Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component fromEscherichia coliobserved at 2.32 Å resolution-Reference-Cited by-同舟云学术

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Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component fromEscherichia coliobserved at 2.32 Å resolution

Published:2006-10-18 Issue:11 Volume:62 Page:1382-1386
ISSN:0907-4449
Container-title:Acta Crystallographica Section D Biological Crystallography
language:
Short-container-title:Acta Crystallogr D Biol Cryst

Author:

Chandrasekhar Krishnamoorthy,Arjunan Palaniappa,Sax Martin,Nemeria Natalia,Jordan Frank,Furey William

Publisher

International Union of Crystallography (IUCr)

Subject

General Medicine,Structural Biology

Link

http://journals.iucr.org/d/issues/2006/11/00/hm5040/hm5040.pdf

Cited by 13 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion;Nature Communications;2021-09-06

2. Emerging regulatory roles of mitochondrial sirtuins on pyruvate dehydrogenase complex and the related metabolic diseases: Review;Biomedical Research and Therapy;2020-02-29

3. An Update on Developments in the Field of Thiamin Diphosphate-Dependent Enzymes;Comprehensive Natural Products III;2020

4. The N-terminal 1–55 residues domain of pyruvate dehydrogenase from Escherichia coli assembles as a dimer in solution;Protein Engineering, Design and Selection;2019-06

5. Pyruvate dehydrogenase complex deficiency and its relationship with epilepsy frequency – An overview;Epilepsy Research;2015-10

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