Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1.
about
Transport of bile acids in multidrug-resistance-protein 3-overexpressing cells co-transfected with the ileal Na+-dependent bile-acid transporterMultidrug resistance proteins (MRPs/ABCCs) in cancer chemotherapy and genetic diseasesPulmonary metabolism of resveratrol: in vitro and in vivo evidenceThe Regulation of Steroid Action by Sulfation and DesulfationThe blood-testis barrier and its implications for male contraceptionLocalization and functional characterization of the rat Oatp4c1 transporter in an in vitro cell system and rat tissuesAnalysis of estrogens and androgens in postmenopausal serum and plasma by liquid chromatography-mass spectrometry.Role of the NH2-terminal membrane spanning domain of multidrug resistance protein 1/ABCC1 in protein processing and traffickingMice lacking Mrp1 have reduced testicular steroid hormone levels and alterations in steroid biosynthetic enzymesIntermediate structural states involved in MRP1-mediated drug transport. Role of glutathione.Multidrug resistance protein 1 (MRP1, ABCC1), a "multitasking" ATP-binding cassette (ABC) transporter.The MRP family of drug efflux pumps.Molecular and cellular physiology of renal organic cation and anion transport.Long-term exposure to estrogen enhances chemotherapeutic efficacy potentially through epigenetic mechanism in human breast cancer cells.On the putative co-transport of drugs by multidrug resistance proteins.Substrate recognition and transport by multidrug resistance protein 1 (ABCC1).Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins.Structure and function of the MRP2 (ABCC2) protein and its role in drug disposition.Use of in vitro transporter assays to understand hepatic and renal disposition of new drug candidates.Metabolism of ATP-binding cassette drug transporter inhibitors: complicating factor for multidrug resistance.Functional diversification of sea urchin ABCC1 (MRP1) by alternative splicingPlasma membrane glutathione transporters and their roles in cell physiology and pathophysiologyIntestinal transporters for endogenic and pharmaceutical organic anions: the challenges of deriving in-vitro kinetic parameters for the prediction of clinically relevant drug-drug interactions.Minireview: SLCO and ABC transporters: a role for steroid transport in prostate cancer progression.Regulation of function by dimerization through the amino-terminal membrane-spanning domain of human ABCC1/MRP1.Placental control of drug delivery.Placental ABC Transporters: Biological Impact and Pharmaceutical Significance.Folates provoke cellular efflux and drug resistance of substrates of the multidrug resistance protein 1 (MRP1).Selenium-dependent and -independent transport of arsenic by the human multidrug resistance protein 2 (MRP2/ABCC2): implications for the mutual detoxification of arsenic and selenium.Glutathione export during apoptosis requires functional multidrug resistance-associated proteins.Role of GSH in estrone sulfate binding and translocation by the multidrug resistance protein 1 (MRP1/ABCC1).Identification and characterization of functionally important elements in the multidrug resistance protein 1 COOH-terminal region.Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): glutamate 1204 is important for both the expression and catalytic activity of the transpArsenic transport by the human multidrug resistance protein 1 (MRP1/ABCC1). Evidence that a tri-glutathione conjugate is required.Identification of proline residues in the core cytoplasmic and transmembrane regions of multidrug resistance protein 1 (MRP1/ABCC1) important for transport function, substrate specificity, and nucleotide interactions.Functional importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1): identification of an aspartate residue critical for conversion from a high to low affinity substrate binding staLocalization of the GSH-dependent photolabelling site of an agosterol A analog on human MRP1.Evidence for two interacting ligand binding sites in human multidrug resistance protein 2 (ATP binding cassette C2).Multiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1.Photolabeling of human and murine multidrug resistance protein 1 with the high affinity inhibitor [125I]LY475776 and azidophenacyl-[35S]glutathione.
P2860
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P2860
Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1.
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1.
@ast
Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1.
@en
type
label
Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1.
@ast
Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1.
@en
prefLabel
Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1.
@ast
Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1.
@en
P2093
P2860
P356
P1476
Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1.
@en
P2093
P2860
P304
P356
10.1074/JBC.M008251200
P407
P577
2000-12-01T00:00:00Z