Aspirin inhibits proteasomal degradation and promotes α-synuclein aggregate clearance through K63 ub...
Aspirin inhibits proteasomal degradation and promotes α-synuclein aggregate clearance through K63 ubiquitination
About this item
Full title
Author / Creator
Gao, Jing , Liu, Yang , Si, Chenfang , Guo, Rui , Hou, Shouqiao , Liu, Xiaosong , Long, Houfang , Liu, Di , Xu, Daichao , Zhang, Zai-Rong , Liu, Cong , Shan, Bing , Turck, Christoph W. , He, Kaiwen and Zhang, Yaoyang
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
Aspirin is a potent lysine acetylation inducer, but its impact on lysine ubiquitination and ubiquitination-directed protein degradation is unclear. Herein, we develop the reversed-pulsed-SILAC strategy to systematically profile protein degradome in response to aspirin. By integrating degradome, acetylome, and ubiquitinome analyses, we show that asp...
Alternative Titles
Full title
Aspirin inhibits proteasomal degradation and promotes α-synuclein aggregate clearance through K63 ubiquitination
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_2ef8077f05864986a86dd1919afa5d1e
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_2ef8077f05864986a86dd1919afa5d1e
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-025-56737-6
