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

Implications of ALS-Associated Mutations on Biochemical and Biophysical Features of hSOD1 and Aggregation Formation.

Biochemical genetics - 1 Oct 2024

Mohammadi Saeede, Seyedalipour Bagher, Hashemi Seyedeh Zohreh, Hosseinkhani Saman, Mohseni Mojtaba

Abstract excerpt

One of the recognized motor neuron degenerative disorders is amyotrophic lateral sclerosis (ALS). By now, several mutations have been reported and linked to ALS patients, some of which are induced by mutations in the human superoxide dismutase (hSOD1) gene. The ALS-provoking mutations are located throughout the structure of hSOD1 and promote the propensity to aggregate. Despite numerous investigations, the...

Topics

Amyotrophic Lateral Sclerosis
Humans
Superoxide Dismutase-1
Mutation
Amyloid
Protein Aggregates
Protein Aggregation, Pathological

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 38196030
DOI: 10.1007/s10528-023-10619-y

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Implications of ALS-Associated Mutations on Biochemical and Biophysical Features of hSOD1 and Aggregation Formation.PMID 38196030Read ↗

Zinc binding loop mutations of hSOD1 promote amyloid fibrils under physiological conditions: Implications for initiation of amyotrophic lateral sclerosis.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 ↗

Uncovering the protein aggregation process through effect of G41D mutant SOD1 charge variation in ALS disease.Semantic proximity Read ↗

Inhibitory effect of silymarin on amyloid formation in ALS-associated hSOD1 P66R mutant.Semantic proximity Read ↗

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

Biochemical and biophysical properties of the novel ALS-linked hSOD1 mutants: an experimental study accompanied by in silico analysisSemantic proximity Read ↗

Insight Into Factors Influencing the Aggregation Process in Wild-Type and P66R Mutant SOD1: Computational and Spectroscopic Approaches.Semantic proximity Read ↗

Bisdemethoxycurcumin, a novel potent polyphenolic compound, effectively inhibits the formation of amyloid aggregates in ALS-associated hSOD1 mutant (L38R).Semantic proximity Read ↗

Exploring the cause of aggregation and reduced Zn binding affinity by G85R mutation in SOD1 rendering amyotrophic lateral sclerosis.Semantic proximity Read ↗

Mechanism of the N87D mutation in SOD1-atypical amyotrophic lateral sclerosis case report and literature review molecular mechanism of N87D mutation in SOD1.Semantic proximity Read ↗

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

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