PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7857967-5	1995	At 10 micrograms synexin/ml, DIDS and SITS inhibited synexin-mediated liposome aggregation with an EC50 of 3.5 microM and 148 microM, respectively.	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid	29-33	annexin A7	Homo sapiens	17-24	
7857967-5	1995	At 10 micrograms synexin/ml, DIDS and SITS inhibited synexin-mediated liposome aggregation with an EC50 of 3.5 microM and 148 microM, respectively.	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid	29-33	annexin A7	Homo sapiens	53-60	
7857967-11	1995	Ca(2+)-induced synexin polymerization, measured by 90 degrees light scattering, was increased by DIDS, suggesting binding of stilbene disulfonic acids to synexin.	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid	97-101	annexin A7	Homo sapiens	15-22	
7857967-11	1995	Ca(2+)-induced synexin polymerization, measured by 90 degrees light scattering, was increased by DIDS, suggesting binding of stilbene disulfonic acids to synexin.	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid	97-101	annexin A7	Homo sapiens	154-161	
7857967-12	1995	The binding of DIDS to synexin was dependent on the molar ratio of synexin to DIDS.	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid	15-19	annexin A7	Homo sapiens	23-30	
7857967-12	1995	The binding of DIDS to synexin was dependent on the molar ratio of synexin to DIDS.	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid	15-19	annexin A7	Homo sapiens	67-74	
7857967-12	1995	The binding of DIDS to synexin was dependent on the molar ratio of synexin to DIDS.	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid	78-82	annexin A7	Homo sapiens	23-30	
7857967-14	1995	Our results suggest that such inhibition of synexin activity may contribute towards inhibition of surfactant secretion by DIDS, and support a physiological role for synexin in lung surfactant secretion.	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid	122-126	annexin A7	Homo sapiens	44-51