{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T12:42:11Z","timestamp":1792154531737,"version":"4.4.0"},"reference-count":85,"publisher":"Elsevier BV","issue":"50","license":[{"start":{"date-parts":[[2017,12,1]],"date-time":"2017-12-01T00:00:00Z","timestamp":1512086400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,1]],"date-time":"2020-09-01T00:00:00Z","timestamp":1598918400000},"content-version":"vor","delay-in-days":1005,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100004917","name":"Cancer Prevention and Research Institute of Texas","doi-asserted-by":"publisher","award":["RP101073"],"award-info":[{"award-number":["RP101073"]}],"id":[{"id":"10.13039\/100004917","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["RGM102928"],"award-info":[{"award-number":["RGM102928"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01GM118594"],"award-info":[{"award-number":["R01GM118594"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2017,12]]},"DOI":"10.1074\/jbc.m117.814186","type":"journal-article","created":{"date-parts":[[2017,10,10]],"date-time":"2017-10-10T04:50:14Z","timestamp":1507611014000},"page":"20412-20424","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":71,"title":["Substrate-induced conformational changes in the nucleotide-binding domains of lipid bilayer\u2013associated P-glycoprotein during ATP hydrolysis"],"prefix":"10.1016","volume":"292","author":[{"given":"Maria E.","family":"Zoghbi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leo","family":"Mok","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Douglas J.","family":"Swartz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anukriti","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregory A.","family":"Fendley","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ina L.","family":"Urbatsch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guillermo A.","family":"Altenberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M117.814186_bib1","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1042\/bse0500161","article-title":"The P-glycoprotein multidrug transporter","volume":"50","author":"Sharom","year":"2011","journal-title":"Essays Biochem"},{"key":"10.1074\/jbc.M117.814186_bib2","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1016\/j.febslet.2005.12.060","article-title":"The molecular basis of multidrug resistance in cancer: the early years of P-glycoprotein research","volume":"580","author":"Gottesman","year":"2006","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.M117.814186_bib3","doi-asserted-by":"crossref","first-page":"2989","DOI":"10.1021\/cr9000226","article-title":"ABC efflux pump-based resistance to chemotherapy drugs","volume":"109","author":"Eckford","year":"2009","journal-title":"Chem. Rev"},{"key":"10.1074\/jbc.M117.814186_bib4","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1038\/nrd3028","article-title":"Membrane transporters in drug development","volume":"9","author":"International Transporter Consortium","year":"2010","journal-title":"Nat. Rev. Drug Discov"},{"key":"10.1074\/jbc.M117.814186_bib5","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.addr.2017.07.020","article-title":"Evaluation of transporters in drug development: current status and contemporary issues","volume":"116","author":"Lee","year":"2017","journal-title":"Adv. Drug Deliv. Rev"},{"key":"10.1074\/jbc.M117.814186_bib6","doi-asserted-by":"crossref","first-page":"1718","DOI":"10.1126\/science.1168750","article-title":"Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding","volume":"323","author":"Aller","year":"2009","journal-title":"Science"},{"key":"10.1074\/jbc.M117.814186_bib7","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1002\/pro.2387","article-title":"Refined structures of mouse P-glycoprotein","volume":"23","author":"Li","year":"2014","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.M117.814186_bib8","doi-asserted-by":"crossref","first-page":"13386","DOI":"10.1073\/pnas.1309275110","article-title":"Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain","volume":"110","author":"Ward","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.814186_bib9","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1038\/nature11448","article-title":"Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans","volume":"490","author":"Jin","year":"2012","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.814186_bib10","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1107\/S1399004715000978","article-title":"Snapshots of ligand entry, malleable binding and induced helical movement in P-glycoprotein","volume":"71","author":"Szewczyk","year":"2015","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M117.814186_bib11","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1016\/j.sbi.2007.07.003","article-title":"Structure and mechanism of ABC transporter proteins","volume":"17","author":"Hollenstein","year":"2007","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.M117.814186_bib12","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1016\/j.bbrc.2010.04.057","article-title":"Human P-glycoprotein is active when the two halves are clamped together in the closed conformation","volume":"395","author":"Loo","year":"2010","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M117.814186_bib13","doi-asserted-by":"crossref","first-page":"8484","DOI":"10.1074\/jbc.M114.552075","article-title":"Identification of the distance between the homologous halves of P-glycoprotein that triggers the high\/low ATPase activity switch","volume":"289","author":"Loo","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib14","doi-asserted-by":"crossref","first-page":"1413","DOI":"10.1021\/bi002035h","article-title":"FRET analysis indicates that the two ATPase active sites of the P-glycoprotein multidrug transporter are closely associated","volume":"40","author":"Qu","year":"2001","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M117.814186_bib15","doi-asserted-by":"crossref","first-page":"e271","DOI":"10.1371\/journal.pbio.0050271","article-title":"Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis","volume":"5","author":"Borbat","year":"2007","journal-title":"PLoS Biol"},{"key":"10.1074\/jbc.M117.814186_bib16","doi-asserted-by":"crossref","first-page":"20785","DOI":"10.1074\/jbc.M113.477976","article-title":"Association\/dissociation of the nucleotide-binding domains of the ATP-binding cassette protein MsbA measured during continuous hydrolysis","volume":"288","author":"Cooper","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib17","doi-asserted-by":"crossref","first-page":"1112","DOI":"10.1074\/jbc.M111.301192","article-title":"Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy","volume":"287","author":"Verhalen","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib18","doi-asserted-by":"crossref","first-page":"4453","DOI":"10.1074\/jbc.M115.698498","article-title":"The lipid bilayer modulates the structure and function of an ATP-binding cassette exporter","volume":"291","author":"Zoghbi","year":"2016","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib19","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1016\/j.jmb.2009.08.050","article-title":"Conformational cycle of the ABC transporter MsbA in liposomes: detailed analysis using double electron-electron resonance spectroscopy","volume":"393","author":"Zou","year":"2009","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M117.814186_bib20","doi-asserted-by":"crossref","first-page":"19211","DOI":"10.1074\/jbc.M113.450114","article-title":"On the origin of large flexibility of P-glycoprotein in the inward-facing state","volume":"288","author":"Wen","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib21","doi-asserted-by":"crossref","first-page":"2190","DOI":"10.1111\/febs.12773","article-title":"The central cavity of ABCB1 undergoes alternating access during ATP hydrolysis","volume":"281","author":"van Wonderen","year":"2014","journal-title":"FEBS J"},{"key":"10.1074\/jbc.M117.814186_bib22","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1038\/nature21414","article-title":"Energy transduction and alternating access of the mammalian ABC transporter P-glycoprotein","volume":"543","author":"Verhalen","year":"2017","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.814186_bib23","doi-asserted-by":"crossref","first-page":"9704","DOI":"10.1073\/pnas.1303888110","article-title":"Mass spectrometry reveals synergistic effects of nucleotides, lipids, and drugs binding to a multidrug resistance efflux pump","volume":"110","author":"Marcoux","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.814186_bib24","doi-asserted-by":"crossref","first-page":"40125","DOI":"10.1074\/jbc.M206871200","article-title":"Projection structure of P-glycoprotein by electron microscopy. Evidence for a closed conformation of the nucleotide-binding domains","volume":"277","author":"Lee","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib25","doi-asserted-by":"crossref","first-page":"5769","DOI":"10.1074\/jbc.M707028200","article-title":"Nucleotide-induced structural changes in P-glycoprotein observed by electron microscopy","volume":"283","author":"Lee","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib26","doi-asserted-by":"crossref","first-page":"2059","DOI":"10.1016\/j.jmb.2014.03.002","article-title":"3D cryo-electron reconstruction of BmrA, a bacterial multidrug ABC transporter in an inward-facing conformation and in a lipidic environment","volume":"426","author":"Fribourg","year":"2014","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M117.814186_bib27","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.str.2014.12.013","article-title":"Distinct conformational spectrum of homologous multidrug ABC transporters","volume":"23","author":"Moeller","year":"2015","journal-title":"Structure"},{"key":"10.1074\/jbc.M117.814186_bib28","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S1097-2765(02)00576-2","article-title":"ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer","volume":"10","author":"Smith","year":"2002","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M117.814186_bib29","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1016\/S0092-8674(00)80890-9","article-title":"Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily","volume":"101","author":"Hopfner","year":"2000","journal-title":"Cell"},{"key":"10.1074\/jbc.M117.814186_bib30","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1038\/nature05630","article-title":"Multiple molecular mechanisms for multidrug resistance transporters","volume":"446","author":"Higgins","year":"2007","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.814186_bib31","doi-asserted-by":"crossref","first-page":"26862","DOI":"10.1074\/jbc.M301227200","article-title":"The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p","volume":"278","author":"Janas","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib32","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1038\/nature03313","article-title":"CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains","volume":"433","author":"Vergani","year":"2005","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.814186_bib33","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1007\/s00210-005-0031-4","article-title":"The motor domains of ABC-transporters. What can structures tell us?","volume":"372","author":"Oswald","year":"2006","journal-title":"Naunyn Schmiedebergs Arch. Pharmacol"},{"key":"10.1074\/jbc.M117.814186_bib34","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1038\/nature05155","article-title":"Structure of a bacterial multidrug ABC transporter","volume":"443","author":"Dawson","year":"2006","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.814186_bib35","doi-asserted-by":"crossref","first-page":"22793","DOI":"10.1074\/jbc.M700809200","article-title":"Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette: a computational study of the MJ0796 dimer","volume":"282","author":"Jones","year":"2007","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib36","doi-asserted-by":"crossref","first-page":"3025","DOI":"10.1016\/j.bpj.2011.05.028","article-title":"Molecular-dynamics simulations of the ATP\/apo-state of a multidrug ATP-binding cassette transporter provide a structural and mechanistic basis for the asymmetric occluded state","volume":"100","author":"Jones","year":"2011","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M117.814186_bib37","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1002\/prot.22250","article-title":"Opening of the ADP-bound active site in the ABC transporter ATPase dimer: evidence for a constant contact, alternating sites model for the catalytic cycle","volume":"75","author":"Jones","year":"2009","journal-title":"Proteins"},{"key":"10.1074\/jbc.M117.814186_bib38","doi-asserted-by":"crossref","first-page":"13787","DOI":"10.1021\/bi701385t","article-title":"Catalytic cycle of ATP hydrolysis by P-glycoprotein: evidence for formation of the E.S reaction intermediate with ATP-\u03b3-S, a nonhydrolyzable analogue of ATP","volume":"46","author":"Sauna","year":"2007","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M117.814186_bib39","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/S0076-6879(09)64011-8","article-title":"Reconstitution of membrane proteins in phospholipid bilayer nanodiscs","volume":"464","author":"Ritchie","year":"2009","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.M117.814186_bib40","doi-asserted-by":"crossref","first-page":"14994","DOI":"10.1074\/jbc.M112.340281","article-title":"Dissociation of ATP-binding cassette nucleotide-binding domain dimers into monomers during the hydrolysis cycle","volume":"287","author":"Zoghbi","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib41","doi-asserted-by":"crossref","first-page":"4157","DOI":"10.1074\/jbc.M111.318378","article-title":"Kinetics of the association\/dissociation cycle of an ATP-binding cassette nucleotide-binding domain","volume":"287","author":"Zoghbi","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib42","doi-asserted-by":"crossref","first-page":"848","DOI":"10.1038\/nature03819","article-title":"Small vertical movement of a K+ channel voltage sensor measured with luminescence energy transfer","volume":"436","author":"Posson","year":"2005","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.814186_bib43","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1146\/annurev.biophys.31.101101.140927","article-title":"Principles and biophysical applications of lanthanide-based probes","volume":"31","author":"Selvin","year":"2002","journal-title":"Annu. Rev. Biophys. Biomol. Struct"},{"key":"10.1074\/jbc.M117.814186_bib44","doi-asserted-by":"crossref","first-page":"e00116","DOI":"10.1042\/BSR20140062","article-title":"Directed evolution of P-glycoprotein cysteines reveals site-specific, non-conservative substitutions that preserve multidrug resistance","volume":"34","author":"Swartz","year":"2014","journal-title":"Biosci. Rep"},{"key":"10.1074\/jbc.M117.814186_bib45","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.abb.2005.11.004","article-title":"Expression, purification, and characterization of cysteine-free mouse P-glycoprotein","volume":"445","author":"Tombline","year":"2006","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.M117.814186_bib46","doi-asserted-by":"crossref","first-page":"7880","DOI":"10.1038\/srep07880","article-title":"Equilibrated atomic models of outward-facing P-glycoprotein and effect of ATP binding on structural dynamics","volume":"5","author":"Pan","year":"2015","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.M117.814186_bib47","doi-asserted-by":"crossref","first-page":"31212","DOI":"10.1074\/jbc.M404689200","article-title":"Combined mutation of catalytic glutamate residues in the two nucleotide-binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly","volume":"279","author":"Tombline","year":"2004","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib48","doi-asserted-by":"crossref","first-page":"23171","DOI":"10.1074\/jbc.M301957200","article-title":"P-glycoprotein catalytic mechanism: studies of the ADP-vanadate inhibited state","volume":"278","author":"Urbatsch","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib49","doi-asserted-by":"crossref","first-page":"34259","DOI":"10.1074\/jbc.M113.500371","article-title":"Hydrolysis at one of the two nucleotide-binding sites drives the dissociation of ATP-binding cassette nucleotide-binding domain dimers","volume":"288","author":"Zoghbi","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib50","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1124\/mol.116.104190","article-title":"Cryo-EM analysis of the conformational landscape of human P-glycoprotein (ABCB1) during its catalytic cycle","volume":"90","author":"Frank","year":"2016","journal-title":"Mol. Pharmacol"},{"key":"10.1074\/jbc.M117.814186_bib51","doi-asserted-by":"crossref","first-page":"10476","DOI":"10.1074\/jbc.M110.193151","article-title":"P-glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide-binding domains at their C-terminal ends","volume":"286","author":"Verhalen","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib52","doi-asserted-by":"crossref","first-page":"1575","DOI":"10.1074\/jbc.M211307200","article-title":"Drug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains","volume":"278","author":"Loo","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib53","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/0009-2614(86)85107-7","article-title":"Recovery of underlying distributions of lifetimes from fluorescence decay data","volume":"126","author":"James","year":"1986","journal-title":"Chem. Phys. Lett"},{"key":"10.1074\/jbc.M117.814186_bib54","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1021\/j100367a080","article-title":"Comparison of the maximum entropy and exponential series methods for the recovery of distributions of lifetimes from fluorescence lifetime data","volume":"94","author":"Siemiarczuk","year":"1990","journal-title":"J. Phys. Chem"},{"key":"10.1074\/jbc.M117.814186_bib55","doi-asserted-by":"crossref","first-page":"52629","DOI":"10.1074\/jbc.M308175200","article-title":"Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein","volume":"278","author":"Al-Shawi","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib56","doi-asserted-by":"crossref","first-page":"8472","DOI":"10.1073\/pnas.89.18.8472","article-title":"Partial purification and reconstitution of the human multidrug-resistance pump: characterization of the drug-stimulatable ATP hydrolysis","volume":"89","author":"Ambudkar","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.814186_bib57","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1042\/bse0500063","article-title":"Catalytic and transport cycles of ABC exporters","volume":"50","author":"Al-Shawi","year":"2011","journal-title":"Essays Biochem"},{"key":"10.1074\/jbc.M117.814186_bib58","doi-asserted-by":"crossref","first-page":"541","DOI":"10.2174\/1389203023380486","article-title":"Phylogenetic and functional classification of ATP-binding cassette (ABC) systems","volume":"3","author":"Bouige","year":"2002","journal-title":"Curr. Protein Pept. Sci"},{"key":"10.1074\/jbc.M117.814186_bib59","doi-asserted-by":"crossref","first-page":"105","DOI":"10.2217\/14622416.9.1.105","article-title":"ABC multidrug transporters: structure, function and role in chemoresistance","volume":"9","author":"Sharom","year":"2008","journal-title":"Pharmacogenomics"},{"key":"10.1074\/jbc.M117.814186_bib60","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1016\/j.tibs.2009.06.004","article-title":"ABC transporters: a riddle wrapped in a mystery inside an enigma","volume":"34","author":"Jones","year":"2009","journal-title":"Trends Biochem. Sci"},{"key":"10.1074\/jbc.M117.814186_bib61","doi-asserted-by":"crossref","first-page":"21111","DOI":"10.1074\/jbc.C200228200","article-title":"Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters","volume":"277","author":"Moody","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib62","doi-asserted-by":"crossref","first-page":"39","DOI":"10.3109\/10409238.2012.735644","article-title":"Mechanism of the ABC transporter ATPase domains: catalytic models and the biochemical and biophysical record","volume":"48","author":"Jones","year":"2013","journal-title":"Crit. Rev. Biochem. Mol. Biol"},{"key":"10.1074\/jbc.M117.814186_bib63","doi-asserted-by":"crossref","first-page":"e59854","DOI":"10.1371\/journal.pone.0059854","article-title":"An asymmetric post-hydrolysis state of the ABC transporter ATPase dimer","volume":"8","author":"George","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.M117.814186_bib64","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1038\/nsmb.3216","article-title":"Mechanistic diversity in ATP-binding cassette (ABC) transporters","volume":"23","author":"Locher","year":"2016","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.M117.814186_bib65","doi-asserted-by":"crossref","first-page":"19005","DOI":"10.1073\/pnas.0709388104","article-title":"Flexibility in the ABC transporter MsbA: Alternating access with a twist","volume":"104","author":"Ward","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.814186_bib66","doi-asserted-by":"crossref","first-page":"7066","DOI":"10.1074\/jbc.M116.771634","article-title":"Effects of a detergent micelle environment on P-glycoprotein (ABCB1)-ligand interactions","volume":"292","author":"Shukla","year":"2017","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib67","doi-asserted-by":"crossref","first-page":"12840","DOI":"10.1074\/jbc.M708274200","article-title":"Functional characterization of Escherichia coli MsbA: interaction with nucleotides and substrates","volume":"283","author":"Eckford","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib68","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.ab.2008.08.001","article-title":"Spin-labeled lipid A","volume":"382","author":"Bretscher","year":"2008","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.M117.814186_bib69","doi-asserted-by":"crossref","first-page":"21638","DOI":"10.1074\/jbc.M113.485714","article-title":"Substrate binding stabilizes a pre-translocation intermediate in the ATP-binding cassette transport protein MsbA","volume":"288","author":"Doshi","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib70","doi-asserted-by":"crossref","first-page":"e22577","DOI":"10.1371\/journal.pone.0022577","article-title":"A gene optimization strategy that enhances production of fully functional P-glycoprotein in Pichia pastoris","volume":"6","author":"Bai","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.M117.814186_bib71","doi-asserted-by":"crossref","first-page":"35193","DOI":"10.1074\/jbc.M306226200","article-title":"The ATP binding cassette multidrug transporter LmrA and lipid transporter MsbA have overlapping substrate specificities","volume":"278","author":"Reuter","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib72","doi-asserted-by":"crossref","first-page":"20449","DOI":"10.1074\/jbc.C300154200","article-title":"Permanent activation of the human P-glycoprotein by covalent modification of a residue in the drug-binding site","volume":"278","author":"Loo","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib73","doi-asserted-by":"crossref","first-page":"11865","DOI":"10.1021\/bi960823u","article-title":"Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide-binding domains","volume":"35","author":"Liu","year":"1996","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M117.814186_bib74","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1042\/bj3280897","article-title":"Conformational changes of P-glycoprotein by nucleotide binding","volume":"328","author":"Wang","year":"1997","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M117.814186_bib75","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1042\/bj3080381","article-title":"Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells","volume":"308","author":"Sharom","year":"1995","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M117.814186_bib76","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.bbrc.2016.02.124","article-title":"P-glycoprotein ATPase activity requires lipids to activate a switch at the first transmission interface","volume":"472","author":"Loo","year":"2016","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M117.814186_bib77","doi-asserted-by":"crossref","first-page":"e20562","DOI":"10.1371\/journal.pone.0020562","article-title":"Heterologous overexpression and mutagenesis of the human bile salt export pump (ABCB11) using DREAM (Directed REcombination-Assisted Mutagenesis)","volume":"6","author":"Stindt","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.M117.814186_bib78","doi-asserted-by":"crossref","first-page":"17159","DOI":"10.1074\/jbc.270.29.17159","article-title":"Functional dissection of P-glycoprotein nucleotide-binding domains in chimeric and mutant proteins. Modulation of drug resistance profiles","volume":"270","author":"Beaudet","year":"1995","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib79","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1002\/(SICI)1097-0061(19980130)14:2<115::AID-YEA204>3.0.CO;2-2","article-title":"Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications","volume":"14","author":"Brachmann","year":"1998","journal-title":"Yeast"},{"key":"10.1074\/jbc.M117.814186_bib80","doi-asserted-by":"crossref","first-page":"34711","DOI":"10.1074\/jbc.274.49.34711","article-title":"Large scale purification of detergent-soluble P-glycoprotein from Pichia pastoris cells and characterization of nucleotide binding properties of wild-type, Walker A, and Walker B mutant proteins","volume":"274","author":"Lerner-Marmarosh","year":"1999","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib81","doi-asserted-by":"crossref","first-page":"25031","DOI":"10.1074\/jbc.M003962200","article-title":"Conserved Walker A Ser residues in the catalytic sites of P-glycoprotein are critical for catalysis and involved primarily at the transition state step","volume":"275","author":"Urbatsch","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.814186_bib82","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1021\/bc980113w","article-title":"Thiol-reactive luminescent chelates of terbium and europium","volume":"10","author":"Chen","year":"1999","journal-title":"Bioconjug. Chem"},{"key":"10.1074\/jbc.M117.814186_bib83","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.bbrc.2013.11.050","article-title":"ATP binding to two sites is necessary for dimerization of nucleotide-binding domains of ABC proteins","volume":"443","author":"Zoghbi","year":"2014","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M117.814186_bib84","doi-asserted-by":"crossref","first-page":"e00177","DOI":"10.1042\/BSR20140089","article-title":"Functional hemichannels formed by human connexin 26 expressed in bacteria","volume":"35","author":"Fiori","year":"2015","journal-title":"Biosci. Rep"},{"key":"10.1074\/jbc.M117.814186_bib85","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1006\/abio.2000.4925","article-title":"Luminescence energy transfer with lanthanide chelates: interpretation of sensitized acceptor decay amplitudes","volume":"289","author":"Heyduk","year":"2001","journal-title":"Anal. Biochem"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820327782?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820327782?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M117.814186","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T00:15:36Z","timestamp":1641255336000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820327782"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,12]]},"references-count":85,"journal-issue":{"issue":"50","published-print":{"date-parts":[[2017,12]]}},"alternative-id":["S0021925820327782"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m117.814186","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.731966588.793569210","asserted-by":"object"}]},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2017,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Substrate-induced conformational changes in the nucleotide-binding domains of lipid bilayer\u2013associated P-glycoprotein during ATP hydrolysis","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M117.814186","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}