PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15340165-0	2004	Crystallographic identification of Ca2+ and Sr2+ coordination sites in synaptotagmin I C2B domain.	strontium cation	44-48	synaptotagmin 1	Homo sapiens	71-86	
28111077-4	2017	Our experiments showed that the slowed endocytosis phenotype previously reported after syt1 loss of function can also be triggered by other manipulations that promote asynchronous release such as Sr2+ substitution and complexin loss of function.	strontium cation	196-200	synaptotagmin 1	Homo sapiens	87-91	
16093350-0	2005	Synaptotagmin isoforms couple distinct ranges of Ca2+, Ba2+, and Sr2+ concentration to SNARE-mediated membrane fusion.	strontium cation	65-69	synaptotagmin 1	Homo sapiens	0-13	
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.	strontium cation	82-86	synaptotagmin 1	Homo sapiens	36-39	
16093350-5	2005	Using Sr2+ and Ba2+, we found that binding of syt to PS and t-SNAREs can be dissociated from activation of fusion, uncovering posteffector-binding functions for syt.	strontium cation	6-10	synaptotagmin 1	Homo sapiens	46-49