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

Mutant SOD1 forms ion channel: implications for ALS pathophysiology.

Neurobiology of disease - 1 Mar 2012

Allen Michael J, Lacroix Jérome J, Ramachandran Srinivasan, Capone Ricardo, Whitlock Jenny L, Ghadge Ghanashyam D, Arnsdorf Morton F, Roos Raymond P, Lal Ratnesh

Abstract excerpt

Point mutations in the gene encoding copper-zinc superoxide dismutase (SOD1) impart a gain-of-function to this protein that underlies 20-25% of all familial amyotrophic lateral sclerosis (FALS) cases. However, the specific mechanism of mutant SOD1 toxicity has remained elusive. Using the complementary techniques of atomic force microscopy (AFM), electrophysiology, and cell and molecular biology, here we examine...

Read the complete abstract on PubMed

Topics

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

Share to Ion Channel Gating
Share to Biophysical Phenomena

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Biophysics

Share to Electric Stimulation

Share to Lipid Bilayers

Share to Membranes, Artificial

Share to Microscopy, Atomic Force

Share to Neuroblastoma

Source

Open in PubMed Open full text

Identifiers

PMID: 21930207
DOI: 10.1016/j.nbd.2011.08.031
PMCID: PMC3384721

Genes

SOD1
AFM

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

Mutant SOD1 forms ion channel: implications for ALS pathophysiology.PMID 21930207Read ↗

Cu/Zn superoxide dismutase can form pore-like structures.Semantic proximity Read ↗

Mechanism for transforming cytosolic SOD1 into integral membrane proteins of organelles by ALS-causing mutations.Semantic proximity Read ↗

In vivo pathogenic role of mutant SOD1 localized in the mitochondrial intermembrane space.Semantic proximity Read ↗

Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS.Semantic proximity Read ↗

Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutations.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 ↗

Mutation/metal deficiency in the "electrostatic loop" enhanced aggregation process in apo/holo SOD1 variants: implications for ALS diseasesSemantic proximity Read ↗

Structural Analysis of SOD1 Fibrils with Mass Spectrometry, Limited Proteolysis, and Atomic Force Microscopy (AFM).Semantic proximity Read ↗

Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 MutantsSemantic proximity Read ↗

Destabilized Soluble SOD1 Species as Potential Determinants of Disease Severity in Familial Amyotrophic Lateral Sclerosis.Semantic proximity Read ↗

Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A.Semantic proximity Read ↗

Misfolded SOD1 forms high-density molecular complexes with synaptic molecules in mutant SOD1-linked familial amyotrophic lateral sclerosis cases.Semantic proximity Read ↗

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