PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24028651-9	2013	The latter could be abolished by blocking aquaporin-1 with mercury and restored by incubation in beta-mercaptoethanol, which abrogated the action of mercury inhibition.	Mercury	59-66	aquaporin 1 (Colton blood group)	Homo sapiens	42-53	
24028651-9	2013	The latter could be abolished by blocking aquaporin-1 with mercury and restored by incubation in beta-mercaptoethanol, which abrogated the action of mercury inhibition.	Mercury	149-156	aquaporin 1 (Colton blood group)	Homo sapiens	42-53	
20409470-0	2010	Molecular mechanisms of how mercury inhibits water permeation through aquaporin-1: understanding by molecular dynamics simulation.	Mercury	28-35	aquaporin 1 (Colton blood group)	Homo sapiens	70-81	
20409470-3	2010	Although site-directed mutagenesis has shown that mercury binds to Cys189 during the inhibition process, it is not fully understood how this inhibits the water permeation through AQP1.	Mercury	50-57	aquaporin 1 (Colton blood group)	Homo sapiens	179-183	
20409470-11	2010	We suggest that mercury disrupts the water pore of AQP1 through local conformational changes in the ar/R region.	Mercury	16-23	aquaporin 1 (Colton blood group)	Homo sapiens	51-55	
15561410-5	2004	Mercury inhibits the water permeability of AQP1 and AQP9, but not AQP4.	Mercury	0-7	aquaporin 1 (Colton blood group)	Homo sapiens	43-47	
17376483-3	2007	To elucidate the mechanism we designed a mutant, T183C, of aquaporin Z (AqpZ) patterned after the known mercury-sensitive site of aquaporin 1 (AQP1) and determined the X-ray crystal structures of the unbound and mercury blocked states.	Mercury	104-111	aquaporin 1 (Colton blood group)	Homo sapiens	130-141	
16534851-6	2006	RESULTS: An 813 bp cDNA encoding a 271 amino acid porcine aquaporin (designated pAQP1) was cloned from liver mRNA (pAQP1 has a 93% identity with human AQP1 and contains two NPA motifs conserved in AQP family, one consensus sequence for N-linked glycosylation, and one mercury-sensitive site at cysteine 191).	Mercury	268-275	aquaporin 1 (Colton blood group)	Homo sapiens	81-85	
10779387-2	2000	For AQP1, inhibition by mercury has been attributed to the formation of a mercaptide bond with cysteine residue 189 found in the putative pore-forming region loop E. Here we show that the nonmercurial compound, tetraethylammonium (TEA) chloride, reduces the water permeability of human AQP1 channels expressed in Xenopus oocytes.	Mercury	24-31	aquaporin 1 (Colton blood group)	Homo sapiens	4-8	
10779387-7	2000	Using polymerase chain reaction, tyrosine 186 in AQP1, selected for its proximity to the mercury-binding site, was mutated to phenylalanine (Y186F), alanine (Y186A), or asparagine (Y186N).	Mercury	89-96	aquaporin 1 (Colton blood group)	Homo sapiens	49-53	
10779387-2	2000	For AQP1, inhibition by mercury has been attributed to the formation of a mercaptide bond with cysteine residue 189 found in the putative pore-forming region loop E. Here we show that the nonmercurial compound, tetraethylammonium (TEA) chloride, reduces the water permeability of human AQP1 channels expressed in Xenopus oocytes.	Mercury	24-31	aquaporin 1 (Colton blood group)	Homo sapiens	286-290	
7528931-3	1994	Like aquaporin 1 (AQP1, also known as CHIP, channel-forming integral membrane protein of 28 kDa), the deduced polypeptide has six putative transmembrane domains but lacks cysteines at the known mercury-sensitive sites.	Mercury	194-201	aquaporin 1 (Colton blood group)	Homo sapiens	5-16	
7528931-3	1994	Like aquaporin 1 (AQP1, also known as CHIP, channel-forming integral membrane protein of 28 kDa), the deduced polypeptide has six putative transmembrane domains but lacks cysteines at the known mercury-sensitive sites.	Mercury	194-201	aquaporin 1 (Colton blood group)	Homo sapiens	18-22	
7528931-3	1994	Like aquaporin 1 (AQP1, also known as CHIP, channel-forming integral membrane protein of 28 kDa), the deduced polypeptide has six putative transmembrane domains but lacks cysteines at the known mercury-sensitive sites.	Mercury	194-201	aquaporin 1 (Colton blood group)	Homo sapiens	44-95	
31676353-3	2020	Inhibition of AQP-1 with either mercury ions (Hg2+) or a specific siRNA led to an impaired migration of EA.hy926 endothelial cells exposed to Epo (wound-healing assays).	Mercury	32-39	aquaporin 1 (Colton blood group)	Homo sapiens	14-19	
9369468-11	1997	Mutation of Tyr-212, a position corresponding to the mercury-sensitive residues in AQP1 and AQP2, to cysteine enhanced the mercurial inhibition of Pf.	Mercury	53-60	aquaporin 1 (Colton blood group)	Homo sapiens	83-87	
9321919-0	1997	Importance of the mercury-sensitive cysteine on function and routing of AQP1 and AQP2 in oocytes.	Mercury	18-25	aquaporin 1 (Colton blood group)	Homo sapiens	72-76	
9321919-3	1997	Oocytes expressing hAQP1 C189S revealed a Pf comparable to wild-type hAQP1, but mercury sensitivity was lost.	Mercury	80-87	aquaporin 1 (Colton blood group)	Homo sapiens	19-24	
8624437-3	1996	Many aquaporins are mercury sensitive, and in AQP1, a mercury-sensitive cysteine residue (Cys-189) is present adjacent to a conserved Asn-Pro-Ala motif.	Mercury	54-61	aquaporin 1 (Colton blood group)	Homo sapiens	46-50