PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22683417-2 2012 The aim of our study was to identify transporters involved in the efflux of raloxifene and its glucuronide metabolites by various in vitro models and by an in vivo study to explore the possible involvement of P-glycoprotein (Pgp), multidrug resistance-associated protein (MRP)1, MRP2, MRP3, and breast cancer resistance protein in the observed high interindividual variability. Glucuronides 95-106 ATP binding cassette subfamily C member 1 Homo sapiens 231-277 28566636-3 2017 Recently, our laboratory found inhibitory effects of NSAIDs-glucuronide (NSAIDs-Glu), a major metabolite of NSAIDs, on MRP-mediated MTX transport as a new site of interaction between MTX and NSAIDs. Glucuronides 60-71 ATP binding cassette subfamily C member 1 Homo sapiens 119-122 31268744-4 2019 Estrone 3-sulfate transport is also unaffected, but both hMRP1-Met1093 mutations eliminate estradiol glucuronide transport, demonstrating that these steroid conjugates have binding sites distinct from each other and from LTC4. Glucuronides 101-112 ATP binding cassette subfamily C member 1 Homo sapiens 57-62 29318243-11 2018 In conclusion, chemical inhibition and gene silencing results suggested that BCRP, MRP1, MRP3 and MRP4 were significant contributors to excretion of wushanicaritin glucuronides. Glucuronides 164-176 ATP binding cassette subfamily C member 1 Homo sapiens 83-87 18079363-1 2008 Members of the multidrug resistance protein (MRP/ABCC) subfamily of ATP-binding cassette proteins transport a wide array of anionic compounds, including sulfate, glucuronide, and glutathione (GSH) conjugates. Glucuronides 162-173 ATP binding cassette subfamily C member 1 Homo sapiens 15-43 18079363-1 2008 Members of the multidrug resistance protein (MRP/ABCC) subfamily of ATP-binding cassette proteins transport a wide array of anionic compounds, including sulfate, glucuronide, and glutathione (GSH) conjugates. Glucuronides 162-173 ATP binding cassette subfamily C member 1 Homo sapiens 45-48 18079363-1 2008 Members of the multidrug resistance protein (MRP/ABCC) subfamily of ATP-binding cassette proteins transport a wide array of anionic compounds, including sulfate, glucuronide, and glutathione (GSH) conjugates. Glucuronides 162-173 ATP binding cassette subfamily C member 1 Homo sapiens 49-53 14643890-2 2004 ABCC1 (MRP1), ABCC2 (MRP2) and ABCC3 (MRP3) are all able to facilitate the efflux of anionic conjugates including glutathione (GSH), glucuronide and sulfate conjugates of xenobiotics and endogenous molecules. Glucuronides 133-144 ATP binding cassette subfamily C member 1 Homo sapiens 0-5 16041243-1 2005 The 190-kDa ATP-binding cassette (ABC) multidrug resistance protein 1 (MRP1) encoded by the MRP1/ABCC1 gene mediates the active cellular efflux of glucuronide, glutathione and sulfate conjugates. Glucuronides 147-158 ATP binding cassette subfamily C member 1 Homo sapiens 97-102 15795089-0 2005 Limited modulation of the transport activity of the human multidrug resistance proteins MRP1, MRP2 and MRP3 by nicotine glucuronide metabolites. Glucuronides 120-131 ATP binding cassette subfamily C member 1 Homo sapiens 88-92 17507208-7 2007 The intracellularly formed glucuronide and sulfate of B were efficiently extruded to both apical and basolateral sides of the Caco-2 monolayer, which were reduced in the presence of MRP inhibitors. Glucuronides 27-38 ATP binding cassette subfamily C member 1 Homo sapiens 182-185 14643890-2 2004 ABCC1 (MRP1), ABCC2 (MRP2) and ABCC3 (MRP3) are all able to facilitate the efflux of anionic conjugates including glutathione (GSH), glucuronide and sulfate conjugates of xenobiotics and endogenous molecules. Glucuronides 133-144 ATP binding cassette subfamily C member 1 Homo sapiens 7-11 9823323-2 1998 However, it has not been possible to demonstrate that MRP can actively transport unmodified forms of these compounds, although the protein has been shown to transport structurally diverse glutathione (GSH)- and glucuronide-conjugated molecules. Glucuronides 211-222 ATP binding cassette subfamily C member 1 Homo sapiens 54-57 14667926-6 2004 The major glucuronide of NU/ICRF 505 inhibited ATP-dependent transport of estradiol 17-beta-glucuronide in Sf9 insect cell membrane vesicles containing MRP1 or MRP3, while co-incubation of HT29 cells with the MRP antagonist, MK571, significantly restored intracellular concentrations of NU/ICRF 505. Glucuronides 10-21 ATP binding cassette subfamily C member 1 Homo sapiens 152-156 14667926-6 2004 The major glucuronide of NU/ICRF 505 inhibited ATP-dependent transport of estradiol 17-beta-glucuronide in Sf9 insect cell membrane vesicles containing MRP1 or MRP3, while co-incubation of HT29 cells with the MRP antagonist, MK571, significantly restored intracellular concentrations of NU/ICRF 505. Glucuronides 10-21 ATP binding cassette subfamily C member 1 Homo sapiens 152-155 11444977-2 2001 MRP1 transports a large number of glutathione, glucuronide, and sulfate-conjugated organic anions by an ATP-dependent efflux mechanism. Glucuronides 47-58 ATP binding cassette subfamily C member 1 Homo sapiens 0-4 11278867-3 2001 In addition, in contrast to wild-type MRP1, leukotriene C(4) transport by the W1246C-MRP1 protein was no longer inhibitable by E(2)17betaG, indicating that the mutant protein had lost the ability to bind the glucuronide. Glucuronides 208-219 ATP binding cassette subfamily C member 1 Homo sapiens 85-89 11004020-9 2000 Given the cellular distribution of these transporters, we hypothesize that MRP isoforms serve to protect fetal blood from entry of organic anions and to promote the excretion of glutathione/glucuronide metabolites in the maternal circulation. Glucuronides 190-201 ATP binding cassette subfamily C member 1 Homo sapiens 75-78 11097346-3 2000 MRP1 operates as an ATP-dependent primary active transporter for substrates conjugated with glucuronide, sulfate or glutathione. Glucuronides 92-103 ATP binding cassette subfamily C member 1 Homo sapiens 0-4 9794919-3 1998 Mrp2, the apical isoform of the multidrug resistance protein, alternatively termed canalicular Mrp (cMrp) or canalicular multispecific organic anion transporter (cMoat), is a 190-kd membrane glycoprotein mediating adenosine triphosphate (ATP)-dependent transport of glucuronides, glutathione S-conjugates, and other amphiphilic anions across the hepatocyte canalicular membrane into bile. Glucuronides 266-278 ATP binding cassette subfamily C member 1 Homo sapiens 0-3 9460989-1 1998 The human multidrug resistance protein (MRP1) confers resistance of cells to a number of different cytostatic drugs and functions as an export pump for glutathione S-conjugates, glucuronides and other amphiphilic anions. Glucuronides 178-190 ATP binding cassette subfamily C member 1 Homo sapiens 40-44 9377473-0 1997 Transport of glutathione conjugates and glucuronides by the multidrug resistance proteins MRP1 and MRP2. Glucuronides 40-52 ATP binding cassette subfamily C member 1 Homo sapiens 90-94 9426231-1 1997 The human multidrug resistance protein MRP1 mediates transport of organic substrates conjugated to glutathione, glucuronide, or sulfate. Glucuronides 112-123 ATP binding cassette subfamily C member 1 Homo sapiens 39-43 9355767-2 1997 We demonstrate for the first time that ATP-dependent transport of both bilirubin glucuronides is mediated by the multidrug resistance protein (MRP1) as well as by the distinct canalicular (apical) isoform MRP2, also termed cMRP or cMOAT (canalicular multispecific organic anion transporter). Glucuronides 81-93 ATP binding cassette subfamily C member 1 Homo sapiens 143-147 9355767-0 1997 ATP-dependent transport of bilirubin glucuronides by the multidrug resistance protein MRP1 and its hepatocyte canalicular isoform MRP2. Glucuronides 37-49 ATP binding cassette subfamily C member 1 Homo sapiens 86-90 9187270-7 1997 MRP-mediated transport was inhibited by an MRP-specific monoclonal antibody and by a variety of GSH derivatives and cholestatic steroid glucuronides. Glucuronides 136-148 ATP binding cassette subfamily C member 1 Homo sapiens 0-3 35148019-7 2022 We initially found that baicalein in the Caco-2 monolayer would be metabolized into glucuronide conjugates BG and B6G under the action of UGT1A8 and UGT1A9 on the endoplasmic reticulum membrane, and then mainly excreted to different sides by acting of MRP and BCRP. Glucuronides 84-95 ATP binding cassette subfamily C member 1 Homo sapiens 252-255