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.
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Cryo-EM Analysis of the Conformational Landscape of Human P-glycoprotein (ABCB1) During its Catalytic Cycle.Kinetics of the Association/Dissociation Cycle of an ATP-binding Cassette Nucleotide-binding DomainThe Nucleotide-Free State of the Multidrug Resistance ABC Transporter LmrA: Sulfhydryl Cross-Linking Supports a Constant Contact, Head-to-Tail Configuration of the Nucleotide-Binding DomainsCatalytic and transport cycles of ABC exporters.Structural consequences of ATP hydrolysis on the ABC transporter NBD dimer: molecular dynamics studies of HlyB.Exhaustive sampling of docking poses reveals binding hypotheses for propafenone type inhibitors of P-glycoprotein.The ABC transporter MsbA interacts with lipid A and amphipathic drugs at different sitesCharacterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: implications for catalysisAn asymmetric post-hydrolysis state of the ABC transporter ATPase dimer.P-glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide binding domains at their C-terminal ends.Inhibition of multidrug resistance-linked P-glycoprotein (ABCB1) function by 5'-fluorosulfonylbenzoyl 5'-adenosine: evidence for an ATP analogue that interacts with both drug-substrate-and nucleotide-binding sitesMolecular-dynamics simulations of the ATP/apo state of a multidrug ATP-binding cassette transporter provide a structural and mechanistic basis for the asymmetric occluded stateKinetic validation of the models for P-glycoprotein ATP hydrolysis and vanadate-induced trapping. Proposal for additional steps.Conformational analysis of human ATP-binding cassette transporter ABCB1 in lipid nanodiscs and inhibition by the antibodies MRK16 and UIC2.Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy.Pore-exposed tyrosine residues of P-glycoprotein are important hydrogen-bonding partners for drugs.Dissociation of ATP-binding cassette nucleotide-binding domain dimers into monomers during the hydrolysis cycleThe 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 togetherA single active catalytic site is sufficient to promote transport in P-glycoproteinConverting nonhydrolyzable nucleotides to strong cystic fibrosis transmembrane conductance regulator (CFTR) agonists by gain of function (GOF) mutationsOn the origin of large flexibility of P-glycoprotein in the inward-facing stateHuman P-glycoprotein contains a greasy ball-and-socket joint at the second transmission interface.Association/dissociation of the nucleotide-binding domains of the ATP-binding cassette protein MsbA measured during continuous hydrolysisCoupling sigma factor conformation to RNA polymerase reorganisation for DNA meltingNucleotide dependent packing differences in helical crystals of the ABC transporter MsbAConserved Walker A cysteines 431 and 1074 in human P-glycoprotein are accessible to thiol-specific agents in the apo and ADP-vanadate trapped conformations.Exploring conformational equilibria of a heterodimeric ABC transporter.Structures of the Multidrug Transporter P-glycoprotein Reveal Asymmetric ATP Binding and the Mechanism of Polyspecificity.Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.The P-glycoprotein multidrug transporter.Mechanism of the ABC transporter ATPase domains: catalytic models and the biochemical and biophysical record.The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoproteinCysteines 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.Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesisAnalyzing conformational dynamics of single P-glycoprotein transporters by Förster resonance energy transfer using hidden Markov models.Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein.Time-resolved Fourier transform infrared spectroscopy of the nucleotide-binding domain from the ATP-binding Cassette transporter MsbA: ATP hydrolysis is the rate-limiting step in the catalytic cycle.Functional reconstitution of an ABC transporter in nanodiscs for use in electron paramagnetic resonance spectroscopy.Nucleotide-induced structural changes in P-glycoprotein observed by electron microscopy.Substrate-induced conformational changes in the nucleotide-binding domains of lipid bilayer-associated P-glycoprotein during ATP hydrolysis.
P2860
Q27345028-ABFE2AEE-8678-4A80-883E-D4DAFC634F1CQ27676117-BE4F0D7B-9925-4700-BA27-471EF0E9EB9CQ28545890-3EC39B1D-A797-46D9-A882-27F9A63E83E9Q30454423-94DC67BA-9BEC-4634-B874-CCEC6BE53577Q30503207-F810EFCE-D989-4708-BFB3-8BCA6A64D762Q31011332-41FDD464-B3BE-45A0-961E-1F6615A1CE10Q33398632-262B5B0C-56C8-44AB-96A0-71B3E583E5EDQ33748171-CA05F6F2-C933-40A3-82A5-D78A5587BEA3Q34661740-B3913201-9C7B-43A1-9573-CEB43FAC7F0BQ34695826-59D2C5F5-CE6C-44B3-B9B1-F54B70A97E60Q35025897-62BAF6AD-3F03-44BE-9CDD-EC18C2C500C7Q35070510-53DD95CE-B38E-4D4B-B3F6-C2325BE41264Q35181545-54276F94-E388-4EBA-8A41-7A51DD14BD28Q35604412-3255B0A3-9FB4-41EE-A9DF-593A03D1189EQ35668939-79B83590-C524-4B95-A757-6FBA10032AEDQ35854911-434381D4-3369-4904-9989-35D626550EFCQ35922531-3615A7A9-7308-47D2-AFA5-D20871CA9E72Q36137412-10052F93-E216-422E-9ADA-0664A8D45B50Q36840944-6AA4AC9B-D913-497D-9DC7-A206AB9F5650Q36928934-60EB4D54-4394-4600-B810-49C829A743FAQ36967408-EC47A662-0ED7-4582-8B16-79256B6DF0F6Q37012424-28AE3973-5A29-4B17-BA14-25CD3FF321B8Q37175045-23A9D157-7DA6-4BFA-A0A4-8BCC67FED3CAQ37207559-5AC98850-05A3-44DF-8D1D-9363FF8B0EAEQ37244231-E7C86A61-BABA-4067-A4F4-000D6831458FQ37362505-5071FC4A-B494-497C-8E38-5BF813D55705Q37564876-44476920-5CFD-4A2A-ADDC-FC3CFFFBE28AQ37591245-ED04616A-15F7-4E3E-97FB-43021EE61457Q37653308-D82B7EC2-4D90-4D0B-9480-35DFD09D35F5Q37941756-926C4A3A-B7F3-4B03-9605-66D3034ECE23Q38058157-29A0C569-3832-4E40-AE01-C3381F205050Q38873295-FBF56D0B-E540-4218-B7E7-8A2445CB5C4EQ38972586-45A2A61A-E015-4765-A00F-70396DCB1443Q39828462-12D4C6BD-B0A2-4AE0-881F-AA3903DE284CQ41827860-B0F3943F-03C1-45CC-A923-BE543FED1902Q41848364-0E3F0007-DE67-4DF1-AA27-7EB4A2D22C3CQ41997470-2D46804D-59B4-4E9C-830C-A0B8F57BEE46Q42499973-404BB550-F1E7-4524-B74A-4530788571DBQ46416788-D537210B-B760-4FFF-8C25-725968E6CE3FQ47669250-A92311F3-DB52-4AA2-BA18-F90251D77862
P2860
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.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
Catalytic cycle of ATP hydroly ...... nhydrolyzable analogue of ATP.
@en
Catalytic cycle of ATP hydroly ...... nhydrolyzable analogue of ATP.
@nl
type
label
Catalytic cycle of ATP hydroly ...... nhydrolyzable analogue of ATP.
@en
Catalytic cycle of ATP hydroly ...... nhydrolyzable analogue of ATP.
@nl
prefLabel
Catalytic cycle of ATP hydroly ...... nhydrolyzable analogue of ATP.
@en
Catalytic cycle of ATP hydroly ...... nhydrolyzable analogue of ATP.
@nl
P2093
P356
P1433
P1476
Catalytic cycle of ATP hydroly ...... nhydrolyzable analogue of ATP.
@en
P2093
In-Wha Kim
Krishnamachary Nandigama
Peter Chiba
Stephan Kopp
Suresh V Ambudkar
Zuben E Sauna
P304
13787-13799
P356
10.1021/BI701385T
P407
P577
2007-11-08T00:00:00Z