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Deubiquitinating enzyme specificity for ubiquitin chain topology profiled by di-ubiquitin activity probes.

Abstract:

Posttranslational modification with ubiquitin (Ub) controls many cellular processes, and aberrant ubiquitination can contribute to cancer, immunopathology, and neurodegeneration. The versatility arises from the ability of Ub to form polymer chains with eight distinct linkages via lysine side chains and the N terminus. In this study, we engineered Di-Ub probes mimicking all eight different poly-Ub linkages and profiled the deubiquitinating enzyme (DUB) selectivity for recognizing Di-Ub moietie...

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Publication status:
Published

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Authors


McGouran, JF More by this author
Gaertner, SR More by this author
Kramer, HB More by this author
Kessler, BM More by this author
Journal:
Chemistry and biology
Volume:
20
Issue:
12
Pages:
1447-1455
Publication date:
2013-12-05
DOI:
EISSN:
1879-1301
ISSN:
1074-5521
URN:
uuid:2fe70287-0e8d-4133-b446-d25d0bdc54de
Source identifiers:
440077
Local pid:
pubs:440077

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