PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 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 9321919-3 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 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