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

Temperature-sensitive glycosaminoglycan biosynthesis in a Chinese hamster ovary cell mutant containing a point mutation in glucuronyltransferase I.

The Journal of biological chemistry - 13 Feb 2004

Wei Ge, Bai Xiaomei, Esko Jeffrey D

Abstract excerpt

In previous studies, we reported the isolation and characterization of a Chinese hamster ovary cell mutant (pgsG) defective in glucuronyltransferase I (GlcATI). This enzyme adds the terminal GlcA residue in the core protein-linkage tetrasaccharide (GlcAbeta1,3Galbeta1,3Galbeta1, 4Xylbeta-O-) on which glycosaminoglycan assembly occurs (Bai, X. M., Wei, G., Sinha, A., and Esko, J. D. (1999) J. Biol. Chem. 274,...

Read the complete abstract on PubMed

Topics

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

Share to Glucuronosyltransferase
Share to Glycosaminoglycans

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

Share to Immunoglobulin G

Share to Luminescent Proteins

Share to Methionine

Share to Polysaccharides

Share to Rabbits

Share to Valine

Source

Identifiers

PMID: 14623881
DOI: 10.1074/jbc.M311621200

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

Temperature-sensitive glycosaminoglycan biosynthesis in a Chinese hamster ovary cell mutant containing a point mutation in glucuronyltransferase I.PMID 14623881Read ↗

Chinese hamster ovary cell mutants defective in glycosaminoglycan assembly and glucuronosyltransferase I.Semantic proximity Read ↗

CHO glycosylation mutants: proteoglycans.Semantic proximity Read ↗

Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I.Semantic proximity Read ↗

CHO cells provide access to novel N-glycans and developmentally regulated glycosyltransferases.Semantic proximity Read ↗

Chinese hamster ovary (CHO) cells may express six beta 4-galactosyltransferases (beta 4GalTs). Consequences of the loss of functional beta 4GalT-1, beta 4GalT-6, or both in CHO glycosylation mutants.Semantic proximity Read ↗

Generation of Chinese hamster ovary cell glycosylation mutants by retroviral insertional mutagenesis. Integration into a discrete locus generates mutants expressing high levels of N-glycolylneuraminic acid.Semantic proximity Read ↗

Lectin-resistant CHO glycosylation mutants.Semantic proximity Read ↗

Protein glycosylation in heat-sensitive and thermotolerance-deficient mutants of Chinese hamster ovary cells.Semantic proximity Read ↗

Chinese hamster ovary cells with reduced hexokinase activity maintain normal GDP-mannose levels.Semantic proximity Read ↗

Glycosyltransferase mutants: key to new insights in glycobiology.Semantic proximity Read ↗

Molecular analysis of three gain-of-function CHO mutants that add the bisecting GlcNAc to N-glycans.Semantic proximity Read ↗

A single mutation affects both N-acetylglucosaminyltransferase and glucuronosyltransferase activities in a Chinese hamster ovary cell mutant defective in heparan sulfate biosynthesis.Semantic proximity Read ↗

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