PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18331597-3	2008	We found that staphylokinase (SAK), a well-known Plg activator of bacterial origin, inhibits Plg activation mediated by endogenous tPA and uPA.	Tetradecanoylphorbol Acetate	131-134	plasminogen	Homo sapiens	49-52	
18331597-3	2008	We found that staphylokinase (SAK), a well-known Plg activator of bacterial origin, inhibits Plg activation mediated by endogenous tPA and uPA.	Tetradecanoylphorbol Acetate	131-134	plasminogen	Homo sapiens	93-96	
18331597-4	2008	Furthermore, mixture of SAK with tPA led to a significantly reduced Plg-dependent fibrinolysis.	Tetradecanoylphorbol Acetate	33-36	plasminogen	Homo sapiens	68-71	
18331597-7	2008	Finally, we show that NH2-terminal residues of SAK are important for the inhibitory effect of SAK on tPA- and uPA-mediated Plg activation.	Tetradecanoylphorbol Acetate	101-104	plasminogen	Homo sapiens	123-126	
18331597-8	2008	In conclusion, SAK reduces tPA/uPA-mediated Plg activation by means of SAK.Plg complex formation, consequently downregulating tPA/uPA-induced fibrinolysis.	Tetradecanoylphorbol Acetate	27-30	plasminogen	Homo sapiens	44-47	
18331597-8	2008	In conclusion, SAK reduces tPA/uPA-mediated Plg activation by means of SAK.Plg complex formation, consequently downregulating tPA/uPA-induced fibrinolysis.	Tetradecanoylphorbol Acetate	27-30	plasminogen	Homo sapiens	75-78	
18331597-8	2008	In conclusion, SAK reduces tPA/uPA-mediated Plg activation by means of SAK.Plg complex formation, consequently downregulating tPA/uPA-induced fibrinolysis.	Tetradecanoylphorbol Acetate	126-129	plasminogen	Homo sapiens	44-47	
18331597-8	2008	In conclusion, SAK reduces tPA/uPA-mediated Plg activation by means of SAK.Plg complex formation, consequently downregulating tPA/uPA-induced fibrinolysis.	Tetradecanoylphorbol Acetate	126-129	plasminogen	Homo sapiens	75-78