PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23422796-11	2013	Moreover, propofol and thiopental suppressed GM1-induced fibril formation in a cell-free system (propofol, 75.8 +- 1.9%; thiopental, 83.6 +- 1.9%) and reduced the neurotoxicity of a mixture containing Abeta and GM1 liposomes (propofol, 35.3 +- 16.4%; thiopental, 21.3 +- 11.6%).	G(M1) Ganglioside	45-48	beta amyloid protein precursor-like	Drosophila melanogaster	201-206	
17256880-4	2007	Abeta exhibited direct and favorable interactions with GM1 as Abeta insertion monotonically increased with GM1 concentration, despite increases in monolayer rigidity at low GM1 levels.	G(M1) Ganglioside	55-58	beta amyloid protein precursor-like	Drosophila melanogaster	0-5	
17256880-4	2007	Abeta exhibited direct and favorable interactions with GM1 as Abeta insertion monotonically increased with GM1 concentration, despite increases in monolayer rigidity at low GM1 levels.	G(M1) Ganglioside	55-58	beta amyloid protein precursor-like	Drosophila melanogaster	62-67	
17256880-4	2007	Abeta exhibited direct and favorable interactions with GM1 as Abeta insertion monotonically increased with GM1 concentration, despite increases in monolayer rigidity at low GM1 levels.	G(M1) Ganglioside	107-110	beta amyloid protein precursor-like	Drosophila melanogaster	0-5	
17256880-4	2007	Abeta exhibited direct and favorable interactions with GM1 as Abeta insertion monotonically increased with GM1 concentration, despite increases in monolayer rigidity at low GM1 levels.	G(M1) Ganglioside	107-110	beta amyloid protein precursor-like	Drosophila melanogaster	62-67	
17256880-4	2007	Abeta exhibited direct and favorable interactions with GM1 as Abeta insertion monotonically increased with GM1 concentration, despite increases in monolayer rigidity at low GM1 levels.	G(M1) Ganglioside	107-110	beta amyloid protein precursor-like	Drosophila melanogaster	0-5	
17256880-4	2007	Abeta exhibited direct and favorable interactions with GM1 as Abeta insertion monotonically increased with GM1 concentration, despite increases in monolayer rigidity at low GM1 levels.	G(M1) Ganglioside	107-110	beta amyloid protein precursor-like	Drosophila melanogaster	62-67	
17256880-5	2007	At low GM1 concentrations, Abeta preferentially inserted into the disordered, liquid expanded phase.	G(M1) Ganglioside	7-10	beta amyloid protein precursor-like	Drosophila melanogaster	27-32	
17256880-6	2007	At higher GM1 concentrations, Abeta inserted more uniformly into the monolayer, resulting in no detectable preferences for either the disordered or condensed phase.	G(M1) Ganglioside	10-13	beta amyloid protein precursor-like	Drosophila melanogaster	30-35	
17256880-7	2007	Abeta insertion led to the disruption of membrane morphology, specifically to the expansion of the disordered phase at low GM1 concentrations and significant disruption of the condensed domains at higher GM1 concentrations.	G(M1) Ganglioside	123-126	beta amyloid protein precursor-like	Drosophila melanogaster	0-5	
17256880-7	2007	Abeta insertion led to the disruption of membrane morphology, specifically to the expansion of the disordered phase at low GM1 concentrations and significant disruption of the condensed domains at higher GM1 concentrations.	G(M1) Ganglioside	204-207	beta amyloid protein precursor-like	Drosophila melanogaster	0-5	
17256880-8	2007	During incubation with POPC vesicles containing physiological levels of GM1, the association of Abeta with vesicles seeded the formation of Abeta fibrils.	G(M1) Ganglioside	72-75	beta amyloid protein precursor-like	Drosophila melanogaster	96-101	
17256880-8	2007	During incubation with POPC vesicles containing physiological levels of GM1, the association of Abeta with vesicles seeded the formation of Abeta fibrils.	G(M1) Ganglioside	72-75	beta amyloid protein precursor-like	Drosophila melanogaster	140-145	
17256880-9	2007	In conclusion, favorable interactions between Abeta and GM1 in the cell membrane may provide a mechanism for Abeta fibrillogenesis in vivo, and Abeta-induced disruption of the cell membrane may provide a pathway by which Abeta exerts toxicity.	G(M1) Ganglioside	56-59	beta amyloid protein precursor-like	Drosophila melanogaster	109-114	
17256880-9	2007	In conclusion, favorable interactions between Abeta and GM1 in the cell membrane may provide a mechanism for Abeta fibrillogenesis in vivo, and Abeta-induced disruption of the cell membrane may provide a pathway by which Abeta exerts toxicity.	G(M1) Ganglioside	56-59	beta amyloid protein precursor-like	Drosophila melanogaster	109-114	
17161396-0	2006	Chloroquine-induced endocytic pathway abnormalities: Cellular model of GM1 ganglioside-induced Abeta fibrillogenesis in Alzheimer"s disease.	G(M1) Ganglioside	71-74	beta amyloid protein precursor-like	Drosophila melanogaster	95-100	
17161396-4	2006	Notably, an increase in GM1 level on the cell surface was sufficient to induce Abeta assembly.	G(M1) Ganglioside	24-27	beta amyloid protein precursor-like	Drosophila melanogaster	79-84	
16941490-7	2006	Because it has been claimed that amyloid-beta protein (Abeta) interacts with GM1 in PC12 cells to provide "seeding" for amyloid to accumulate, we further evaluated this possibility and found that Abeta is mostly likely interacting with fucosyl-GM1 in this cell line.	G(M1) Ganglioside	77-80	beta amyloid protein precursor-like	Drosophila melanogaster	55-60	
16941490-7	2006	Because it has been claimed that amyloid-beta protein (Abeta) interacts with GM1 in PC12 cells to provide "seeding" for amyloid to accumulate, we further evaluated this possibility and found that Abeta is mostly likely interacting with fucosyl-GM1 in this cell line.	G(M1) Ganglioside	77-80	beta amyloid protein precursor-like	Drosophila melanogaster	196-201