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

Structural basis of fibrillar collagen trimerization and related genetic disorders.

Nature structural & molecular biology - 1 Oct 2012

Bourhis Jean-Marie, Mariano Natacha, Zhao Yuguang, Harlos Karl, Exposito Jean-Yves, Jones E Yvonne, Moali Catherine, Aghajari Nushin, Hulmes David J S

Abstract excerpt

The C propeptides of fibrillar procollagens have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. Mutations in C propeptides are associated with several, often lethal, genetic disorders affecting bone, cartilage, blood vessels and skin. Here we report the crystal structure of a C-propeptide domain...

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 Collagen Type III

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Mutation, Missense

Share to Protein Multimerization

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 23001006
DOI: 10.1038/nsmb.2389
PMCID: PMC3465578

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

Structural basis of fibrillar collagen trimerization and related genetic disorders.PMID 23001006Read ↗

Structural basis of homo- and heterotrimerization of collagen I.Semantic proximity Read ↗

Type I procollagen C-propeptide defects: study of genotype-phenotype correlation and predictive role of crystal structure.Semantic proximity Read ↗

The collagenopathies: review of clinical phenotypes and molecular correlations.Semantic proximity Read ↗

Defective C-propeptides of the proalpha2(I) chain of type I procollagen impede molecular assembly and result in osteogenesis imperfecta.Semantic proximity Read ↗

Mutations in collagen genes: causes of rare and some common diseases in humans.Semantic proximity Read ↗

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

Skeletal diseases caused by mutations that affect collagen structure and function.Semantic proximity Read ↗

Defective Proteolytic Processing of Fibrillar Procollagens and Prodecorin Due to Biallelic BMP1 Mutations Results in a Severe, Progressive Form of Osteogenesis Imperfecta.Semantic proximity Read ↗

Enigmatic insight into collagenSemantic proximity Read ↗

Mutations That Alter the Carboxy-Terminal-Propeptide Cleavage Site of the Chains of Type I Procollagen Are Associated With a Unique Osteogenesis Imperfecta Phenotype.Semantic proximity Read ↗

A C-Propeptide Variant in COL1A1 Potentially Perturbing Disulfide Bonding in Osteogenesis Imperfecta Type III.Semantic proximity Read ↗

Folding defects in fibrillar collagens.Semantic proximity Read ↗

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