Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex - Test2 - elhamkhani - TriplyDB

Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex

Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex

http://www.wikidata.org/entity/Q24601847

about

Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex Cryptic proteolytic activity of dihydrolipoamide dehydrogenase Targeting Cancer Metabolism - Revisiting the Warburg Effects Structural and Thermodynamic Basis for Weak Interactions between Dihydrolipoamide Dehydrogenase and Subunit-binding Domain of the Branched-chain -Ketoacid Dehydrogenase Complex Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural Approaches Biochemical and structural characterization of the apicoplast dihydrolipoamide dehydrogenase of Plasmodium falciparum Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry: Implications for the structural basis of E3 deficiency.The pyruvate dehydrogenase complexes: structure-based function and regulation.Characterization of interactions of dihydrolipoamide dehydrogenase with its binding protein in the human pyruvate dehydrogenase complex.Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate.Novel binding motif and new flexibility revealed by structural analyses of a pyruvate dehydrogenase-dihydrolipoyl acetyltransferase subcomplex from the Escherichia coli pyruvate dehydrogenase multienzyme complex Determination of protein complex stoichiometry through multisignal sedimentation velocity experiments.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 Evaluating the stoichiometry of macromolecular complexes using multisignal sedimentation velocity.Mutations in the dimer interface of dihydrolipoamide dehydrogenase promote site-specific oxidative damages in yeast and human cells.Approaching rational epitope vaccine design for hepatitis C virus with meta-server and multivalent scaffolding Modeling mitochondrial function.Interaction-site prediction for protein complexes: a critical assessment.The pyruvate dehydrogenase complex as a therapeutic target for age-related diseases.A new level of architectural complexity in the human pyruvate dehydrogenase complex.New insights into the role of the branched-chain aminotransferase proteins in the human brain.Rearrangement of mitochondrial pyruvate dehydrogenase subunit dihydrolipoamide dehydrogenase protein-protein interactions by the MDM2 ligand nutlin-3.Interaction of E1 and E3 components with the core proteins of the human pyruvate dehydrogenase complex.The human peripheral subunit-binding domain folds rapidly while overcoming repulsive Coulomb forces.Identification of Sirtuin4 (SIRT4) Protein Interactions: Uncovering Candidate Acyl-Modified Mitochondrial Substrates and Enzymatic Regulators Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components.PDB-scale analysis of known and putative ligand-binding sites with structural sketches.The Pyruvate Dehydrogenase Complex and Related Assemblies in Health and Disease.Variation in the organization and subunit composition of the mammalian pyruvate dehydrogenase complex E2/E3BP core assembly.Structure of the subunit binding domain and dynamics of the di-domain region from the core of human branched chain alpha-ketoacid dehydrogenase complex.

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P2860

Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex

http://www.wikidata.org/entity/Q24601847

description

2006 nî lūn-bûn

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2006 թուականի Մարտին հրատարակուած գիտական յօդուած

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2006年の論文

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2006年論文

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Structural insight into intera ...... pyruvate dehydrogenase complex

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Structural insight into intera ...... pyruvate dehydrogenase complex

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Structural insight into intera ...... pyruvate dehydrogenase complex

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Structural insight into intera ...... pyruvate dehydrogenase complex

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Structural insight into intera ...... pyruvate dehydrogenase complex

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Structural insight into intera ...... pyruvate dehydrogenase complex

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Structural insight into intera ...... pyruvate dehydrogenase complex

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Structural insight into intera ...... pyruvate dehydrogenase complex

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Structural insight into intera ...... pyruvate dehydrogenase complex

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Structural insight into intera ...... pyruvate dehydrogenase complex

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David T Chuang

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Jacinta L Chuang

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R Max Wynn

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P2860

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

Mutations in PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase-complex gene on chromosome 11p1, in congenital lactic acidosis

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase

Global prevalence of diabetes: estimates for the year 2000 and projections for 2030

Structure validation by Calpha geometry: phi,psi and Cbeta deviation

Likelihood-enhanced fast rotation functions

Pushing the boundaries of molecular replacement with maximum likelihood

On the unique structural organization of the Saccharomyces cerevisiae pyruvate dehydrogenase complex

Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene encoding the protein X component of the pyruvate dehydrogenase complex.

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10.1016/J.STR.2006.01.001

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Diana R. Tomchick

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7330536

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dihydrolipoyl dehydrogenase activity

Dihydrolipoamide dehydrogenase

structural biology

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2879633

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