PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	334-338	galactosidase alpha	Homo sapiens	154-158	
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	334-338	galactosidase alpha	Homo sapiens	154-158	
3255105-8	1988	A DMPC-GALA:19/1 (molar ratio) complex can be isolated by gel-permeation chromatography.	Dimyristoylphosphatidylcholine	2-6	galactosidase alpha	Homo sapiens	7-11	
3255105-10	1988	GALA activates LCAT with DMPC but not with unsaturated phospholipids as the substrate.	Dimyristoylphosphatidylcholine	25-29	galactosidase alpha	Homo sapiens	0-4	
3255105-11	1988	The apparent partition coefficient of GALA into DMPC vesicles is 100-fold larger than into egg phosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	48-52	galactosidase alpha	Homo sapiens	38-42	
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	68-98	galactosidase alpha	Homo sapiens	0-4	
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	68-98	galactosidase alpha	Homo sapiens	154-158	
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	68-98	galactosidase alpha	Homo sapiens	154-158	
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	100-104	galactosidase alpha	Homo sapiens	0-4	
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	100-104	galactosidase alpha	Homo sapiens	154-158	
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	100-104	galactosidase alpha	Homo sapiens	154-158	
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	334-338	galactosidase alpha	Homo sapiens	0-4	
1997324-8	1991	At neutral pH, in the presence of dimyristoylglycerophosphocholine (Myr2GroPCho), GALA is known to form discoidal structures similar to those formed under the same conditions by apolipoproteins AI and AII.	Dimyristoylphosphatidylcholine	34-66	galactosidase alpha	Homo sapiens	82-86