PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21544180-1	2010	Present study shows that non-covalent interaction of kaouthiotoxin (KTX) with their respective pohospholipase A(2) (PLA(2)) from the venom of N. kaouthia displayed marked synergism to exert cytotoxicity without altering the biochemical properties of PLA(2).	ktx	68-71	phospholipase A2 group IIA	Homo sapiens	116-122	
21544180-1	2010	Present study shows that non-covalent interaction of kaouthiotoxin (KTX) with their respective pohospholipase A(2) (PLA(2)) from the venom of N. kaouthia displayed marked synergism to exert cytotoxicity without altering the biochemical properties of PLA(2).	ktx	68-71	phospholipase A2 group IIA	Homo sapiens	250-256	
21544180-5	2010	Therefore, it may be suggested that KTX first destabilize the target cell membrane followed by higher enzymatic activity of PLA(2) on dislocated and disorganized phospholipid bilayers resulting in a significantly higher (p < 0.05) membrane damage by NK-PLA(2)-KTX complex compared to individual components of the complex.	ktx	36-39	phospholipase A2 group IIA	Homo sapiens	124-130	
21544180-5	2010	Therefore, it may be suggested that KTX first destabilize the target cell membrane followed by higher enzymatic activity of PLA(2) on dislocated and disorganized phospholipid bilayers resulting in a significantly higher (p < 0.05) membrane damage by NK-PLA(2)-KTX complex compared to individual components of the complex.	ktx	36-39	phospholipase A2 group IIA	Homo sapiens	256-262