Article

Transient interactions between the fuzzy coat and the cross-β core of brain-derived Aβ42 filaments

2024-01-09

Abstract excerpt

A wide range of human disorders, including Alzheimer’s disease (AD), are characterised by the aberrant formation of amyloid fibrils. Amyloid fibrils are filamentous structures characterized by the presence of a highly-ordered cross-β core. In many cases, this core structure is flanked by disordered regions, often referred to as fuzzy coat. The structural properties of fuzzy coats, and the way in which they interac...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 76a03467-3f9e-53a8-a1e4-5bce74534178
DOI: 10.1101/2024.01.08.574772

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Transient interactions between the fuzzy coat and the cross-β core of brain-derived Aβ42 filamentsDOI 10.1101/2024.01.08.574772Read

Transient interactions between the fuzzy coat and the cross-β core of brain-derived Aβ42 filamentsSemantic proximity Read

Energetic profiling reveals thermodynamic principles underlying amyloid fibril maturationSemantic 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

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

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

Alzheimer's Protective Cross-Interaction between Wild-Type and A2T Variants Alters Aβ42 Dimer Structure.Semantic proximity Read

Exploring the aggregation free energy landscape of the amyloid-β protein (1-40).Semantic proximity Read

Reconstitution of the Alzheimer’s Disease Tau Core Structure from Recombinant Tau 297–391 Yields Variable Quaternary Structures as Seen by Negative Stain and Cryo-EMSemantic 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

An electrostatic cluster guides Aβ40 fibril formation in cerebral amyloid angiopathySemantic proximity Read

Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriersSemantic proximity Read

An electrostatic cluster guides Aβ40 fibril formation in sporadic and Dutch-type cerebral amyloid angiopathy.Semantic proximity Read