Glycerolipid Headgroups Control Rate and Mechanism of Superoxide Dismutase-1 Aggregation and Accelerate Fibrillization of Slowly Aggregating Amyotrophic Lateral Sclerosis Mutants
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, Baylor University, Waco, Texas 76706, United States
2. Institute of Biomedical Studies, Baylor University, Waco, Texas 76706, United States
Funder
Division of Chemistry
Welch Foundation
Publisher
American Chemical Society (ACS)
Subject
Cell Biology,Cognitive Neuroscience,Physiology,Biochemistry,General Medicine
Link
https://pubs.acs.org/doi/pdf/10.1021/acschemneuro.8b00086
Reference62 articles.
1. Lipid molecules induce the cytotoxic aggregation of Cu/Zn superoxide dismutase with structurally disordered regions
2. Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms
3. Prion Properties of SOD1 in Amyotrophic Lateral Sclerosis and Potential Therapy
4. Small Liposomes Accelerate the Fibrillation of Amyloid β (1–40)
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2. Kinetic Variability in Seeded Formation of ALS-Linked SOD1 Fibrils Across Multiple Generations;ACS Chemical Neuroscience;2020-01-02
3. The prion-like nature of amyotrophic lateral sclerosis;Progress in Molecular Biology and Translational Science;2020
4. The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis;Quarterly Reviews of Biophysics;2019
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