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Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics
The human protein methyltransferases (PMTs) constitute a large enzyme class composed of two families, the protein lysine methyltransferases (PKMTs) and the protein arginine methyltransferases (PRMTs). Examples have been reported of both PKMTs and PRMTs that are genetically altered in specific human...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3579158/ https://www.ncbi.nlm.nih.gov/pubmed/23160372 http://dx.doi.org/10.1038/onc.2012.552 |
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author | Copeland, R A Moyer, M P Richon, V M |
author_facet | Copeland, R A Moyer, M P Richon, V M |
author_sort | Copeland, R A |
collection | PubMed |
description | The human protein methyltransferases (PMTs) constitute a large enzyme class composed of two families, the protein lysine methyltransferases (PKMTs) and the protein arginine methyltransferases (PRMTs). Examples have been reported of both PKMTs and PRMTs that are genetically altered in specific human cancers, and in several cases these alterations have been demonstrated to confer a unique dependence of the cancer cells on PMT enzymatic activity for the tumorigenic phenotype. Examples of such driver alterations in PMTs will be presented together with a review of current efforts towards the discovery and development of small-molecule inhibitors of these enzymes as personalized cancer therapeutics. |
format | Online Article Text |
id | pubmed-3579158 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-35791582013-02-22 Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics Copeland, R A Moyer, M P Richon, V M Oncogene Review The human protein methyltransferases (PMTs) constitute a large enzyme class composed of two families, the protein lysine methyltransferases (PKMTs) and the protein arginine methyltransferases (PRMTs). Examples have been reported of both PKMTs and PRMTs that are genetically altered in specific human cancers, and in several cases these alterations have been demonstrated to confer a unique dependence of the cancer cells on PMT enzymatic activity for the tumorigenic phenotype. Examples of such driver alterations in PMTs will be presented together with a review of current efforts towards the discovery and development of small-molecule inhibitors of these enzymes as personalized cancer therapeutics. Nature Publishing Group 2013-02-21 2012-11-19 /pmc/articles/PMC3579158/ /pubmed/23160372 http://dx.doi.org/10.1038/onc.2012.552 Text en Copyright © 2013 Macmillan Publishers Limited http://creativecommons.org/licenses/by-nc-nd/3.0/ This work is licensed under the Creative Commons Attribution-NonCommercial-No Derivative Works 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/ |
spellingShingle | Review Copeland, R A Moyer, M P Richon, V M Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics |
title | Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics |
title_full | Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics |
title_fullStr | Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics |
title_full_unstemmed | Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics |
title_short | Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics |
title_sort | targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3579158/ https://www.ncbi.nlm.nih.gov/pubmed/23160372 http://dx.doi.org/10.1038/onc.2012.552 |
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