Identification of the active site residues in ATP‐citrate lyase's carboxy‐terminal portion-Reference-Cited by-同舟云学术

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Identification of the active site residues in ATP‐citrate lyase's carboxy‐terminal portion

Published:2019-08-27 Issue:10 Volume:28 Page:1840-1849
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Nguyen Vinh H.¹,Singh Noreen¹,Medina Ana²,Usón Isabel²³,Fraser Marie E.¹^ORCID

Affiliation:

1. Department of Biological Sciences University of Calgary Calgary Alberta Canada

2. Structural Biology Unit CSIC Barcelona Spain

3. ICREA Barcelona Spain

Funder

Natural Sciences and Engineering Research Council of Canada

Argonne National Laboratory

Canadian Institutes of Health Research

National Research Council Canada

Western Economic Diversification Canada

University of Saskatchewan

Canada Foundation for Innovation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3708

Reference52 articles.

1. ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation

2. Current Drug Targets for Antihyperlipidemic Therapy

3. ATP Citrate Lyase Inhibitors as Novel Cancer Therapeutic Agents

4. Acetyl-CoA Synthetase from the Amitochondriate EukaryoteGiardia lamblia Belongs to the Newly Recognized Superfamily of Acyl-CoA Synthetases (Nucleoside Diphosphate-forming)

5. The preparation, properties, and reactions of succinyl coenzyme A synthetase and its phosphorylated form;Ramaley RF;J Biol Chem,1967

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3. Allosteric role of the citrate synthase homology domain of ATP citrate lyase;Nature Communications;2023-04-19

4. Synthesis, X-ray crystallography, molecular electronic property investigation, and leukopoiesis activity of novel 4,6-dimethyl-1,6-dihydropyridin-2-amino nitrate hybrid material;Journal of Molecular Structure;2022-11

5. The structure of succinyl-CoA synthetase bound to the succinyl-phosphate intermediate clarifies the catalytic mechanism of ATP-citrate lyase;Acta Crystallographica Section F Structural Biology Communications;2022-09-26

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