Sirtuin-1 Sensitive Lysine-136 Acetylation Drives Phase Separation and Pathological Aggregation of T...
Sirtuin-1 Sensitive Lysine-136 Acetylation Drives Phase Separation and Pathological Aggregation of TDP-43
About this item
Full title
Author / Creator
Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
Journal title
Language
English
Formats
Publication information
Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
Subjects
More information
Scope and Contents
Contents
The trans-activation response DNA-binding protein TDP-43 regulates RNA processing and forms neuropathological aggregates in patients with amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Investigating TDP-43 post-translational modifications, we discovered that K84 acetylation reduced nuclear import whereas K136 acetylation impai...
Alternative Titles
Full title
Sirtuin-1 Sensitive Lysine-136 Acetylation Drives Phase Separation and Pathological Aggregation of TDP-43
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_proquest_journals_2406735245
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2406735245
Other Identifiers
E-ISSN
2692-8205
DOI
10.1101/2020.05.26.104356
How to access this item
https://www.proquest.com/docview/2406735245?pq-origsite=primo&accountid=13902
