{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T12:42:07Z","timestamp":1792154527900,"version":"4.4.0"},"reference-count":104,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,10,1]],"date-time":"2016-10-01T00:00:00Z","timestamp":1475280000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000968","name":"American Heart Association","doi-asserted-by":"publisher","award":["14GRNT20450044"],"award-info":[{"award-number":["14GRNT20450044"]}],"id":[{"id":"10.13039\/100000968","id-type":"DOI","asserted-by":"publisher"}]},{"name":"National Institute of Health","award":["1R15GM107913-01A1"],"award-info":[{"award-number":["1R15GM107913-01A1"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical Pharmacology"],"published-print":{"date-parts":[[2016,10]]},"DOI":"10.1016\/j.bcp.2016.08.013","type":"journal-article","created":{"date-parts":[[2016,8,15]],"date-time":"2016-08-15T03:44:50Z","timestamp":1471232690000},"page":"96-108","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":64,"special_numbering":"C","title":["Cooperativity between verapamil and ATP bound to the efflux transporter P-glycoprotein"],"prefix":"10.1016","volume":"118","author":[{"given":"Kaitlyn V.","family":"Ledwitch","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Morgan E.","family":"Gibbs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert W.","family":"Barnes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arthur G.","family":"Roberts","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bcp.2016.08.013_b0005","series-title":"ABC Transporters and Multidrug Resistance","author":"Boumendjel","year":"2009"},{"key":"10.1016\/j.bcp.2016.08.013_b0010","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1080\/00498250701867889","article-title":"Structure, function and regulation of P-glycoprotein and its clinical relevance in drug disposition","volume":"38","author":"Zhou","year":"2008","journal-title":"Xenobiotica"},{"key":"10.1016\/j.bcp.2016.08.013_b0015","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/S0889-8588(18)30097-2","article-title":"MDR expression in normal tissues. Pharmacologic implications for the clinical use of P-glycoprotein inhibitors","volume":"9","author":"Lum","year":"1995","journal-title":"Hematol. Oncol. Clin. North Am."},{"key":"10.1016\/j.bcp.2016.08.013_b0020","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1016\/j.reprotox.2006.01.007","article-title":"P-glycoprotein in the placenta: expression, localization, regulation and function","volume":"22","author":"Ceckova-Novotna","year":"2006","journal-title":"Reprod. Toxicol."},{"key":"10.1016\/j.bcp.2016.08.013_b0025","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.1177\/002215540205001008","article-title":"Expression and localization of P-glycoprotein in human heart: effects of cardiomyopathy","volume":"50","author":"Meissner","year":"2002","journal-title":"J. Histochem. Cytochem."},{"key":"10.1016\/j.bcp.2016.08.013_b0030","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.cardiores.2004.06.003","article-title":"Pharmacogenomics of heart failure \u2013 focus on drug disposition and action","volume":"64","author":"Cascorbi","year":"2004","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.bcp.2016.08.013_b0035","first-page":"160","article-title":"The role of p-glycoprotein in the blood-brain barrier","volume":"19","author":"Ramakrishnan","year":"2003","journal-title":"Einstein Q. J. Biol. Med."},{"key":"10.1016\/j.bcp.2016.08.013_b0040","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1038\/nrd1668","article-title":"Drug resistance: passing on protection","volume":"4","author":"Owens","year":"2005","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.bcp.2016.08.013_b0045","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":"10.1016\/j.bcp.2016.08.013_b0050","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":"10.1016\/j.bcp.2016.08.013_b0055","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1111\/j.1365-2958.2007.05792.x","article-title":"Uptake or extrusion: crystal structures of full ABC transporters suggest a common mechanism","volume":"65","author":"Dawson","year":"2007","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.bcp.2016.08.013_b0060","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":"10.1016\/j.bcp.2016.08.013_b0065","doi-asserted-by":"crossref","first-page":"11025","DOI":"10.1073\/pnas.1400485111","article-title":"Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter","volume":"111","author":"Hohl","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.bcp.2016.08.013_b0070","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/1472-6807-9-3","article-title":"Molecular models of human P-glycoprotein in two different catalytic states","volume":"9","author":"Becker","year":"2009","journal-title":"BMC Struct. Biol."},{"key":"10.1016\/j.bcp.2016.08.013_b0075","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":"10.1016\/j.bcp.2016.08.013_b0080","doi-asserted-by":"crossref","first-page":"13603","DOI":"10.1074\/jbc.C300073200","article-title":"Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein. Direct evidence for the substrate-induced fit mechanism for drug binding","volume":"278","author":"Loo","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0085","doi-asserted-by":"crossref","first-page":"39489","DOI":"10.1074\/jbc.M111.284554","article-title":"Conformational analysis of human ATP-binding cassette transporter ABCB1 in lipid nanodiscs and inhibition by the antibodies MRK16 and UIC2","volume":"286","author":"Ritchie","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0090","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":"10.1016\/j.bcp.2016.08.013_b0095","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1146\/annurev.pa.17.040177.001053","article-title":"Specific pharmacology of calcium in myocardium, cardiac pacemakers, and vascular smooth muscle","volume":"17","author":"Fleckenstein","year":"1977","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.bcp.2016.08.013_b0100","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1161\/01.CIR.65.1.22","article-title":"The 24-hour ambulatory blood pressure profile with verapamil","volume":"65","author":"Gould","year":"1982","journal-title":"Circulation"},{"key":"10.1016\/j.bcp.2016.08.013_b0105","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1111\/j.1445-5994.1979.tb04115.x","article-title":"Verapamil in the management of hypertensive patients","volume":"9","author":"Lewis","year":"1979","journal-title":"Aust. N. Z. J. Med."},{"key":"10.1016\/j.bcp.2016.08.013_b0110","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1093\/cvr\/12.4.247","article-title":"Comparative cardiovascular actions of verapamil and its major metabolites in the anaesthetised dog","volume":"12","author":"Neugebauer","year":"1978","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.bcp.2016.08.013_b0115","doi-asserted-by":"crossref","first-page":"2495","DOI":"10.1016\/j.jacc.2013.02.058","article-title":"The P-glycoprotein transport system and cardiovascular drugs","volume":"61","author":"Wessler","year":"2013","journal-title":"J. Am. Coll. Cardiol."},{"key":"10.1016\/j.bcp.2016.08.013_b0120","doi-asserted-by":"crossref","first-page":"3394","DOI":"10.1021\/bi0619526","article-title":"P-Glycoprotein kinetics measured in plasma membrane vesicles and living cells","volume":"46","author":"Aanismaa","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2016.08.013_b0125","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/S0925-4439(97)00026-4","article-title":"Structure-activity relationships of P-glycoprotein interacting drugs: kinetic characterization of their effects on ATPase activity","volume":"1361","author":"Litman","year":"1997","journal-title":"Biochim. Biophys. Acta"},{"issue":"Pt 2","key":"10.1016\/j.bcp.2016.08.013_b0130","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1042\/bj3170515","article-title":"Effects of steroids and verapamil on P-glycoprotein ATPase activity: progesterone, desoxycorticosterone, corticosterone and verapamil are mutually non-exclusive modulators","volume":"317","author":"Orlowski","year":"1996","journal-title":"Biochem. J."},{"issue":"Pt 2","key":"10.1016\/j.bcp.2016.08.013_b0135","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":"10.1016\/j.bcp.2016.08.013_b0140","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0925-4439(97)00025-2","article-title":"ATPase activity of P-glycoprotein related to emergence of drug resistance in Ehrlich ascites tumor cell lines","volume":"1361","author":"Litman","year":"1997","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bcp.2016.08.013_b0145","doi-asserted-by":"crossref","first-page":"3163","DOI":"10.1074\/jbc.271.6.3163","article-title":"Competition of hydrophobic peptides, cytotoxic drugs, and chemosensitizers on a common P-glycoprotein pharmacophore as revealed by its ATPase activity","volume":"271","author":"Borgnia","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0150","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":"10.1016\/j.bcp.2016.08.013_b0155","doi-asserted-by":"crossref","DOI":"10.1042\/BSR20150317","article-title":"Unraveling the complex drug-drug interactions of the cardiovascular drugs, verapamil and digoxin, with P-glycoprotein","volume":"36","author":"Ledwitch","year":"2016","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.bcp.2016.08.013_b0160","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":"10.1016\/j.bcp.2016.08.013_b0165","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0003-2697(88)90002-4","article-title":"A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: application to lens ATPases","volume":"168","author":"Chifflet","year":"1988","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bcp.2016.08.013_b0170","series-title":"Enzyme Kinetics and Mechanism","author":"Cook","year":"2007"},{"key":"10.1016\/j.bcp.2016.08.013_b0175","series-title":"Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady State Enzyme Systems","author":"Segel","year":"1975"},{"key":"10.1016\/j.bcp.2016.08.013_b0180","doi-asserted-by":"crossref","first-page":"1238","DOI":"10.1021\/ed074p1238","article-title":"Disadvantages of double reciprocal plots","volume":"74","author":"Martin","year":"1997","journal-title":"J. Chem. Educ."},{"key":"10.1016\/j.bcp.2016.08.013_b0185","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1016\/0968-0004(90)90295-M","article-title":"Using linear and non-linear regression to fit biochemical data","volume":"15","author":"Leatherbarrow","year":"1990","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bcp.2016.08.013_b0190","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/S0307-4412(98)00301-X","article-title":"What students must know about the determination of enzyme kinetic parameters","volume":"27","author":"Ranaldi","year":"1999","journal-title":"Biochem. Educ."},{"key":"10.1016\/j.bcp.2016.08.013_b0195","doi-asserted-by":"crossref","first-page":"10804","DOI":"10.1021\/bi200924t","article-title":"The structural basis for homotropic and heterotropic cooperativity of midazolam metabolism by human cytochrome P450 3A4","volume":"50","author":"Roberts","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2016.08.013_b0200","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1529\/biophysj.104.058479","article-title":"Resolution of Two substrate-binding sites in an engineered cytochrome P450eryF bearing a fluorescent probe","volume":"89","author":"Davydov","year":"2005","journal-title":"Biophys. J."},{"key":"10.1016\/j.bcp.2016.08.013_b0205","doi-asserted-by":"crossref","first-page":"3067","DOI":"10.1093\/bioinformatics\/btl485","article-title":"COPASI\u2013a COmplex PAthway SImulator","volume":"22","author":"Hoops","year":"2006","journal-title":"Bioinformatics"},{"key":"10.1016\/j.bcp.2016.08.013_b0210","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1021\/ja044434w","article-title":"Direct observation of ligand binding to membrane proteins in living cells by a saturation transfer double difference (STDD) NMR spectroscopy method shows a significantly higher affinity of integrin alpha(IIb)beta3 in native platelets than in liposomes","volume":"127","author":"Claasen","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bcp.2016.08.013_b0215","series-title":"Membrane Protein Structure and Dynamics: Methods and Protocols","first-page":"47","article-title":"Use of NMR saturation transfer difference spectroscopy to study ligand binding to membrane proteins","author":"Venkitakrishnan","year":"2012"},{"key":"10.1016\/j.bcp.2016.08.013_b0220","doi-asserted-by":"crossref","first-page":"6108","DOI":"10.1021\/ja0100120","article-title":"Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor","volume":"123","author":"Mayer","year":"2001","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bcp.2016.08.013_b0225","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1016\/j.bbrc.2007.05.204","article-title":"Direct detection of ligand binding to Sepharose-immobilised protein using saturation transfer double difference (STDD) NMR spectroscopy","volume":"359","author":"Haselhorst","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bcp.2016.08.013_b0230","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1007\/BF02192855","article-title":"Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions","volume":"2","author":"Piotto","year":"1992","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.bcp.2016.08.013_b0235","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1002\/bdd.1877","article-title":"Pharmacokinetic variability of flecainide in younger Japanese patients and mechanisms for renal excretion and intestinal absorption","volume":"35","author":"Horie","year":"2014","journal-title":"Biopharm. Drug Dispos."},{"key":"10.1016\/j.bcp.2016.08.013_b0240","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1002\/jps.2600800618","article-title":"Nuclear magnetic resonance investigations of calcium antagonist drugs. II: conformational and dynamic features of verapamil in [2H6]DMSO","volume":"80","author":"Maccotta","year":"1991","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.bcp.2016.08.013_b0245","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1021\/jm00060a009","article-title":"Interaction of calcium channel antagonists with calcium: structural studies on verapamil and its Ca2+ complex","volume":"36","author":"Tetreault","year":"1993","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0250","doi-asserted-by":"crossref","first-page":"D402","DOI":"10.1093\/nar\/gkm957","article-title":"BioMagResBank","volume":"36","author":"Ulrich","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bcp.2016.08.013_b0255","doi-asserted-by":"crossref","first-page":"14927","DOI":"10.1021\/bi0018786","article-title":"Intrinsic fluorescence of the P-glycoprotein multidrug transporter: sensitivity of tryptophan residues to binding of drugs and nucleotides","volume":"39","author":"Liu","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2016.08.013_b0260","first-page":"109","article-title":"Fluorescence techniques for studying membrane transport proteins: the P-glycoprotein multidrug transporter","volume":"227","author":"Sharom","year":"2003","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.bcp.2016.08.013_b0265","series-title":"Principles of Fluorescence Spectroscopy","author":"Lakowicz","year":"1999"},{"key":"10.1016\/j.bcp.2016.08.013_b0270","series-title":"Principles of Fluorescence Spectroscopy","author":"Lakowicz","year":"1983"},{"key":"10.1016\/j.bcp.2016.08.013_b0275","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1023\/A:1011965707998","article-title":"Radioligand-binding assay employing P-glycoprotein-overexpressing cells: testing drug affinities to the secretory intestinal multidrug transporter","volume":"15","author":"Doppenschmitt","year":"1998","journal-title":"Pharm. Res."},{"key":"10.1016\/j.bcp.2016.08.013_b0280","doi-asserted-by":"crossref","first-page":"17649","DOI":"10.1074\/jbc.274.25.17649","article-title":"Ligand-mediated tertiary structure changes of reconstituted P-glycoprotein. A tryptophan fluorescence quenching analysis","volume":"274","author":"Sonveaux","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0285","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1042\/BJ20060015","article-title":"Conformational and functional characterization of trapped complexes of the P-glycoprotein multidrug transporter","volume":"399","author":"Russell","year":"2006","journal-title":"Biochem. J."},{"key":"10.1016\/j.bcp.2016.08.013_b0290","doi-asserted-by":"crossref","first-page":"16400","DOI":"10.1021\/bi980871+","article-title":"Contribution to substrate specificity and transport of nonconserved residues in transmembrane domain 12 of human P-glycoprotein","volume":"37","author":"Hafkemeyer","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2016.08.013_b0295","doi-asserted-by":"crossref","first-page":"8657","DOI":"10.1074\/jbc.M010044200","article-title":"Correlation between steady-state ATP hydrolysis and vanadate-induced ADP trapping in Human P-glycoprotein. Evidence for ADP release as the rate-limiting step in the catalytic cycle and its modulation by substrates","volume":"276","author":"Kerr","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0300","doi-asserted-by":"crossref","first-page":"20986","DOI":"10.1074\/jbc.272.34.20986","article-title":"Drug-stimulated ATPase activity of human P-glycoprotein requires movement between transmembrane segments 6 and 12","volume":"272","author":"Loo","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0305","doi-asserted-by":"crossref","first-page":"3745","DOI":"10.1016\/S0021-9258(17)41923-5","article-title":"ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells","volume":"269","author":"Shapiro","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0310","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/S0006-2952(99)00139-2","article-title":"Interaction of the P-glycoprotein multidrug transporter (MDR1) with high affinity peptide chemosensitizers in isolated membranes, reconstituted systems, and intact cells","volume":"58","author":"Sharom","year":"1999","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.bcp.2016.08.013_b0315","doi-asserted-by":"crossref","first-page":"30046","DOI":"10.1074\/jbc.M001010200","article-title":"A novel method for measurement of submembrane ATP concentration","volume":"275","author":"Gribble","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0320","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/S0005-2736(03)00210-4","article-title":"Extracellular ATP as a signaling molecule for epithelial cells","volume":"1615","author":"Schwiebert","year":"2003","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bcp.2016.08.013_b0325","doi-asserted-by":"crossref","first-page":"13281","DOI":"10.1074\/jbc.274.19.13281","article-title":"Glucose generates sub-plasma membrane ATP microdomains in single islet beta-cells. Potential role for strategically located mitochondria","volume":"274","author":"Kennedy","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0330","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/S1046-2023(02)00037-3","article-title":"Measurements of ATP in mammalian cells","volume":"26","author":"Manfredi","year":"2002","journal-title":"Methods"},{"key":"10.1016\/j.bcp.2016.08.013_b0335","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1023\/A:1022069718709","article-title":"What determines the intracellular ATP concentration","volume":"22","author":"Ataullakhanov","year":"2002","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.bcp.2016.08.013_b0340","doi-asserted-by":"crossref","first-page":"1716","DOI":"10.1378\/chest.102.6.1716","article-title":"Skeletal muscle metabolism in the chronic fatigue syndrome. In vivo assessment by 31P nuclear magnetic resonance spectroscopy","volume":"102","author":"Wong","year":"1992","journal-title":"Chest"},{"key":"10.1016\/j.bcp.2016.08.013_b0345","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1158\/0008-5472.CAN-11-1674","article-title":"Intracellular ATP levels are a pivotal determinant of chemoresistance in colon cancer cells","volume":"72","author":"Zhou","year":"2012","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2016.08.013_b0350","doi-asserted-by":"crossref","first-page":"3628","DOI":"10.1091\/mbc.E02-12-0796","article-title":"New insights into the bioenergetics of mitochondrial disorders using intracellular ATP reporters","volume":"14","author":"Gajewski","year":"2003","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bcp.2016.08.013_b0355","doi-asserted-by":"crossref","first-page":"1372","DOI":"10.1038\/cr.2010.123","article-title":"Physiological levels of ATP negatively regulate proteasome function","volume":"20","author":"Huang","year":"2010","journal-title":"Cell Res."},{"key":"10.1016\/j.bcp.2016.08.013_b0360","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1084\/jem.185.8.1481","article-title":"Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis","volume":"185","author":"Leist","year":"1997","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.bcp.2016.08.013_b0365","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1146\/annurev.ph.48.030186.000301","article-title":"ATP and the regulation of renal cell function","volume":"48","author":"Soltoff","year":"1986","journal-title":"Annu. Rev. Physiol."},{"key":"10.1016\/j.bcp.2016.08.013_b0370","doi-asserted-by":"crossref","first-page":"3020","DOI":"10.1021\/bi051380+","article-title":"Quantification and characterization of P-glycoprotein-substrate interactions","volume":"45","author":"Gatlik-Landwojtowicz","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2016.08.013_b0375","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":"10.1016\/j.bcp.2016.08.013_b0380","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/S0925-4439(97)00027-6","article-title":"Competitive, non-competitive and cooperative interactions between substrates of P-glycoprotein as measured by its ATPase activity","volume":"1361","author":"Litman","year":"1997","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bcp.2016.08.013_b0385","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1006\/abbi.1995.1020","article-title":"Effects of lipids on ATPase activity of purified Chinese hamster P-glycoprotein","volume":"316","author":"Urbatsch","year":"1995","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bcp.2016.08.013_b0390","doi-asserted-by":"crossref","first-page":"1170","DOI":"10.1021\/bi026555j","article-title":"Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle","volume":"42","author":"Qu","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2016.08.013_b0395","doi-asserted-by":"crossref","first-page":"8294","DOI":"10.1074\/jbc.M211758200","article-title":"Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding","volume":"278","author":"Rosenberg","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0400","doi-asserted-by":"crossref","first-page":"7575","DOI":"10.1074\/jbc.M109.047290","article-title":"Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: implications for catalysis","volume":"285","author":"Siarheyeva","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0405","doi-asserted-by":"crossref","first-page":"7069","DOI":"10.1021\/bi00189a008","article-title":"Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein","volume":"33","author":"Urbatsch","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2016.08.013_b0410","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1016\/j.febslet.2007.01.073","article-title":"Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP","volume":"581","author":"Dawson","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bcp.2016.08.013_b0415","doi-asserted-by":"crossref","first-page":"16039","DOI":"10.1021\/bi00049a018","article-title":"Adenosine 5\u2019-(gamma-thiotriphosphate): an ATP analog that should be used with caution in muscle contraction studies","volume":"34","author":"Resetar","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2016.08.013_b0420","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/S0005-2736(99)00166-2","article-title":"Insights into the structure and substrate interactions of the P-glycoprotein multidrug transporter from spectroscopic studies","volume":"1461","author":"Sharom","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bcp.2016.08.013_b0425","doi-asserted-by":"crossref","first-page":"39706","DOI":"10.1074\/jbc.M308559200","article-title":"Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoprotein","volume":"278","author":"Loo","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0430","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1046\/j.1432-1327.1998.2550383.x","article-title":"Dissection of drug-binding-induced conformational changes in P-glycoprotein","volume":"255","author":"Wang","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bcp.2016.08.013_b0435","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1046\/j.1432-1327.2001.02122.x","article-title":"P-Glycoprotein conformational changes detected by antibody competition","volume":"268","author":"Nagy","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bcp.2016.08.013_b0440","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":"10.1016\/j.bcp.2016.08.013_b0445","doi-asserted-by":"crossref","DOI":"10.1124\/mol.116.104190","article-title":"Cryo-EM analysis of the conformational landscape of human P-glycoprotein (ABCB1) during its catalytic cycle","author":"Frank","year":"2016","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.bcp.2016.08.013_b0450","doi-asserted-by":"crossref","first-page":"13887","DOI":"10.1021\/bi991115m","article-title":"Both ATP sites of human P-glycoprotein are essential but not symmetric","volume":"38","author":"Hrycyna","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2016.08.013_b0455","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/j.bbamem.2007.10.021","article-title":"Structure-based interpretation of the mutagenesis database for the nucleotide binding domains of P-glycoprotein","volume":"1778","author":"Lawson","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bcp.2016.08.013_b0460","doi-asserted-by":"crossref","first-page":"26806","DOI":"10.1074\/jbc.M112.376202","article-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","volume":"287","author":"Loo","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0465","doi-asserted-by":"crossref","first-page":"26956","DOI":"10.1074\/jbc.270.45.26956","article-title":"Both P-glycoprotein nucleotide-binding sites are catalytically active","volume":"270","author":"Urbatsch","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0470","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1006\/bbrc.1995.2665","article-title":"Drug-stimulated ATPase activity of a deletion mutant of the human multidrug-resistance protein (MDR1)","volume":"216","author":"Welker","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bcp.2016.08.013_b0475","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":"10.1016\/j.bcp.2016.08.013_b0480","doi-asserted-by":"crossref","first-page":"27482","DOI":"10.1074\/jbc.271.44.27482","article-title":"Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates","volume":"271","author":"Loo","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0485","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1091\/mbc.7.10.1485","article-title":"Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a vaccinia-based transient expression system","volume":"7","author":"Ramachandra","year":"1996","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bcp.2016.08.013_b0490","doi-asserted-by":"crossref","first-page":"3917","DOI":"10.1021\/bi035365l","article-title":"Improved energy coupling of human P-glycoprotein by the glycine 185 to valine mutation","volume":"43","author":"Omote","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2016.08.013_b0495","doi-asserted-by":"crossref","first-page":"6686","DOI":"10.1016\/S0021-9258(18)82708-9","article-title":"Mutation of glycine 185 to valine alters the ATPase function of the human P-glycoprotein expressed in Sf9 cells","volume":"270","author":"Rao","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0500","doi-asserted-by":"crossref","first-page":"45688","DOI":"10.1074\/jbc.M206479200","article-title":"A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein","volume":"277","author":"Omote","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0505","doi-asserted-by":"crossref","first-page":"1716","DOI":"10.1021\/jm021012t","article-title":"Comparison of in vitro P-glycoprotein screening assays: recommendations for their use in drug discovery","volume":"46","author":"Schwab","year":"2003","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bcp.2016.08.013_b0510","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/S0378-5173(03)00372-7","article-title":"Caco-2 permeability, P-glycoprotein transport ratios and brain penetration of heterocyclic drugs","volume":"263","author":"Faassen","year":"2003","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.bcp.2016.08.013_b0515","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/S0022-3565(24)39245-6","article-title":"Characterization of the major metabolites of verapamil as substrates and inhibitors of P-glycoprotein","volume":"293","author":"Pauli-Magnus","year":"2000","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"10.1016\/j.bcp.2016.08.013_b0520","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1080\/00498250802050880","article-title":"Validation and application of Caco-2 assays for the in vitro evaluation of development candidate drugs as substrates or inhibitors of P-glycoprotein to support regulatory submissions","volume":"38","author":"Elsby","year":"2008","journal-title":"Xenobiotica"}],"container-title":["Biochemical Pharmacology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006295216302313?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006295216302313?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,6,4]],"date-time":"2025-06-04T14:07:40Z","timestamp":1749046060000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006295216302313"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,10]]},"references-count":104,"alternative-id":["S0006295216302313"],"URL":"https:\/\/doi.org\/10.1016\/j.bcp.2016.08.013","relation":{},"ISSN":["0006-2952"],"issn-type":[{"value":"0006-2952","type":"print"}],"subject":[],"published":{"date-parts":[[2016,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Cooperativity between verapamil and ATP bound to the efflux transporter P-glycoprotein","name":"articletitle","label":"Article Title"},{"value":"Biochemical Pharmacology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bcp.2016.08.013","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}