Chemical approaches for functionally probing the proteome.

Doron Greenbaum, Amos Baruch, Linda Hayrapetian, Zsuzsanna Darula, Alma Burlingame, Katlin F. Medzihradszky, Matthew Bogyo

Research output: Contribution to journalArticle

238 Citations (Scopus)

Abstract

With the availability of complete genome sequences, emphasis has shifted toward the understanding of protein function. We have developed a functional proteomic methodology that makes use of chemically reactive fluorescent probes to profile and identify enzymes in complex mixtures by virtue of their catalytic activity. This methodology allows a comparison of changes in activity of multiple enzymes under a variety of conditions using a single two-dimensional separation. The probes can also be used to localize active enzymes in intact cells using fluorescence microscopy. Furthermore, the probes enable screens for selective small molecule inhibitors of each enzyme family member within crude lysates or intact cells. Ultimately, this technology allows the rapid identification of potential drug targets and small molecule lead compounds targeted to them.

Original languageEnglish
Pages (from-to)60-68
Number of pages9
JournalMolecular & cellular proteomics : MCP
Volume1
Issue number1
DOIs
Publication statusPublished - Jan 2002

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Molecular Biology

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  • Cite this

    Greenbaum, D., Baruch, A., Hayrapetian, L., Darula, Z., Burlingame, A., Medzihradszky, K. F., & Bogyo, M. (2002). Chemical approaches for functionally probing the proteome. Molecular & cellular proteomics : MCP, 1(1), 60-68. https://doi.org/10.1074/mcp.T100003-MCP200