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

Consequences of Glycine Mutations in the Fibronectin-binding Sequence of Collagen.

The Journal of biological chemistry - 30 Dec 2016

Chhum Panharith, Yu Hongtao, An Bo, Doyon Brian R, Lin Yu-Shan, Brodsky Barbara

Abstract excerpt

Collagen and fibronectin (Fn) are two key extracellular matrix proteins, which are known to interact and jointly shape matrix structure and function. Most proteins that interact with collagen bind only to the native triple-helical form, whereas Fn is unusual in binding strongly to denatured collagen and more weakly to native collagen. The consequences of replacing a Gly by Ser at each position in the required...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Collagen Type I
Share to Collagen Type II

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Fibronectins

Share to Glycine

Share to Mutant Proteins

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 27799304
DOI: 10.1074/jbc.M116.753566
PMCID: PMC5207138

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

Consequences of Glycine Mutations in the Fibronectin-binding Sequence of Collagen.PMID 27799304Read ↗

Disrupting Effects of Osteogenesis Imperfecta Mutations Could Be Predicted by Local Hydrogen Bonding Energy.Semantic proximity Read ↗

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

Thermodynamic and kinetic consequences of substituting glycine at different positions in a Pro-Hyp-Gly repeat collagen model peptide.Semantic proximity Read ↗

Osteogenesis Imperfecta Missense Mutations in Collagen: Structural Consequences of a Glycine to Alanine Replacement at a Highly Charged SiteSemantic proximity Read ↗

Recombinant collagen studies link the severe conformational changes induced by osteogenesis imperfecta mutations to the disruption of a set of interchain salt bridges.Semantic proximity Read ↗

Disrupted collagen architecture in the crystal structure of a triple-helical peptide with a Gly-->Ala substitution.Semantic proximity Read ↗

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

Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen.Semantic proximity Read ↗

Guilty by association: some collagen II mutants alter the formation of ECM as a result of atypical interaction with fibronectin.Semantic proximity Read ↗

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

Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta.Semantic proximity Read ↗

A Collagen Triple Helix without the Super Helical TwistSemantic proximity Read ↗

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