Lou Gehrig’s Disease (ALS): UBQLN2 Mutations Strike Out of Phase-Reference-Cited by-同舟云学术

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Lou Gehrig’s Disease (ALS): UBQLN2 Mutations Strike Out of Phase

Published:2019-06 Issue:6 Volume:27 Page:879-881
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Higgins Nicole,Lin Brian,Monteiro Mervyn J.

Funder

Robert Packard Center for ALS Research

ALS Association

National Institutes of Health

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference10 articles.

1. Ubiquilin 2 modulates ALS/FTD-linked FUS-RNA complex dynamics and stress granule formation;Alexander;Proc. Natl. Acad. Sci. USA,2018

2. Defective proteasome delivery of polyubiquitinated proteins by ubiquilin-2 proteins containing ALS mutations;Chang;PLoS ONE,2015

3. Mutant UBQLN2P497H in motor neurons leads to ALS-like phenotypes and defective autophagy in rats;Chen;Acta Neuropathol. Commun.,2018

4. Ubiquitin modulates liquid-liquid phase separation of UBQLN2 via disruption of multivalent interactions;Dao;Mol. Cell,2018

5. ALS-linked mutations affect UBQLN2 oligomerization and phase separation in a position- and amino acid-dependent manner;Dao;Structure,2019

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1. Brain–body mechanisms contribute to sexual dimorphism in amyotrophic lateral sclerosis;Nature Reviews Neurology;2024-07-04

2. Hippocampal aggregation signatures of pathogenic UBQLN2 in amyotrophic lateral sclerosis and frontotemporal dementia;Brain;2024-05-04

3. Masitinib: The promising actor in the next season of the Amyotrophic Lateral Sclerosis treatment series;Biomedicine & Pharmacotherapy;2023-04

4. UBQLN2 undergoes a reversible temperature-induced conformational switch that regulates binding with HSPA1B: ALS/FTD mutations cripple the switch but do not destroy HSPA1B binding;Biochimica et Biophysica Acta (BBA) - General Subjects;2023-02

5. Neuronal Puncta/Aggregate Formation by WT and Mutant UBQLN2;Methods in Molecular Biology;2022-10-31

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