- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/j.chembiol.2013.10.012
-
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- 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
- Language:
- English
- Keywords:
- Copyright date:
- 2013
Journal article
Deubiquitinating enzyme specificity for ubiquitin chain topology profiled by di-ubiquitin activity probes.
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