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- W332460211 abstract "Guanylyl cyclase (GC) C, identified from cDNA libraries of several mammalian small intestines, is a membrane-associated receptor for a heat-stable enterotoxin (STa) produced by enterotoxigenic Escherichia coli and an endogenous peptide, guanylin [1, 2]. The extracellular domain of guanylyl cyclase C, which includes the ligand-binding site, activates the cytoplasmic domain, catalyzing the conversion of GTP to cGMP as an intracellular signal. GC-C exhibits glyco-modifications and contains seven or eight potential N -glycosylation sites in the extracellular domain. To investigate the role of the N-glycosylation, each asparagine residue at the potential sites of porcine GC-C was converted to alanine by site-directed mutagenesis." @default.
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- W332460211 date "2006-03-24" @default.
- W332460211 modified "2023-09-23" @default.
- W332460211 title "74]Interaction between heat-stable enterotoxin and its receptor (guanylyl cyclase C): Influence of mutation at N-linked glycosylation sites on its ligand binding" @default.
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- W332460211 doi "https://doi.org/10.1007/0-306-46864-6_74" @default.
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