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Discovering disease-associated enzymes by proteome reactivity profiling

Academic Article
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Overview

related to degree

  • Barglow, Katy, Ph.D. in Biochemistry, Scripps Research 2002 - 2008

authors

  • Barglow, Katy
  • Cravatt, Benjamin

publication date

  • 2004

journal

  • Chemistry & Biology  Journal

abstract

  • Proteomics aims to identify new markers and targets for the diagnosis and treatment of human disease. To realize this goal, methods and reagents are needed to profile proteins based on their functional properties, rather than mere abundance. Here, we describe a general strategy for synthesizing and evaluating structurally diverse libraries of activity-based proteomic probes. Quantitative screening of probe-proteome reactions coupled with bioinformatic analysis enabled the selection of a suite of probes that exhibit complementary protein reactivity profiles. This optimal probe set was applied to discover several enzyme activities differentially expressed in lean and obese (ob/ob) mice. Interestingly, one of these enzymes, hydroxypyruvate reductase, which was 6-fold upregulated in ob/ob livers, participates in the conversion of serine to glucose, suggesting that this unusual metabolic pathway may contribute to gluconeogenesis selectively in states of obesity.

subject areas

  • Acetamides
  • Alcohol Oxidoreductases
  • Animals
  • Brain
  • Computational Biology
  • Diabetes Mellitus, Type 2
  • Disease
  • Disease Models, Animal
  • Drug Design
  • Humans
  • Hydroxypyruvate Reductase
  • Liver
  • Mice
  • Mice, Obese
  • Molecular Probes
  • Myocardium
  • Obesity
  • Peptide Library
  • Proteomics
  • Up-Regulation
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Identity

International Standard Serial Number (ISSN)

  • 1074-5521

Digital Object Identifier (DOI)

  • 10.1016/j.chembiol.2004.08.023

PubMed ID

  • 15556003
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Additional Document Info

start page

  • 1523

end page

  • 1531

volume

  • 11

issue

  • 11

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