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

Potential modifier role of the R618Q variant of proalpha2(I)collagen in type I collagen fibrillogenesis: in vitro assembly analysis.

Molecular genetics and metabolism - 1 Jun 2004

Vomund Anthony N, Braddock Stephen R, Krause Gary F, Phillips Charlotte L

Abstract excerpt

An arginine to glutamine substitution in the triple helix of proalpha2(I)collagen (R618Q) was first reported in a patient with a variant of Marfan syndrome and later identified in conjunction with a second mutation in a patient with osteogenesis imperfecta (OI). The presence of the R618Q proalpha2(I)collagen allele in unaffected or mildly affected family members suggests that the R618Q allele is either a...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Cells, Cultured

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Collagen Type I

Share to Fibroblasts

Share to Hot Temperature

Share to Peptide Hydrolases

Share to Procollagen

Share to Protein Structure, Quaternary

Source

Identifiers

PMID: 15172002
DOI: 10.1016/j.ymgme.2004.03.004

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Potential modifier role of the R618Q variant of proalpha2(I)collagen in type I collagen fibrillogenesis: in vitro assembly analysis.PMID 15172002Read ↗

Position of single amino acid substitutions in the collagen triple helix determines their effect on structure of collagen fibrils.Semantic proximity Read ↗

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

Fibrillin microfibril structure identifies long-range effects of inherited pathogenic mutations affecting a key regulatory TGFβ-binding siteSemantic proximity Read ↗

Nanoscale Structural and Functional Impacts of Disease-Associated Collagen MutationsSemantic proximity Read ↗

Fibrillin microfibril structure identifies long-range effects of inherited pathogenic mutations affecting a key regulatory latent TGFβ-binding site.Semantic proximity Read ↗

Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates.Semantic proximity Read ↗

Collagen fibril assembly: New approaches to unanswered questionsSemantic proximity Read ↗

New insights into the structure, assembly and biological roles of 10-12 nm connective tissue microfibrils from fibrillin-1 studies.Semantic proximity Read ↗

Fibrillin-containing microfibrils: structure and function in health and disease.Semantic proximity Read ↗

The fibrillin-Marfan syndrome connection.Semantic proximity Read ↗

Fibrillin microfibril structure identifies long-range effects of inherited pathogenic mutations affecting a key regulatory latent TGFβ-binding siteSemantic proximity Read ↗

Phenotypic comparison of an osteogenesis imperfecta type IV proband with a de novo alpha2(I) Gly922 --> Ser substitution in type I collagen and an unrelated patient with an identical mutation.Semantic proximity Read ↗

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