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