PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3349050-5	1988	At saturation, there was 9 X 10(-3) pmol of protein 4.1 bound/pmol of PS with a Kd of 3.3 X 10(-7) M. When the protein 4.1 containing liposomes were examined in an electron microscope, the protein 4.1 was found uniformly decorating the vesicles in a rosettelike fashion.	Phosphatidylserines	70-72	erythrocyte membrane protein band 4.1	Homo sapiens	44-55	
3337803-3	1988	Protein 4.1 penetrated into monolayers of brain phosphatidylserine (PS) and egg phosphatidylcholine (PC), even above surface pressures of 30 mN/m.	Phosphatidylserines	68-70	erythrocyte membrane protein band 4.1	Homo sapiens	0-11	
3337803-4	1988	Protein 4.1 increased the permeability of negatively charged PS, but not PC, liposomes, measured as the increase in fluorescence when encapsulated 1-aminonaphthalene-3,6,8-trisulfonic acid (ANTS) and p-xylenebispyridinium bromide (DPX) or carboxyfluorescein were released into the medium.	Phosphatidylserines	61-63	erythrocyte membrane protein band 4.1	Homo sapiens	0-11	
3335640-7	1988	Addition of purified protein 4.1 to PS liposomes resulted in saturable binding with the extent of binding being proportional to the liposome PS content.	Phosphatidylserines	36-38	erythrocyte membrane protein band 4.1	Homo sapiens	21-32	
6297895-1	1983	Interactions of band 4.1 with mixed phospholipid membranes [phosphatidylserine (PtdSer), phosphatidylethanolamine, phosphatidylcholine, etc.]	Phosphatidylserines	60-78	erythrocyte membrane protein band 4.1	Homo sapiens	16-24	
17030343-2	1999	The protein 4.1-phosphatidyl serine (PS) interactions served as the model system to demonstrate the membrane lipid-protein interactions.	Phosphatidylserines	16-35	erythrocyte membrane protein band 4.1	Homo sapiens	4-15	
7811947-16	1994	These rest suggest that 1) protein 4.1 binds to membrane or submembrane sites at least in part reversibly ; 2) the most reversible sites are probably not proteinaceous and not glycophorin C, but possibly are phospholipids (especially phosphatidylserine); and 3) TIWRFRAP can successfully examine the fast reversible dynamics of cytoskeletal components binding to biological membranes.	Phosphatidylserines	234-252	erythrocyte membrane protein band 4.1	Homo sapiens	27-38