PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17365148-0	2007	Mercury activates vascular endothelial cell phospholipase D through thiols and oxidative stress.	Mercury	0-7	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	44-59	
17365148-2	2007	Here, the authors tested the hypothesis that mercury modulates the activity of the endothelial lipid signaling enzyme, phospholipase D (PLD), which is an important player in the endothelial cell (EC) barrier functions.	Mercury	45-52	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	119-134	
17365148-2	2007	Here, the authors tested the hypothesis that mercury modulates the activity of the endothelial lipid signaling enzyme, phospholipase D (PLD), which is an important player in the endothelial cell (EC) barrier functions.	Mercury	45-52	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	136-139	
17365148-4	2007	All three forms of mercury significantly activated PLD in BPAECs in a dose-dependent (0 to 50 microM) and time-dependent (0 to 60 min) fashion.	Mercury	19-26	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	51-54	
17365148-5	2007	Metal chelators significantly attenuated mercury-induced PLD activation, suggesting that cellular mercury-ligand interaction(s) is required for the enzyme activation and that chelators are suitable blockers for mercury-induced PLD activation.	Mercury	41-48	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	57-60	
17365148-5	2007	Metal chelators significantly attenuated mercury-induced PLD activation, suggesting that cellular mercury-ligand interaction(s) is required for the enzyme activation and that chelators are suitable blockers for mercury-induced PLD activation.	Mercury	41-48	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	227-230	
17365148-5	2007	Metal chelators significantly attenuated mercury-induced PLD activation, suggesting that cellular mercury-ligand interaction(s) is required for the enzyme activation and that chelators are suitable blockers for mercury-induced PLD activation.	Mercury	98-105	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	57-60	
17365148-5	2007	Metal chelators significantly attenuated mercury-induced PLD activation, suggesting that cellular mercury-ligand interaction(s) is required for the enzyme activation and that chelators are suitable blockers for mercury-induced PLD activation.	Mercury	98-105	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	57-60	
17365148-6	2007	Sulfhydryl (thiol-protective) agents and antioxidants also significantly attenuated the mercury-induced PLD activation in BPAECs.	Mercury	88-95	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	104-107	
17365148-9	2007	For the first time, this study revealed that mercury induced the activation of PLD in the vascular ECs wherein cellular thiols and oxidative stress acted as signal mediators for the enzyme activation.	Mercury	45-52	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	79-82	
17365148-10	2007	The results underscore the importance of PLD signaling in mercury-induced endothelial dysfunctions ultimately leading to cardiovascular diseases.	Mercury	58-65	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	41-44