Ontology highlight
ABSTRACT:
SUBMITTER: Yu Y
PROVIDER: S-EPMC8717942 | biostudies-literature | 2021 Aug
REPOSITORIES: biostudies-literature
Yu Yuanyuan Y Zheng Qingyun Q Erramilli Satchal K SK Pan Man M Park Seongjin S Xie Yuan Y Li Jingxian J Fei Jingyi J Kossiakoff Anthony A AA Liu Lei L Zhao Minglei M
Nature chemical biology 20210708 8
Protein ubiquitination shows remarkable topological and functional diversity through the polymerization of ubiquitin via different linkages. Deciphering the cellular ubiquitin code is of central importance to understand the physiology of the cell. However, our understanding of its function is rather limited due to the lack of specific binders as tools to detect K29-linked polyubiquitin. In this study, we screened and characterized a synthetic antigen-binding fragment, termed sAB-K29, that can sp ...[more]