Cargando…
The Redox Proteome
The redox proteome consists of reversible and irreversible covalent modifications that link redox metabolism to biologic structure and function. These modifications, especially of Cys, function at the molecular level in protein folding and maturation, catalytic activity, signaling, and macromolecula...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3772199/ https://www.ncbi.nlm.nih.gov/pubmed/23861437 http://dx.doi.org/10.1074/jbc.R113.464131 |
_version_ | 1782284296342470656 |
---|---|
author | Go, Young-Mi Jones, Dean P. |
author_facet | Go, Young-Mi Jones, Dean P. |
author_sort | Go, Young-Mi |
collection | PubMed |
description | The redox proteome consists of reversible and irreversible covalent modifications that link redox metabolism to biologic structure and function. These modifications, especially of Cys, function at the molecular level in protein folding and maturation, catalytic activity, signaling, and macromolecular interactions and at the macroscopic level in control of secretion and cell shape. Interaction of the redox proteome with redox-active chemicals is central to macromolecular structure, regulation, and signaling during the life cycle and has a central role in the tolerance and adaptability to diet and environmental challenges. |
format | Online Article Text |
id | pubmed-3772199 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-37721992013-09-16 The Redox Proteome Go, Young-Mi Jones, Dean P. J Biol Chem Minireviews The redox proteome consists of reversible and irreversible covalent modifications that link redox metabolism to biologic structure and function. These modifications, especially of Cys, function at the molecular level in protein folding and maturation, catalytic activity, signaling, and macromolecular interactions and at the macroscopic level in control of secretion and cell shape. Interaction of the redox proteome with redox-active chemicals is central to macromolecular structure, regulation, and signaling during the life cycle and has a central role in the tolerance and adaptability to diet and environmental challenges. American Society for Biochemistry and Molecular Biology 2013-09-13 2013-07-16 /pmc/articles/PMC3772199/ /pubmed/23861437 http://dx.doi.org/10.1074/jbc.R113.464131 Text en © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version full access. Creative Commons Attribution Unported License (http://creativecommons.org/licenses/by/3.0/) applies to Author Choice Articles |
spellingShingle | Minireviews Go, Young-Mi Jones, Dean P. The Redox Proteome |
title | The Redox Proteome |
title_full | The Redox Proteome |
title_fullStr | The Redox Proteome |
title_full_unstemmed | The Redox Proteome |
title_short | The Redox Proteome |
title_sort | redox proteome |
topic | Minireviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3772199/ https://www.ncbi.nlm.nih.gov/pubmed/23861437 http://dx.doi.org/10.1074/jbc.R113.464131 |
work_keys_str_mv | AT goyoungmi theredoxproteome AT jonesdeanp theredoxproteome AT goyoungmi redoxproteome AT jonesdeanp redoxproteome |