Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops - Wikidata - wikimedia - TriplyDB

Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops

Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops

http://www.wikidata.org/entity/Q24329273

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Overexpression of pyruvate dehydrogenase kinase 3 increases drug resistance and early recurrence in colon cancer Pivotal role of the C-terminal DW-motif in mediating inhibition of pyruvate dehydrogenase kinase 2 by dichloroacetate Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex Phosphorylation regulates assembly of the caspase-6 substrate-binding groove.Structure-guided Development of Specific Pyruvate Dehydrogenase Kinase Inhibitors Targeting the ATP-binding Pocket Heart mitochondrial proteome study elucidates changes in cardiac energy metabolism and antioxidant PRDX3 in human dilated cardiomyopathy A Proteomics Approach to Investigate miR-153-3p and miR-205-5p Targets in Neuroblastoma Cells AMASS: a database for investigating protein structures.The pyruvate dehydrogenase complexes: structure-based function and regulation.Regulation of pyruvate metabolism and human disease Phenylbutyrate therapy for pyruvate dehydrogenase complex deficiency and lactic acidosis.Diphenyl urea derivatives as inhibitors of transketolase: a structure-based virtual screening.Asp295 stabilizes the active-site loop structure of pyruvate dehydrogenase, facilitating phosphorylation of ser292 by pyruvate dehydrogenase-kinase.Elucidation of the interaction loci of the human pyruvate dehydrogenase complex E2·E3BP core with pyruvate dehydrogenase kinase 1 and kinase 2 by H/D exchange mass spectrometry and nuclear magnetic resonance Stimulation of oxidative phosphorylation by calcium in cardiac mitochondria is not influenced by cAMP and PKA activity DXP synthase-catalyzed C-N bond formation: nitroso substrate specificity studies guide selective inhibitor design.Conservation of coevolving protein interfaces bridges prokaryote-eukaryote homologies in the twilight zone.Nuclear magnetic resonance approaches in the study of 2-oxo acid dehydrogenase multienzyme complexes--a literature review.The pyruvate dehydrogenase complex in cancer: An old metabolic gatekeeper regulated by new pathways and pharmacological agents.Pheochromocytoma: Gasping for Air.Determination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step.Src drives the Warburg effect and therapy resistance by inactivating pyruvate dehydrogenase through tyrosine-289 phosphorylation Extreme anoxia tolerance in crucian carp and goldfish through neofunctionalization of duplicated genes creating a new ethanol-producing pyruvate decarboxylase pathway."Scanning mutagenesis" of the amino acid sequences flanking phosphorylation site 1 of the mitochondrial pyruvate dehydrogenase complex.Post-translational regulation of metabolism in fumarate hydratase deficient cancer cells.Therapeutic Targeting of the Pyruvate Dehydrogenase Complex/Pyruvate Dehydrogenase Kinase (PDC/PDK) Axis in Cancer.Development of Dihydroxyphenyl Sulfonylisoindoline Derivatives as Liver-Targeting Pyruvate Dehydrogenase Kinase Inhibitors.The Pyruvate Dehydrogenase Complex and Related Assemblies in Health and Disease.Linked homozygous BMPR1B and PDHA2 variants in a consanguineous family with complex digit malformation and male infertility.How phosphorylation influences E1 subunit pyruvate dehydrogenase: A computational study

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P2860

Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops

http://www.wikidata.org/entity/Q24329273

description

2008 nî lūn-bûn

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2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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Structural basis for inactivat ...... sordered phosphorylation loops

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David T Chuang

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Jacinta L Chuang

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Jun Li

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Masato Kato

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R Max Wynn

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Shih-Chia Tso

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P2860

Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase

Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase

Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex

Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase: refined phosphorylation loop structure in the active site

Pyruvate dehydrogenase kinase-4 structures reveal a metastable open conformation fostering robust core-free basal activity

Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation

Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex

Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites

Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase

The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism

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1849-59

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10.1016/J.STR.2008.10.010

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19081061

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Pyruvate dehydrogenase E1 subunit alpha 1

Pyruvate dehydrogenase E1 subunit beta

phosphorylation

structural biology

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2849990

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