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

Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F.

The Journal of biological chemistry - 26 Mar 2004

Sirangelo Ivana, Malmo Clorinda, Iannuzzi Clara, Mezzogiorno Antonio, Bianco Maria Rosaria, Papa Michele, Irace Gaetano

Abstract excerpt

The apomyoglobin mutant W7FW14F forms amyloid-like fibrils at physiological pH. We examined the kinetics of fibrillogenesis using three techniques: the time dependence of the fluorescence emission of thioflavin T and 1-anilino-8-naphthalenesulfonate, circular dichroism measurements, and electron microscopy. We found that in the early stage of fibril formation, non-native apomyoglobin molecules containing...

Read the complete abstract on PubMed

Topics

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

Share to Apoproteins
Share to Benzothiazoles

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Coloring Agents

Share to Myoglobin

Share to NIH 3T3 Cells

Share to Spectrometry, Fluorescence

Share to Tetrazolium Salts

Share to Thiazoles

Source

Identifiers

PMID: 14701846
DOI: 10.1074/jbc.M308207200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F.PMID 14701846Read ↗

Tetracycline inhibits W7FW14F apomyoglobin fibril extension and keeps the amyloid protein in a pre-fibrillar, highly cytotoxic state.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 ↗

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

Driving amyloid toxicity in a yeast model by structural changes: a molecular approach.Semantic proximity Read ↗

Fibril fragmentation generates diversity in seed populationSemantic proximity Read ↗

Glycation of Wild-Type Apomyoglobin Induces Formation of Highly Cytotoxic Oligomeric Species.Semantic proximity Read ↗

Cell toxicity and conformational disease.Semantic proximity Read ↗

Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity.Semantic proximity Read ↗

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

Role of conformational change in the C-terminus of beta2-microglobulin in dialysis-related amyloidosis.Semantic proximity Read ↗

Fibrillar conformation of an apolipoprotein A-I variant involved in amyloidosis and atherosclerosis.Semantic proximity Read ↗

Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions.Semantic proximity Read ↗

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