PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
21062953-5	2011	The phospholipase activity detected by the PLA1 substrate could be inhibited with the small molecule esterase inhibitor ebelactone B.	ebelactone B	120-132	lipase H	Homo sapiens	43-47
22861813-4	2012	Pharmacological inhibition of CatA by the natural product ebelactone B increased renal bradykinin levels and prevented the development of salt-induced hypertension.	ebelactone B	58-70	cathepsin A	Homo sapiens	30-34
22861813-4	2012	Pharmacological inhibition of CatA by the natural product ebelactone B increased renal bradykinin levels and prevented the development of salt-induced hypertension.	ebelactone B	58-70	kininogen 1	Homo sapiens	87-97
15842622-7	2005	Ebelactone B, a known lipase inhibitor, repressed the lipolytic activity of the enzyme.	ebelactone B	0-12	probable feruloyl esterase A	Triticum aestivum	22-28
14737963-0	2003	Effects of ebelactone B on cathepsin A activity in intact platelets and on platelet activation.	ebelactone B	11-23	cathepsin A	Homo sapiens	27-38
12576084-4	2003	The deamidase activity was inhibited by Ebelactone B and the serine protease inhibitor, phenylmethanesulfonyl fluoride (PMSF), while the degradation of the synthetic stereoisomer, Asn-Trp-Phe-NH(2) (N(l)WF-NH(2)), was sensitive to the divalent cation-chelating agent, o-phenanthroline, and aminopeptidase inhibitors, amastatin and bestatin.	ebelactone B	40-52	cathepsin A	Homo sapiens	4-13
14737963-1	2003	PURPOSE: Previous in vitro studies have demonstrated that a potent antihypertensive agent ebelactone B inhibits cathepsin A/deamidase activity.	ebelactone B	90-102	cathepsin A	Homo sapiens	112-133
14737963-6	2003	RESULTS: Pre-treatment of platelets for up to 60 minutes with 10 mumol/l ebelactone B, that effectively inhibits cathepsin A activity in platelet lysate, did not affect this activity in intact platelets.	ebelactone B	73-85	cathepsin A	Homo sapiens	113-124
14737963-7	2003	Exposure of PRP to 10 mumol/l ebelactone B alone, or before platelet activation with ADP or TRAP caused only a small but non-significant increase in P-selectin and GpIIb/IIIa expression on the platelet surface, as demonstrated by flow cytometry analysis.	ebelactone B	30-42	prion protein	Homo sapiens	12-15
14737963-7	2003	Exposure of PRP to 10 mumol/l ebelactone B alone, or before platelet activation with ADP or TRAP caused only a small but non-significant increase in P-selectin and GpIIb/IIIa expression on the platelet surface, as demonstrated by flow cytometry analysis.	ebelactone B	30-42	selectin P	Homo sapiens	149-159
14737963-7	2003	Exposure of PRP to 10 mumol/l ebelactone B alone, or before platelet activation with ADP or TRAP caused only a small but non-significant increase in P-selectin and GpIIb/IIIa expression on the platelet surface, as demonstrated by flow cytometry analysis.	ebelactone B	30-42	integrin subunit alpha 2b	Homo sapiens	164-169
8835930-0	1996	Effects of ebelactone B, a lipase inhibitor, on intestinal fat absorption in the rat.	ebelactone B	11-23	lipase G, endothelial type	Rattus norvegicus	27-33
11180979-6	2001	Both the acylpeptide hydrolase activity and the protease activity of the 55 kDa enzyme were completely inhibited by diisopropylfluorophosphate, p -chloromercuribenzoate and ebelactone, and moderately inhibited by N -tosyl phenylalanine chloromethyl ketone.	ebelactone B	173-183	acylaminoacyl-peptide hydrolase	Bos taurus	9-30
8835628-0	1995	Degradation of bradykinin in human urine by carboxypeptidase Y-like exopeptidase and neutral endopeptidase and their inhibition by ebelactone B and phosphoramidon.	ebelactone B	131-143	kininogen 1	Homo sapiens	15-25
8835628-3	1995	The combination of phosphoramidon and ebelactone B completely (by 95%) inhibited bradykinin degradation in human urine.	ebelactone B	38-50	kininogen 1	Homo sapiens	81-91
8089934-1	1994	Ebelactone B (EB) (10(-7)-10(-5) M) inhibited dose-dependently carboxypeptidase (CP) Y-like exopeptidase, one of the major kininases separated from rat urine, whereas it inhibited neither CPA, CPB or neutral endopeptidase (NEP).	ebelactone B	0-12	carboxypeptidase B1	Rattus norvegicus	193-196
8089934-1	1994	Ebelactone B (EB) (10(-7)-10(-5) M) inhibited dose-dependently carboxypeptidase (CP) Y-like exopeptidase, one of the major kininases separated from rat urine, whereas it inhibited neither CPA, CPB or neutral endopeptidase (NEP).	ebelactone B	0-12	membrane metallo-endopeptidase	Rattus norvegicus	200-221
8089934-1	1994	Ebelactone B (EB) (10(-7)-10(-5) M) inhibited dose-dependently carboxypeptidase (CP) Y-like exopeptidase, one of the major kininases separated from rat urine, whereas it inhibited neither CPA, CPB or neutral endopeptidase (NEP).	ebelactone B	0-12	membrane metallo-endopeptidase	Rattus norvegicus	223-226
8089934-1	1994	Ebelactone B (EB) (10(-7)-10(-5) M) inhibited dose-dependently carboxypeptidase (CP) Y-like exopeptidase, one of the major kininases separated from rat urine, whereas it inhibited neither CPA, CPB or neutral endopeptidase (NEP).	ebelactone B	14-16	carboxypeptidase B1	Rattus norvegicus	193-196
8089934-1	1994	Ebelactone B (EB) (10(-7)-10(-5) M) inhibited dose-dependently carboxypeptidase (CP) Y-like exopeptidase, one of the major kininases separated from rat urine, whereas it inhibited neither CPA, CPB or neutral endopeptidase (NEP).	ebelactone B	14-16	membrane metallo-endopeptidase	Rattus norvegicus	200-221
8089934-1	1994	Ebelactone B (EB) (10(-7)-10(-5) M) inhibited dose-dependently carboxypeptidase (CP) Y-like exopeptidase, one of the major kininases separated from rat urine, whereas it inhibited neither CPA, CPB or neutral endopeptidase (NEP).	ebelactone B	14-16	membrane metallo-endopeptidase	Rattus norvegicus	223-226