Structures of ZYG11B-EloB-EloC-substrate complex reveal mechanisms of CRL2ZYG11B assembly and function
-mediated ubiquitination and offer mechanistic insights that may inform the rational design of ZYG11B-based applications.
Authors
- Yina Gao
- Ni Lin
- Yushan Geng
- Songqing Liu
- Pu Gao
- Miao Shi
- Han Feng
Institutions
- Chinese Academy of Sciences (CN)
- Institute of Biophysics (CN)
- Shandong First Medical University (CN)
- University of Chinese Academy of Sciences (CN)
Publication Details
- Journal
- Nature Communications
- Published
- 2026-03-31
- DOI
- https://doi.org/10.1038/s41467-026-71318-x
- Primary Topic
- Ubiquitin and proteasome pathways
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China
- Chinese Academy of Sciences
- Natural Science Foundation of Shandong Province
- University of Science and Technology of China
- Shandong First Medical University
- National Science and Technology Major Project
- Institute of Biophysics, Chinese Academy of Sciences