Glycomics Profiling of Chinese Hamster Ovary Cell Glycosylation Mutants Reveals N-Glycans of a Novel Size and Complexity-Reference-Cited by-同舟云学术

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Glycomics Profiling of Chinese Hamster Ovary Cell Glycosylation Mutants Reveals N-Glycans of a Novel Size and Complexity

Published:2010-02 Issue:8 Volume:285 Page:5759-5775
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

North Simon J.,Huang Hung-Hsiang,Sundaram Subha,Jang-Lee Jihye,Etienne A. Tony,Trollope Alana,Chalabi Sara,Dell Anne,Stanley Pamela,Haslam Stuart M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. Lectin‐Resistant CHO Glycosylation Mutants

2. GLYCOSYLATION MUTANTS OF ANIMAL CELLS

3. Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide beta 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides.

4. The GDP-fucose:N-acetylglucosaminide 3-alpha-L-fucosyltransferases of LEC11 and LEC12 Chinese hamster ovary mutants exhibit novel specificities for glycolipid substrates.

5. Structural characterisation of neutrophil glycans by ultra sensitive mass spectrometric glycomics methodology

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