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Genetic alterations of protein tyrosine phosphatases in human cancers

Protein tyrosine phosphatases (PTPs) are enzymes that remove phosphate from tyrosine residues in proteins. Recent whole-exome sequencing of human cancer genomes reveals that many PTPs are frequently mutated in a variety of cancers. Among these mutated PTPs, protein tyrosine phosphatase T (PTPRT) app...

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Detalles Bibliográficos
Autores principales: Zhao, Shuliang, Sedwick, David, Wang, Zhenghe
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4377308/
https://www.ncbi.nlm.nih.gov/pubmed/25263441
http://dx.doi.org/10.1038/onc.2014.326
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author Zhao, Shuliang
Sedwick, David
Wang, Zhenghe
author_facet Zhao, Shuliang
Sedwick, David
Wang, Zhenghe
author_sort Zhao, Shuliang
collection PubMed
description Protein tyrosine phosphatases (PTPs) are enzymes that remove phosphate from tyrosine residues in proteins. Recent whole-exome sequencing of human cancer genomes reveals that many PTPs are frequently mutated in a variety of cancers. Among these mutated PTPs, protein tyrosine phosphatase T (PTPRT) appears to be the most frequently mutated PTP in human cancers. Beside PTPN11 which functions as an oncogene in leukemia, genetic and functional studies indicate that most of mutant PTPs are tumor suppressor genes. Identification of the substrates and corresponding kinases of the mutant PTPs may provide novel therapeutic targets for cancers harboring these mutant PTPs.
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spelling pubmed-43773082016-01-23 Genetic alterations of protein tyrosine phosphatases in human cancers Zhao, Shuliang Sedwick, David Wang, Zhenghe Oncogene Article Protein tyrosine phosphatases (PTPs) are enzymes that remove phosphate from tyrosine residues in proteins. Recent whole-exome sequencing of human cancer genomes reveals that many PTPs are frequently mutated in a variety of cancers. Among these mutated PTPs, protein tyrosine phosphatase T (PTPRT) appears to be the most frequently mutated PTP in human cancers. Beside PTPN11 which functions as an oncogene in leukemia, genetic and functional studies indicate that most of mutant PTPs are tumor suppressor genes. Identification of the substrates and corresponding kinases of the mutant PTPs may provide novel therapeutic targets for cancers harboring these mutant PTPs. 2014-09-29 2015-07-23 /pmc/articles/PMC4377308/ /pubmed/25263441 http://dx.doi.org/10.1038/onc.2014.326 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Zhao, Shuliang
Sedwick, David
Wang, Zhenghe
Genetic alterations of protein tyrosine phosphatases in human cancers
title Genetic alterations of protein tyrosine phosphatases in human cancers
title_full Genetic alterations of protein tyrosine phosphatases in human cancers
title_fullStr Genetic alterations of protein tyrosine phosphatases in human cancers
title_full_unstemmed Genetic alterations of protein tyrosine phosphatases in human cancers
title_short Genetic alterations of protein tyrosine phosphatases in human cancers
title_sort genetic alterations of protein tyrosine phosphatases in human cancers
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4377308/
https://www.ncbi.nlm.nih.gov/pubmed/25263441
http://dx.doi.org/10.1038/onc.2014.326
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