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 - Wikidata - awgldk - TriplyDB

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

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

http://www.wikidata.org/entity/Q34397043

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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.Altered acetylation and succinylation profiles in Corynebacterium glutamicum in response to conditions inducing glutamate overproduction The Pyruvate Dehydrogenase Complex and Related Assemblies in Health and Disease.

P2860

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P2860

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

http://www.wikidata.org/entity/Q34397043

description

2014 nî lūn-bûn

@nan

2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Novel binding motif and new fl ...... ydrogenase multienzyme complex

@ast

Novel binding motif and new fl ...... ydrogenase multienzyme complex

@en

Novel binding motif and new fl ...... ydrogenase multienzyme complex

@nl

type

label

Novel binding motif and new fl ...... ydrogenase multienzyme complex

@ast

Novel binding motif and new fl ...... ydrogenase multienzyme complex

@en

Novel binding motif and new fl ...... ydrogenase multienzyme complex

@nl

prefLabel

Novel binding motif and new fl ...... ydrogenase multienzyme complex

@ast

Novel binding motif and new fl ...... ydrogenase multienzyme complex

@en

Novel binding motif and new fl ...... ydrogenase multienzyme complex

@nl

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JBC.M114.592915

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Journal of Biological Chemistry

P1476

Novel binding motif and new fl ...... ydrogenase multienzyme complex

@en

P2093

Frank Jordan

http://www.w3.org/2001/XMLSchema#string

Guillermo Calero

http://www.w3.org/2001/XMLSchema#string

Ian Brown

http://www.w3.org/2001/XMLSchema#string

Krishnamoorthy Chandrasekhar

http://www.w3.org/2001/XMLSchema#string

Natalia S Nemeria

http://www.w3.org/2001/XMLSchema#string

Palaniappa Arjunan

http://www.w3.org/2001/XMLSchema#string

Shelley Reynolds

http://www.w3.org/2001/XMLSchema#string

William Furey

http://www.w3.org/2001/XMLSchema#string

P2860

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

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes

Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution

Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex

A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component

Communication between Thiamin Cofactors in the Escherichia coli Pyruvate Dehydrogenase Complex E1 Component Active Centers: EVIDENCE FOR A"DIRECT PATHWAY"BETWEEN THE 4'-AMINOPYRIMIDINE N1' ATOMS

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

Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex

P304

30161-30176

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scholarly article

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10.1074/JBC.M114.592915

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43

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289

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2014-09-10T00:00:00Z

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25210042

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4208021

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