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

BRICHOS domain associated with lung fibrosis, dementia and cancer--a chaperone that prevents amyloid fibril formation?

The FEBS journal - 1 Oct 2011

Willander Hanna, Hermansson Erik, Johansson Jan, Presto Jenny

Abstract excerpt

The BRICHOS domain was initially defined from sequence alignments of the Bri protein associated with familial dementia, chondromodulin associated with chondrosarcoma and surfactant protein C precursor (proSP-C) associated with respiratory distress syndrome and interstitial lung disease (ILD). Tod...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Amyloid
Share to Dementia

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Glycoproteins

Share to Molecular Chaperones

Share to Neoplasms

Share to Protein Structure, Tertiary

Share to Pulmonary Fibrosis

Source

Identifiers

PMID: 21668643
DOI: 10.1111/j.1742-4658.2011.08209.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-21668643-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

BRICHOS domain associated with lung fibrosis, dementia and cancer--a chaperone that prevents amyloid fibril formation?PMID 21668643Read ↗

BRICHOS - a superfamily of multidomain proteins with diverse functionsSemantic proximity Read ↗

BRICHOS: a conserved domain in proteins associated with dementia, respiratory distress and cancerSemantic proximity Read ↗

Molecular chaperone ability to inhibit amyloid-derived neurotoxicity, but not amorphous protein aggregation, depends on a conserved pH-sensitive Asp residueSemantic proximity Read ↗

Mapping SP-C co-chaperone binding sites reveals molecular consequences of disease-causing mutations on protein maturation.Semantic proximity Read ↗

Specific inhibition of α-synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOSSemantic proximity Read ↗

Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formationSemantic proximity Read ↗

Surfactant protein C biosynthesis and its emerging role in conformational lung disease.Semantic proximity Read ↗

BRI2 as a central protein involved in neurodegeneration.Semantic proximity Read ↗

Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C.Semantic proximity Read ↗

BRI2 inhibits amyloid beta-peptide precursor protein processing by interfering with the docking of secretases to the substrate.Semantic proximity Read ↗

CBS domains: structure, function, and pathology in human proteins.Semantic proximity Read ↗

BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2.Semantic proximity Read ↗

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