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Nature Cell Biology  4, E121 - E123 (2002)
doi:10.1038/ncb0502-e121

Ubiquitin chained and crosslinked

Daniel Finley

Daniel Finley is at the Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115, USA
daniel_finley@hms.harvard.edu

Polyubiquitin chains are assembled onto proteins destined for degradation. The target protein is then unfolded by the proteasome and translocated through a channel leading from the unfolding site to an internal chamber of the enzyme for hydrolysis. A recent paper illuminates the long-elusive polyubiquitin chain recognition step that initiates this sequence of events at the proteasome.

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REFERENCE
Protease Complexes
Nature Encyclopaedia of Life Sciences
 See all 2 matches for Reference

NEWS AND VIEWS
Cell biology: Unchaining the condemned
Nature News and Views (26 Sep 2002)

RESEARCH
A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
Nature Letters to Editor (18 Apr 2002)
Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome
The EMBO Journal Article (17 Dec 2001)
Developmentally regulated, alternative splicing of the Rpn10 gene generates multiple forms of 26S proteasomes
The EMBO Journal Article (01 Aug 2000)
 See all 6 matches for Research

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Nature Cell Biology
ISSN: 1465-7392
EISSN: 1476-4679
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