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

scientific article

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 is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M112.376202
P932PMC publication ID3411018
P698PubMed publication ID22700974

P50authorTip W. LooQ43098486
P2093author name stringMichael R Detty
David M Clarke
M Claire Bartlett
P2860cites workRepacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycleQ24535845
ABC transporters: the power to changeQ24634548
Structure of P-glycoprotein reveals a molecular basis for poly-specific drug bindingQ24657908
Alternating Access in Maltose Transporter Mediated by Rigid-Body RotationsQ27653974
Predicting P-glycoprotein-mediated drug transport based on support vector machine and three-dimensional crystal structure of P-glycoproteinQ28477346
Structural and functional asymmetry of the nucleotide-binding domains of P-glycoprotein investigated by attenuated total reflection Fourier transform infrared spectroscopyQ28585772
Structure of a bacterial multidrug ABC transporterQ29617308
A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoproteinQ30309937
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 outcomesQ31821882
Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulersQ43717027
The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing walker A sequenceQ44133854
Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoproteinQ44543802
Val133 and Cys137 in transmembrane segment 2 are close to Arg935 and Gly939 in transmembrane segment 11 of human P-glycoproteinQ44746508
Properties of P-glycoprotein with mutations in the "catalytic carboxylate" glutamate residuesQ45028072
Nucleotide-induced structural changes in P-glycoprotein observed by electron microscopy.Q46416788
Nucleotide binding to the multidrug resistance P-glycoprotein as studied by ESR spectroscopyQ46756646
Identification of putative binding sites of P-glycoprotein based on its homology modelQ46823202
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 12Q57976942
Drug binding sites on P-glycoprotein are altered by ATP binding prior to nucleotide hydrolysisQ73015474
The human multidrug resistance P-glycoprotein is inactive when its maturation is inhibited: potential for a role in cancer chemotherapyQ73042152
Allosteric disulfide bondsQ83973641
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 transporterQ33636699
Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: implications for catalysisQ33748171
Vanadate trapping of nucleotide at the ATP-binding sites of human multidrug resistance P-glycoprotein exposes different residues to the drug-binding siteQ34018799
The catalytic cycle of P-glycoproteinQ34370183
A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutantsQ34488592
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 endsQ34695826
Understanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1Q35007411
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 spectroscopyQ35668939
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 permeaseQ36499114
Evidence for two nonidentical drug-interaction sites in the human P-glycoproteinQ36589430
Quantitative evaluation of the lengths of homobifunctional protein cross-linking reagents used as molecular rulersQ36640538
Tariquidar (XR9576): a P-glycoprotein drug efflux pump inhibitorQ36788463
Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificitiesQ36895030
ABC efflux pump-based resistance to chemotherapy drugs.Q37543408
ABC transporters: a riddle wrapped in a mystery inside an enigmaQ37596128
Evidence for modulatory sites at the lipid-protein interface of the human multidrug transporter P-glycoproteinQ38327473
Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complexQ38353484
Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocketQ38663320
Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesisQ39828462
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 segmentsQ40106045
Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocketQ40313463
Permanent Activation of the Human P-glycoprotein by Covalent Modification of a Residue in the Drug-binding SiteQ40652649
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 activityQ41293154
P-glycoprotein. Associations between domains and between domains and molecular chaperonesQ41295494
P-glycoprotein Is Stably Inhibited by Vanadate-induced Trapping of Nucleotide at a Single Catalytic SiteQ41310191
Membrane topology of a cysteine-less mutant of human P-glycoproteinQ41380800
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-glycoproteinQ42031200
Both ATP sites of human P-glycoprotein are essential but not symmetricQ42479018
Allosteric modulation of the human P-glycoprotein involves conformational changes mimicking catalytic transition intermediatesQ42803213
Human P-glycoprotein is active when the two halves are clamped together in the closed conformationQ43098331
Defining the drug-binding site in the human multidrug resistance P-glycoprotein using a methanethiosulfonate analog of verapamil, MTS-verapamilQ43560244
Cysteines 431 and 1074 are responsible for inhibitory disulfide cross-linking between the two nucleotide-binding sites in human P-glycoproteinQ43610789
P433issue32
P407language of work or nameEnglishQ1860
P304page(s)26806-26816
P577publication date2012-06-14
P1433published inJournal of Biological ChemistryQ867727
P1476titleThe 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
P478volume287

Reverse relations

cites work (P2860)
Q53705160A Conformationally Gated Model of Methadone and Loperamide Transport by P-Glycoprotein.
Q37415627Analyses of conformational states of the transporter associated with antigen processing (TAP) protein in a native cellular membrane environment.
Q64092396Cav3.2 T-type calcium channels shape electrical firing in mouse Lamina II neurons
Q89701702Conversion of chemical to mechanical energy by the nucleotide binding domains of ABCB1
Q42284764Cooperativity between verapamil and ATP bound to the efflux transporter P-glycoprotein
Q37311836Crucial role for phylogenetically conserved cytoplasmic loop 3 in ABCC4 protein expression
Q27345028Cryo-EM Analysis of the Conformational Landscape of Human P-glycoprotein (ABCB1) During its Catalytic Cycle.
Q38972586Cysteines 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.
Q39296933Danio rerio ABC transporter genes abcb3 and abcb7 play a protecting role against metal contamination
Q33802134Directed evolution of P-glycoprotein cysteines reveals site-specific, non-conservative substitutions that preserve multidrug resistance.
Q53461492Dissecting the Forces that Dominate Dimerization of the Nucleotide Binding Domains of ABCB1.
Q40297334Effects of a detergent micelle environment on P-glycoprotein (ABCB1)-ligand interactions
Q30636997Equilibrated atomic models of outward-facing P-glycoprotein and effect of ATP binding on structural dynamics
Q36910890Factors that limit positron emission tomography imaging of p-glycoprotein density at the blood-brain barrier.
Q37012424Human P-glycoprotein contains a greasy ball-and-socket joint at the second transmission interface.
Q37333861Hydrolysis at one of the two nucleotide-binding sites drives the dissociation of ATP-binding cassette nucleotide-binding domain dimers.
Q37653308Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.
Q47562583Inhibit or Evade Multidrug Resistance P-Glycoprotein in Cancer Treatment.
Q48269107Insights Into the Molecular Mechanism of Triptan Transport by P-glycoprotein.
Q41848364Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein.
Q43099273Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoprotein.
Q27301793Multiple Drug Transport Pathways through Human P-Glycoprotein
Q28536673Multiple transport-active binding sites are available for a single substrate on human P-glycoprotein (ABCB1)
Q60044934Novel features in the structure of P-glycoprotein (ABCB1) in the post-hydrolytic state as determined at 7.9 Å resolution
Q89818966Replacing the eleven native tryptophans by directed evolution produces an active P-glycoprotein with site-specific, non-conservative substitutions
Q38873295The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoprotein
Q96576495Theoretical insights on helix repacking as the origin of P-glycoprotein promiscuity
Q36691249Unravelling the complex drug-drug interactions of the cardiovascular drugs, verapamil and digoxin, with P-glycoprotein

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