PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21834184-9	2004	The C2A domain of synaptotagmin I (Syt1) binds two to three Ca(2+) ions and also binds anionic phospholipids including PS.	Phosphatidylserines	119-121	synaptotagmin 1	Homo sapiens	35-39	
32075747-6	2020	In full-length Syt1, both Pb2+-complexed C2 domains associate with phosphatidylserine-containing membranes.	Phosphatidylserines	67-85	synaptotagmin 1	Homo sapiens	15-19	
28821560-2	2017	The C2A domain of Synaptotagmin-I (C2Am), which binds to the phosphatidylserine (PS) exposed by apoptotic and necrotic cells, has been developed as an imaging probe for detecting cell death.	Phosphatidylserines	61-79	synaptotagmin 1	Homo sapiens	18-33	
21834184-9	2004	The C2A domain of synaptotagmin I (Syt1) binds two to three Ca(2+) ions and also binds anionic phospholipids including PS.	Phosphatidylserines	119-121	synaptotagmin 1	Homo sapiens	18-33	
21610074-6	2011	Independent evidence for lipid demixing is obtained from fluorescence self-quenching of labeled lipid and from natural abundance (13)C NMR, where heteronuclear single quantum correlation spectra reveal Ca(2+)-dependent chemical shift changes for PS, but not for phosphatidylcholine, in the presence of the syt1 C2 domains.	Phosphatidylserines	246-248	synaptotagmin 1	Homo sapiens	306-310	
21610074-7	2011	The ability of syt1 to demix PS is observed in a range of lipid mixtures that includes cholesterol, phosphatidylethanolamine, and varied PS content.	Phosphatidylserines	29-31	synaptotagmin 1	Homo sapiens	15-19	
16093350-3	2005	We found that different isoforms of syt couple distinct ranges of Ca2+, Ba2+, and Sr2+ to membrane fusion; syt VII was approximately 400-fold more sensitive to Ca2+ than was syt I. Omission of phosphatidylserine (PS) from both populations of liposomes completely abrogated the ability of all three isoforms of syt to stimulate fusion.	Phosphatidylserines	193-211	synaptotagmin 1	Homo sapiens	36-39	
21344950-2	2011	Using site-directed spin labeling, the position and membrane interactions of a fragment of syt1 containing its two C2 domains (syt1C2AB) were assessed in bilayers containing phosphatidylcholine (PC), phosphatidylserine (PS), and phosphatidylinositol 4,5-bisphosphate (PIP(2)).	Phosphatidylserines	220-222	synaptotagmin 1	Homo sapiens	91-95	
19302798-2	2009	The second C2 domain of syt1, C2B, binds to membranes containing phosphatidylserine and phosphatidylcholine in a Ca2+-independent manner with a lipid partition coefficient of approximately 3.0 x 10(2) M(-1).	Phosphatidylserines	65-83	synaptotagmin 1	Homo sapiens	24-28	
18508778-5	2008	Biochemical analysis revealed a strong correlation between the ability of syt isoforms to bind 1,2-dioleoyl phosphatidylserine (PS) and t-SNAREs in a Ca(2+)-promoted manner with their abilities to enhance fusion, further establishing PS and SNAREs as critical effectors for syt action.	Phosphatidylserines	128-130	synaptotagmin 1	Homo sapiens	74-77	
18508778-5	2008	Biochemical analysis revealed a strong correlation between the ability of syt isoforms to bind 1,2-dioleoyl phosphatidylserine (PS) and t-SNAREs in a Ca(2+)-promoted manner with their abilities to enhance fusion, further establishing PS and SNAREs as critical effectors for syt action.	Phosphatidylserines	128-130	synaptotagmin 1	Homo sapiens	274-277	
17182843-6	2007	Notably, the binding activity to phosphatidylserine is inhibited by a physiological range of the Ca(2+) concentration attained after secretagogue stimulation, which presents a striking contrast to the Ca(2+)-stimulatory activity of the C2A domain of synaptotagmin I.	Phosphatidylserines	33-51	synaptotagmin 1	Homo sapiens	250-265	
16093350-6	2005	Our data demonstrate that different syt isoforms are specialized to sense different ranges of divalent cations and that PS is an essential effector of Ca2+.syt action.	Phosphatidylserines	120-122	synaptotagmin 1	Homo sapiens	36-39	
16093350-6	2005	Our data demonstrate that different syt isoforms are specialized to sense different ranges of divalent cations and that PS is an essential effector of Ca2+.syt action.	Phosphatidylserines	120-122	synaptotagmin 1	Homo sapiens	156-159	
15628842-1	2005	Site-directed spin labeling is used to determine the orientation and depth of insertion of the second C2 domain from synaptotagmin I (C2B) into membrane vesicles composed of phosphatidylcholine (PC) and phosphatidylserine (PS).	Phosphatidylserines	203-221	synaptotagmin 1	Homo sapiens	117-132