Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase
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Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complexStructural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complexSequence-structure analysis of FAD-containing proteinsSubunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complexMolecular structure of a 9-MDa icosahedral pyruvate dehydrogenase subcomplex containing the E2 and E3 enzymes using cryoelectron microscopyStructure of GlgS from Escherichia coli suggests a role in protein-protein interactionsStructures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains.Structural and Thermodynamic Basis for Weak Interactions between Dihydrolipoamide Dehydrogenase and Subunit-binding Domain of the Branched-chain -Ketoacid Dehydrogenase ComplexInsight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural ApproachesOn the unique structural organization of the Saccharomyces cerevisiae pyruvate dehydrogenase complexWhen fast is better: protein folding fundamentals and mechanisms from ultrafast approachesHow dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complexSubunit Interactions in the Mammalian -Ketoglutarate Dehydrogenase Complex: EVIDENCE FOR DIRECT ASSOCIATION OF THE -KETOGLUTARATE DEHYDROGENASE AND DIHYDROLIPOAMIDE DEHYDROGENASE COMPONENTSNuclear magnetic resonance evidence for the role of the flexible regions of the E1 component of the pyruvate dehydrogenase complex from gram-negative bacteria.The pyruvate dehydrogenase complexes: structure-based function and regulation.Lipoic acid metabolism in microbial pathogens.Catabolism of branched-chain alpha-keto acids in Enterococcus faecalis: the bkd gene cluster, enzymes, and metabolic route.Molecular architecture and mechanism of an icosahedral pyruvate dehydrogenase complex: a multifunctional catalytic machineNovel binding motif and new flexibility revealed by structural analyses of a pyruvate dehydrogenase-dihydrolipoyl acetyltransferase subcomplex from the Escherichia coli pyruvate dehydrogenase multienzyme complexEffects of two solvent conditions on the free energy landscape of the BBL peripheral subunit binding domainMolecular flip-flops formed by overlapping Fis sites.Thermodynamic analysis of the binding of component enzymes in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.A new level of architectural complexity in the human pyruvate dehydrogenase complex.Comparative analysis of protein domain organizationImprovement of diffraction quality upon rehydration of dehydrated icosahedral Enterococcus faecalis pyruvate dehydrogenase core crystals.Molecular mechanism of synergy between the antimicrobial peptides PGLa and magainin 2.Interactions of the peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase component in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.Prediction of the binding site on E1 in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.Interplay between the folding mechanism and binding modes in folding coupled to binding processes.Expression and characterisation of the homodimeric E1 component of the Azotobacter vinelandii pyruvate dehydrogenase complex.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.FAD insertion is essential for attaining the assembly competence of the dihydrolipoamide dehydrogenase (E3) monomer from Escherichia coli.Structure of the subunit binding domain and dynamics of the di-domain region from the core of human branched chain alpha-ketoacid dehydrogenase complex.
P2860
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P2860
Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase
description
1996 nî lūn-bûn
@nan
1996 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մարտին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Protein-protein interactions i ...... drolipoamide acetyltransferase
@ast
Protein-protein interactions i ...... drolipoamide acetyltransferase
@en
Protein-protein interactions i ...... drolipoamide acetyltransferase
@nl
type
label
Protein-protein interactions i ...... drolipoamide acetyltransferase
@ast
Protein-protein interactions i ...... drolipoamide acetyltransferase
@en
Protein-protein interactions i ...... drolipoamide acetyltransferase
@nl
prefLabel
Protein-protein interactions i ...... drolipoamide acetyltransferase
@ast
Protein-protein interactions i ...... drolipoamide acetyltransferase
@en
Protein-protein interactions i ...... drolipoamide acetyltransferase
@nl
P2093
P3181
P1433
P1476
Protein-protein interactions i ...... drolipoamide acetyltransferase
@en
P2093
P304
P3181
P356
10.1016/S0969-2126(96)00032-9
P577
1996-03-15T00:00:00Z