PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11952151-6	2002	Annexin V was found to be stable to intrinsic lung proteases in the presence of either Ca2+ or EGTA while annexin XI was found to be partially degraded by intrinsic lung proteases in the presence of EGTA.	Egtazic Acid	95-99	annexin A5	Homo sapiens	0-9	
7758749-0	1995	EGTA-resistant binding of annexin V to platelet membranes can be induced by physiological calcium concentrations.	Egtazic Acid	0-4	annexin A5	Homo sapiens	26-35	
10600485-5	1999	Reduction of the extracellular Ca(2+) concentration by EGTA abolished the anti-apoptotic effect, suggesting that annexin V favors Ca(2+) influx and that Ca(2+) acts as an inhibitor rather than an activator of apoptosis in CEM T cells.	Egtazic Acid	55-59	annexin A5	Homo sapiens	113-122	
7772046-6	1995	In contrast a higher [Ca2+] was required to induce maximal binding of the annexin V which could be extracted with EGTA.	Egtazic Acid	114-118	annexin A5	Homo sapiens	74-83	
7772046-12	1995	This suggests that the EGTA-resistant form of annexin V is binding to a membrane component other than phosphatidylserine.	Egtazic Acid	23-27	annexin A5	Homo sapiens	46-55	
2148529-3	1990	Homogenization and further processing of heart in the presence of EGTA resulted in the recovery of annexin V (CaBP33) in the cytosolic fraction and in an EGTA-resistant, Triton X-100-soluble fraction from cardiac membranes.	Egtazic Acid	66-70	annexin A5	Homo sapiens	99-108	
8031848-4	1994	Thrombin stimulation also induces the association of annexin V (11.0 +/- 4.6% of the total) with the membrane in a manner which requires prolonged treatment with EGTA for its release from the membrane.	Egtazic Acid	162-166	annexin A5	Homo sapiens	53-62