Proteomic analysis of post-translational modifications View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-03

AUTHORS

Matthias Mann, Ole N Jensen

ABSTRACT

Post-translational modifications modulate the activity of most eukaryote proteins. Analysis of these modifications presents formidable challenges but their determination generates indispensable insight into biological function. Strategies developed to characterize individual proteins are now systematically applied to protein populations. The combination of function- or structure-based purification of modified 'subproteomes', such as phosphorylated proteins or modified membrane proteins, with mass spectrometry is proving particularly successful. To map modification sites in molecular detail, novel mass spectrometric peptide sequencing and analysis technologies hold tremendous potential. Finally, stable isotope labeling strategies in combination with mass spectrometry have been applied successfully to study the dynamics of modifications. More... »

PAGES

255-261

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nbt0303-255

    DOI

    http://dx.doi.org/10.1038/nbt0303-255

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1045890250

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/12610572


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