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Electrostatic and steric effects underlie acetylation-induced changes in ubiquitin structure and function
- Source :
- Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
- Publication Year :
- 2022
- Publisher :
- Nature Portfolio, 2022.
-
Abstract
- Ubiquitin is not only a posttranslational modifier but itself is subject to modifications, such as acetylation. Characterization of distinct acetylated ubiquitin variants reveals that each acetylation site has a particular impact on ubiquitin structure and its protein-protein interaction properties.
- Subjects :
- Science
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Volume :
- 13
- Issue :
- 1
- Database :
- Directory of Open Access Journals
- Journal :
- Nature Communications
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.1e21cc4548474d48816030ee2117176a
- Document Type :
- article
- Full Text :
- https://doi.org/10.1038/s41467-022-33087-1