Allosteric Regulation of PKM2 Allows Cellular Adaptation to Different Physiological States
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Title
Allosteric Regulation of PKM2 Allows Cellular Adaptation to Different Physiological States
Authors
Keywords
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Journal
Science Signaling
Volume 6, Issue 263, Pages pe7-pe7
Publisher
American Association for the Advancement of Science (AAAS)
Online
2013-02-20
DOI
10.1126/scisignal.2003925
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Note: Only part of the references are listed.- 1-(sulfonyl)-5-(arylsulfonyl)indoline as activators of the tumor cell specific M2 isoform of pyruvate kinase
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- When more is less
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- Pyruvate kinase M2 promotes de novo serine synthesis to sustain mTORC1 activity and cell proliferation
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- Evidence for an Alternative Glycolytic Pathway in Rapidly Proliferating Cells
- (2010) M. G. Vander Heiden et al. SCIENCE
- Evaluation of SubstitutedN,N′-Diarylsulfonamides as Activators of the Tumor Cell Specific M2 Isoform of Pyruvate Kinase
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- Tyrosine Phosphorylation Inhibits PKM2 to Promote the Warburg Effect and Tumor Growth
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- Pyruvate kinase M2 is a phosphotyrosine-binding protein
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