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

Disease-causing mutations in cartilage oligomeric matrix protein cause an unstructured Ca2+ binding domain.

The Journal of biological chemistry - 22 Mar 2002

Kleerekoper Quinn, Hecht Jacqueline T, Putkey John A

Abstract excerpt

Chondrocytes from pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (EDM1) patients display an enlarged rough endoplasmic reticulum that accumulates extracellular matrix proteins, including cartilage oligomeric matrix protein (COMP). Mutations that cause PSACH and EDM1 are restricted to a 27-kDa Ca(2+) binding domain (type 3 repeat). This domain has 13 Ca(2+)-binding loops with a consensus sequence...

Read the complete abstract on PubMed

Topics

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

Share to Achondroplasia
Share to Cartilage Oligomeric Matrix Protein

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

Share to Circular Dichroism

Share to Extracellular Matrix Proteins

Share to Glycoproteins

Share to Magnetic Resonance Spectroscopy

Share to Matrilin Proteins

Share to Osteochondrodysplasias

Source

Identifiers

PMID: 11782471
DOI: 10.1074/jbc.M109944200

Genes

COMP

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

Disease-causing mutations in cartilage oligomeric matrix protein cause an unstructured Ca2+ binding domain.PMID 11782471Read ↗

Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX.Semantic proximity Read ↗

Delta 469 mutation in the type 3 repeat calcium binding domain of cartilage oligomeric matrix protein (COMP) disrupts calcium binding.Semantic proximity Read ↗

COMP mutations, chondrocyte function and cartilage matrix.Semantic proximity Read ↗

Novel and recurrent mutations in the C-terminal domain of COMP cluster in two distinct regions and result in a spectrum of phenotypes within the pseudoachondroplasia -- multiple epiphyseal dysplasia disease group.Semantic proximity Read ↗

Cartilage oligomeric matrix protein: COMPopathies and beyond.Semantic proximity Read ↗

The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding.Semantic proximity Read ↗

Characterization of a pseudoachondroplasia-associated mutation (His587-->Arg) in the C-terminal, collagen-binding domain of cartilage oligomeric matrix protein (COMP).Semantic proximity Read ↗

Novel mutation in exon 18 of the cartilage oligomeric matrix protein gene causes a severe pseudoachondroplasia.Semantic proximity Read ↗

Retention of cartilage oligomeric matrix protein (COMP) and cell death in redifferentiated pseudoachondroplasia chondrocytes.Semantic proximity Read ↗

Trinucleotide expansion mutations in the cartilage oligomeric matrix protein (COMP) gene.Semantic proximity Read ↗

Identification of twelve mutations in cartilage oligomeric matrix protein (COMP) in patients with pseudoachondroplasia.Semantic proximity Read ↗

COMP mutations: domain-dependent relationship between abnormal chondrocyte trafficking and clinical PSACH and MED phenotypes.Semantic proximity Read ↗

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