Three-dimensional structure of the bifunctional protein PCD/DCoH, a cytoplasmic enzyme interacting with transcription factor HNF1
about
Tetrahydrobiopterin biosynthesis, regeneration and functionsStudies on the enzymatic and transcriptional activity of the dimerization cofactor for hepatocyte nuclear factor 1Characterization of the wild-type form of 4a-carbinolamine dehydratase and two naturally occurring mutants associated with hyperphenylalaninemiaDimerization co-factor of hepatocyte nuclear factor 1/pterin-4alpha-carbinolamine dehydratase is necessary for pigmentation in Xenopus and overexpressed in primary human melanoma lesionsThe 1.25 A crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters.The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14.Diabetes-associated mutations in a beta-cell transcription factor destabilize an antiparallel "mini-zipper" in a dimerization interface.Interactions with the bifunctional interface of the transcriptional coactivator DCoH1 are kinetically regulated.Identification of hepatic nuclear factor 1 binding sites in the 5' flanking region of the human phenylalanine hydroxylase gene: implication of a dual function of phenylalanine hydroxylase stimulator in the phenylalanine hydroxylation system.Mutations in PCBD1 cause hypomagnesemia and renal magnesium wasting.PhhB, a Pseudomonas aeruginosa homolog of mammalian pterin 4a-carbinolamine dehydratase/DCoH, does not regulate expression of phenylalanine hydroxylase at the transcriptional levelMultiple steps in the regulation of transcription-factor level and activity.High-resolution structures of the bifunctional enzyme and transcriptional coactivator DCoH and its complex with a product analogue4a-hydroxytetrahydrobiopterin => q-dihydrobiopterin + H2O
P2860
Q24531994-D631DDDE-3628-4088-ABDB-1FF52342D47DQ24633231-2E41603E-E7B1-46C5-97AE-80B912AD29E7Q28277309-5E843EB3-B1EA-42EC-9320-7481CC2AD6ACQ28366488-07C3A0E8-B125-4BDA-A4B8-AB1113382DA7Q28587841-49096231-27A2-4130-8D7E-0E2429312DE0Q33886909-233209E9-867F-490F-A1DF-29F9DA6D2B6BQ35046351-C3D376BD-D7D3-4BB7-93F5-CC8327D54F41Q35080345-0D30AEE1-4FDD-4B9A-9A85-44E069F64D51Q35868114-D70A13DF-8DBB-4915-A51F-706444EAD05AQ37604723-8CC2E4EA-723A-402E-92B3-CA850670C9DBQ39495505-09CD483D-918D-4DD3-9C1B-389751EF5F45Q41036772-B7085135-84C7-49CC-9DD8-92F566FE4FB5Q42015563-1F8887B2-3330-4A76-9D5F-21AD00D3DCB0Q50295028-6DE93A3F-DB1E-4375-83E7-5B2E2EB5F2E8
P2860
Three-dimensional structure of the bifunctional protein PCD/DCoH, a cytoplasmic enzyme interacting with transcription factor HNF1
description
1995 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մայիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1995
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im Mai 1995 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
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vedecký článok (publikovaný 1995/05/01)
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vědecký článek publikovaný v roce 1995
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wetenschappelijk artikel (gepubliceerd op 1995/05/01)
@nl
наукова стаття, опублікована в травні 1995
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مقالة علمية (نشرت في مايو 1995)
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name
Three-dimensional structure of ...... with transcription factor HNF1
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Three-dimensional structure of ...... with transcription factor HNF1
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Three-dimensional structure of ...... with transcription factor HNF1
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type
label
Three-dimensional structure of ...... with transcription factor HNF1
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Three-dimensional structure of ...... with transcription factor HNF1
@en
Three-dimensional structure of ...... with transcription factor HNF1
@nl
prefLabel
Three-dimensional structure of ...... with transcription factor HNF1
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Three-dimensional structure of ...... with transcription factor HNF1
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Three-dimensional structure of ...... with transcription factor HNF1
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P2093
P2860
P1433
P1476
Three-dimensional structure of ...... with transcription factor HNF1
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P2093
P2860
P304
P356
10.1002/J.1460-2075.1995.TB07195.X
P407
P577
1995-05-01T00:00:00Z