Systems-wide proteomic characterization of combinatorial post-translational modification patterns
Protein post-translational modifications (PTMs) have been widely shown to influence protein-protein interactions, direct subcellular location and transduce a variety of both internal and externally generated signals into cellular/phenotypic outcomes. Mass spectrometry has been a key tool for the elu...
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Published in | Expert review of proteomics Vol. 7; no. 1; pp. 79 - 92 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
England
Taylor & Francis
01.02.2010
Expert Reviews Ltd Informa Healthcare |
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Abstract | Protein post-translational modifications (PTMs) have been widely shown to influence protein-protein interactions, direct subcellular location and transduce a variety of both internal and externally generated signals into cellular/phenotypic outcomes. Mass spectrometry has been a key tool for the elucidation of several types of PTMs in both qualitative and quantitative manners. As large datasets on the proteome-wide level are now being generated on a daily basis, the identification of combinatorial PTM patterns has become feasible. A survey of the recent literature in this area shows that many proteins undergo multiple modifications and that sequential or hierarchal patterns exist on many proteins; the biology of these modification patterns is only starting to be unraveled. This review will outline combinatorial PTM examples in biology, and the mass spectrometry-based techniques and applications utilized in the investigations of these combinatorial PTMs. |
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AbstractList | Protein post-translational modifications (PTMs) have been widely shown to influence protein-âprotein interactions, direct subcellular location and transduce a variety of both internal and externally generated signals into cellular/phenotypic outcomes. Mass spectrometry has been a key tool for the elucidation of several types of PTMs in both qualitative and quantitative manners. As large datasets on the proteome-wide level are now being generated on a daily basis, the identification of combinatorial PTM patterns has become feasible. A survey of the recent literature in this area shows that many proteins undergo multiple modifications and that sequential or hierarchal patterns exist on many proteins; the biology of these modification patterns is only starting to be unraveled. This review will outline combinatorial PTM examples in biology, and the mass spectrometry-based techniques and applications utilized in the investigations of these combinatorial PTMs. Protein post-translational modifications (PTMs) have been widely shown to influence protein-protein interactions, direct subcellular location and transduce a variety of both internal and externally generated signals into cellular/phenotypic outcomes. Mass spectrometry has been a key tool for the elucidation of several types of PTMs in both qualitative and quantitative manners. As large datasets on the proteome-wide level are now being generated on a daily basis, the identification of combinatorial PTM patterns has become feasible. A survey of the recent literature in this area shows that many proteins undergo multiple modifications and that sequential or hierarchal patterns exist on many proteins; the biology of these modification patterns is only starting to be unraveled. This review will outline combinatorial PTM examples in biology, and the mass spectrometry-based techniques and applications utilized in the investigations of these combinatorial PTMs. |
Audience | Academic |
Author | Plazas-Mayorca, Mariana D Garcia, Benjamin A Young, Nicolas L |
Author_xml | – sequence: 1 givenname: Nicolas L surname: Young fullname: Young, Nicolas L – sequence: 2 givenname: Mariana D surname: Plazas-Mayorca fullname: Plazas-Mayorca, Mariana D – sequence: 3 givenname: Benjamin A surname: Garcia fullname: Garcia, Benjamin A |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20121478$$D View this record in MEDLINE/PubMed |
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Snippet | Protein post-translational modifications (PTMs) have been widely shown to influence protein-protein interactions, direct subcellular location and transduce a... Protein post-translational modifications (PTMs) have been widely shown to influence protein-âprotein interactions, direct subcellular location and transduce a... |
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SubjectTerms | electron-capture dissociation electron-transfer dissociation histone code Mass spectrometry Mass Spectrometry - methods Methods middle-down approach Observations Post-translational modification Properties Protein Processing, Post-Translational Proteins - analysis Proteomics Proteomics - methods top-down approach |
Title | Systems-wide proteomic characterization of combinatorial post-translational modification patterns |
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