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Showing 1–5 of 5 results
Advanced filters: Author: "Allan M Weissman" Clear advanced filters

  • Substrate specificity in ubiquitylation is conferred by ubiquitin ligases (E3s). Now, several ways that E3s can interact to mediate ubiquitylation are illustrated for Ubr1 (a RING finger E3) and Ufd4 (a HECT domain E3), in Saccharomyces cerevisiae. These interactions and the related concept of E4 activity are discussed.

    • Meredith B. Metzger
    • Allan M. Weissman
    News & Views
    Nature Cell Biology
    Volume: 12, P: 1124-1126

  • Ubiquitylation regulates essentially all of the intracellular processes in eukaryotes by modifying numerous cellular proteins in a spatially and temporally controlled manner. Many components of the ubiquitin–proteasome system are themselves modified by ubiquitylation; this regulates their activity or targets them for degradation.

    • Allan M. Weissman
    • Nitzan Shabek
    • Aaron Ciechanover
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 12, P: 605-620

  • Several members of the tripartite motif (TRIM) proteins (one of the subfamilies of the RING type E3 ubiquitin ligases) seem to function as important regulators for carcinogenesis. This Review focuses on TRIM proteins that are involved in tumour development and progression.

    • Shigetsugu Hatakeyama
    Reviews
    Nature Reviews Cancer
    Volume: 11, P: 792-804