New tools for quantitative phosphoproteome analysis.

Thomas P. Conrads*, Haleem J. Issaq, Timothy D. Veenstra

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

60 Scopus citations


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.

Original languageEnglish
Pages (from-to)885-890
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - 25 Jan 2002
Externally publishedYes


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