Drug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains.
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Plant Lessons: Exploring ABCB Functionality Through Structural ModelingABC transporters as multidrug resistance mechanisms and the development of chemosensitizers for their reversalMultiple Drug Transport Pathways through Human P-Glycoprotein.Methanethiosulfonate derivatives of rhodamine and verapamil activate human P-glycoprotein at different sites.Molecular models of human P-glycoprotein in two different catalytic statesData-driven homology modelling of P-glycoprotein in the ATP-bound state indicates flexibility of the transmembrane domains.Probing the conformation of the resting state of a bacterial multidrug ABC transporter, BmrA, by a site-directed spin labeling approachPharmacological enhancement of beta-hexosaminidase activity in fibroblasts from adult Tay-Sachs and Sandhoff Patients.P-glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide binding domains at their C-terminal ends.Chapter 11 - Reconstitution of membrane proteins in phospholipid bilayer nanodiscsSnapshots of ligand entry, malleable binding and induced helical movement in P-glycoprotein.Structure and function of efflux pumps that confer resistance to drugsConformational analysis of human ATP-binding cassette transporter ABCB1 in lipid nanodiscs and inhibition by the antibodies MRK16 and UIC2.Identification and characterization of the binding sites of P-glycoprotein for multidrug resistance-related drugs and modulators.Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy.The ATPase activity of the P-glycoprotein drug pump is highly activated when the N-terminal and central regions of the nucleotide-binding domains are linked closely togetherNew horizon of MDR1 (P-glycoprotein) study.Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins.Unravelling the complex drug-drug interactions of the cardiovascular drugs, verapamil and digoxin, with P-glycoprotein.Bilayer mechanical properties regulate the transmembrane helix mobility and enzymatic state of CD39.Substrate binding stabilizes a pre-translocation intermediate in the ATP-binding cassette transport protein MsbAIdentification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.Structure of ABC transporters.Reversal of ATP-binding cassette drug transporter activity to modulate chemoresistance: why has it failed to provide clinical benefit?Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket.Attempts to characterize the NBD heterodimer of MRP1: transient complex formation involves Gly771 of the ABC signature sequence but does not enhance the intrinsic ATPase activity.Chemical conjugation of DeltaF508-CFTR corrector deoxyspergualin to transporter human serum albumin enhances its ability to rescue Cl- channel functions.Substrate-dependent effects of human ABCB1 coding polymorphismsUsing a cysteine-less mutant to provide insight into the structure and mechanism of CFTR.Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket.Involvement of P-glycoprotein in regulating cellular levels of Ginkgo flavonols: quercetin, kaempferol, and isorhamnetin.Processing mutations located throughout the human multidrug resistance P-glycoprotein disrupt interactions between the nucleotide binding domains.Disulfide cross-linking analysis shows that transmembrane segments 5 and 8 of human P-glycoprotein are close together on the cytoplasmic side of the membrane.ATP binding to the first nucleotide binding domain of multidrug resistance-associated protein plays a regulatory role at low nucleotide concentration, whereas ATP hydrolysis at the second plays a dominant role in ATP-dependent leukotriene C4 transpoPermanent activation of the human P-glycoprotein by covalent modification of a residue in the drug-binding site.Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein. Direct evidence for the substrate-induced fit mechanism for drug binding.Towards the Analysis of High Molecular Weight Proteins and Protein complexes using TIMS-MS.Cooperativity between verapamil and ATP bound to the efflux transporter P-glycoprotein.Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoprotein.P-glycoprotein catalytic mechanism: studies of the ADP-vanadate inhibited state.
P2860
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P2860
Drug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains.
description
2002 nî lūn-bûn
@nan
2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Drug binding in human P-glycop ...... th nucleotide-binding domains.
@ast
Drug binding in human P-glycop ...... th nucleotide-binding domains.
@en
type
label
Drug binding in human P-glycop ...... th nucleotide-binding domains.
@ast
Drug binding in human P-glycop ...... th nucleotide-binding domains.
@en
prefLabel
Drug binding in human P-glycop ...... th nucleotide-binding domains.
@ast
Drug binding in human P-glycop ...... th nucleotide-binding domains.
@en
P2860
P356
P1476
Drug binding in human P-glycop ...... oth nucleotide-binding domains
@en
P2093
David M Clarke
M Claire Bartlett
P2860
P304
P356
10.1074/JBC.M211307200
P407
P50
P577
2002-11-05T00:00:00Z