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

Alternative splicing of exon 12 of the COL2A1 gene interrupts the triple helix of type-II collagen in the Kniest form of spondyloepiphyseal dysplasia.

Journal of orthopaedic research : official publication of the Orthopaedic Research Society - 1 Sept 1996

Chen L, Yang W, Cole W G

Abstract excerpt

An autosomal dominant mutation in the COL2A1 gene was identified in a child with the Kniest form of spondyloepiphyseal dysplasia. A C to T transition at nucleotide 35 of exon 12 changed the codon GCG for alanine 102 of the triple helical domain of alpha 1(II) chains of type-II collagen to GTG for valine. The transition also introduced a GT dinucleotide into exon 12. Analysis of cDNA prepared from Kniest cartilage...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Amino Acid Sequence

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

Share to Base Sequence

Share to Cells, Cultured

Share to Mutation

Share to Sequence Analysis, DNA

Source

Identifiers

PMID: 8893763
DOI: 10.1002/jor.1100140506

Genes

GCG

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

Alternative splicing of exon 12 of the COL2A1 gene interrupts the triple helix of type-II collagen in the Kniest form of spondyloepiphyseal dysplasia.PMID 8893763Read ↗

A single amino acid substitution (G103D) in the type II collagen triple helix produces Kniest dysplasia.Semantic proximity Read ↗

Abnormal skeletal growth in Kniest dysplasia caused by type II collagen mutations.Semantic proximity Read ↗

Small deletions in the type II collagen triple helix produce Kniest dysplasiaSemantic proximity Read ↗

Tandem duplication within a type II collagen gene (COL2A1) exon in an individual with spondyloepiphyseal dysplasia.Semantic proximity Read ↗

Low basal transcripts of the COL2A1 collagen gene from lymphoblasts show alternative splicing of exon 12 in the Kniest form of spondyloepiphyseal dysplasia.Semantic proximity Read ↗

Kniest dysplasia is caused by dominant collagen II (COL2A1) mutations: parental somatic mosaicism manifesting as Stickler phenotype and mild spondyloepiphyseal dysplasia.Semantic proximity Read ↗

Structurally abnormal type II collagen in a severe form of Kniest dysplasia caused by an exon 24 skipping mutation.Semantic proximity Read ↗

Characterization of an arginine 789 to cysteine substitution in alpha 1 (II) collagen chains of a patient with spondyloepiphyseal dysplasia.Semantic proximity Read ↗

The phenotypic spectrum of COL2A1 mutations.Semantic proximity Read ↗

Association of a p.Pro786Leu variant in COL2A1 with mild spondyloepiphyseal dysplasia congenita in a three-generation family.Semantic proximity Read ↗

A mutation in the amino-terminal end of the triple helix of type II collagen causing severe osteochondrodysplasia.Semantic proximity Read ↗

Report of five novel and one recurrent COL2A1 mutations with analysis of genotype-phenotype correlation in patients with a lethal type II collagen disorder.Semantic proximity Read ↗

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