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

Contribution of EXT1, EXT2, and EXTL3 to heparan sulfate chain elongation.

The Journal of biological chemistry - 9 Nov 2007

Busse Marta, Feta Almir, Presto Jenny, Wilén Maria, Grønning Mona, Kjellén Lena, Kusche-Gullberg Marion

Abstract excerpt

The exostosin (EXT) family of genes encodes glycosyltransferases involved in heparan sulfate biosynthesis. Five human members of this family have been cloned to date: EXT1, EXT2, EXTL1, EXTL2, and EXTL3. EXT1 and EXT2 are believed to form a Golgi-located hetero-oligomeric complex that catalyzes the chain elongation step in heparan sulfate biosynthesis, whereas the EXTL proteins exhibit overlapping...

Read the complete abstract on PubMed

Topics

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

Share to Cell Line
Share to Gene Expression Regulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Golgi Apparatus

Share to Heparitin Sulfate

Share to Membrane Proteins

Share to N-Acetylglucosaminyltransferases

Share to RNA, Small Interfering

Share to Tumor Suppressor Proteins

Source

Identifiers

PMID: 17761672
DOI: 10.1074/jbc.M703560200

Genes

EXT2
EXT1
EXTL3
EXTL1
EXTL2

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Contribution of EXT1, EXT2, and EXTL3 to heparan sulfate chain elongation.PMID 17761672Read ↗

The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate.Semantic proximity Read ↗

Embryonic fibroblasts with a gene trap mutation in Ext1 produce short heparan sulfate chains.Semantic proximity Read ↗

A novel mutation in ext2 caused hereditary multiple exostoses through reducing the synthesis of heparan sulfateSemantic proximity Read ↗

Identification of four novel EXT1 and EXT2 mutations in five Chinese pedigrees with hereditary multiple exostoses.Semantic proximity Read ↗

Hereditary multiple exostoses and heparan sulfate polymerization.Semantic proximity Read ↗

Transgenic expression of the EXT2 gene in developing chondrocytes enhances the synthesis of heparan sulfate and bone formation in mice.Semantic proximity Read ↗

Mice deficient in Ext2 lack heparan sulfate and develop exostosesSemantic proximity Read ↗

Heparan sulfate abnormalities in exostosis growth plates.Semantic proximity Read ↗

The pathogenic roles of heparan sulfate deficiency in hereditary multiple exostoses.Semantic proximity Read ↗

EXT genes are differentially expressed in bone and cartilage during mouse embryogenesisSemantic proximity Read ↗

Heparan sulfate in skeletal development, growth, and pathology: The case of hereditary multiple exostosesSemantic proximity Read ↗

Novel EXT1 mutation identified in a pedigree with hereditary multiple exostoses.Semantic proximity Read ↗

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