Hsp90 and its co‐chaperone Sti1 control TDP‐43 misfolding and toxicity-Reference-Cited by-同舟云学术

Hsp90 and its co‐chaperone Sti1 control TDP‐43 misfolding and toxicity

Published:2021-04-28 Issue:5 Volume:35 Page:
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

Lin Lilian Tsai‐Wei¹,Razzaq Abdul²,Di Gregorio Sonja E.¹,Hong Soojie¹,Charles Brendan¹,Lopes Marilene H.²³⁴,Beraldo Flavio²⁵,Prado Vania F.²³⁵,Prado Marco A. M.²³⁵,Duennwald Martin L.¹³

Affiliation:

1. Department of Pathology and Laboratory Medicine Schulich School of Medicine and Dentistry University of Western Ontario London ON Canada

2. Robarts Research Institute Schulich School of Medicine and Dentistry University of Western Ontario London ON Canada

3. Department of Anatomy & Cell Biology Schulich School of Medicine and Dentistry University of Western Ontario London ON Canada

4. Department of Cell and Developmental Biology Institute of Biomedical Sciences University of São Paulo São Paulo Brazil

5. Department of Physiology and Pharmacology Schulich School of Medicine and Dentistry University of Western Ontario London ON Canada

Funder

ALS Society of Canada

Canadian Institutes of Health Research

Natural Sciences and Engineering Research Council of Canada

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.202002645R

Reference80 articles.

1. Protein aggregation and neurodegenerative disease

2. Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases

3. Toxic Proteins in Neurodegenerative Disease

4. Amyotrophic lateral sclerosis

5. Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis

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