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

Polyanion binding accelerates the formation of stable and low-toxic aggregates of ALS-linked SOD1 mutant A4V.

Proteins - 1 Dec 2014

Zhao Dan, Zhang Shibing, Meng Yan, Xiongwei Dong, Zhang Dan, Liang Yi, Wang Li, Liu Changlin

Abstract excerpt

The toxic property thus far shared by both ALS-linked SOD1 variants and wild-type SOD1 is an increased propensity to aggregation. However, whether SOD1 oligomers or aggregates are toxic to cells remains to be well defined. Moreover, how the toxic SOD1 species are removed from intra- and extracellular environments also needs to be further explored. The DNA binding has been shown to be capable of accelerating the...

Read the complete abstract on PubMed

Topics

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

Share to Amyotrophic Lateral Sclerosis
Share to Binding, Competitive

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Protein Aggregation, Pathological

Share to Protein Stability

Share to Superoxide Dismutase

Share to Superoxide Dismutase-1

Share to Surface Properties

Source

Identifiers

PMID: 25220364
DOI: 10.1002/prot.24691

Genes

SOD1
SDS

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Polyanion binding accelerates the formation of stable and low-toxic aggregates of ALS-linked SOD1 mutant A4V.PMID 25220364Read ↗

Exposure of a cryptic Hsp70 binding site determines the cytotoxicity of the ALS-associated SOD1-mutant A4V.Semantic proximity Read ↗

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.Semantic proximity Read ↗

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

Destabilizing the AXH Tetramer by Mutations: Mechanisms and Potential Antiaggregation Strategies.Semantic proximity Read ↗

Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins.Semantic proximity Read ↗

A double point mutation of SOD1 targeting net charge promotes aggregation under destabilizing conditions: Correlation of charge distribution and ALS-provoking mutation.Semantic proximity Read ↗

Aggregation landscapes of Huntingtin exon 1 protein fragments and the critical repeat length for the onset of Huntington’s diseaseSemantic proximity Read ↗

Cupric ions induce the oxidation and trigger the aggregation of human superoxide dismutase 1.Semantic proximity Read ↗

Charged nanobubbles in culture media differentially affect viability of human iPSC-derived neuronsSemantic proximity Read ↗

Divalent cation-induced conformational changes of influenza virus hemagglutinin.Semantic proximity Read ↗

Voltage-Induced Misfolding of Zinc-Replete ALS Mutant Superoxide Dismutase-1.Semantic proximity Read ↗

Interaction of heparins and dextran sulfates with a mesoscopic protein nanopore.Semantic proximity Read ↗

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