PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26250646-2 2015 In this work, we conducted coarse-grained simulation to investigate the interactions of binding units of chorela toxin (CTB) with mixed ganglioside GM1 and dipalmitoylphosphatidylcholine (DPPC) lipid bilayer membrane. G(M1) Ganglioside 148-151 chitobiase Homo sapiens 120-123 26250646-3 2015 We determine that the binding of CTB pentamers cross-links GM1 molecules into protein-sized nanodomains that have distinct lipid order compared with the bulk. G(M1) Ganglioside 59-62 chitobiase Homo sapiens 33-36 26250646-6 2015 Comparison simulations on CTB binding to a membrane that is composed of various lipid components demonstrate that several factors are responsible for the nanodomain formation: (a) the negatively charged headgroup of a GM1 receptor is responsible for the multivalent binding; (b) the head groups being full of hydrogen-bonding donors and receptors stabilize the GM1 cluster itself and ensure the toxin binding with high affinity; and G(M1) Ganglioside 218-221 chitobiase Homo sapiens 26-29 10822616-1 1998 The interactions between the protein, cholera toxin B subunit attached to an atomic force microscope, AFM, cantilever, CTB and its receptor the ganglioside, GM1 have been measured in a dilute electrolyte solution, pH 5.5. G(M1) Ganglioside 157-160 chitobiase Homo sapiens 119-122 19037902-5 2009 Virtually all of the CTB-MPR(649-684) proteins expressed in the selected line were shown to have assembled into pentameric, GM1 ganglioside-binding complexes. G(M1) Ganglioside 124-139 chitobiase Homo sapiens 21-24 10822616-5 1998 This gives us confidence that in the earlier experiments, a specific interaction between the CTB and GM1 was measured. G(M1) Ganglioside 101-104 chitobiase Homo sapiens 93-96 9064322-3 1996 Coupling of antigen-containing particles to the pentameric binding subunit of cholera toxin (CTB) has been proposed as a means for increasing antigen uptake because the CTB receptor, ganglioside GM1, is a glycolipid present in apical membranes of all intestinal epithelial cells. G(M1) Ganglioside 195-198 chitobiase Homo sapiens 93-96 9064322-3 1996 Coupling of antigen-containing particles to the pentameric binding subunit of cholera toxin (CTB) has been proposed as a means for increasing antigen uptake because the CTB receptor, ganglioside GM1, is a glycolipid present in apical membranes of all intestinal epithelial cells. G(M1) Ganglioside 195-198 chitobiase Homo sapiens 169-172 3104072-4 1987 Supplementation of the cells with exogenous GM1, but not GD1a, identified a larger population of cells adherent on CTB (comparable to pFN-adherent cells) and dramatically increased the proportion of cells capable of forming neurites without reducing the time requirement. G(M1) Ganglioside 44-47 chitobiase Homo sapiens 115-118 2966069-1 1988 Human neuroblastoma cells (Platt and La-N1) adhere and extend neurites on a ganglioside GM1-binding substratum provided by cholera toxin B (CTB). G(M1) Ganglioside 88-91 chitobiase Homo sapiens 140-143 2966069-5 1988 The involvement of two pFN receptor molecules in ganglioside GM1-mediated responses on CTB have now been tested. G(M1) Ganglioside 61-64 chitobiase Homo sapiens 87-90 7665899-6 1995 The biological activity of CT or CTB bound to liposomes was confirmed by a hemagglutination assay using GM1-enriched human erythrocytes. G(M1) Ganglioside 104-107 chitobiase Homo sapiens 33-36 2436487-7 1987 Exposure of the tissue"s mucosal surface to GM1 ganglioside, (the natural receptor for the CT b subunit) yielded maximal stimulation of water flow and near-maximal urea transport, presumably by increasing CT"s binding to the cell membrane. G(M1) Ganglioside 44-59 chitobiase Homo sapiens 91-95 3104072-5 1987 In ultrastructural studies using the scanning electron microscope (SEM) and immunofluorescence (IF) analyses to discriminate microtubule distributions, neurites of GM1-supplemented cells on CTB were virtually identical with pFN-adherent neurites, whereas unsupplemented cells on CTB generated processes with fine-structural differences. G(M1) Ganglioside 164-167 chitobiase Homo sapiens 190-193 3104072-6 1987 Treatment of cells during the GM1 supplementation period with cycloheximide completely abolished the ability of cells to generate neurites on CTB and decreased the adhesive capacity of cells as well; a similar treatment of cells had no adverse effect on adherence or neurite extension on pFN. G(M1) Ganglioside 30-33 chitobiase Homo sapiens 142-145 3104072-7 1987 The importance of one or more proteins in GM1-dependent processes was further confirmed by demonstrating the trypsin sensitivity of a cell surface component(s) required to achieve maximal attachment on CTB; in contrast, adherence and neurite extension on pFN were much more resistant to this treatment process. G(M1) Ganglioside 42-45 chitobiase Homo sapiens 202-205