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

Flanking regions, amyloid cores, and polymorphism: the potential interplay underlying structural diversity

1 Aug 2023

Abstract excerpt

The β-sheet-rich amyloid core is the defining feature of protein aggregates associated with neurodegenerative disorders. Recent investigations have revealed that there exist multiple examples of the same protein, with the same sequence, forming a variety of amyloid cores with distinct structural characteristics. These structural variants, termed as polymorphs, are hypothesized to influence the pathological...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer's disease research and treatments
Share to Endoplasmic Reticulum Stress and Disease
Share to Prion Diseases and Protein Misfolding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 37536631
DOI: 10.1016/j.jbc.2023.105122

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Flanking regions, amyloid cores, and polymorphism: the potential interplay underlying structural diversityPMID 37536631Read ↗

Molecular rules governing the structural polymorphism of amyloid fibrils in neurodegenerative diseasesSemantic proximity Read ↗

An atlas of amyloid aggregation: the impact of substitutions, insertions, deletions and truncations on amyloid beta fibril nucleationSemantic proximity Read ↗

Polymorphism in alpha-synuclein oligomers and its implications in toxicity under disease conditionsSemantic proximity Read ↗

Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis.Semantic proximity Read ↗

An atlas of amyloid aggregation: the impact of substitutions, insertions, deletions and truncations on amyloid beta fibril nucleationSemantic proximity Read ↗

Aggregation prone regions and gatekeeping residues in protein sequences.Semantic proximity Read ↗

Molecular determinants of protein pathogenicity at the single-aggregate levelSemantic proximity Read ↗

The Amyloid Phenomenon and Its Links with Human Disease.Semantic proximity Read ↗

The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseasesSemantic proximity Read ↗

Amyloid fibril polymorphism: a challenge for molecular imaging and therapySemantic proximity Read ↗

Natural and Pathogenic Protein Sequence Variation Affecting Prion-Like Domains Within and Across Human ProteomesSemantic proximity Read ↗

Prion-like disorders: blurring the divide between transmissibility and infectivitySemantic proximity Read ↗

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