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1 s appear distinct from any characterized IMP cyclohydrolase.
2 constituents confirms their origin as PR-AMP cyclohydrolase.
3 of methylene tetrahydrofolate dehydrogenase/cyclohydrolase.
4 mino acid dopa decarboxylase (AADC), and GTP cyclohydrolase 1 (CH1) in a single transcription unit ha
5 Endothelium-targeted overexpression of GTP cyclohydrolase 1 (GCH), the rate limiting enzyme in BH4
9 The Parkinson's disease (PD) risk gene GTP cyclohydrolase 1 (GCH1) catalyzes the rate-limiting step
10 Here we report that reduction of cardiac GTP cyclohydrolase 1 (GCH1) degradation by genetic and pharm
16 ssociated viruses expressing human TH or GTP cyclohydrolase 1 (GTPCH1) were injected into the striatu
17 ant degradation of guanosine 5'-triphosphate cyclohydrolase 1 (GTPCH1) with consequent deficiency of
19 n (a BH4 precursor) or overexpression of GTP cyclohydrolase 1 (the rate-limiting enzyme for BH4 biosy
20 ional adhesion molecule-like protein and GTP cyclohydrolase 1 feedback regulatory protein, stained in
21 ies have revealed an association between GTP cyclohydrolase 1 polymorphisms, which decrease tetrahydr
22 secondary to trangenic overexpression of GTP-cyclohydrolase 1) and reversed in wild-type mice receivi
25 of this biopterin increases with age in GTP cyclohydrolase 1-deficient hyperphenylalaninemia-1 (hph-
28 ference RNA (siRNA)-mediated "knockdown" GTP cyclohydrolase-1 (GTPCH1), the rate-limiting enzyme in B
30 e expression of an unregulated bacterial GTP cyclohydrolase-1 in plants would increase pterin biosynt
33 e hydroxylase and guanosine-5'-tri-phosphate-cyclohydrolase-1, bilaterally into the dopamine-depleted
34 sine hydroxylase and guanosine-tri-phosphate-cyclohydrolase-1, offers a new approach to a more refine
36 zyme methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2 (MTHFD2) is a promising therapeutic tar
37 ally methylenetetrahydrofolate dehydrogenase-cyclohydrolase 2 (MTHFD2), emerged as a top candidate in
38 e (FTL) and/or 5,10-methenyltetrahydrofolate cyclohydrolase/5,10-methylene tetrahydrofolate dehydroge
40 osynthesis, the AICAR transformylase and IMP cyclohydrolase activities of the bifunctional enzyme ATI
41 ncompasses both AICAR transformylase and IMP cyclohydrolase activities that are responsible for the c
42 olate-dependent AICAR transformylase and IMP cyclohydrolase activities that catalyzes the last two st
43 ide transformylase and inosine monophosphate cyclohydrolase activities, and exist as homodimers based
46 e activity is co-located with a methenyl-THF cyclohydrolase activity as part of bifunctional or trifu
47 at Lys137 is responsible for the increase in cyclohydrolase activity for dimeric ATIC, which was repo
48 We previously reported that deficits in GTP cyclohydrolase activity in Drosophila heterozygous for m
50 ared to test the hypothesis that the lack of cyclohydrolase activity in yMTD was due to the substitut
52 d for site-directed mutagenesis to study the cyclohydrolase activity of this bifunctional enzyme.
53 e activity requires dimerization whereas the cyclohydrolase activity only slightly prefers the dimeri
56 f the interaction include an increase in GTP cyclohydrolase activity, with concomitant protection fro
60 arboxamide ribonucleotide transformylase IMP cyclohydrolase, an enzyme not previously known to be reg
61 that regulate biopterin bioavailability, GTP cyclohydrolase and dihydrofolate reductase exhibited a c
62 D1 (methylenetetrahydrofolate dehydrogenase, cyclohydrolase and formyltetrahydrofolate synthetase 1).
63 nalogues and inhibitors suggest that the GTP cyclohydrolase and pyrophosphate phosphohydrolase activi
64 l protein ATIC (AICAR transformylase and IMP cyclohydrolase) and is responsible for catalyzing the pe
65 al methylene-THF dehydrogenase, methenyl-THF cyclohydrolase, and 10-formyl-THF synthetase activities.
66 10-formyl-THF synthetase, 5,10-methenyl-THF cyclohydrolase, and 5,10-methylene-THF dehydrogenase.
67 in methylenetetrahydrofolate dehydrogenase, cyclohydrolase, and formyltetrahydrofolate synthetase 1
68 ggest that both tyrosine hydroxylase and GTP cyclohydrolase are induced in a coordinate and transcrip
69 tide formyltransferase/inosine monophosphate cyclohydrolase (ATIC) and thereby slows the metabolism o
70 de ribonucleotide (AICAR) transformylase/IMP cyclohydrolase (ATIC) is a bifunctional enzyme with fola
71 arboxamide ribonucleotide transformylase/IMP cyclohydrolase (ATIC) is a bifunctional protein possessi
72 leotide transformylase/inosine monophosphate cyclohydrolase (ATIC) is responsible for catalysis of th
73 CAR) transformylase/5'-inosine monophosphate cyclohydrolase (ATIC), a bifunctional enzyme that cataly
74 oxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC), a bifunctional homodimeric enzyme
75 oxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC), a single enzyme in de novo purine
76 tide formyltransferase/inosine monophosphate cyclohydrolase (ATIC), SHMT1, and folate receptor (FR) a
80 exhibits sequence homology to the type I GTP cyclohydrolases characterized by FolE, but contrary to t
84 antly inherited guanosine triphosphate (GTP)-cyclohydrolase deficiency, otherwise known as Segawa's d
86 tead, it uses a new type of thermostable GTP cyclohydrolase enzyme that produces 2-amino-5-formylamin
87 recognizable homologues of the canonical GTP cyclohydrolase enzymes that are required for riboflavin
90 olate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase (MTHFD1
91 olate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase (MTHFD1
92 olate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase (MTHFD1
93 r the rate-limiting BH4 synthetic enzyme GTP cyclohydrolase (GCH) became undetectable in the sweat gl
94 Endothelium-targeted overexpression of GTP cyclohydrolase (GCH) I increased levels of the endotheli
98 ces the expression of guanosine triphosphate cyclohydrolase (GCH1), the rate-limiting enzyme in pteri
100 ether AMPK suppresses the degradation of GTP-cyclohydrolase (GTPCH I), a key event in vascular endoth
101 synthesis is controlled enzymatically by GTP cyclohydrolase (GTPCH), we used GTPCH-depleted mice [hyp
102 ses H4B levels and enzymatic activity of GTP cyclohydrolase (GTPCH)-1, the first step of H4B biosynth
103 pain sensitivity and chronicity, and the GTP cyclohydrolase haplotype is a marker for these traits.
104 onofunctional Methanococcus vannielii PR-AMP cyclohydrolase has been developed, and the first charact
105 5'-Phosphoribosyl)adenosine-5'-monophosphate cyclohydrolase (HisI, PR-AMP cyclohydrolase) is a centra
107 similar situation in Escherichia coli: a GTP cyclohydrolase I (folE) mutant, deficient in pterin synt
108 by targeted transgenic overexpression of GTP-cyclohydrolase I (GCH), prevented hypoxia-induced pulmon
110 c l-amino acid decarboxylase (AADC), and GTP cyclohydrolase I (GCH1) transcription; increases striata
111 B1), carbonyl reductase (CBR1 and CBR3), GTP-cyclohydrolase I (GCH1), and 6-pyruvoyltetrahydrobiopter
116 the first enzyme of the folate pathway, GTP cyclohydrolase I (GCYH-I), encoded in Escherichia coli b
118 fer of human guanosine 5'-triphosphate (GTP) cyclohydrolase I (GTPCH I), the first and rate-limiting
119 levels, in part through the induction of GTP cyclohydrolase I (GTPCH I), the rate-limiting enzyme for
124 ent degradation of guanosine 5'-triphosphate cyclohydrolase I (GTPCH), a rate-limiting enzyme in the
125 me in catecholamine (CA) biosynthesis of GTP cyclohydrolase I (GTPCH), rate-limiting enzyme in biosyn
126 selective and direct-acting inhibitor of GTP cyclohydrolase I (GTPCH), the first and rate-limiting en
127 ctor alpha (TNF-alpha) without affecting GTP cyclohydrolase I (GTPCH), the rate-limiting enzyme in th
130 ey enzyme involved in BH(4) synthesis is GTP-cyclohydrolase I (GTPCH-I), which is stimulated by endot
131 s controlled by guanosine triphosphate (GTP) cyclohydrolase I (GTPCHI) and its feedback regulatory pr
135 uman tyrosine hydroxylase (hTH) or human GTP-cyclohydrolase I [GTPCHI, the rate-limiting enzyme for t
136 n (GFRP) mediates feedback inhibition of GTP cyclohydrolase I activity by tetrahydrobiopterin and als
137 , arginine decarboxylase gene activator, GTP cyclohydrolase I and a repressor of purine biosynthesis,
138 HPS, where activities of the key enzyme GTP-cyclohydrolase I are in the normal range, but total biop
140 increased de novo synthesis for 6BH4 via GTP-cyclohydrolase I concomitant with high levels of 6BH4, a
141 ) and the activity of guanosine triphosphate cyclohydrolase I decreased in ihMCs exposed to HG and wa
142 II increased vascular guanosine triphosphate cyclohydrolase I expression and biopterin synthesis in p
145 ylalanine through complex formation with GTP cyclohydrolase I feedback regulatory protein (GFRP).
146 olved in 6BH4 biosynthesis/recycling and GTP-cyclohydrolase I feedback regulatory protein were expres
147 iopterin bioavailability by upregulating GTP-cyclohydrolase I gene expression and activity, resulting
148 and those additionally modified with the GTP cyclohydrolase I gene indicate that BH4 is critical for
149 with fibro-blasts possessing both TH and GTP cyclohydrolase I genes displayed biochemical restoration
150 To examine further the importance of GTP cyclohydrolase I in gene therapy for PD, in vivo micro-d
151 single enzyme, as is known to occur with GTP cyclohydrolase I in the Eucarya and Bacteria, but rather
153 estoration in a rat model of PD and that GTP cyclohydrolase I is sufficient for production of BH4.
154 s with Tet-regulated expression of human GTP cyclohydrolase I to regulate intracellular BH4 availabil
157 ne prevented the coordinate induction of GTP cyclohydrolase I with NOS2 after exposure to interleukin
158 used a synthetic gene based on mammalian GTP cyclohydrolase I, because this enzyme is predicted to es
159 ino-6-hydroxypyrimidine, an inhibitor of GTP cyclohydrolase I, decreased endothelium-dependent vasodi
160 nzyme in the cofactor synthesis pathway, GTP cyclohydrolase I, is activated by phosphorylation and in
161 ent increase of iNOS, guanosine triphosphate cyclohydrolase I, tetrahydrobiopterin, NO formation, and
162 line by fruit-specific overexpression of GTP cyclohydrolase I, the first enzyme of pteridine synthesi
163 o fruit up to 140-fold by overexpressing GTP cyclohydrolase I, the first enzyme of pteridine synthesi
164 ro data demonstrate that NAMDA inhibited GTP cyclohydrolase I, the rate-limiting enzyme for BH4 biosy
165 tracycline-regulated expression of human GTP cyclohydrolase I, the rate-limiting enzyme in BH4 synthe
166 (X haplotype) in the GCH1 gene, encoding GTP-cyclohydrolase I, the rate-limiting enzyme in biopterin
174 ignificant (>40%) amino acid identity to GTP cyclohydrolase II (GCH II), which catalyzes the committe
177 ene encoding a putative dual-functioning GTP cyclohydrolase II-3,4-dihydroxy-2-butanone-4-phosphate s
178 FLU encoding the dual-functional protein GTP cyclohydrolase II/3,4-dihydroxy-2-butanone-4-phosphate s
179 this enzyme confirms the involvement of GTP cyclohydrolase III (ArfA) in archaeal riboflavin and Fo
180 This activity has been reported for a GTP cyclohydrolase III protein from Methanocaldococcus janna
181 posed to begin with an archaeal-specific GTP cyclohydrolase III that hydrolyzes the imidazole ring of
182 hese compounds were potent inhibitors of IMP cyclohydrolase (IMP CHase), a second activity of the bif
184 but not the NGF effect, NGF also induced GTP cyclohydrolase in a cAMP-dependent manner, while the EGF
186 cetylcholine, which was inhibited by the GTP-cyclohydrolase inhibitor 2,4-diamino-6-hydroxypyrimidine
187 fase substrate AICAR, as well as with an IMP cyclohydrolase inhibitor, XMP, to 1.93 A resolution.
193 '-monophosphate cyclohydrolase (HisI, PR-AMP cyclohydrolase) is a central enzyme in histidine biosynt
194 sine-5'-monophosphate cyclohydrolase (PR-AMP cyclohydrolase) is a Zn(2+) metalloprotein encoded by th
195 additionally modified with the gene for GTP cyclohydrolase l; an enzyme critical for BH4 synthesis.
196 thesis, QueF was proposed to be the putative cyclohydrolase-like enzyme responsible for this reaction
197 GTP is the precursor to queuosine and that a cyclohydrolase-like reaction was postulated as the initi
199 n, we focus on the IMPCH active site and the cyclohydrolase mechanism through comparison of crystal s
200 oxamide ribonucleotide formyltransferase/IMP cyclohydrolase-mediated glucose transporter type 4 (GLUT
202 '-phosphoribosyl) adenosine-5'-monophosphate cyclohydrolase (PR-AMP cyclohydrolase) is a Zn(2+) metal
203 active respectively as a phosphoribosyl-AMP cyclohydrolase (PRA-CH) and phosphoribosyl-ATP pyrophosp
205 boxamide ribonucleotideformyltransferase/IMP cyclohydrolase (PurH), an enzyme involved in de novo pur
208 an the forward rate (2.9 s(-1)), whereas the cyclohydrolase reaction is essentially unidirectional in
209 PurH but catalyzes a similar intramolecular cyclohydrolase reaction required for chromophore maturat
211 THFD2 enzyme catalyzes the dehydrogenase and cyclohydrolase reactions, but the enzyme responsible for
212 leotide transformylase/inosine monophosphate cyclohydrolase, Steps 9 and 10), were studied in a polye
213 ethylene THF dehydrogenase/5,10-methenyl THF cyclohydrolase that acts upstream of 5-formyl THF format
214 re we report the identification of a new GTP cyclohydrolase that converts GTP to 7,8-dihydro-d-neopte
215 MptA is the archetype of a new class of GTP cyclohydrolases that catalyzes a series of reactions mos
217 e activities of tyrosine hydroxylase and GTP cyclohydrolase, the rate-limiting enzymes in catecholami
219 0-methenyl tetrahydromethanopterin (H(4)MPT) cyclohydrolase, was constructed in vitro and recombined
220 release, and we found that the gene for GTP cyclohydrolase, which effectively regulates TH through s