Destabilization of the SHP2 and SHP1 protein tyrosine phosphatase domains by a non-conserved “backdoor” cysteine-Reference-Cited by-同舟云学术

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Destabilization of the SHP2 and SHP1 protein tyrosine phosphatase domains by a non-conserved “backdoor” cysteine

Published:2022-12 Issue: Volume:32 Page:101370
ISSN:2405-5808
Container-title:Biochemistry and Biophysics Reports
language:en
Short-container-title:Biochemistry and Biophysics Reports

Author:

Yarnall Matthew T.N.,Kim Sean H.,Korntner Samuel,Bishop Anthony C.^ORCID

Funder

National Institute of General Medical Sciences

Amherst College

National Institutes of Health

National Health Research Institutes

Publisher

Elsevier BV

Subject

Biochemistry,Biophysics

Reference40 articles.

1. Structural and evolutionary relationships among protein tyrosine phosphatase domains;Andersen;Mol. Cell Biol.,2001

2. Protein tyrosine phosphatases: prospects for therapeutics;Zhang;Curr. Opin. Chem. Biol.,2001

3. Druggable cancer phosphatases;Vainonen;Sci. Transl. Med.,2021

4. Protein tyrosine phosphatase structure-function relationships in regulation and pathogenesis;Bohmer;FEBS J.,2013

5. Recent advances of SHP2 inhibitors in cancer therapy: current development and clinical application;Yuan;J. Med. Chem.,2020

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1. Protein Tyrosine Phosphatase regulation by Reactive Oxygen Species;Advances in Cancer Research;2024

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