review summarizes knowledge on the effects of stress on two catecholamine biosynthetic enzymes, tyrosine hydroxylase (TH) and phenylethanolamine N-methyltransferase (PNMT). Catecholamines 65-78 tyrosine hydroxylase Homo sapiens 101-121 17514580-1 2007 This review summarizes knowledge on the effects of stress on two catecholamine biosynthetic enzymes, tyrosine hydroxylase (TH) and phenylethanolamine N-methyltransferase (PNMT). Catecholamines 65-78 tyrosine hydroxylase Homo sapiens 123-125 16985181-2 2007 Here, we show that human Tregs constitutively express tyrosine hydroxylase (TH, EC 1.14.16.2), the rate-limiting enzyme in the synthesis of catecholamines, and contain substantial amounts of dopamine, norepinephrine, and epinephrine, which are released upon treatment with reserpine. Catecholamines 140-154 tyrosine hydroxylase Homo sapiens 54-74 25792770-0 2007 The catecholamine system in health and disease -Relation to tyrosine 3-monooxygenase and other catecholamine-synthesizing enzymes. Catecholamines 4-17 tyrosine hydroxylase Homo sapiens 60-84 25792770-0 2007 The catecholamine system in health and disease -Relation to tyrosine 3-monooxygenase and other catecholamine-synthesizing enzymes. Catecholamines 95-108 tyrosine hydroxylase Homo sapiens 60-84 17054915-1 2006 Tyrosine hydroxylase (tyrosine 3-monooxygenase, EC 1.14.16.2, TH) is the rate-limiting enzyme in the biosynthesis of catecholamine neurotransmitters, dopamine (DA), noradrenaline (NE), and adrenaline, in the neurons. Catecholamines 117-130 tyrosine hydroxylase Homo sapiens 0-20 17054915-1 2006 Tyrosine hydroxylase (tyrosine 3-monooxygenase, EC 1.14.16.2, TH) is the rate-limiting enzyme in the biosynthesis of catecholamine neurotransmitters, dopamine (DA), noradrenaline (NE), and adrenaline, in the neurons. Catecholamines 117-130 tyrosine hydroxylase Homo sapiens 22-46 16805833-2 2006 In this study, we investigated whether the retinoic acid receptor (RAR), a transcription factor specifically activated by all-trans-RA, could directly regulate transcription of tyrosine hydroxylase (TH), the first and rate-limiting step in the catecholamine biosynthesis pathway. Catecholamines 244-257 tyrosine hydroxylase Homo sapiens 177-197 16764822-1 2006 Tyrosine hydroxylase (TH), the biosynthetic enzyme of catecholamine, is synthesized specifically in catecholaminergic neurons. Catecholamines 54-67 tyrosine hydroxylase Homo sapiens 0-20 16764822-1 2006 Tyrosine hydroxylase (TH), the biosynthetic enzyme of catecholamine, is synthesized specifically in catecholaminergic neurons. Catecholamines 54-67 tyrosine hydroxylase Homo sapiens 22-24 16741673-17 2006 The presence of these additional populations of TH-positive neurons in the adult primate CNS has implications for functional catecholamine neurotransmission, its derangement in disease and drug abuse, and its rescue by gene therapeutic maneuvers in neurodegenerative diseases such as Parkinson"s disease. Catecholamines 125-138 tyrosine hydroxylase Homo sapiens 48-50 16805833-2 2006 In this study, we investigated whether the retinoic acid receptor (RAR), a transcription factor specifically activated by all-trans-RA, could directly regulate transcription of tyrosine hydroxylase (TH), the first and rate-limiting step in the catecholamine biosynthesis pathway. Catecholamines 244-257 tyrosine hydroxylase Homo sapiens 199-201 16644734-1 2006 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline, and adrenaline. Catecholamines 81-95 tyrosine hydroxylase Homo sapiens 0-20 16644734-1 2006 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline, and adrenaline. Catecholamines 81-95 tyrosine hydroxylase Homo sapiens 22-24 16672262-1 2006 Tyrosine hydroxylase (TH), an iron-containing enzyme, catalyzes the first and rate-limiting step of catecholamine biosynthesis, and requires tetrahydrobiopterin (BH4) as a cofactor. Catecholamines 100-113 tyrosine hydroxylase Homo sapiens 0-20 16360899-4 2006 In the present study, we investigated the association between personality traits and systematic combination of functional polymorphisms in three genes that regulate the metabolism of catecholamines, namely, tyrosine hydroxylase (TH), monoamine oxidase A (MAOA), and catechol-O-methyltransferase (COMT). Catecholamines 183-197 tyrosine hydroxylase Homo sapiens 207-227 16360899-4 2006 In the present study, we investigated the association between personality traits and systematic combination of functional polymorphisms in three genes that regulate the metabolism of catecholamines, namely, tyrosine hydroxylase (TH), monoamine oxidase A (MAOA), and catechol-O-methyltransferase (COMT). Catecholamines 183-197 tyrosine hydroxylase Homo sapiens 229-231 16052322-2 2005 Here, we demonstrate that four enzymes involved in the biosynthesis of catecholamines, namely, tyrosine hydroxylase (TH), aromatic amino acid decarboxylase (AADC), dopamine beta-hydroxylase (DBH) and phenylethanolamine- N-methyltransferase (PNMT), are expressed in Leydig cells of the human testis. Catecholamines 71-85 tyrosine hydroxylase Homo sapiens 95-115 17329957-2 2006 A tetranucleotide repeat polymorphism in the first intron of the tyrosine hydroxylase (TH) gene, encoding a rate-limiting enzyme for the synthesis of catecholamines, is reported to have the potential to control expression of the gene and to be associated with suicidal behavior in patients with adjustment disorders. Catecholamines 150-164 tyrosine hydroxylase Homo sapiens 65-85 17329957-2 2006 A tetranucleotide repeat polymorphism in the first intron of the tyrosine hydroxylase (TH) gene, encoding a rate-limiting enzyme for the synthesis of catecholamines, is reported to have the potential to control expression of the gene and to be associated with suicidal behavior in patients with adjustment disorders. Catecholamines 150-164 tyrosine hydroxylase Homo sapiens 87-89 17135716-1 2006 Tyrosine hydroxylase (TH), the first and limiting enzyme for catecholamine synthesis, has been identified immunohistochemically (IHC) in human neurosecretory neurons where it is found to colocalize with vasopressin (AVP) or oxytocin. Catecholamines 61-74 tyrosine hydroxylase Homo sapiens 0-20 17135716-1 2006 Tyrosine hydroxylase (TH), the first and limiting enzyme for catecholamine synthesis, has been identified immunohistochemically (IHC) in human neurosecretory neurons where it is found to colocalize with vasopressin (AVP) or oxytocin. Catecholamines 61-74 tyrosine hydroxylase Homo sapiens 22-24 17135716-3 2006 Since GTP cyclohydrolase I (GCHI), the first enzyme for tetrahydrobiopterin synthesis, the essential cofactor of TH, and aromatic L-amino acid decarboxylase (AADC) have so far not been detected in neurosecretory neurons, the functional role of TH in catecholamine synthesis is still questionable. Catecholamines 250-263 tyrosine hydroxylase Homo sapiens 113-115 16052322-2 2005 Here, we demonstrate that four enzymes involved in the biosynthesis of catecholamines, namely, tyrosine hydroxylase (TH), aromatic amino acid decarboxylase (AADC), dopamine beta-hydroxylase (DBH) and phenylethanolamine- N-methyltransferase (PNMT), are expressed in Leydig cells of the human testis. Catecholamines 71-85 tyrosine hydroxylase Homo sapiens 117-119 16052322-3 2005 Tyrosine hydroxylase, the key enzyme of the biosynthesis of catecholamines, was localized to Leydig cells both at the transcript level (by RT-PCR analyses and by in situ hybridization assays) and at the protein level (by immunoblotting and by immunohistochemistry). Catecholamines 60-74 tyrosine hydroxylase Homo sapiens 0-20 15787695-1 2005 The regulation of gene expression of tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis, was studied in brainstem noradrenergic nuclei, locus coeruleus (LC), A2 and A1, in vitro. Catecholamines 92-105 tyrosine hydroxylase Homo sapiens 37-57 15787695-1 2005 The regulation of gene expression of tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis, was studied in brainstem noradrenergic nuclei, locus coeruleus (LC), A2 and A1, in vitro. Catecholamines 92-105 tyrosine hydroxylase Homo sapiens 59-61 16210867-1 2005 Previous studies indicated that in the human paraventricular nucleus (PVN) and in the supraoptic nucleus (SON) tyrosine hydroxylase (TH) - the first and rate-limiting enzyme in catecholamine synthesis - is localized mainly in magnocellular neurosecretory neurons. Catecholamines 177-190 tyrosine hydroxylase Homo sapiens 111-131 16210867-1 2005 Previous studies indicated that in the human paraventricular nucleus (PVN) and in the supraoptic nucleus (SON) tyrosine hydroxylase (TH) - the first and rate-limiting enzyme in catecholamine synthesis - is localized mainly in magnocellular neurosecretory neurons. Catecholamines 177-190 tyrosine hydroxylase Homo sapiens 133-135 15367723-0 2004 Functional allelic heterogeneity and pleiotropy of a repeat polymorphism in tyrosine hydroxylase: prediction of catecholamines and response to stress in twins. Catecholamines 112-126 tyrosine hydroxylase Homo sapiens 76-96 15367723-1 2004 Tyrosine hydroxylase, the rate-limiting enzyme in catecholamine biosynthesis, has a common tetranucleotide repeat polymorphism, (TCAT)(n). Catecholamines 50-63 tyrosine hydroxylase Homo sapiens 0-20 15451190-14 2004 Tyrosine hydroxylase is the rate-limiting enzyme in catecholamine synthesis. Catecholamines 52-65 tyrosine hydroxylase Homo sapiens 0-20 15287903-1 2004 Tyrosine hydroxylase (TyrH), the catalyst for the key regulatory step in catecholamine biosynthesis, is phosphorylated by cAMP-dependent protein kinase A (PKA) on a serine residue in a regulatory domain. Catecholamines 73-86 tyrosine hydroxylase Homo sapiens 0-20 15322424-2 2004 DDC, like tyrosine hydroxylase (TH), is an enzyme involved in the catecholamine synthesis pathway and has recently been proposed as a specific marker of NB among pediatric malignancies. Catecholamines 66-79 tyrosine hydroxylase Homo sapiens 10-30 15675612-1 2004 The aim of this study was to shed more light on the developmental characteristics of human paraventricular nucleus (PVN) and hypothalamus in general, using modern immunohistochemical techniques to detect the activity of tyrosine hydroxylase (TH) in the synthesis of catecholamine (CA). Catecholamines 266-279 tyrosine hydroxylase Homo sapiens 220-240 15287903-0 2004 Effects of phosphorylation by protein kinase A on binding of catecholamines to the human tyrosine hydroxylase isoforms. Catecholamines 61-75 tyrosine hydroxylase Homo sapiens 89-109 15287903-1 2004 Tyrosine hydroxylase (TyrH), the catalyst for the key regulatory step in catecholamine biosynthesis, is phosphorylated by cAMP-dependent protein kinase A (PKA) on a serine residue in a regulatory domain. Catecholamines 73-86 tyrosine hydroxylase Homo sapiens 22-26 15104239-1 2004 Activation of human peripheral blood mononuclear cells (PBMC) triggers endogenous production of catecholamines (CA) through protein kinase (PK) C-dependent induction of tyrosine hydroxylase (TH; EC 1.14.16.2), the first and rate-limiting enzyme in the synthesis of CA. Catecholamines 96-110 tyrosine hydroxylase Homo sapiens 169-189 14993794-3 2004 In the adrenal medulla, tyrosine hydroxylase (TH) is the first enzyme in the pathway of catecholamine synthesis. Catecholamines 88-101 tyrosine hydroxylase Homo sapiens 24-44 14993794-3 2004 In the adrenal medulla, tyrosine hydroxylase (TH) is the first enzyme in the pathway of catecholamine synthesis. Catecholamines 88-101 tyrosine hydroxylase Homo sapiens 46-48 15104239-1 2004 Activation of human peripheral blood mononuclear cells (PBMC) triggers endogenous production of catecholamines (CA) through protein kinase (PK) C-dependent induction of tyrosine hydroxylase (TH; EC 1.14.16.2), the first and rate-limiting enzyme in the synthesis of CA. Catecholamines 96-110 tyrosine hydroxylase Homo sapiens 191-193 14758053-2 2004 METHODS: Immunohistochemistry for lymphoid organs (mesenteric lymph nodes, spleen and thymus) and lymphocytes was used to observe their expression of tyrosine hydroxylase (TH), an initial rate-limiting enzyme of the catecholamine synthesis. Catecholamines 216-229 tyrosine hydroxylase Homo sapiens 150-170 12694388-1 2003 Tyrosine hydroxylase (TH) catalyzes the first and rate-limiting step of catecholamine synthesis and its expression is necessary for neurotransmitter specification of all catecholaminergic neurons, while dopamine beta-hydroxylase (DBH) is essential for the noradrenergic phenotype. Catecholamines 72-85 tyrosine hydroxylase Homo sapiens 0-20 15579641-8 2004 Neurons expressing tyrosine hydroxylase (TH) were killed by 6-hydroxydopamine (6-OHDA), a neurotoxic catecholamine. Catecholamines 101-114 tyrosine hydroxylase Homo sapiens 19-39 14651989-1 2003 Tyrosine hydroxylase (TH), the rate-limiting enzyme of catecholamine biosynthesis, is predominantly expressed in several cell groups within the brain, including the dopaminergic (DA) neurons of the substantia nigra and ventral tegmental area, and the noradrenergic neurons of the locus coeruleus. Catecholamines 55-68 tyrosine hydroxylase Homo sapiens 0-20 14651989-1 2003 Tyrosine hydroxylase (TH), the rate-limiting enzyme of catecholamine biosynthesis, is predominantly expressed in several cell groups within the brain, including the dopaminergic (DA) neurons of the substantia nigra and ventral tegmental area, and the noradrenergic neurons of the locus coeruleus. Catecholamines 55-68 tyrosine hydroxylase Homo sapiens 22-24 12694388-1 2003 Tyrosine hydroxylase (TH) catalyzes the first and rate-limiting step of catecholamine synthesis and its expression is necessary for neurotransmitter specification of all catecholaminergic neurons, while dopamine beta-hydroxylase (DBH) is essential for the noradrenergic phenotype. Catecholamines 72-85 tyrosine hydroxylase Homo sapiens 22-24 12428766-2 2002 The microsatellite HUMTH01, located in the first intron of the Tyrosine Hydroxylase (TH) gene (encoding the rate-limiting enzyme in the synthesis of catecholamines), is characterized by a TCAT repeated motif and has been used in genetic studies of neuropsychiatric and other complex diseases, in which catecholaminergic neurotransmission is implicated. Catecholamines 149-163 tyrosine hydroxylase Homo sapiens 63-83 12571119-1 2003 In the mammalian neocortex, neurons containing tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis, constitute an enigmatic and ill-defined group of aspiny non-pyramidal cells. Catecholamines 102-115 tyrosine hydroxylase Homo sapiens 47-67 12571119-1 2003 In the mammalian neocortex, neurons containing tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis, constitute an enigmatic and ill-defined group of aspiny non-pyramidal cells. Catecholamines 102-115 tyrosine hydroxylase Homo sapiens 69-71 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 tyrosine hydroxylase Homo sapiens 146-148 12891655-1 2003 Tyrosine hydroxylase (TH) is the key enzyme in the biosynthesis of the catecholamines dopamine, epinephrine, and norepinephrine. Catecholamines 71-85 tyrosine hydroxylase Homo sapiens 0-20 12891655-1 2003 Tyrosine hydroxylase (TH) is the key enzyme in the biosynthesis of the catecholamines dopamine, epinephrine, and norepinephrine. Catecholamines 71-85 tyrosine hydroxylase Homo sapiens 22-24 12457228-1 2002 Using immunocytochemistry coupled to fluorescence and electron microscopy, we investigated the expression and ultrastructural localization of tyrosine hydroxylase (TH, EC 1.14.16.2), the rate-limiting enzyme in the biosynthesis of catecholamines, in human peripheral blood mononuclear cells (PBMCs), with PC12 cells as positive controls. Catecholamines 231-245 tyrosine hydroxylase Homo sapiens 142-162 12457228-1 2002 Using immunocytochemistry coupled to fluorescence and electron microscopy, we investigated the expression and ultrastructural localization of tyrosine hydroxylase (TH, EC 1.14.16.2), the rate-limiting enzyme in the biosynthesis of catecholamines, in human peripheral blood mononuclear cells (PBMCs), with PC12 cells as positive controls. Catecholamines 231-245 tyrosine hydroxylase Homo sapiens 164-166 12411742-1 2002 Our previous studies indicated that in the human paraventricular (PVN) and supraoptic (SON) nuclei, tyrosine hydroxylase (TH)--the first and rate-limiting enzyme in catecholamine synthesis--is localized mainly in magnocellular neurons and that antemortem factors regulate its expression. Catecholamines 165-178 tyrosine hydroxylase Homo sapiens 100-120 12411742-1 2002 Our previous studies indicated that in the human paraventricular (PVN) and supraoptic (SON) nuclei, tyrosine hydroxylase (TH)--the first and rate-limiting enzyme in catecholamine synthesis--is localized mainly in magnocellular neurons and that antemortem factors regulate its expression. Catecholamines 165-178 tyrosine hydroxylase Homo sapiens 122-124 12399106-3 2002 One manifestation of the behavioral changes resulting from chronic use of morphine is the upregulation of tyrosine hydroxylase (TH, the rate-limiting enzyme in catecholamine biosynthesis), which contributes to the dramatic increases in catecholamine release in the target regions of the locus coeruleus (LC) and the ventral tegmental area (VTA). Catecholamines 160-173 tyrosine hydroxylase Homo sapiens 106-126 12399106-3 2002 One manifestation of the behavioral changes resulting from chronic use of morphine is the upregulation of tyrosine hydroxylase (TH, the rate-limiting enzyme in catecholamine biosynthesis), which contributes to the dramatic increases in catecholamine release in the target regions of the locus coeruleus (LC) and the ventral tegmental area (VTA). Catecholamines 160-173 tyrosine hydroxylase Homo sapiens 128-130 12399106-3 2002 One manifestation of the behavioral changes resulting from chronic use of morphine is the upregulation of tyrosine hydroxylase (TH, the rate-limiting enzyme in catecholamine biosynthesis), which contributes to the dramatic increases in catecholamine release in the target regions of the locus coeruleus (LC) and the ventral tegmental area (VTA). Catecholamines 236-249 tyrosine hydroxylase Homo sapiens 106-126 12399106-3 2002 One manifestation of the behavioral changes resulting from chronic use of morphine is the upregulation of tyrosine hydroxylase (TH, the rate-limiting enzyme in catecholamine biosynthesis), which contributes to the dramatic increases in catecholamine release in the target regions of the locus coeruleus (LC) and the ventral tegmental area (VTA). Catecholamines 236-249 tyrosine hydroxylase Homo sapiens 128-130 12428766-2 2002 The microsatellite HUMTH01, located in the first intron of the Tyrosine Hydroxylase (TH) gene (encoding the rate-limiting enzyme in the synthesis of catecholamines), is characterized by a TCAT repeated motif and has been used in genetic studies of neuropsychiatric and other complex diseases, in which catecholaminergic neurotransmission is implicated. Catecholamines 149-163 tyrosine hydroxylase Homo sapiens 22-24 11108136-1 2000 The conversion of L-tyrosine to 3,4-dihydroxy-L-phenylalanine by tyrosine hydroxylase (TH) is the first and rate-limiting step in biosynthesis of catecholamine neurotransmitters. Catecholamines 146-159 tyrosine hydroxylase Homo sapiens 65-85 12023049-1 2002 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of catecholamines. Catecholamines 74-88 tyrosine hydroxylase Homo sapiens 0-20 12023049-1 2002 Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of catecholamines. Catecholamines 74-88 tyrosine hydroxylase Homo sapiens 22-24 12113410-1 2002 Tyrosine hydroxylase (TH) is a rate-limiting enzyme for catecholamine biosynthesis. Catecholamines 56-69 tyrosine hydroxylase Homo sapiens 0-20 12113410-1 2002 Tyrosine hydroxylase (TH) is a rate-limiting enzyme for catecholamine biosynthesis. Catecholamines 56-69 tyrosine hydroxylase Homo sapiens 22-24 11799093-5 2002 Tyrosine hydroxylase (TH) is a rate-limiting enzyme involved in the biosynthesis of catecholamine, and this catecholamine synthesis depends both on TH enzyme activity and on the levels of TH protein after TH gene transcription. Catecholamines 84-97 tyrosine hydroxylase Homo sapiens 0-20 11799093-5 2002 Tyrosine hydroxylase (TH) is a rate-limiting enzyme involved in the biosynthesis of catecholamine, and this catecholamine synthesis depends both on TH enzyme activity and on the levels of TH protein after TH gene transcription. Catecholamines 108-121 tyrosine hydroxylase Homo sapiens 0-20 11520498-1 2001 Previous studies from this laboratory have demonstrated that fibroblast growth factor 1 together with a number of co-activator molecules (dopamine, TPA, IBMX/forskolin), will induce the expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in 10% of human neurons (hNTs) derived from the NT2 cell line [10]. Catecholamines 204-217 tyrosine hydroxylase Homo sapiens 238-258 11520498-1 2001 Previous studies from this laboratory have demonstrated that fibroblast growth factor 1 together with a number of co-activator molecules (dopamine, TPA, IBMX/forskolin), will induce the expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in 10% of human neurons (hNTs) derived from the NT2 cell line [10]. Catecholamines 204-217 tyrosine hydroxylase Homo sapiens 260-262 11532988-3 2001 The TH gene encodes the rate-limiting enzyme in the synthesis of catecholamines, and the microsatellite HUMTH01 has been used in genetic studies of neuropsychiatric and cardiovascular diseases, in which disturbances of catecholaminergic neurotransmission have been implicated. Catecholamines 65-79 tyrosine hydroxylase Homo sapiens 4-6 11483656-0 2001 L-DOPA and glia-conditioned medium have additive effects on tyrosine hydroxylase expression in human catecholamine-rich neuroblastoma NB69 cells. Catecholamines 101-114 tyrosine hydroxylase Homo sapiens 60-80 11401575-0 2001 Effects of substitution at serine 40 of tyrosine hydroxylase on catecholamine binding. Catecholamines 64-77 tyrosine hydroxylase Homo sapiens 40-60 11401575-1 2001 Phosphorylation of Ser40 in the regulatory domain of tyrosine hydroxylase activates the enzyme by increasing the rate of dissociation of inhibitory catecholamines [Ramsey, A. J., and Fitzpatrick, P. F. (1998) Biochemistry 37, 8980-8986]. Catecholamines 148-162 tyrosine hydroxylase Homo sapiens 53-73 11344198-1 2001 This study examined the mechanisms linking different biochemical and clinical phenotypes of pheochromocytoma in multiple endocrine neoplasia type 2 (MEN 2) and von Hippel-Lindau (VHL) syndrome to underlying differences in the expression of tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis, and of phenylethanolamine N-methyltransferase (PNMT), the enzyme that converts norepinephrine to epinephrine. Catecholamines 295-308 tyrosine hydroxylase Homo sapiens 240-260 10833449-6 2000 Tyrosine hydroxylase (TH) is a rate-limiting enzyme in the biosynthesis of catecholamine, and its activity is regulated by both TH-enzyme activity and TH-synthesis. Catecholamines 75-88 tyrosine hydroxylase Homo sapiens 0-20 10731621-7 2000 Similarly, axons labeled for tyrosine hydroxylase, the rate-limiting enzyme in catecholamine biosynthesis, were also present in high density in the granule cell layer of the same lobules of the vermis. Catecholamines 79-92 tyrosine hydroxylase Homo sapiens 29-49 11702234-5 2001 Most of them coexpressed the low affinity neurotrophin receptor (p75NTR), and some were catecholaminergic, as determined by their content of immunoreactive tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 88-101 tyrosine hydroxylase Homo sapiens 156-176 11702234-5 2001 Most of them coexpressed the low affinity neurotrophin receptor (p75NTR), and some were catecholaminergic, as determined by their content of immunoreactive tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 88-101 tyrosine hydroxylase Homo sapiens 178-180 11076506-1 2000 Tetrahydropterins are obligatory cofactors for tyrosine hydroxylase (TH), the rate-limiting enzyme of catecholamine biosynthesis. Catecholamines 102-115 tyrosine hydroxylase Homo sapiens 47-67 11076506-1 2000 Tetrahydropterins are obligatory cofactors for tyrosine hydroxylase (TH), the rate-limiting enzyme of catecholamine biosynthesis. Catecholamines 102-115 tyrosine hydroxylase Homo sapiens 69-71 11018298-1 2000 Factors regulating tyrosine hydroxylase (TH) gene transcription are of major importance in the studies of malignant and degenerative diseases of catecholamine-synthesizing tissues. Catecholamines 145-158 tyrosine hydroxylase Homo sapiens 19-39 11018298-1 2000 Factors regulating tyrosine hydroxylase (TH) gene transcription are of major importance in the studies of malignant and degenerative diseases of catecholamine-synthesizing tissues. Catecholamines 145-158 tyrosine hydroxylase Homo sapiens 41-43 10915581-8 2000 Tyrosine hydroxylase immunoreactivity indicated prolonged transplant survival and production of catecholamines. Catecholamines 96-110 tyrosine hydroxylase Homo sapiens 0-20 11108136-1 2000 The conversion of L-tyrosine to 3,4-dihydroxy-L-phenylalanine by tyrosine hydroxylase (TH) is the first and rate-limiting step in biosynthesis of catecholamine neurotransmitters. Catecholamines 146-159 tyrosine hydroxylase Homo sapiens 87-89 9814544-1 1998 One of the significant factors that affect brain dopamine function is the activity of tyrosine hydroxylase (TH), the first and rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 151-164 tyrosine hydroxylase Homo sapiens 86-106 10585338-1 1999 BACKGROUND: Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the biosynthesis of the catecholamines dopamine, norepinephrine, and epinephrine. Catecholamines 98-112 tyrosine hydroxylase Homo sapiens 12-32 10585338-1 1999 BACKGROUND: Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the biosynthesis of the catecholamines dopamine, norepinephrine, and epinephrine. Catecholamines 98-112 tyrosine hydroxylase Homo sapiens 34-36 10634688-1 1999 Single and double-label immunofluorescence methods were used to determine the distribution and patterns of colocalisation of various neuropeptides and nitric oxide synthase (NOS) with the catecholamine synthesising enzymes tyrosine hydroxylase (TH) and dopamine-beta-hydroxylase (DbetaH) in nerve fibres within specimens of adult human vas deferens obtained at vasectomy (age range 28 to 83 y). Catecholamines 188-201 tyrosine hydroxylase Homo sapiens 223-243 10490711-1 1999 Tyrosine hydroxylase (TH), the rate-limiting enzyme in the metabolism of catecholamines, is considered a candidate gene in bipolar affective disorder (BPAD) and has been the subject of numerous linkage and association studies. Catecholamines 73-87 tyrosine hydroxylase Homo sapiens 0-20 10490711-1 1999 Tyrosine hydroxylase (TH), the rate-limiting enzyme in the metabolism of catecholamines, is considered a candidate gene in bipolar affective disorder (BPAD) and has been the subject of numerous linkage and association studies. Catecholamines 73-87 tyrosine hydroxylase Homo sapiens 22-24 10217296-1 1999 Tyrosine hydroxylase (TH), which converts L-tyrosine to L-DOPA, is a rate-limiting enzyme in the biosynthesis of catecholamines; its activity is regulated by feedback inhibition by catecholamine products including dopamine. Catecholamines 113-127 tyrosine hydroxylase Homo sapiens 0-20 10217296-1 1999 Tyrosine hydroxylase (TH), which converts L-tyrosine to L-DOPA, is a rate-limiting enzyme in the biosynthesis of catecholamines; its activity is regulated by feedback inhibition by catecholamine products including dopamine. Catecholamines 113-126 tyrosine hydroxylase Homo sapiens 0-20 10620706-1 2000 Tyrosine hydroxylase (TH), which converts L-tyrosine to L-3, 4-dihydroxyphenylalanine, is a rate-limiting enzyme in the biosynthesis of catecholamines; its activity is regulated by the feedback inhibition of the catecholamine products including dopamine. Catecholamines 136-150 tyrosine hydroxylase Homo sapiens 0-20 10620706-1 2000 Tyrosine hydroxylase (TH), which converts L-tyrosine to L-3, 4-dihydroxyphenylalanine, is a rate-limiting enzyme in the biosynthesis of catecholamines; its activity is regulated by the feedback inhibition of the catecholamine products including dopamine. Catecholamines 136-149 tyrosine hydroxylase Homo sapiens 0-20 10800597-9 2000 Tyrosine hydroxylase is regulated by phosphorylation and feedback inhibition by catecholamines. Catecholamines 80-94 tyrosine hydroxylase Homo sapiens 0-20 11193127-1 2000 OBJECTIVE: We have studied possible association between predisposition to essential hypertension, plasma noradrenaline level and two polymorphisms of the gene for tyrosine hydroxylase (TH), the rate-limiting enzyme of catecholamine biosynthesis. Catecholamines 218-231 tyrosine hydroxylase Homo sapiens 163-183 11193127-1 2000 OBJECTIVE: We have studied possible association between predisposition to essential hypertension, plasma noradrenaline level and two polymorphisms of the gene for tyrosine hydroxylase (TH), the rate-limiting enzyme of catecholamine biosynthesis. Catecholamines 218-231 tyrosine hydroxylase Homo sapiens 185-187 10079965-2 1999 Catecholamine (dopamine, norepinephrine, and epinephrine) biosynthesis is regulated by tyrosine hydroxylase (TH). Catecholamines 0-13 tyrosine hydroxylase Homo sapiens 87-107 10079965-2 1999 Catecholamine (dopamine, norepinephrine, and epinephrine) biosynthesis is regulated by tyrosine hydroxylase (TH). Catecholamines 0-13 tyrosine hydroxylase Homo sapiens 109-111 9814544-1 1998 One of the significant factors that affect brain dopamine function is the activity of tyrosine hydroxylase (TH), the first and rate-limiting enzyme in catecholamine biosynthesis. Catecholamines 151-164 tyrosine hydroxylase Homo sapiens 108-110 9774362-2 1998 The position of tyrosine hydroxylase (TH) as the rate-limiting enzyme in catecholamine biosynthesis renders it a candidate gene for the etiology of hypertension. Catecholamines 73-86 tyrosine hydroxylase Homo sapiens 16-36 9774362-2 1998 The position of tyrosine hydroxylase (TH) as the rate-limiting enzyme in catecholamine biosynthesis renders it a candidate gene for the etiology of hypertension. Catecholamines 73-86 tyrosine hydroxylase Homo sapiens 38-40 9774362-22 1998 A common and potentially functional variant at codon 81(Val-->Met) within exon 2 of the TH gene (which we show to be in linkage disequilibrium with TH-STR) was also typed in our YHT but did not associate with catecholamine levels and is therefore unlikely to account for our findings with D and E TH-STR. Catecholamines 212-225 tyrosine hydroxylase Homo sapiens 91-93 9774362-22 1998 A common and potentially functional variant at codon 81(Val-->Met) within exon 2 of the TH gene (which we show to be in linkage disequilibrium with TH-STR) was also typed in our YHT but did not associate with catecholamine levels and is therefore unlikely to account for our findings with D and E TH-STR. Catecholamines 212-225 tyrosine hydroxylase Homo sapiens 151-153 9774362-22 1998 A common and potentially functional variant at codon 81(Val-->Met) within exon 2 of the TH gene (which we show to be in linkage disequilibrium with TH-STR) was also typed in our YHT but did not associate with catecholamine levels and is therefore unlikely to account for our findings with D and E TH-STR. Catecholamines 212-225 tyrosine hydroxylase Homo sapiens 151-153 9754624-1 1998 Tyrosine hydroxylase is the rate-limiting step in the biosynthesis of catecholamines. Catecholamines 70-84 tyrosine hydroxylase Homo sapiens 0-20 9724817-2 1998 Recently, intraovarian neurons containing tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine biosynthesis, were described in the ovary of nonhuman primates. Catecholamines 97-110 tyrosine hydroxylase Homo sapiens 42-62 9724817-2 1998 Recently, intraovarian neurons containing tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine biosynthesis, were described in the ovary of nonhuman primates. Catecholamines 97-110 tyrosine hydroxylase Homo sapiens 64-66 9502265-4 1998 The present study using the cat carotid body demonstrates profound changes in the levels of immunoreactivity of the catecholamine-synthesizing enzyme, tyrosine hydroxylase, and the neuropeptide, substance P, in response to a two-week exposure to hypoxia (10% O2 in 90% N2). Catecholamines 116-129 tyrosine hydroxylase Homo sapiens 151-171 9578138-3 1998 Additionally, cDNA-polymerase chain reaction (cDNA-PCR) analysis of relative mRNA levels corresponding to the enzymes involved in catecholamine synthesis revealed a 3-fold increase of tyrosine hydroxylase gene expression after 5 days of incubation with ascorbic acid (200 microM), whereas expression of dopamine-beta-hydroxylase was found to be unaltered. Catecholamines 130-143 tyrosine hydroxylase Homo sapiens 184-204 9613851-1 1998 Tyrosine hydroxylase (TH) gene is the rate-limiting enzyme in the synthesis of catecholamines. Catecholamines 79-93 tyrosine hydroxylase Homo sapiens 0-20 9613851-1 1998 Tyrosine hydroxylase (TH) gene is the rate-limiting enzyme in the synthesis of catecholamines. Catecholamines 79-93 tyrosine hydroxylase Homo sapiens 22-24