Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
about
Characterization of a cDNA clone for human NAD(+)-specific isocitrate dehydrogenase alpha-subunit and structural comparison with its isoenzymes from different speciesNAD(+)-dependent formate dehydrogenaseNondecarboxylating and decarboxylating isocitrate dehydrogenases: oxalosuccinate reductase as an ancestral form of isocitrate dehydrogenaseAn automatic method involving cluster analysis of secondary structures for the identification of domains in proteinsCrystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphataseCrystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanismCrystal structure of the monomeric isocitrate dehydrogenase in the presence of NADP+: insight into the cofactor recognition, catalysis, and evolutionStructural studies ofSaccharomyces cerevesiaemitochondrial NADP-dependent isocitrate dehydrogenase in different enzymatic states reveal substantial conformational changes during the catalytic reactionStructural characterization of tartrate dehydrogenase: a versatile enzyme catalyzing multiple reactionsMolecular mechanisms of "off-on switch" of activities of human IDH1 by tumor-associated mutation R132HInduced Fit and the Catalytic Mechanism of Isocitrate DehydrogenaseStructure of a highly NADP+-specific isocitrate dehydrogenaseCrystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombeEvolution of a Transition State: Role of Lys100 in the Active Site of Isocitrate DehydrogenaseStructure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinaseMillisecond Laue structures of an enzyme-product complex using photocaged substrate analogsPrinciples of protein-protein interactionsSubunit interactions of yeast NAD+-specific isocitrate dehydrogenase.Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activityIsocitrate dehydrogenase from Streptococcus mutans: biochemical properties and evaluation of a putative phosphorylation site at Ser102Adenine recognition: a motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins.Creating a community resource for protein science.Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase.Structural trees for protein superfamilies.Ser/Thr/Tyr protein phosphorylation in the archaeon Halobacterium salinarum--a representative of the third domain of life.Molecular mechanism of the allosteric regulation of the αγ heterodimer of human NAD-dependent isocitrate dehydrogenase.Heteroexpression and characterization of a monomeric isocitrate dehydrogenase from the multicellular prokaryote Streptomyces avermitilis MA-4680.Isocitrate dehydrogenase 1 and 2 mutations in cancer: alterations at a crossroads of cellular metabolismEvaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase.Escherichia coli D-malate dehydrogenase, a generalist enzyme active in the leucine biosynthesis pathwayThe tricarboxylic acid cycle of Helicobacter pylori.Isocitrate dehydrogenase from Thermus aquaticus YT1: purification of the enzyme and cloning, sequencing, and expression of the geneA mechanism for the evolution of phosphorylation sitesEvolutionary genetics of the isocitrate dehydrogenase gene (icd) in Escherichia coli and Salmonella enterica.Molecular cloning of the isocitrate dehydrogenase gene of an extreme thermophile, Thermus thermophilus HB8Protein engineering reveals ancient adaptive replacements in isocitrate dehydrogenase.Molecular recognition analyzed by docking simulations: the aspartate receptor and isocitrate dehydrogenase from Escherichia coliThe role of glutamate 87 in the kinetic mechanism of Thermus thermophilus isopropylmalate dehydrogenase.Second-site suppression of regulatory phosphorylation in Escherichia coli isocitrate dehydrogenase.Determinants of performance in the isocitrate dehydrogenase of Escherichia coli.
P2860
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P2860
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
description
1989 nî lūn-bûn
@nan
1989 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
@ast
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
@en
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
@nl
type
label
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
@ast
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
@en
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
@nl
prefLabel
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
@ast
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
@en
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
@nl
P2093
P2860
P356
P1476
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
@en
P2093
D E Koshland
N H Helmers
P E Thorsness
R M Stroud
V Ramalingam
P2860
P304
P356
10.1073/PNAS.86.22.8635
P407
P577
1989-11-01T00:00:00Z