About: Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific journal article

Attributes	Values
rdf:type	Item
description	artículu científicu espublizáu en 2004 (ast) vědecký článek publikovaný v roce 2004 (cs) 2004 թվականի օգոստոսին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в серпні 2004 (uk) 2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած (hyw) vedecký článok (publikovaný 2004/08/06) (sk) wetenschappelijk artikel (gepubliceerd op 2004/08/06) (nl) مقالة علمية (نشرت في 6-8-2004) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im August 2004 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28116883-BD160D62-DD21-442E-A664-24457725BB9C
publication date	2004-08-06 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28116883-18EEA1BC-EB98-410B-AE9B-D404ADAEF061
language of work or name	English
cites work	wds:Q28116883-023030FA-D24F-4454-84EF-FDCBFEC7A15B wds:Q28116883-0A753402-6316-4F32-9FBF-B0DA17924936 wds:Q28116883-0D0299E9-F5DC-4002-B06D-EE0F894D394B wds:Q28116883-0D8B827F-CFE4-4390-BA75-581C0FDA28B9 wds:Q28116883-16AF1A61-22BB-4859-A2BD-86E5E62A7C89 wds:Q28116883-1F254563-0F43-4DD6-AEA0-3EA98E4C3F7F wds:Q28116883-20770662-74C1-4782-8EBC-A5E9050150C8 wds:Q28116883-2F8FF17B-01B6-4746-A9F3-FBF319D41173 wds:Q28116883-37A76DC7-F26A-41A9-90C5-9CD5798EFDBD wds:Q28116883-3AEFDA74-DA1A-4245-A499-5973AA052F18 wds:Q28116883-509BC59B-CA2F-49EF-8538-22754886D82F wds:Q28116883-5800D39F-D2F0-4DD8-9F71-12F400AC4E6F wds:Q28116883-5D741989-797C-431A-9CC7-16A6E30BD5C1 wds:Q28116883-634DD42C-7CA0-4015-820C-8B3D7D389160 wds:Q28116883-6528CEF9-A28D-42E1-9E24-53ACB9AF946D wds:Q28116883-716C658D-AE5C-4773-BC43-E2E3C0DD08EC wds:Q28116883-75EBFD59-33F5-43EF-BBA5-8294B4D61227 wds:Q28116883-97F0C9FA-1F23-446A-9E93-C03021BA038F wds:Q28116883-BB8B8C99-D47F-4137-9CCE-45C3E6E801C8 wds:Q28116883-BD8158BB-9B42-43CC-BD02-D614F7C3DFFC wds:Q28116883-C6CC7167-66D2-4660-9875-4E280ED5CD2E wds:Q28116883-C7E1BB74-EE92-4DBC-959A-291AF333BEF4 wds:Q28116883-D22729DF-CB33-44D7-8EF6-43A60D90D522 wds:Q28116883-DCE08B67-F25A-42A8-B06C-DC368A175528 wds:Q28116883-DD3A0781-052E-4F95-892D-CCC55856818F wds:Q28116883-E6B267FF-9B66-40E1-A5B2-79ECF88DA6E1 wds:Q28116883-ED8378F2-AEDB-47B8-BB0A-817D184D7FC6 wds:Q28116883-F7713E7B-FC94-416D-8515-6DEB5901328C wds:Q28116883-F7DAB4B2-0A80-4AD6-9400-9039DCA00F86
cites work	Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-A resolution: a pseudo-Michaelis ternary complex Cytosolic NADP(+)-dependent isocitrate dehydrogenase status modulates oxidative damage to cells Gapped BLAST and PSI-BLAST: a new generation of protein database search programs The human PICD gene encodes a cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase ESPript: analysis of multiple sequence alignments in PostScript Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase Improved methods for building protein models in electron density maps and the location of errors in these models Processing of X-ray diffraction data collected in oscillation mode Localization of cytosolic NADP-dependent isocitrate dehydrogenase in the peroxisomes of rat liver cells: biochemical and immunocytochemical studies. IDP3 encodes a peroxisomal NADP-dependent isocitrate dehydrogenase required for the beta-oxidation of unsaturated fatty acids Cytosolic isocitrate dehydrogenase in humans, mice, and voles and phylogenetic analysis of the enzyme family Regulation of an enzyme by phosphorylation at the active site The finer things in X-ray diffraction data collection Opinion: peroxisomal-protein import: is it really that complex? Control of mitochondrial redox balance and cellular defense against oxidative damage by mitochondrial NADP+-dependent isocitrate dehydrogenase Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences Access to phosphorylation in isocitrate dehydrogenase may occur by domain shifting Cellular defense against singlet oxygen-induced oxidative damage by cytosolic NADP+-dependent isocitrate dehydrogenase Inactivation of NADP(+)-dependent isocitrate dehydrogenase by nitric oxide The isocitrate dehydrogenase phosphorylation cycle: regulation and enzymology Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for Escherichia coli isocitrate dehydrogenase kinase/phosphatase Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart NADP-dependent isocitrate dehydrogenase Cardiac mitochondrial NADP+-isocitrate dehydrogenase is inactivated through 4-hydroxynonenal adduct formation: an event that precedes hypertrophy development Electrostatic and steric contributions to regulation at the active site of isocitrate dehydrogenase Dependence of peroxisomal beta-oxidation on cytosolic sources of NADPH. Peroxisomal beta-oxidation of polyunsaturated fatty acids in Saccharomyces cerevisiae: isocitrate dehydrogenase provides NADPH for reduction of double bonds at even positions
author name string	wds:Q28116883-0D221D25-B4E9-4CD0-8ABC-1505AB62887B wds:Q28116883-228F4A10-D0F9-4F92-937A-45085B4500B8 wds:Q28116883-2E4C290C-7808-4100-B7C6-92C6604947B3 wds:Q28116883-3EE1A5D6-FA8E-4FE7-A855-B051A31A720B wds:Q28116883-B6905048-2A79-4439-863E-5B20244B6656 wds:Q28116883-DE0DEBA1-9E24-41B8-9FE9-4EA67E75A678
OpenCitations bibliographic resource ID	wds:Q28116883-910443BD-B7CA-443F-81B1-24CEEBBD003E
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/686645
author name string	Xiang Xu Jianping Ding Zhen Xu Baozhen Peng Jingyue Zhao Qiuhua Huang
OpenCitations bibliographic resource ID	686645
rdfs:label	Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity (en) Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity (nl) Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity (ast)
skos:prefLabel	Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity (en) Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity (nl) Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity (ast)
name	Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity (en) Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity (nl) Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity (ast)
author	wds:Q28116883-D5D6D22E-504C-4238-B0AB-909382C451DE
author	Eddy Arnold

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 188 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software