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- W1992823317 endingPage "446" @default.
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- W1992823317 abstract "Glutathione (GSH)-conjugated xenobiotics and GSH-conjugated metabolites (e.g. the cysteinyl leukotriene C4) must be exported from the cells in which they are formed before they can be eliminated from the body or act on their cellular targets. This efflux is often mediated by the multidrug resistance protein 1 (MRP1) transporter, which also confers drug resistance to tumour cells and can protect normal cells from toxic insults. In addition to drugs and GSH conjugates, MRP1 exports GSH and GSH disulfide, and might thus have a role in cellular responses to oxidative stress. The transport of several drugs and conjugated organic anions by MRP1 requires the presence of GSH, but it is not well understood how GSH (and its analogues) enhances transport. Site-directed mutagenesis studies and biophysical analyses have provided important insights into the structural determinants of MRP1 that influence GSH and GSH conjugate binding and transport." @default.
- W1992823317 created "2016-06-24" @default.
- W1992823317 creator A5009648988 @default.
- W1992823317 creator A5044399566 @default.
- W1992823317 date "2006-08-01" @default.
- W1992823317 modified "2023-10-18" @default.
- W1992823317 title "Transport of glutathione and glutathione conjugates by MRP1" @default.
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- W1992823317 doi "https://doi.org/10.1016/j.tips.2006.06.008" @default.
- W1992823317 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16820223" @default.
- W1992823317 hasPublicationYear "2006" @default.
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