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Biochemistry. Ubiquitination - more than two to tango

Academic Article
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Overview

authors

  • Joazeiro, Claudio Antonio
  • Hunter, T.

publication date

  • September 2000

journal

  • Science  Journal

abstract

  • The ubiquitin pathway in the cell is an elegant system for targeting unwanted proteins for degradation. Three enzymes, E1, E2, and E3, are responsible for attaching the ubiquitin tag to proteins destined to be chopped up. In their Perspective, Joazeiro and Hunter discuss new structural findings that reveal the part played by an E3 called c-Cbl in this ubiquitinating process.

subject areas

  • Amino Acid Motifs
  • Binding Sites
  • Ligases
  • Models, Molecular
  • Phosphorylation
  • Phosphotyrosine
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Proteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-cbl
  • Receptor Protein-Tyrosine Kinases
  • Substrate Specificity
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligases
  • Ubiquitins
  • src Homology Domains
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.289.5487.2061

PubMed ID

  • 11032556
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Additional Document Info

start page

  • 2061

end page

  • 2062

volume

  • 289

issue

  • 5487

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