Functional Organization of Golgi N- and O-Glycosylation Pathways Involves pH-dependent Complex Formation That Is Impaired in Cancer Cells
Open Access
- 1 November 2011
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 286 (44) , 38329-38340
- https://doi.org/10.1074/jbc.m111.277681
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Scaffold Proteins: Hubs for Controlling the Flow of Cellular InformationScience, 2011
- A testis-specific regulator of complex and hybrid N-glycan synthesisThe Journal of cell biology, 2010
- Golgi N-Glycosyltransferases Form Both Homo- and Heterodimeric Enzyme Complexes in Live CellsJournal of Biological Chemistry, 2010
- A Flow Cytometry-Based FRET Assay to Identify and Analyse Protein-Protein Interactions in Living CellsPLOS ONE, 2010
- High-efficiency labeling of sialylated glycoproteins on living cellsNature Methods, 2009
- Recent insights into the biological roles of mucin-type O-glycosylationGlycoconjugate Journal, 2008
- Mucin‐type O‐glycans in human colon and breast cancer: glycodynamics and functionsEMBO Reports, 2006
- An improved cyan fluorescent protein variant useful for FRETNature Biotechnology, 2004
- A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applicationsNature Biotechnology, 2002
- GlycosylationCurrent Opinion in Cell Biology, 1992