Isolation of new CHO cell mutants defective in CMP-sialic acid biosynthesis and transport.

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

Back to search

Article

Isolation of new CHO cell mutants defective in CMP-sialic acid biosynthesis and transport.

Molecules and cells - 31 Dec 2006

Shin Dong-Jun, Kang Ji Young, Kim Youn Uck, Yoon Joong Sik, Choy Hyon E, Maeda Yusuke, Kinoshita Taroh, Hong Yeongjin

Abstract excerpt

Sialic acid is a sugar typically found at the N-glycan termini of glycoproteins in mammalian cells. Lec3 CHO cell mutants are deficient in epimerase activity, due to a defect in the gene that encodes a bifunctional UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE). Sialic acid modification on the cell surface is partially affected in these cells. We have mutagenized Lec3 CHO cells and isolated six mutants (termed C2m)...

Topics

Animals
Biological Transport
Blotting, Northern
CHO Cells
Carbohydrate Epimerases
Cricetinae
Cricetulus
Cytidine Monophosphate N-Acetylneuraminic Acid
Glycosylation
Membrane Glycoproteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation, Missense

Neural Cell Adhesion Molecules

Nucleotide Transport Proteins

Phenotype

Reverse Transcriptase Polymerase Chain Reaction

Sialic Acids

Source

Open in PubMed

Identifiers

PMID: 17202864

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Isolation of new CHO cell mutants defective in CMP-sialic acid biosynthesis and transport.PMID 17202864Read ↗

Lec3 Chinese hamster ovary mutants lack UDP-N-acetylglucosamine 2-epimerase activity because of mutations in the epimerase domain of the Gne gene.Semantic proximity Read ↗

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

Molecular defects that cause loss of polysialic acid in the complementation group 2A10.Semantic proximity Read ↗

alpha(1,3)fucosyltransferases expressed by the gain-of-function Chinese hamster ovary glycosylation mutants LEC12, LEC29, and LEC30.Semantic proximity Read ↗

Functional expression of human golgi CMP-sialic acid transporter in the Golgi complex of a transporter-deficient Chinese hamster ovary cell mutant.Semantic proximity Read ↗

A mutation causing a reduced level of expression of six beta4-galactosyltransferase genes is the basis of the Lec19 CHO glycosylation mutant.Semantic proximity Read ↗

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

Suppressors of alpha(1,3)fucosylation identified by expression cloning in the LEC11B gain-of-function CHO mutant.Semantic proximity Read ↗

Expression cloning of a novel suppressor of the Lec15 and Lec35 glycosylation mutations of Chinese hamster ovary cells.Semantic proximity Read ↗

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

Enhancing recombinant glycoprotein sialylation through CMP‐sialic acid transporter over expression in Chinese hamster ovary cellsSemantic proximity Read ↗

Molecular cloning of the hamster CMP-sialic acid transporter.Semantic proximity Read ↗

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