scholarly article | Q13442814 |
P50 | author | Tip W. Loo | Q43098486 |
P2093 | author name string | Michael R Detty | |
David M Clarke | |||
M Claire Bartlett | |||
P2860 | cites work | Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle | Q24535845 |
ABC transporters: the power to change | Q24634548 | ||
Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding | Q24657908 | ||
Alternating Access in Maltose Transporter Mediated by Rigid-Body Rotations | Q27653974 | ||
Predicting P-glycoprotein-mediated drug transport based on support vector machine and three-dimensional crystal structure of P-glycoprotein | Q28477346 | ||
Structural and functional asymmetry of the nucleotide-binding domains of P-glycoprotein investigated by attenuated total reflection Fourier transform infrared spectroscopy | Q28585772 | ||
Structure of a bacterial multidrug ABC transporter | Q29617308 | ||
A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein | Q30309937 | ||
Characterization of the catalytic cycle of ATP hydrolysis by human P-glycoprotein. The two ATP hydrolysis events in a single catalytic cycle are kinetically similar but affect different functional outcomes | Q31821882 | ||
Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers | Q43717027 | ||
The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing walker A sequence | Q44133854 | ||
Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoprotein | Q44543802 | ||
Val133 and Cys137 in transmembrane segment 2 are close to Arg935 and Gly939 in transmembrane segment 11 of human P-glycoprotein | Q44746508 | ||
Properties of P-glycoprotein with mutations in the "catalytic carboxylate" glutamate residues | Q45028072 | ||
Nucleotide-induced structural changes in P-glycoprotein observed by electron microscopy. | Q46416788 | ||
Nucleotide binding to the multidrug resistance P-glycoprotein as studied by ESR spectroscopy | Q46756646 | ||
Identification of putative binding sites of P-glycoprotein based on its homology model | Q46823202 | ||
Catalytic cycle of ATP hydrolysis by P-glycoprotein: evidence for formation of the E.S reaction intermediate with ATP-gamma-S, a nonhydrolyzable analogue of ATP. | Q46910980 | ||
Shedding light on drug transport: structure and function of the P-glycoprotein multidrug transporter (ABCB1). | Q48313444 | ||
Human (MDR1) and mouse (mdr1, mdr3) P-glycoproteins can be distinguished by their respective drug resistance profiles and sensitivity to modulators. | Q54182645 | ||
Chalcogenopyrylium Compounds as Modulators of the ATP-Binding Cassette Transporters P-Glycoprotein (P-gp/ABCB1) and Multidrug Resistance Protein 1 (MRP1/ABCC1) | Q57976867 | ||
Drug-stimulated ATPase Activity of Human P-glycoprotein Requires Movement between Transmembrane Segments 6 and 12 | Q57976942 | ||
Drug binding sites on P-glycoprotein are altered by ATP binding prior to nucleotide hydrolysis | Q73015474 | ||
The human multidrug resistance P-glycoprotein is inactive when its maturation is inhibited: potential for a role in cancer chemotherapy | Q73042152 | ||
Allosteric disulfide bonds | Q83973641 | ||
Drug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains. | Q33185124 | ||
Interaction of LDS-751 with P-glycoprotein and mapping of the location of the R drug binding site. | Q33210733 | ||
Biochemical, cellular, and pharmacological aspects of the multidrug transporter | Q33636699 | ||
Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: implications for catalysis | Q33748171 | ||
Vanadate trapping of nucleotide at the ATP-binding sites of human multidrug resistance P-glycoprotein exposes different residues to the drug-binding site | Q34018799 | ||
The catalytic cycle of P-glycoprotein | Q34370183 | ||
A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants | Q34488592 | ||
Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells. | Q34559072 | ||
P-glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide binding domains at their C-terminal ends | Q34695826 | ||
Understanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1 | Q35007411 | ||
Conformational analysis of human ATP-binding cassette transporter ABCB1 in lipid nanodiscs and inhibition by the antibodies MRK16 and UIC2. | Q35604412 | ||
Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy | Q35668939 | ||
The "specific" P-glycoprotein inhibitor Tariquidar is also a substrate and an inhibitor for breast cancer resistance protein (BCRP/ABCG2). | Q36015358 | ||
Opening and closing of the periplasmic gate in lactose permease | Q36499114 | ||
Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein | Q36589430 | ||
Quantitative evaluation of the lengths of homobifunctional protein cross-linking reagents used as molecular rulers | Q36640538 | ||
Tariquidar (XR9576): a P-glycoprotein drug efflux pump inhibitor | Q36788463 | ||
Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities | Q36895030 | ||
ABC efflux pump-based resistance to chemotherapy drugs. | Q37543408 | ||
ABC transporters: a riddle wrapped in a mystery inside an enigma | Q37596128 | ||
Evidence for modulatory sites at the lipid-protein interface of the human multidrug transporter P-glycoprotein | Q38327473 | ||
Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex | Q38353484 | ||
Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket | Q38663320 | ||
Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis | Q39828462 | ||
Suppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites. | Q40082401 | ||
Nucleotide binding, ATP hydrolysis, and mutation of the catalytic carboxylates of human P-glycoprotein cause distinct conformational changes in the transmembrane segments | Q40106045 | ||
Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket | Q40313463 | ||
Permanent Activation of the Human P-glycoprotein by Covalent Modification of a Residue in the Drug-binding Site | Q40652649 | ||
Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein. Direct evidence for the substrate-induced fit mechanism for drug binding. | Q40667534 | ||
Cross-linking of human multidrug resistance P-glycoprotein by the substrate, tris-(2-maleimidoethyl)amine, is altered by ATP hydrolysis. Evidence for rotation of a transmembrane helix. | Q40795985 | ||
Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity | Q41293154 | ||
P-glycoprotein. Associations between domains and between domains and molecular chaperones | Q41295494 | ||
P-glycoprotein Is Stably Inhibited by Vanadate-induced Trapping of Nucleotide at a Single Catalytic Site | Q41310191 | ||
Membrane topology of a cysteine-less mutant of human P-glycoprotein | Q41380800 | ||
Processing mutations disrupt interactions between the nucleotide binding and transmembrane domains of P-glycoprotein and the cystic fibrosis transmembrane conductance regulator (CFTR). | Q41993227 | ||
The molecular interaction of the high affinity reversal agent XR9576 with P-glycoprotein | Q42031200 | ||
Both ATP sites of human P-glycoprotein are essential but not symmetric | Q42479018 | ||
Allosteric modulation of the human P-glycoprotein involves conformational changes mimicking catalytic transition intermediates | Q42803213 | ||
Human P-glycoprotein is active when the two halves are clamped together in the closed conformation | Q43098331 | ||
Defining the drug-binding site in the human multidrug resistance P-glycoprotein using a methanethiosulfonate analog of verapamil, MTS-verapamil | Q43560244 | ||
Cysteines 431 and 1074 are responsible for inhibitory disulfide cross-linking between the two nucleotide-binding sites in human P-glycoprotein | Q43610789 | ||
P433 | issue | 32 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 26806-26816 | |
P577 | publication date | 2012-06-14 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | 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 together | |
P478 | volume | 287 |
Q53705160 | A Conformationally Gated Model of Methadone and Loperamide Transport by P-Glycoprotein. |
Q37415627 | Analyses of conformational states of the transporter associated with antigen processing (TAP) protein in a native cellular membrane environment. |
Q64092396 | Cav3.2 T-type calcium channels shape electrical firing in mouse Lamina II neurons |
Q89701702 | Conversion of chemical to mechanical energy by the nucleotide binding domains of ABCB1 |
Q42284764 | Cooperativity between verapamil and ATP bound to the efflux transporter P-glycoprotein |
Q37311836 | Crucial role for phylogenetically conserved cytoplasmic loop 3 in ABCC4 protein expression |
Q27345028 | Cryo-EM Analysis of the Conformational Landscape of Human P-glycoprotein (ABCB1) During its Catalytic Cycle. |
Q38972586 | Cysteines introduced into extracellular loops 1 and 4 of human P-glycoprotein that are close only in the open conformation spontaneously form a disulfide bond that inhibits drug efflux and ATPase activity. |
Q39296933 | Danio rerio ABC transporter genes abcb3 and abcb7 play a protecting role against metal contamination |
Q33802134 | Directed evolution of P-glycoprotein cysteines reveals site-specific, non-conservative substitutions that preserve multidrug resistance. |
Q53461492 | Dissecting the Forces that Dominate Dimerization of the Nucleotide Binding Domains of ABCB1. |
Q40297334 | Effects of a detergent micelle environment on P-glycoprotein (ABCB1)-ligand interactions |
Q30636997 | Equilibrated atomic models of outward-facing P-glycoprotein and effect of ATP binding on structural dynamics |
Q36910890 | Factors that limit positron emission tomography imaging of p-glycoprotein density at the blood-brain barrier. |
Q37012424 | Human P-glycoprotein contains a greasy ball-and-socket joint at the second transmission interface. |
Q37333861 | Hydrolysis at one of the two nucleotide-binding sites drives the dissociation of ATP-binding cassette nucleotide-binding domain dimers. |
Q37653308 | Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch. |
Q47562583 | Inhibit or Evade Multidrug Resistance P-Glycoprotein in Cancer Treatment. |
Q48269107 | Insights Into the Molecular Mechanism of Triptan Transport by P-glycoprotein. |
Q41848364 | Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein. |
Q43099273 | Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoprotein. |
Q27301793 | Multiple Drug Transport Pathways through Human P-Glycoprotein |
Q28536673 | Multiple transport-active binding sites are available for a single substrate on human P-glycoprotein (ABCB1) |
Q60044934 | Novel features in the structure of P-glycoprotein (ABCB1) in the post-hydrolytic state as determined at 7.9 Å resolution |
Q89818966 | Replacing the eleven native tryptophans by directed evolution produces an active P-glycoprotein with site-specific, non-conservative substitutions |
Q38873295 | The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoprotein |
Q96576495 | Theoretical insights on helix repacking as the origin of P-glycoprotein promiscuity |
Q36691249 | Unravelling the complex drug-drug interactions of the cardiovascular drugs, verapamil and digoxin, with P-glycoprotein |
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