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Cysteine tagging for MS-based proteomics

Published in Mass Spectrometry Reviews. 2011, vol. 30, no. 3, p. 366-95
Abstract Amino acid-tagging strategies are widespread in proteomics. Because of the central role of mass spectrometry (MS) as a detection technique in protein sciences, the term "mass tagging" was coined to describe the attachment of a label, which serves MS analysis and/or adds analytical value to the measurements. These so-called mass tags can be used for separation, enrichment, detection, and quantitation of peptides and proteins. In this context, cysteine is a frequent target for modifications because the thiol function can react specifically by nucleophilic substitution or addition. Furthermore, cysteines present natural modifications of biological importance and a low occurrence in the proteome that justify the development of strategies to specifically target them in peptides or proteins. In the present review, the mass-tagging methods directed to cysteine residues are comprehensively discussed, and the advantages and drawbacks of these strategies are addressed. Some concrete applications are given to underline the relevance of cysteine-tagging techniques for MS-based proteomics.
Keywords AnimalsCysteine/analysis/chemistry/metabolismHumansMass Spectrometry/methodsProteome/analysis/chemistry/metabolismProteomics/methods
PMID: 21500242
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Research group Groupe de Protéomique biomédicale (635)
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GIRON, Priscille, DAYON, Loic, SANCHEZ, Jean-Charles. Cysteine tagging for MS-based proteomics. In: Mass Spectrometry Reviews, 2011 , vol. 30, n° 3, p. 366-95. doi: 10.1002/mas.20285 https://archive-ouverte.unige.ch/unige:25566

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Deposited on : 2013-01-16

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