PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19164471-3	2009	We have recently shown that like ACE, ACE2 undergoes ectodomain shedding and that this shedding event is up-regulated by phorbol esters.	Phorbol Esters	121-135	angiotensin I converting enzyme	Homo sapiens	33-36	
19164471-3	2009	We have recently shown that like ACE, ACE2 undergoes ectodomain shedding and that this shedding event is up-regulated by phorbol esters.	Phorbol Esters	121-135	angiotensin converting enzyme 2	Homo sapiens	38-42	
19164471-4	2009	In the present study, we used gel shift assays to demonstrate that calmodulin, an intracellular calcium-binding protein implicated in the regulation of other ectodomain shedding events, binds a 16-amino acid synthetic peptide corresponding to residues 762-777 within the cytoplasmic domain of human ACE2, forming a calcium-dependent calmodulin-peptide complex.	Calcium	96-103	calmodulin 1	Homo sapiens	67-77	
19164471-4	2009	In the present study, we used gel shift assays to demonstrate that calmodulin, an intracellular calcium-binding protein implicated in the regulation of other ectodomain shedding events, binds a 16-amino acid synthetic peptide corresponding to residues 762-777 within the cytoplasmic domain of human ACE2, forming a calcium-dependent calmodulin-peptide complex.	Calcium	96-103	angiotensin converting enzyme 2	Homo sapiens	299-303	
19164471-4	2009	In the present study, we used gel shift assays to demonstrate that calmodulin, an intracellular calcium-binding protein implicated in the regulation of other ectodomain shedding events, binds a 16-amino acid synthetic peptide corresponding to residues 762-777 within the cytoplasmic domain of human ACE2, forming a calcium-dependent calmodulin-peptide complex.	Calcium	96-103	calmodulin 1	Homo sapiens	333-343	
19164471-4	2009	In the present study, we used gel shift assays to demonstrate that calmodulin, an intracellular calcium-binding protein implicated in the regulation of other ectodomain shedding events, binds a 16-amino acid synthetic peptide corresponding to residues 762-777 within the cytoplasmic domain of human ACE2, forming a calcium-dependent calmodulin-peptide complex.	Calcium	315-322	calmodulin 1	Homo sapiens	67-77	
19164471-7	2009	Both trifluoperazine (25 micromol/liter) and calmidazolium, (25 micromol/liter) significantly increased the release of ACE2 into the medium (44.1 +/- 10.8%, P < 0.05, Student"s t test; unpaired, two-tailed, and 51.1 +/- 7.4% P < 0.05, one-way ANOVA, respectively;), as analyzed by an ACE2-specific quenched fluorescence substrate assay.	Trifluoperazine	5-20	angiotensin converting enzyme 2	Homo sapiens	119-123	
19164471-7	2009	Both trifluoperazine (25 micromol/liter) and calmidazolium, (25 micromol/liter) significantly increased the release of ACE2 into the medium (44.1 +/- 10.8%, P < 0.05, Student"s t test; unpaired, two-tailed, and 51.1 +/- 7.4% P < 0.05, one-way ANOVA, respectively;), as analyzed by an ACE2-specific quenched fluorescence substrate assay.	Trifluoperazine	5-20	angiotensin converting enzyme 2	Homo sapiens	284-288	
19164471-7	2009	Both trifluoperazine (25 micromol/liter) and calmidazolium, (25 micromol/liter) significantly increased the release of ACE2 into the medium (44.1 +/- 10.8%, P < 0.05, Student"s t test; unpaired, two-tailed, and 51.1 +/- 7.4% P < 0.05, one-way ANOVA, respectively;), as analyzed by an ACE2-specific quenched fluorescence substrate assay.	calmidazolium	45-58	angiotensin converting enzyme 2	Homo sapiens	119-123	
19164471-7	2009	Both trifluoperazine (25 micromol/liter) and calmidazolium, (25 micromol/liter) significantly increased the release of ACE2 into the medium (44.1 +/- 10.8%, P < 0.05, Student"s t test; unpaired, two-tailed, and 51.1 +/- 7.4% P < 0.05, one-way ANOVA, respectively;), as analyzed by an ACE2-specific quenched fluorescence substrate assay.	calmidazolium	45-58	angiotensin converting enzyme 2	Homo sapiens	284-288