Reversible oxidation of PRL family protein-tyrosine phosphatases
Author:
Publisher
Elsevier BV
Subject
General Biochemistry, Genetics and Molecular Biology,Molecular Biology
Reference37 articles.
1. Oxidants, oxidative stress and the biology of ageing
2. Regulation of Nox and Duox enzymatic activity and expression
3. Redox Regulation of Protein Tyrosine Phosphatases: Structural and Chemical Aspects
4. Regulation of protein tyrosine phosphatases by reversible oxidation
5. Thioredoxin-related Protein 32 (TRP32) Specifically Reduces Oxidized Phosphatase of Regenerating Liver (PRL)
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1. Burst kinetics and CNNM binding are evolutionarily conserved properties of phosphatases of regenerating liver;Journal of Biological Chemistry;2023-04
2. HSC70 mediated autophagic degradation of oxidized PRL2 is responsible for osteoclastogenesis and inflammatory bone destruction;Cell Death & Differentiation;2022-10-01
3. The double lives of phosphatases of regenerating liver: A structural view of their catalytic and noncatalytic activities;Journal of Biological Chemistry;2022-01
4. Phosphatase, pseudo-phosphatase, or both? Understanding PRL oncogenicity;British Journal of Cancer;2020-12-03
5. PRL3 pseudophosphatase activity is necessary and sufficient to promote metastatic growth;Journal of Biological Chemistry;2020-08
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