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

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

Nature communications - 5 Apr 2022

Pobre-Piza Kristine F R, Mann Melissa J, Flory Ashley R, Hendershot Linda M

Abstract excerpt

BiP co-chaperones ERdj4, ERdj5, and GRP170 associate in cells with peptides predicted to be aggregation prone. Here, extending these findings to a full-length protein, we examine two Interstitial Lung Disease-associated mutants (ILD) of surfactant protein C (SP-C). The TANGO algorithm, which identifies sequences prone to formation of β strand aggregates, found three such regions in SP-C: the N-terminal...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Molecular Chaperones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Binding

Share to Protein Folding

Share to Pulmonary Surfactant-Associated Protein C

Source

Open in PubMed Open full text

Identifiers

PMID: 35383173
DOI: 10.1038/s41467-022-29478-z
PMCID: PMC8983781

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mapping SP-C co-chaperone binding sites reveals molecular consequences of disease-causing mutations on protein maturation.PMID 35383173Read ↗

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

Multiple ways to die: delineation of the unfolded protein response and apoptosis induced by Surfactant Protein C BRICHOS mutants.Semantic proximity Read ↗

Elucidation of proteostasis defects caused by osteogenesis imperfecta mutations in the collagen-α2(I) C-propeptide domain.Semantic proximity Read ↗

The Double-Edged Sword of αB-Crystallin Chaperone Activity: Insights from P39L Mutant at N-terminal regionSemantic proximity Read ↗

A non-BRICHOS surfactant protein c mutation disrupts epithelial cell function and intercellular signaling.Semantic proximity Read ↗

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

Investigating the Molecular Mechanisms Behind Uncharacterized Cysteine Losses from Prediction of Their Oxidation State.Semantic proximity Read ↗

Diverse Molecular Mechanisms Underlying Pathogenic Protein Mutations: Beyond the Loss-of-Function Paradigm.Semantic proximity Read ↗

Overexpression of human BAG3P209L in mice causes restrictive cardiomyopathy.Semantic proximity Read ↗

Protein-Folding Chaperones Predict Structure-Function Relationships and Cancer Risk in <i>BRCA1</i> Mutation CarriersSemantic proximity Read ↗

The co-chaperone DNAJA2 buffers proteasomal degradation of cytosolic proteins with missense mutationsSemantic proximity Read ↗

A nonaggregating surfactant protein C mutant is misdirected to early endosomes and disrupts phospholipid recycling.Semantic proximity Read ↗

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