PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23852578-2	2013	In addition, recent spectroscopic studies show that the interaction between monosialoganglioside and amyloid beta (Abeta protein promotes the transition of Abeta from the native structure to the cross-beta fold in amyloid aggregates.	sialogangliosides	76-96	amyloid beta precursor protein	Homo sapiens	115-120	
32142821-2	2020	Accumulating evidence, both in vivo and in vitro, suggests that the binding of Abeta to gangliosides, especially monosialoganglioside GM1, plays an important role in the aggregation of Abeta.	sialogangliosides	113-133	amyloid beta precursor protein	Homo sapiens	79-84	
32142821-2	2020	Accumulating evidence, both in vivo and in vitro, suggests that the binding of Abeta to gangliosides, especially monosialoganglioside GM1, plays an important role in the aggregation of Abeta.	sialogangliosides	113-133	amyloid beta precursor protein	Homo sapiens	185-190	
31247730-2	2019	The interaction of Abeta with the monosialoganglioside-rich neuronal cell membrane has been suggested to influence Abeta aggregation.	sialogangliosides	34-54	amyloid beta precursor protein	Homo sapiens	19-24	
23852578-2	2013	In addition, recent spectroscopic studies show that the interaction between monosialoganglioside and amyloid beta (Abeta protein promotes the transition of Abeta from the native structure to the cross-beta fold in amyloid aggregates.	sialogangliosides	76-96	amyloid beta precursor protein	Homo sapiens	156-161	
21682276-4	2011	In this paper, the mechanism by which Abeta-(1-40) fibrillizes in raftlike lipid bilayers composed of monosialoganglioside GM1, cholesterol, and sphingomyelin was investigated in detail on the basis of singular-value decomposition of circular dichroism data and analysis of fibrillization kinetics.	sialogangliosides	102-122	amyloid beta precursor protein	Homo sapiens	38-43	
12659848-3	2003	In this study, using fluorescence resonance energy transfer, we found that after A beta binds to raft-like membranes composed of monosialoganglioside GM1/cholesterol/sphingomyelin (1/1/1), the protein can translocate to the phosphatidylcholine membranes to which soluble A beta does not bind.	sialogangliosides	129-149	amyloid beta precursor protein	Homo sapiens	81-87	
12659848-3	2003	In this study, using fluorescence resonance energy transfer, we found that after A beta binds to raft-like membranes composed of monosialoganglioside GM1/cholesterol/sphingomyelin (1/1/1), the protein can translocate to the phosphatidylcholine membranes to which soluble A beta does not bind.	sialogangliosides	129-149	amyloid beta precursor protein	Homo sapiens	271-277	
11549733-4	2001	The main components of lipids released after the addition of Abeta were cholesterol, phospholipids, and monosialoganglioside (GM1).	sialogangliosides	104-124	amyloid beta precursor protein	Homo sapiens	61-66