Structural Investigation of a Dimeric Variant of Pyruvate Kinase Muscle Isoform 2
Author:
Affiliation:
1. Department of Chemistry, University of Iowa, Iowa City, Iowa 52242, United States
2. Department of Biochemistry, University of Missouri—Columbia, Columbia, Missouri 65211, United States
Funder
Division of Chemistry
Department of Biochemistry, University of Missouri
College of Liberal Arts and Sciences, University of Iowa
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b01013
Reference27 articles.
1. Cancer metabolism meets systems biology: Pyruvate kinase isoform PKM2 is a metabolic master regulator
2. Structural Basis for Tumor Pyruvate Kinase M2 Allosteric Regulation and Catalysis,
3. The M1- and M2-type isozymes of rat pyruvate kinase are produced from the same gene by alternative RNA splicing.
4. Activation of Liver Pyruvate Kinase by Fructose 1,6-Diphosphate
5. Succinyl-5-aminoimidazole-4-carboxamide-1-ribose 5′-Phosphate (SAICAR) Activates Pyruvate Kinase Isoform M2 (PKM2) in Its Dimeric Form
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