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HECT and RING finger families of E3 ubiquitin ligases at a glance
Author(s) -
Meredith B. Metzger,
Ventzislava A. Hristova,
Allan M. Weissman
Publication year - 2012
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.091777
Subject(s) - biology , ubiquitin , ring finger , ubiquitin protein ligases , ubiquitin ligase , ring (chemistry) , ring finger domain , genetics , evolutionary biology , microbiology and biotechnology , zinc finger , transcription factor , gene , chemistry , organic chemistry
The post-translational attachment of ubiquitin, a highly conserved 76-amino-acid polypeptide, directs myriad eukaryotic proteins to a variety of fates and functions. Ubiquitylation is best-known for targeting proteins for degradation by the 26S proteasome. Other functions include internalization and

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