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

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

International journal of biological macromolecules - 31 Dec 2023

Atiya Akhtar, Muhsinah Abdullatif Bin, Alrouji Mohammed, Alhumaydhi Fahad A, Al Abdulmonem Waleed, Aljasir Mohammad A, Sharaf Sharaf E, Furkan Mohammad, Khan Rizwan Hasan, Shahwan Moyad, Shamsi Anas

Abstract excerpt

Superoxide dismutase 1 (SOD1) is a vital enzyme responsible for controlling cellular oxidative stress. Any dysregulation of SOD1 activity is linked with cancer pathogenesis and neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS). Among the inhibitors known to be effective against SOD1, LCS-1 stands out; however, its efficacy, specificity, and safety profiles are somewhat restricted. In this...

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 Molecular Docking Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Neoplasms

Share to Oxidation-Reduction

Share to Superoxide Dismutase

Share to Superoxide Dismutase-1

Source

Identifiers

PMID: 37666395
DOI: 10.1016/j.ijbiomac.2023.126684

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

Unveiling promising inhibitors of superoxide dismutase 1 (SOD1) for therapeutic interventions.PMID 37666395Read ↗

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

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

Discovery and characterization of novel inhibitors against ALS-related SOD1(A4V) aggregation through screening of a chemical library using Differerential Scanning Fluorimetry (DSF)Semantic proximity Read ↗

A small-molecule inhibitor of SOD1-Derlin-1 interaction ameliorates pathology in an ALS mouse modelSemantic proximity Read ↗

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

Fragment based drug discovery for SOD1-ALS and solution X-ray scattering studies on the copper chaperone for SOD1 (hCCS)and its functional complexes with SOD1Semantic proximity Read ↗

Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation.Semantic proximity Read ↗

Structural Insights into the Dynamics of Water in SOD1 Catalysis and Drug InteractionsSemantic proximity Read ↗

SoDCoD: a comprehensive database of Cu/Zn superoxide dismutase conformational diversity caused by ALS-linked gene mutations and other perturbations.Semantic proximity Read ↗

Structural modeling and in silico analysis of human superoxide dismutase 2.Semantic proximity Read ↗

Inhibition of SOD1 trimerization is a novel drug target for ALS diseaseSemantic proximity Read ↗

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