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

Understanding Osaka mutation polymorphic Aβ fibril response to static and oscillating electric fields: insights from computational modeling.

Scientific reports - 27 Sept 2024

Makhkamov Mukhriddin, Baev Artyom, Kurganov Erkin, Razzokov Jamoliddin

Abstract excerpt

Alzheimer's disease (AD) is a prevalent neurodegenerative disorder, impacting millions of individuals worldwide. Among its defining characteristics is the accumulation of senile plaques within the brain's gray matter, formed through the self-assembly of misfolded proteins contributing to the progressive symptoms of AD. This study investigates a polymorphic Aβ fibril under static and oscillating electric fields...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer Disease
Share to Amyloid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Amyloid beta-Peptides

Share to Computer Simulation

Share to Electricity

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Peptide Fragments

Source

Open in PubMed Open full text

Identifiers

PMID: 39333193
DOI: 10.1038/s41598-024-72778-1
PMCID: PMC11436846

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Understanding Osaka mutation polymorphic Aβ fibril response to static and oscillating electric fields: insights from computational modeling.PMID 39333193Read ↗

Stability of Osaka Mutant and Wild-Type Fibril Models.Semantic proximity Read ↗

Transient dynamics of Aβ contribute to toxicity in Alzheimer’s diseaseSemantic proximity Read ↗

Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.Semantic proximity Read ↗

Aggregation Mechanism of Alzheimer's Amyloid β-Peptide Mediated by α-Strand/α-Sheet Structure.Semantic proximity Read ↗

E22G Aβ40 fibril structure and kinetics illuminate how Aβ40 rather than Aβ42 triggers familial Alzheimer's.Semantic proximity Read ↗

Molecular basis for amyloid-β polymorphismSemantic proximity Read ↗

APOE Genotype Difference in the Biphasic Modulation of Amyloid-β Aggregation by Direct Binding and Lowering the Nucleation Barrier.Semantic proximity Read ↗

Effects of Familial Alzheimer's Disease Mutations on the Folding Free Energy and Dipole-Dipole Interactions of the Amyloid β-Peptide.Semantic proximity Read ↗

Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Semantic proximity Read ↗

Examining the Ensembles of Amyloid- <i>β</i> Monomer Variants and their Propensities to Form Fibers Using an Energy Landscape Visualization MethodSemantic proximity Read ↗

Exploring the complexity of amyloid-beta fibrils: structural polymorphisms and molecular interactions.Semantic proximity Read ↗

Structural heterogeneity in familial Alzheimer's disease mutants of amyloid-beta peptides.Semantic proximity Read ↗

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