New tools for quantitative phosphoproteome analysis.

Thomas P Conrads; Haleem J Issaq; Timothy D Veenstra

doi:10.1006/bbrc.2001.6275

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New tools for quantitative phosphoproteome analysis.

Thomas P Conrads·Haleem J Issaq·Timothy D Veenstra

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Abstract

Recent advances in analytical methods, particularly in the area of mass spectrometry, have brought the field of proteomics to the forefront in biological science. The ultimate goal of proteomics--to characterize proteins expressed within a cell under a specific set of conditions--is daunting due to the complexity and dynamic nature the of protein population within the cell. While much of the effort has focused on developing methods to identify expressed proteins, the identification of posttranslational modifications is equally important for comprehensive proteome characterization. Of all the known posttranslational modifications, phosphorylation arguably plays the largest role in the context of cellular homeostasis. This review discusses some of the recent progress made in the development of techniques not only to identify, but also to quantitatively determine sites of phosphorylation.

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Animals Caseins Mass Spectrometry Models, Chemical Peptides Phosphoproteins Phosphorylation Proteome Journal Article Research Support, U.S. Gov't, P.H.S.Review

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Thomas P Conrads, Haleem J Issaq, Timothy D Veenstra. 2002-01-25. New tools for quantitative phosphoproteome analysis.. https://doi.org/10.1006/bbrc.2001.6275

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