Study of o-glycan sialylation in c6 cultured glioma cells: Regulation of a β-galactoside α2,3 sialyltransferase activity by ca2+/calmodulin antagonists and phosphatase inhibitors-Reference-Cited by-同舟云学术

Study of o-glycan sialylation in c6 cultured glioma cells: Regulation of a β-galactoside α2,3 sialyltransferase activity by ca2+/calmodulin antagonists and phosphatase inhibitors

Published:1992-08 Issue:3 Volume:186 Page:1575-1581
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Reboul Pascal,George Pascal,Geoffroy Jocelyne,Louisot Pierre,Broquet Pierre

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference18 articles.

1. Different reactivity of two Brain sialyltransferases towards sulfhydryl reagents. Evidence for a thiol group involved in the nucleotide-sugar binding site of the NeuAc?2-3Gal?1-3GalNAc ?(2?6)sialyltransferase

2. A brain sialyltransferase having a narrow specificity for O-glycosyl-linked oligosaccharide chains

3. Evidence for an O-glycan sialylation system in brain. Characterization of a beta-galactoside alpha2,3-sialytransferase from rat brain regulating the expression of an alpha-N-acetylgalactosaminide alpha2,6-sialyltransferase activity

4. Different reactivity to lysophosphatidylcholine, DIDS and trypsin of two brain sialyltransferases specific for O-glycans: a consequence of their topography in the endoplasmic membranes

5. Study of O-glycan sialylation in C6 cultured glioma cells: Evidence for post-translational regulation of Aβ-galactoside α2,3 sialyltransferase activity by N-glycosylation

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4. The role of protein phosphorylation in α2,6(N)-sialyltransferase activity;Biochemical and Biophysical Research Communications;2003-09

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