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

Probing the polyphenolic flavonoid, morin as a highly efficacious inhibitor against amyloid(A4V) mutant SOD1 in fatal amyotrophic lateral sclerosis.

Archives of biochemistry and biophysics - 30 Sept 2022

Srinivasan E, Chandrasekhar G, Rajasekaran R

Abstract excerpt

Deposition of misfolded protein aggregates in key areas of human brain is the quintessential trait of various pertinent neurodegenerative disorders including amyotrophic lateral sclerosis (ALS). Genetic point mutations in Cu/Zn superoxide dismutase (SOD1) are found to be the most important contributing factor behind familial ALS. Especially, single nucleotide polymorphism (SNP) A4V is the most nocuous since it...

Read the complete abstract on PubMed

Topics

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

Share to Amyloidogenic Proteins
Share to Amyotrophic Lateral Sclerosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Flavonoids

Share to Mutation

Share to Superoxide Dismutase

Share to Superoxide Dismutase-1

Source

Identifiers

PMID: 35690129
DOI: 10.1016/j.abb.2022.109318

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Probing the polyphenolic flavonoid, morin as a highly efficacious inhibitor against amyloid(A4V) mutant SOD1 in fatal amyotrophic lateral sclerosis.PMID 35690129Read ↗

Fighting against amyotrophic lateral sclerosis (ALS) with flavonoids: a computational approach to inhibit superoxide dismutase (SOD1) mutant aggregation.Semantic proximity Read ↗

Myricetin: A Potent Anti-Amyloidogenic Polyphenol against Superoxide Dismutase 1 Aggregation.Semantic proximity Read ↗

Polyphenolic flavonoid compounds act as the inhibitory potential of aggregation process: Implications for the prevention and therapeutics against FALS-associated D101G SOD1 mutant.Semantic proximity Read ↗

Investigating the impact of SOD1 mutations on amyotrophic lateral sclerosis progression and potential drug repurposing through in silico analysis.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 ↗

Unveiling promising inhibitors of superoxide dismutase 1 (SOD1) for therapeutic interventions.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 ↗

Quercetin and Baicalein Act as Potent Antiamyloidogenic and Fibril Destabilizing Agents for SOD1 Fibrils.Semantic proximity Read ↗

Quercitrin and quercetin 3-β-d-glucoside as chemical chaperones for the A4V SOD1 ALS-causing mutant.Semantic proximity Read ↗

Modulating ALS-Related Amyloidogenic TDP-43307-319 Oligomeric Aggregates with Computationally Derived Therapeutic Molecules.Semantic proximity Read ↗

Discovery of Isobavachin, a natural flavonoid, as an Apolipo-protein E4 (ApoE4) structure corrector for Alzheimer’s diseaseSemantic proximity Read ↗

Spondias mombin flavonoids showed super-binder ability with Downstream Molecular Targets of Parkinson’s Disease: Folkloric-therapy assessment as a Scaffold for Structural Studies in Neurodegenerative diseaseSemantic proximity Read ↗

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