2012
Site-specific N-Linked Glycosylation of Receptor Guanylyl Cyclase C Regulates Ligand Binding, Ligand-mediated Activation and Interaction with Vesicular Integral Membrane Protein 36, VIP36*
Arshad N, Ballal S, Visweswariah SS. Site-specific N-Linked Glycosylation of Receptor Guanylyl Cyclase C Regulates Ligand Binding, Ligand-mediated Activation and Interaction with Vesicular Integral Membrane Protein 36, VIP36*. Journal Of Biological Chemistry 2012, 288: 3907-3917. PMID: 23269669, PMCID: PMC3567644, DOI: 10.1074/jbc.m112.413906.Peer-Reviewed Original ResearchMeSH KeywordsCell LineCell MembraneEndoplasmic ReticulumGastrointestinal HormonesGlycosylationHumansLigandsMannose-Binding LectinsMembrane Transport ProteinsNatriuretic PeptidesProtein BindingProtein FoldingProtein Structure, TertiaryReceptors, EnterotoxinReceptors, Guanylate Cyclase-CoupledReceptors, PeptideConceptsLigand bindingVesicular integral membrane proteinGuanylyl cyclase CIntegral membrane proteinsGlycosylation of proteinsHeat‐stable enterotoxin peptideLigand-mediated activationSite of glycosylationTissue-dependent mannerReceptor guanylyl cyclaseReceptor guanylyl cyclase CGlycan-mediated interactionsDifferent cell typesMembrane proteinsSystematic mutagenesisGlycosylation sitesCyclase CCGMP-dependent mannerExtracellular domainProtein 36Endoplasmic reticulumSurface localizationVIP36Cell typesST peptides
2009
Receptor guanylyl cyclase C (GC-C): regulation and signal transduction
Basu N, Arshad N, Visweswariah SS. Receptor guanylyl cyclase C (GC-C): regulation and signal transduction. Molecular And Cellular Biochemistry 2009, 334: 67-80. PMID: 19960363, DOI: 10.1007/s11010-009-0324-x.Peer-Reviewed Original Research