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Disparate proteome reactivity profiles of carbon electrophiles

Academic Article
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Overview

related to degree

  • Simon, Gabriel, Ph.D. in Chemistry, Scripps Research 2004 - 2009

authors

  • Weerapana, E.
  • Simon, Gabriel
  • Cravatt, Benjamin

publication date

  • July 2008

journal

  • Nature Chemical Biology  Journal

abstract

  • Insights into the proteome reactivity of electrophiles are crucial for designing activity-based probes for enzymes lacking cognate affinity labels. Here, we show that different classes of carbon electrophiles exhibit markedly distinct amino acid labeling profiles in proteomes, ranging from selective reactivity with cysteine to adducts with several amino acids. These data specify electrophilic chemotypes with restricted and permissive reactivity profiles to guide the design of next-generation functional proteomics probes.

subject areas

  • Amino Acids
  • Cysteine Endopeptidases
  • Molecular Probes
  • Proteome
  • Proteomics
  • Sensitivity and Specificity
  • Serine Endopeptidases
  • Structure-Activity Relationship
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Identity

PubMed Central ID

  • PMC2440582

International Standard Serial Number (ISSN)

  • 1552-4450

Digital Object Identifier (DOI)

  • 10.1038/nchembio.91

PubMed ID

  • 18488014
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Additional Document Info

start page

  • 405

end page

  • 407

volume

  • 4

issue

  • 7

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