Tryptophan residue 32 in human Cu-Zn superoxide dismutase modulates prion-like propagation and strain selection-Reference-Cited by-同舟云学术

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Tryptophan residue 32 in human Cu-Zn superoxide dismutase modulates prion-like propagation and strain selection

Published:2020-01-30 Issue:1 Volume:15 Page:e0227655
ISSN:1932-6203
Container-title:PLOS ONE
language:en
Short-container-title:PLoS ONE

Author:

Crown Anthony,McAlary Luke,Fagerli Eric,Brown Hilda,Yerbury Justin J.,Galaleldeen Ahmad,Cashman Neil R.,Borchelt David R.,Ayers Jacob I.^ORCID

Funder

National Institute of Neurological Disorders and Stroke

Robert Packard Center for ALS Research, Johns Hopkins University

National Institutes of Health

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

Reference91 articles.

1. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis;DR Rosen;Nature,1993

2. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein);JM McCord;J Biol Chem,1969

3. Superoxide dismutases;I Fridovich;Adv Enzymol Relat Areas Mol Biol,1974

4. ALSoD: A user-friendly online bioinformatics tool for amyotrophic lateral sclerosis genetics;O Abel;Hum Mutat,2012

5. Variation in aggregation propensities among ALS-associated variants of SOD1: correlation to human disease;M Prudencio;Hum Mol Genet,2009

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3. Design and investigation of celastrol‐peptide nanoassemblies and their binding interactions with superoxide dismutase 1 and its mutants;Nano Select;2024-06-11

4. Protein aggregation and therapeutic strategies in SOD1- and TDP-43- linked ALS;Frontiers in Molecular Biosciences;2024-05-24

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