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

The First Step of Amyloidogenic Aggregation.

The journal of physical chemistry. B - 2 Jul 2015

Castello Fabio, Casares Salvador, Ruedas-Rama Maria J, Orte Angel

Abstract excerpt

The structural and dynamic characterization of the on-pathway intermediates involved in the mechanism of amyloid fibril formation is one of the major remaining biomedical challenges of our time. In addition to mature fibrils, various oligomeric structures are implicated in both the rate-limiting step of the nucleation process and the neuronal toxicity of amyloid deposition. Single-molecule fluorescence...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Fluorescence Resonance Energy Transfer
Share to Hydrogen-Ion Concentration

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Fluorescence

Share to Protein Multimerization

Share to Spectrin

Share to Spectrometry, Fluorescence

Share to src Homology Domains

Source

Identifiers

PMID: 26039157
DOI: 10.1021/acs.jpcb.5b01957

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

The First Step of Amyloidogenic Aggregation.PMID 26039157Read ↗

Characterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.Semantic proximity Read ↗

A mechanistic model of tau amyloid aggregation based on direct observation of oligomers.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 ↗

Common Features at the Start of the Neurodegeneration CascadeSemantic proximity Read ↗

Biophysical approaches to characterising protein-protein interactions and intermediate species in protein aggregationSemantic proximity Read ↗

The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization.Semantic proximity Read ↗

Time-resolved small-angle x-ray scattering study of the early stage of amyloid formation of an apomyoglobin mutant.Semantic proximity Read ↗

Conformational evolution of polymorphic amyloid assemblies.Semantic proximity Read ↗

Deciphering the mechanism of protein aggregation and effects of inhibitors using single-molecule mass photometrySemantic proximity Read ↗

Tau AD fragment aggregates proliferate through autocatalytic secondary nucleationSemantic proximity Read ↗

Early sodium dodecyl sulfate induced collapse of α-synuclein correlates with its amyloid formation.Semantic proximity Read ↗

An interdisciplinary approach to studying mechanistic, structural and toxic features of protein aggregates associated with neurodegenerative disordersSemantic proximity Read ↗

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