Direct observation of prion-like propagation of protein misfolding templated by pathogenic mutants-Reference-Cited by-同舟云学术

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Direct observation of prion-like propagation of protein misfolding templated by pathogenic mutants

Published:2024-07-15 Issue:9 Volume:20 Page:1220-1226
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

Neupane Krishna^ORCID,Narayan Abhishek^ORCID,Sen Mojumdar Supratik^ORCID,Adhikari Gaurav,Garen Craig R.^ORCID,Woodside Michael T.^ORCID

Funder

Gouvernement du Canada | National Research Council Canada

Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada

Gouvernement du Canada | Canadian Institutes of Health Research

Alberta Prion Research Institute

Alberta Innovates | Alberta Innovates - Health Solutions

Publisher

Springer Science and Business Media LLC

Link

https://www.nature.com/articles/s41589-024-01672-8.pdf

Reference51 articles.

1. Chiti, F. & Dobson, C. M. Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade. Annu. Rev. Biochem. 86, 27–68 (2017).

2. Colby, D. W. & Prusiner, S. B. Prions. Cold Spring Harb. Perspect. Biol. 3, a006833 (2011).

3. McAlary, L., Plotkin, S. S., Yerbury, J. J. & Cashman, N. R. Prion-like propagation of protein misfolding and aggregation in amyotrophic lateral sclerosis. Front. Mol. Neurosci. 12, 262 (2019).

4. Vaquer-Alicea, J. & Diamond, M. I. Propagation of protein aggregation in neurodegenerative diseases. Annu. Rev. Biochem. 88, 785–810 (2019).

5. Jahn, T. R. & Radford, S. E. Folding versus aggregation: polypeptide conformations on competing pathways. Arch. Biochem. Biophys. 469, 100–117 (2008).

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