Existing Bioinformatics Tools for the Quantitation of Post-Translational Modifications
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Date
Authors
Allmer, Jens
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Volume Title
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Open Access Color
GOLD
Green Open Access
Yes
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Publicly Funded
No
Abstract
Mass spectrometry (MS)-based proteomics, by itself, is a vast and complex area encompassing various mass spectrometers, different spectra, and search result representations. When the aim is quantitation performed in different scanning modes at different MS levels, matters become additionally complex. Quantitation of post-translational modifications (PTM) represents the greatest challenge among these endeavors. Many different approaches to quantitation have been described and some of these can be directly applied to the quantitation of PTMs. The amount of data produced via MS, however, makes manual data interpretation impractical. Therefore, specialized software tools meet this challenge. Any software currently able to quantitate differentially labeled samples may theoretically be adapted to quantitate differential PTM expression among samples as well. Due to the heterogeneity of mass spectrometry-based proteomics; this review will focus on quantitation of PTM using liquid chromatography followed by one or more stages of mass spectrometry. Currently available free software, which either allow analysis of PTM or are easily adaptable for this purpose, is briefly reviewed in this paper. Selected studies, especially those related to phosphoproteomics, shall be used to highlight the current ability to quantitate PTMs. © Springer-Verlag 2010
Description
Keywords
LC-MS, Post-translational modification, PTM, Quantification, PTM, Quantification, Computational Biology, Proteins, Post-translational modification, Protein Processing, Post-Translational, Mass Spectrometry, LC-MS, Chromatography, Liquid
Fields of Science
0301 basic medicine, 03 medical and health sciences
Citation
Allmer, J. (2012). Existing bioinformatics tools for the quantitation of post-translational modifications. Amino Acids, 42(1), 129-138. doi:10.1007/s00726-010-0614-3
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OpenCitations Citation Count
13
Source
Volume
42
Issue
1
Start Page
129
End Page
138
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CrossRef : 7
Scopus : 12
PubMed : 2
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