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Proteomic approaches to the characterization of protein thiol modification
Protein cysteine residues are central to redox signaling and to protection against oxidative damage through their interactions with reactive oxygen and nitrogen species, and electrophiles. Although there is considerable evidence for a functional role for cysteine modifications, the identity and phys...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3087609/ https://www.ncbi.nlm.nih.gov/pubmed/21130020 http://dx.doi.org/10.1016/j.cbpa.2010.11.003 |
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author | Chouchani, Edward T James, Andrew M Fearnley, Ian M Lilley, Kathryn S Murphy, Michael P |
author_facet | Chouchani, Edward T James, Andrew M Fearnley, Ian M Lilley, Kathryn S Murphy, Michael P |
author_sort | Chouchani, Edward T |
collection | PubMed |
description | Protein cysteine residues are central to redox signaling and to protection against oxidative damage through their interactions with reactive oxygen and nitrogen species, and electrophiles. Although there is considerable evidence for a functional role for cysteine modifications, the identity and physiological significance of most protein thiol alterations are unknown. One way to identify candidate proteins involved in these processes is to utilize the proteomic methodologies that have been developed in recent years for the identification of proteins that undergo cysteine modification in response to redox signals or oxidative damage. These tools have proven effective in uncovering novel protein targets of redox modification and are important first steps that allow for a better understanding of how reactive molecules may contribute to signaling and damage. Here, we discuss a number of these approaches and their application to the identification of a variety of cysteine-centered redox modifications. |
format | Text |
id | pubmed-3087609 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-30876092011-05-31 Proteomic approaches to the characterization of protein thiol modification Chouchani, Edward T James, Andrew M Fearnley, Ian M Lilley, Kathryn S Murphy, Michael P Curr Opin Chem Biol Article Protein cysteine residues are central to redox signaling and to protection against oxidative damage through their interactions with reactive oxygen and nitrogen species, and electrophiles. Although there is considerable evidence for a functional role for cysteine modifications, the identity and physiological significance of most protein thiol alterations are unknown. One way to identify candidate proteins involved in these processes is to utilize the proteomic methodologies that have been developed in recent years for the identification of proteins that undergo cysteine modification in response to redox signals or oxidative damage. These tools have proven effective in uncovering novel protein targets of redox modification and are important first steps that allow for a better understanding of how reactive molecules may contribute to signaling and damage. Here, we discuss a number of these approaches and their application to the identification of a variety of cysteine-centered redox modifications. Elsevier 2011-02 /pmc/articles/PMC3087609/ /pubmed/21130020 http://dx.doi.org/10.1016/j.cbpa.2010.11.003 Text en © 2011 Elsevier Ltd. https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license |
spellingShingle | Article Chouchani, Edward T James, Andrew M Fearnley, Ian M Lilley, Kathryn S Murphy, Michael P Proteomic approaches to the characterization of protein thiol modification |
title | Proteomic approaches to the characterization of protein thiol modification |
title_full | Proteomic approaches to the characterization of protein thiol modification |
title_fullStr | Proteomic approaches to the characterization of protein thiol modification |
title_full_unstemmed | Proteomic approaches to the characterization of protein thiol modification |
title_short | Proteomic approaches to the characterization of protein thiol modification |
title_sort | proteomic approaches to the characterization of protein thiol modification |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3087609/ https://www.ncbi.nlm.nih.gov/pubmed/21130020 http://dx.doi.org/10.1016/j.cbpa.2010.11.003 |
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