Pharmaceutical Sciences Faculty Publications

New Tools for Quantitative Phosphoproteome Analysis

Document Type

Article

Publication Date

1-25-2002

Journal Title

Biochemical and Biophysical Research Communications

ISSN

0006-291X

Volume

290

Issue

3

First Page

885

Last Page

890

DOI

10.1006/bbrc.2001.6275

PubMed ID

11798155

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.

Keywords

Caseins, mass spectrometry, models, chemical, peptides, phosphoproteins, phosphorylation, proteome

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