Full Enzyme Complex Simulation: Interactions in Human Pyruvate Dehydrogenase Complex
Author:
Affiliation:
1. Institute of Bioprocess and Biosystems Engineering, Hamburg University of Technology, Denickestr. 15, 21071 Hamburg, Germany
Funder
Bundesministerium f?r Bildung und Forschung
Publisher
American Chemical Society (ACS)
Subject
Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.7b00557
Reference25 articles.
1. Subunit and Catalytic Component Stoichiometries of an in Vitro Reconstituted Human Pyruvate Dehydrogenase Complex
2. Stoichiometry, Organisation and Catalytic Function of Protein X of the Pyruvate Dehydrogenase Complex from Bovine Heart
3. Recognition of a Surface Loop of the Lipoyl Domain Underlies Substrate Channelling in the Pyruvate Dehydrogenase Multienzyme Complex
4. Variation in the organization and subunit composition of the mammalian pyruvate dehydrogenase complex E2/E3BP core assembly
5. Structural Insight into Interactions between Dihydrolipoamide Dehydrogenase (E3) and E3 Binding Protein of Human Pyruvate Dehydrogenase Complex
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