Evolution and functional cross‐talk of protein post‐translational modifications
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- Pedro Beltrao
- European Molecular Biology Laboratory European Bioinformatics Institute (EMBL‐EBI) Cambridge UK
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- Peer Bork
- Structural and Computational Biology Unit European Molecular Biology Laboratory Heidelberg Germany
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- Nevan J. Krogan
- Department of Cellular and Molecular Pharmacology University of California San Francisco California USA
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- Vera van Noort
- Structural and Computational Biology Unit European Molecular Biology Laboratory Heidelberg Germany
書誌事項
- 公開日
- 2013-01
- 権利情報
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- http://creativecommons.org/licenses/by-nc-sa/3.0/
- DOI
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- 10.1002/msb.201304521
- 公開者
- Springer Science and Business Media LLC
この論文をさがす
説明
<jats:title>Abstract</jats:title> <jats:p> Protein post‐translational modifications ( <jats:styled-content style="fixed-case">PTM</jats:styled-content> s) allow the cell to regulate protein activity and play a crucial role in the response to changes in external conditions or internal states. Advances in mass spectrometry now enable proteome wide characterization of <jats:styled-content style="fixed-case">PTM</jats:styled-content> s and have revealed a broad functional role for a range of different types of modifications. Here we review advances in the study of the evolution and function of <jats:styled-content style="fixed-case">PTM</jats:styled-content> s that were spurred by these technological improvements. We provide an overview of studies focusing on the origin and evolution of regulatory enzymes as well as the evolutionary dynamics of modification sites. Finally, we discuss different mechanisms of altering protein activity via post‐translational regulation and progress made in the large‐scale functional characterization of <jats:styled-content style="fixed-case">PTM</jats:styled-content> function. </jats:p>
収録刊行物
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- Molecular Systems Biology
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Molecular Systems Biology 9 (1), 714-, 2013-01
Springer Science and Business Media LLC
