| Literature DB >> 21402121 |
Abstract
A substantial part of soluble, oxidized proteins are degraded by the proteasome. However, it is still under debate whether these oxidized proteins are degraded by the 26S proteasome in an ubiquitin-dependent way or in an ubiquitin-independent way by the 20S proteasome. Therefore, we treated cells with H(2)O(2) and UV-A irradiation and detected protein carbonyls and ubiquitination by immunoblotting. Separation of ubiquitinated proteins from non-ubiquitinated reveals that most oxidized proteins are not ubiquitinated.Mesh：
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Year: 2011 PMID： 21402121 DOI： 10.1016/j.biochi.2011.03.004
Source DB: PubMed Journal: Biochimie ISSN： 0300-9084 Impact factor: 4.079