Native Mass Spectrometry Gives Insight into the Allosteric Binding Mechanism of M2 Pyruvate Kinase to Fructose-1,6-Bisphosphate-Reference-Cited by-同舟云学术

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Native Mass Spectrometry Gives Insight into the Allosteric Binding Mechanism of M2 Pyruvate Kinase to Fructose-1,6-Bisphosphate

Published:2018-03-02 Issue:11 Volume:57 Page:1685-1689
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Gavriilidou Agni F. M.¹,Holding Finn P.²,Mayer Daniel³,Coyle Joseph E.²,Veprintsev Dmitry B.³,Zenobi Renato¹^ORCID

Affiliation:

1. ETH Zurich, Department of Chemistry and Applied Biosciences, CH-8093 Zurich, Switzerland

2. Astex Pharmaceuticals, 436 Cambridge Science Park, Milton Road, Cambridge CB4 0QA, United Kingdom

3. Paul Scherrer Institute, 5232 Villigen PSI, Switzerland

Funder

Schweizerischer Nationalfonds zur F?rderung der Wissenschaftlichen Forschung

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b01270

Reference26 articles.

1. Pyruvate kinase type M2 and its role in tumor growth and spreading

2. Pyruvate kinase type M2: A key regulator of the metabolic budget system in tumor cells

3. Pyruvate Kinase M2: A Metabolic Tuner

4. Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis

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