PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17256880-1	2007	There is increasing evidence that a class of cell membrane glycolipids, gangliosides, can mediate the fibrillogenesis and toxicity of Alzheimer"s disease amyloid-beta peptide (Abeta).	Gangliosides	72-84	beta amyloid protein precursor-like	Drosophila melanogaster	176-181	
17161396-0	2006	Chloroquine-induced endocytic pathway abnormalities: Cellular model of GM1 ganglioside-induced Abeta fibrillogenesis in Alzheimer"s disease.	Gangliosides	75-86	beta amyloid protein precursor-like	Drosophila melanogaster	95-100	
29844375-2	2018	A growing body of evidence indicates that gangliosides form a pathological platform for the generation of ganglioside-bound Abeta, which facilitates the assembly of soluble Abetas; however, the molecular mechanisms underlying the binding of Abeta to gangliosides in the brain remain unclear due to the lack of an in vivo system that may address this issue.	Gangliosides	42-54	beta amyloid protein precursor-like	Drosophila melanogaster	124-129	
29844375-2	2018	A growing body of evidence indicates that gangliosides form a pathological platform for the generation of ganglioside-bound Abeta, which facilitates the assembly of soluble Abetas; however, the molecular mechanisms underlying the binding of Abeta to gangliosides in the brain remain unclear due to the lack of an in vivo system that may address this issue.	Gangliosides	42-54	beta amyloid protein precursor-like	Drosophila melanogaster	173-178	
29844375-2	2018	A growing body of evidence indicates that gangliosides form a pathological platform for the generation of ganglioside-bound Abeta, which facilitates the assembly of soluble Abetas; however, the molecular mechanisms underlying the binding of Abeta to gangliosides in the brain remain unclear due to the lack of an in vivo system that may address this issue.	Gangliosides	42-53	beta amyloid protein precursor-like	Drosophila melanogaster	124-129	
29844375-2	2018	A growing body of evidence indicates that gangliosides form a pathological platform for the generation of ganglioside-bound Abeta, which facilitates the assembly of soluble Abetas; however, the molecular mechanisms underlying the binding of Abeta to gangliosides in the brain remain unclear due to the lack of an in vivo system that may address this issue.	Gangliosides	42-53	beta amyloid protein precursor-like	Drosophila melanogaster	173-178	
29844375-2	2018	A growing body of evidence indicates that gangliosides form a pathological platform for the generation of ganglioside-bound Abeta, which facilitates the assembly of soluble Abetas; however, the molecular mechanisms underlying the binding of Abeta to gangliosides in the brain remain unclear due to the lack of an in vivo system that may address this issue.	Gangliosides	250-262	beta amyloid protein precursor-like	Drosophila melanogaster	124-129	
29844375-4	2018	We herein demonstrate that ganglioside expression is inducible in Drosophila via the expression of transgenes of ganglioside synthesis enzymes and the feeding of exogenous sialic acid, and also that the induction of ganglioside synthesis significantly accelerates Abeta assembly in vivo.	Gangliosides	27-38	beta amyloid protein precursor-like	Drosophila melanogaster	264-269	
29844375-5	2018	Our results support the hypothesis that gangliosides are responsible for Abeta assembly in vivo and also provide an opportunity to develop a valuable model for basic research as well as a therapeutic strategy for AD.	Gangliosides	40-52	beta amyloid protein precursor-like	Drosophila melanogaster	73-78