Associated Papers
Structure and Molecular Basis for Inhibiting Human SOD1 Aggregation by a Promising Decan Derivative Modulator: A Potential Therapeutic Strategy for Treating Amyotrophic Lateral Sclerosis (ALS).
Aouti S et al.
Acs Chemical Neuroscience, 2025
Distinct amyloid fibril structures formed by ALS-causing SOD1 mutants G93A and D101N.
Zhang MY et al.
Embo Reports, 2025
Landscapes of missense variant impact for human superoxide dismutase 1.
Axakova A et al.
Biorxiv : the Preprint Server for Biology, 2025
Bisdemethoxycurcumin, a novel potent polyphenolic compound, effectively inhibits the formation of amyloid aggregates in ALS-associated hSOD1 mutant (L38R).
Kouhi ZH et al.
International Journal of Biological Macromolecules, 2024
Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutations.
Wang LQ et al.
Science Advances, 2024
Role of charged residues of the "electrostatic loop" of hSOD1 in promotion of aggregation: Implications for the mechanism of ALS-associated mutations under amyloidogenic conditions.
Mavadat E et al.
International Journal of Biological Macromolecules, 2023
A Zn-dependent structural transition of SOD1 modulates its ability to undergo phase separation.
Das B et al.
The Embo Journal, 2023
Molecular dynamics analysis of superoxide dismutase 1 mutations suggests decoupling between mechanisms underlying ALS onset and progression.
Kalia M et al.
Computational and Structural Biotechnology Journal, 2023
Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion.
Wang LQ et al.
Nature Communications, 2022
Protein network analysis to prioritize key genes in amyotrophic lateral sclerosis.
Kumar R et al.
Ibro Neuroscience Reports, 2022
Progressive spastic tetraplegia and axial hypotonia (STAHP) due to SOD1 deficiency: is it really a new entity?
de Souza PVS et al.
Orphanet Journal of Rare Diseases, 2021
Comprehensive in silico analysis and molecular dynamics of the superoxide dismutase 1 (SOD1) variants related to amyotrophic lateral sclerosis.
Pereira GRC et al.
Plos One, 2021
Pathogenic Genome Signatures That Damage Motor Neurons in Amyotrophic Lateral Sclerosis.
Yousefian-Jazi A et al.
Cells, 2020
A Systematic and Comprehensive Review on Disease-Causing Genes in Amyotrophic Lateral Sclerosis.
Srinivasan E et al.
Journal of Molecular Neuroscience : Mn, 2020
Common mutations of interest in the diagnosis of amyotrophic lateral sclerosis: how common are common mutations in ALS genes?
Perrone B et al.
Expert Review of Molecular Diagnostics, 2020
A model for gain of function in superoxide dismutase.
Healy EF et al.
Biochemistry and Biophysics Reports, 2020
Canine SOD1 harboring E40K or T18S mutations promotes protein aggregation without reducing the global structural stability.
Kimura S et al.
Peerj, 2020
Oxidative Stress in Amyotrophic Lateral Sclerosis: Pathophysiology and Opportunities for Pharmacological Intervention.
Cunha-Oliveira T et al.
Oxidative Medicine and Cellular Longevity, 2020
The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis.
Wright GSA et al.
Quarterly Reviews of Biophysics, 2019
Cu/Zn-superoxide dismutase and wild-type like fALS SOD1 mutants produce cytotoxic quantities of H2O2 via cysteine-dependent redox short-circuit.
Bakavayev S et al.
Scientific Reports, 2019
Computational Investigation on Electrostatic Loop Mutants Instigating Destabilization and Aggregation on Human SOD1 Protein Causing Amyotrophic Lateral Sclerosis.
Srinivasan E et al.
The Protein Journal, 2019
Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants.
Huai J et al.
Frontiers in Neurology, 2019
Molecular dynamics of a far positioned SOD1 mutant V14M reveals pathogenic misfolding behavior.
Tompa DR et al.
Journal of Biomolecular Structure & Dynamics, 2018
A Proposed Mechanism for Neurodegeneration in Movement Disorders Characterized by Metal Dyshomeostasis and Oxidative Stress.
Trist BG et al.
Cell Chemical Biology, 2018
Phylogenetic spread of sequence data affects fitness of SOD1 consensus enzymes: Insights from sequence statistics and structural analyses.
Goyal VD et al.
Proteins, 2018
Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modelling.
Alemasov NA et al.
Bmc Structural Biology, 2018
Regression model for predicting pathogenic properties of SOD1 mutants based on the analysis of conformational stability and conservation of hydrogen bonds.
Alemasov NA et al.
Journal of Molecular Graphics & Modelling, 2017
The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase.
Sirangelo I et al.
Molecules (basel, Switzerland), 2017
Parsing disease-relevant protein modifications from epiphenomena: perspective on the structural basis of SOD1-mediated ALS.
Schmitt ND et al.
Journal of Mass Spectrometry : Jms, 2017
Insights into the mechanisms of copper dyshomeostasis in amyotrophic lateral sclerosis.
Gil-Bea FJ et al.
Expert Reviews in Molecular Medicine, 2017
Longitudinal assessment of metal concentrations and copper isotope ratios in the G93A SOD1 mouse model of amyotrophic lateral sclerosis.
Enge TG et al.
Metallomics : Integrated Biometal Science, 2017
Dynamic properties of SOD1 mutants can predict survival time of patients carrying familial amyotrophic lateral sclerosis.
Alemasov NA et al.
Journal of Biomolecular Structure & Dynamics, 2017
Gibbs Energy of Superoxide Dismutase Heterodimerization Accounts for Variable Survival in Amyotrophic Lateral Sclerosis.
Shi Y et al.
Journal of the American Chemical Society, 2016
Reduced net charge and heterogeneity of pI isoforms in familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase.
Roudeau S et al.
Electrophoresis, 2015
Mitochondrial membrane disruption by aggregation products of ALS-causing superoxide dismutase-1 mutants.
Salehi M et al.
International Journal of Biological Macromolecules, 2015
Metal-deficient aggregates and diminished copper found in cells expressing SOD1 mutations that cause ALS.
Bourassa MW et al.
Frontiers in Aging Neuroscience, 2014
Prognostic role of "prion-like propagation" in SOD1-linked familial ALS: an alternative view.
Sugaya K et al.
Frontiers in Cellular Neuroscience, 2014
Effect of metal loading and subcellular pH on net charge of superoxide dismutase-1.
Shi Y et al.
Journal of Molecular Biology, 2013
Is SOD1 loss of function involved in amyotrophic lateral sclerosis?
Saccon RA et al.
Brain : a Journal of Neurology, 2013
Mechanical probes of SOD1 predict systematic trends in metal and dimer affinity of ALS-associated mutants.
Das A et al.
Journal of Molecular Biology, 2013
Structural and functional analysis of human SOD1 in amyotrophic lateral sclerosis.
Moreira LG et al.
Plos One, 2013
Structural switching of Cu,Zn-superoxide dismutases at loop VI: insights from the crystal structure of 2-mercaptoethanol-modified enzyme.
Ihara K et al.
Bioscience Reports, 2012
A novel monoclonal antibody reveals a conformational alteration shared by amyotrophic lateral sclerosis-linked SOD1 mutants.
Fujisawa T et al.
Annals of Neurology, 2012
Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding.
Shi Y et al.
Protein Science : a Publication of the Protein Society, 2012