Regulation of Cytokine Receptors by Golgi N-Glycan Processing and Endocytosis

By E. Partridge, Christine Le Roy, G. D. Di Guglielmo, J. Pawling, P. Cheung, M. Granovsky, I. Nabi, Jeffrey L. Wrana, J. Dennis. Science, 2004

708 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/697167aabf0902df1b529a2b243357f1a91d7567

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

1. Gabriel A. Rabinovich
2. A. Varki
3. M. Toscano
4. M. Flögel
5. S. Dabelić
6. J. Dumić
7. Fu-Tong Liu
8. K. Ohtsubo

In Molecular Biology

1. A. Varki
2. Gabriel A. Rabinovich
3. M. Toscano
4. M. Flögel
5. S. Dabelić
6. J. Dumić
7. J. Esko
8. Fu-Tong Liu

Citations in the corpus

• Galectin-3: an open-ended story. (2006, background): “As well, galectin-3 cross-links Mgat5-modified N-glycans on epidermal growth factor (EGF) receptors and transforming growth factor β (TGFβ) receptors and delays their removal by constitutive endocytosis [52].”
• Turning 'sweet' on immunity: galectin–glycan interactions in immune tolerance and inflammation (2009, background): “Consistent with a regulatory function of galectin–glycan lattices in the control of APC physiology, Partridge and colleague”
• Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. (2007, methodology): “herin antibodies as previously described (Partridge et al., 2004).”
• Biological roles of glycans (2016, background): “Thus, there are reports of regulation of cytokine receptors by modulation of endocytosis rates by the type of glycan structure and branching (605), and N-glycan number and degree of branching can cooperate to regulate cell proliferation and differentiation (606) as 10 A Varki”
• Galectins as modulators of tumour progression (2005, background): “, but impedes the endocytosis of epidermal growth factor and transforming growth factor-β receptors by binding to these receptor”
• Protein-glycan interactions in the control of innate and adaptive immune responses (2008, background): “Partridge and colleagues proposed a glycosylation-dependent mechanism by which galectin-3 cross-linking to complex N-glycans on cytokine receptors may delay their cell surface removal by endocytosis and promote sustained cytokine signaling on leukocyte”
• The sweet and sour of cancer: glycans as novel therapeutic targets (2005, background): “alter cytokine-mediated leukocyte signaling [31] and cytokine secretion by splenocytes and proliferation of CD4 T cells [38].”
• Glycosylation in cellular mechanisms of health and disease. (2006, background): “In addition, receptors for EGF and TGF-β on epithelial cells, the IgM B cell antigen receptor (BCR), and the glucose transporter 2 glycoprotein on pancreatic β cells are all profoundly modulated by mammalian glycosylation, indicating that different glycans produced in the Golgi maintain these recept”