Location of the glucuronosyltransferase domain in the heparan sulfate copolymerase EXT1 by analysis of Chinese hamster ovary cell mutants.

By Ge Wei, X. Bai, M. Gabb, K. Bame, T. Koshy, Patricia G. Spear, J. Esko. 2000

93 citations recorded by the source corpus.

Subfields: Cell Biology, Immunology and Allergy

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In Cell Biology

1. B. Crawford
2. Beverly M. Zak
3. J. Esko
4. Xinhua Lin

Citations in the corpus

• The structure of EXTL3 helps to explain the different roles of bi-domain exostosins in heparan sulfate synthesis (2022, background): “Residues (identified by Wei et al.(1)) whose mutation results in loss of CgEXT1”
• The exostosin family: proteins with many functions. (2014, unknown): “Analyses of mutant Chinese hamster ovary (CHO) cells deficient in HS, mapped the GlcA-transferase domain to the N-terminal half of the EXT1 protein (Wei et al., 2000).”
• Hereditary multiple exostoses and heparan sulfate polymerization. (2002, methodology): “However, mutations in EXT1 that abrogate HS biosynthesis cluster around the second DXD [21], which does not have the expected hydrophobic cluster.”