Functional features cause misfolding of the ALS-provoking enzyme SOD1-Reference-Cited by-同舟云学术

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Functional features cause misfolding of the ALS-provoking enzyme SOD1

Published:2009-06-02 Issue:24 Volume:106 Page:9667-9672
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Nordlund A.,Leinartaite L.,Saraboji K.,Aisenbrey C.,Grobner G.,Zetterstrom P.,Danielsson J.,Logan D. T.,Oliveberg M.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference32 articles.

1. Protein Misfolding, Functional Amyloid, and Human Disease

2. Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants

3. How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?

4. Induction of Nitric Oxide -- Dependent Apoptosis in Motor Neurons by Zinc-Deficient Superoxide Dismutase

5. Folding of human superoxide dismutase: Disulfide reduction prevents dimerization and produces marginally stable monomers

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

3. MS785-MS27 Reactive Misfolded/Non-Native Zn-Deficient SOD1 Species Exhibit Cytotoxicity and Adopt Heterozygous Conformations in Motor Neurons;International Journal of Molecular Sciences;2024-05-21

4. Unveiling local and global conformational changes and allosteric communications in SOD1 systems using molecular dynamics simulation and network analyses;Computers in Biology and Medicine;2024-01

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