Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

An in silico study of the effect of SOD1 electrostatic loop dynamics on amyloid‑like filament formation.

European biophysics journal : EBJ - 1 Dec 2016

Healy Eamonn F, Cervantes Luis

Abstract excerpt

Superoxide dismutase [Cu-Zn], or SOD1, is a homo-dimeric protein that functions as an antioxidant by scavenging for superoxides. A wide range of SOD1 variants are linked to inherited, or familial, amyotrophic lateral sclerosis, a progressive and fatal neurodegenerative disease. Aberrant SOD1 oligomerization has been strongly implicated in disease causation, even for sporadic ALS, or SALS, which accounts for ~90 %...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyloid beta-Peptides
Share to Hydrogen Bonding
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Aggregates

Share to Protein Multimerization

Share to Protein Structure, Secondary

Share to Static Electricity

Share to Superoxide Dismutase-1

Source

Open in PubMed Open full text

Identifiers

PMID: 27496206
DOI: 10.1007/s00249-016-1163-9
PMCID: PMC5102758

Genes

SOD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An in silico study of the effect of SOD1 electrostatic loop dynamics on amyloid‑like filament formation.PMID 27496206Read ↗

Structural Comparison of the Human G93A Mutant SOD1 to the Wild-type SOD1 Filaments.Semantic proximity Read ↗

Structural analysis of the overoxidized Cu/Zn-superoxide dismutase in ROS-induced ALS filament formation.Semantic proximity Read ↗

A computational strategy for therapeutic development against superoxide dismutase (SOD1) amyloid formation: effect of polyphenols on the various events in the aggregation pathway.Semantic proximity Read ↗

Amyotrophic lateral sclerosis disease-related mutations disrupt the dimerization of superoxide dismutase 1 - A comparative molecular dynamics simulation study.Semantic proximity Read ↗

An Allosteric Pathway in Copper, Zinc Superoxide Dismutase Unravels the Molecular Mechanism of the G93A Amyotrophic Lateral Sclerosis-Linked Mutation.Semantic proximity Read ↗

Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion.Semantic proximity Read ↗

Comprehensive in silico analysis and molecular dynamics of the superoxide dismutase 1 (SOD1) variants related to amyotrophic lateral sclerosisSemantic proximity Read ↗

Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase.Semantic proximity Read ↗

Superoxide Dismutase 1 Folding Stability as a Target for Molecular Tweezers in SOD1-Related Amyotrophic Lateral Sclerosis.Semantic proximity Read ↗

Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modelling.Semantic proximity Read ↗

Calcium binding to gatekeeper residues flanking aggregation-prone segments underlies non-fibrillar amyloid traits in superoxide dismutase 1 (SOD1).Semantic proximity Read ↗

Effects of Protein Crowders and Charge on the Folding of Superoxide Dismutase 1 Variants: A Computational Study.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.