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

Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation.

Journal of molecular biology - 18 Apr 2008

Platt Geoffrey W, Routledge Katy E, Homans Steve W, Radford Sheena E

Abstract excerpt

Amyloid is a highly ordered form of aggregate comprising long, straight and unbranched proteinaceous fibrils that are formed with characteristic nucleation-dependent kinetics in vitro. Currently, the structural molecular mechanism of fibril nucleation and elongation is poorly understood. Here, we investigate the role of the sequence and structure of the initial monomeric precursor in determining the rates of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Amyloid
Share to beta 2-Microglobulin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Hydrophobic and Hydrophilic Interactions

Share to Kinetics

Share to Protein Conformation

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 18342332
DOI: 10.1016/j.jmb.2008.01.092
PMCID: PMC2627305

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation.PMID 18342332Read ↗

Amyloid formation under physiological conditions proceeds via a native-like folding intermediate.Semantic proximity Read ↗

Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro.Semantic proximity Read ↗

Dynamics in the unfolded state of beta2-microglobulin studied by NMR.Semantic proximity Read ↗

Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis.Semantic proximity Read ↗

Role of the N and C-terminal strands of beta 2-microglobulin in amyloid formation at neutral pH.Semantic proximity Read ↗

Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors.Semantic proximity Read ↗

Properties of some variants of human beta2-microglobulin and amyloidogenesis.Semantic proximity Read ↗

A Self-Consistent Molecular Mechanism of β2-Microglobulin Aggregation.Semantic proximity Read ↗

Kinetics of protein fibril formation: Methods and mechanisms.Semantic proximity Read ↗

Structural defects in amyloid-β fibrils drive secondary nucleationSemantic proximity Read ↗

Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.Semantic proximity Read ↗

How is the Amyloid Fold Built? Polymorphism and the Microscopic Mechanisms of Fibril AssemblySemantic proximity Read ↗

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