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Towards the computational design of protein post-translational regulation

Protein post-translational modifications (PTMs) are a fast and versatility mechanism used by the cell to regulate the function of proteins in response to changing conditions. PTMs can alter the activity of proteins by allosteric regulation or by controlling protein interactions, localization and abu...

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Detalles Bibliográficos
Autores principales: Strumillo, Marta, Beltrao, Pedro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4673319/
https://www.ncbi.nlm.nih.gov/pubmed/25956846
http://dx.doi.org/10.1016/j.bmc.2015.04.056
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author Strumillo, Marta
Beltrao, Pedro
author_facet Strumillo, Marta
Beltrao, Pedro
author_sort Strumillo, Marta
collection PubMed
description Protein post-translational modifications (PTMs) are a fast and versatility mechanism used by the cell to regulate the function of proteins in response to changing conditions. PTMs can alter the activity of proteins by allosteric regulation or by controlling protein interactions, localization and abundance. Recent advances in proteomics have revealed the extent of regulation by PTMs and the different mechanisms used in nature to exert control over protein function via PTMs. These developments can serve as the foundation for the rational design of protein regulation. Here we review the advances in methods to determine the function of PTMs, protein allosteric control and examples of rational design of PTM regulation. These advances create an opportunity to move synthetic biology forward by making use of a level of regulation that is of yet unexplored.
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spelling pubmed-46733192015-12-29 Towards the computational design of protein post-translational regulation Strumillo, Marta Beltrao, Pedro Bioorg Med Chem Article Protein post-translational modifications (PTMs) are a fast and versatility mechanism used by the cell to regulate the function of proteins in response to changing conditions. PTMs can alter the activity of proteins by allosteric regulation or by controlling protein interactions, localization and abundance. Recent advances in proteomics have revealed the extent of regulation by PTMs and the different mechanisms used in nature to exert control over protein function via PTMs. These developments can serve as the foundation for the rational design of protein regulation. Here we review the advances in methods to determine the function of PTMs, protein allosteric control and examples of rational design of PTM regulation. These advances create an opportunity to move synthetic biology forward by making use of a level of regulation that is of yet unexplored. Elsevier Science 2015-06-15 /pmc/articles/PMC4673319/ /pubmed/25956846 http://dx.doi.org/10.1016/j.bmc.2015.04.056 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Strumillo, Marta
Beltrao, Pedro
Towards the computational design of protein post-translational regulation
title Towards the computational design of protein post-translational regulation
title_full Towards the computational design of protein post-translational regulation
title_fullStr Towards the computational design of protein post-translational regulation
title_full_unstemmed Towards the computational design of protein post-translational regulation
title_short Towards the computational design of protein post-translational regulation
title_sort towards the computational design of protein post-translational regulation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4673319/
https://www.ncbi.nlm.nih.gov/pubmed/25956846
http://dx.doi.org/10.1016/j.bmc.2015.04.056
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