Associated Papers
Impact of Cancer-Associated PKM2 Mutations on Enzyme Activity and Allosteric Regulation: Structural and Functional Insights into Metabolic Reprogramming.
Upadhyay S et al.
Biochemistry, 2025
Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation.
Nandi S et al.
The Journal of Biological Chemistry, 2020
Structural insight into mechanisms for dynamic regulation of PKM2.
Wang P et al.
Protein & Cell, 2015
In silico screening, genotyping, molecular dynamics simulation and activity studies of SNPs in pyruvate kinase M2.
Kalaiarasan P et al.
Plos One, 2015
Missense mutations in pyruvate kinase M2 promote cancer metabolism, oxidative endurance, anchorage independence, and tumor growth in a dominant negative manner.
Iqbal MA et al.
The Journal of Biological Chemistry, 2014
Dominant negative mutations affect oligomerization of human pyruvate kinase M2 isozyme and promote cellular growth and polyploidy.
Gupta V et al.
The Journal of Biological Chemistry, 2010
Differential behavior of missense mutations in the intersubunit contact domain of the human pyruvate kinase M2 isozyme.
Akhtar K et al.
The Journal of Biological Chemistry, 2009
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