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Profiling protein function with small molecule microarrays

Academic Article
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Overview

authors

  • Winssinger, Nicolas
  • Ficarro, S.
  • Schultz, Peter
  • Harris, J. L.

publication date

  • August 2002

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • The regulation of protein function through posttranslational modification, local environment, and protein-protein interaction is critical to cellular function. The ability to analyze on a genome-wide scale protein functional activity rather than changes in protein abundance or structure would provide important new insights into complex biological processes. Herein, we report the application of a spatially addressable small molecule microarray to an activity-based profile of proteases in crude cell lysates. The potential of this small molecule-based profiling technology is demonstrated by the detection of caspase activation upon induction of apoptosis, characterization of the activated caspase, and inhibition of the caspase-executed apoptotic phenotype using the small molecule inhibitor identified in the microarray-based profile.

subject areas

  • Amino Acid Sequence
  • Apoptosis
  • Caspase 3
  • Caspases
  • Cathepsin K
  • Cathepsins
  • Enzyme Inhibitors
  • Gene Expression Profiling
  • Humans
  • Jurkat Cells
  • Oligonucleotide Array Sequence Analysis
  • Phenotype
  • Protein Processing, Post-Translational
  • Proteins
  • Sensitivity and Specificity
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Identity

PubMed Central ID

  • PMC123223

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.172286899

PubMed ID

  • 12167675
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Additional Document Info

start page

  • 11139

end page

  • 11144

volume

  • 99

issue

  • 17

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