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Volumn 8, Issue 12, 2013, Pages

Multiple transport-active binding sites are available for a single substrate on human P-glycoprotein (ABCB1)

Author keywords

[No Author keywords available]

Indexed keywords

5' FLUOROSULFONYLBENZOYL 5' ADENOSINE; ADENOSINE DERIVATIVE; ADENOSINE TRIPHOSPHATE; CYCLOSPORIN A; CYSTEINE; GLUTAMINE; MEMBRANE PROTEIN; MULTIDRUG RESISTANCE PROTEIN 1; MUTANT PROTEIN; PACLITAXEL; PHENYLALANINE; SULFUR DERIVATIVE; TARIQUIDAR; TYROSINE; UNCLASSIFIED DRUG; VALINE; VALINOMYCIN;

EID: 84891912095     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0082463     Document Type: Article
Times cited : (88)

References (57)
  • 2
    • 33644840984 scopus 로고    scopus 로고
    • The power of the pump: Mechanisms of action of P-glycoprotein (ABCB1)
    • DOI 10.1016/j.ejps.2005.10.010, PII S0928098705003313, Drug Transporters: Integration in Understanding ADME
    • Ambudkar SV, Kim IW, Sauna ZE (2006) The power of the pump: Mechanisms of action of P-glycoprotein (ABCB1). Eur J Pharm Sci 27: 392-400. doi:10.1016/j.ejps.2005.10.010. PubMed: 16352426. (Pubitemid 43363335)
    • (2006) European Journal of Pharmaceutical Sciences , vol.27 , Issue.5 , pp. 392-400
    • Ambudkar, S.V.1    Kim, I.-W.2    Sauna, Z.E.3
  • 4
    • 78649834084 scopus 로고    scopus 로고
    • Exploring the P-glycoprotein binding cavity with polyoxyethylene alkyl ethers
    • doi: 10.1016/j.bpj.2010.10.033. PubMed: 21112283
    • Blatter XL, Seelig A (2010) Exploring the P-glycoprotein binding cavity with polyoxyethylene alkyl ethers. Biophys J 99: 3589-3598. doi: 10.1016/j.bpj.2010.10.033. PubMed: 21112283.
    • (2010) Biophys J , vol.99 , pp. 3589-3598
    • Blatter, X.L.1    Seelig, A.2
  • 5
    • 73649111071 scopus 로고    scopus 로고
    • Understanding polyspecificity of multidrug ABC transporters: Closing in on the gaps in ABCB1
    • doi:10.1016/ j.tibs.2009.07.009. PubMed: 19819701
    • Gutmann DAP, Ward A, Urbatsch IL, Chang G, van Veen HW (2010) Understanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1. Trends Biochem Sci 35: 36-42. doi:10.1016/ j.tibs.2009.07.009. PubMed: 19819701.
    • (2010) Trends Biochem Sci , vol.35 , pp. 36-42
    • Dap, G.1    Ward, A.2    Urbatsch, I.L.3    Chang, G.4    Van Veen, H.W.5
  • 6
    • 84856271899 scopus 로고    scopus 로고
    • The P-glycoprotein multidrug transporter
    • doi:10.1042/bse0500161. PubMed: 21967057
    • Sharom FJ (2011) The P-glycoprotein multidrug transporter. Essays Biochem 50: 161-178. doi:10.1042/bse0500161. PubMed: 21967057.
    • (2011) Essays Biochem , vol.50 , pp. 161-178
    • Sharom, F.J.1
  • 7
    • 64649090980 scopus 로고    scopus 로고
    • Molecular basis of multidrug transport by ABC transporters
    • doi:10.1016/j.bbapap.2008.12.004. PubMed: 19135557
    • Seeger MA, van Veen HW (2009) Molecular basis of multidrug transport by ABC transporters. Biochim Biophys Acta 1794: 725-737. doi:10.1016/j.bbapap.2008. 12.004. PubMed: 19135557.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 725-737
    • Seeger, M.A.1    Van Veen, H.W.2
  • 8
    • 0030924052 scopus 로고    scopus 로고
    • Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein
    • doi: 10.1073/pnas.94.20.10594. PubMed: 9380680
    • Dey S, Ramachandra M, Pastan I, Gottesman MM, Ambudkar SV (1997) Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein. Proc Natl Acad Sci U S A 94: 10594-10599. doi: 10.1073/pnas.94.20.10594. PubMed: 9380680.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10594-10599
    • Dey, S.1    Ramachandra, M.2    Pastan, I.3    Gottesman, M.M.4    Ambudkar, S.V.5
  • 9
    • 0141994817 scopus 로고    scopus 로고
    • Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoprotein
    • DOI 10.1074/jbc.M308559200
    • Loo TW, Bartlett MC, Clarke DM (2003) Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoprotein. J Biol Chem 278: 39706-39710. doi:10.1074/ jbc.M308559200. PubMed: 12909621. (Pubitemid 37248532)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.41 , pp. 39706-39710
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 10
    • 0035813143 scopus 로고    scopus 로고
    • Determining the dimensions of the drugbinding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers
    • doi: 10.1074/jbc.C100467200. PubMed: 11518701
    • Loo TW, Clarke DM (2001) Determining the dimensions of the drugbinding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers. J Biol Chem 276: 36877-36880. doi: 10.1074/jbc.C100467200. PubMed: 11518701.
    • (2001) J Biol Chem , vol.276 , pp. 36877-36880
    • Loo, T.W.1    Clarke, D.M.2
  • 11
    • 0035805573 scopus 로고    scopus 로고
    • Defining the drug-binding site in the human multidrug resistance P-glycoprotein using a methanethiosulfonate analog of verapamil, MTS-verapamil
    • doi:10.1074/jbc.M100407200. PubMed: 11279063
    • Loo TW, Clarke DM (2001) Defining the drug-binding site in the human multidrug resistance P-glycoprotein using a methanethiosulfonate analog of verapamil, MTS-verapamil. J Biol Chem 276: 14972-14979. doi:10.1074/jbc. M100407200. PubMed: 11279063.
    • (2001) J Biol Chem , vol.276 , pp. 14972-14979
    • Loo, T.W.1    Clarke, D.M.2
  • 12
    • 27144451192 scopus 로고    scopus 로고
    • Interaction of LDS-751 and rhodamine 123 with P-glycoprotein: Evidence for simultaneous binding of both drugs
    • DOI 10.1021/bi0511179
    • Lugo MR, Sharom FJ (2005) Interaction of LDS-751 and rhodamine 123 with P-glycoprotein: Evidence for simultaneous binding of both drugs. Biochemistry 44: 14020-14029. doi:10.1021/bi0511179. PubMed: 16229491. (Pubitemid 41507482)
    • (2005) Biochemistry , vol.44 , Issue.42 , pp. 14020-14029
    • Lugo, M.R.1    Sharom, F.J.2
  • 13
    • 0030782511 scopus 로고    scopus 로고
    • Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities
    • Shapiro AB, Ling V (1997) Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities. Eur J Biochem 250: 130-137. doi:10.1111/j.1432-1033.1997.00130.x. PubMed: 9432000. (Pubitemid 27504592)
    • (1997) European Journal of Biochemistry , vol.250 , Issue.1 , pp. 130-137
    • Shapiro, A.B.1    Ling, V.2
  • 14
    • 0033083015 scopus 로고    scopus 로고
    • Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone: Evidence for a third drug-binding site
    • DOI 10.1046/j.1432-1327.1999.00098.x
    • Shapiro AB, Fox K, Lam P, Ling V (1999) Stimulation of P-glycoproteinmediated drug transport by prazosin and progesterone. Evidence for a third drug-binding site. Eur J Biochem 259: 841-850. PubMed: 10092872. (Pubitemid 29075514)
    • (1999) European Journal of Biochemistry , vol.259 , Issue.3 , pp. 841-850
    • Shapiro, A.B.1    Fox, K.2    Lam, P.3    Ling, V.4
  • 15
    • 0033862765 scopus 로고    scopus 로고
    • Communication between multiple drug binding sites on P-glycoprotein
    • PubMed: 10953057
    • Martin C, Berridge G, Higgins CF, Mistry P, Charlton P et al. (2000) Communication between multiple drug binding sites on P-glycoprotein. Mol Pharmacol 58: 624-632. PubMed: 10953057.
    • (2000) Mol Pharmacol , vol.58 , pp. 624-632
    • Martin, C.1    Berridge, G.2    Higgins, C.F.3    Mistry, P.4    Charlton, P.5
  • 16
    • 0347125101 scopus 로고    scopus 로고
    • Identification and characterization of the binding sites of P-glycoprotein for multidrug resistance-related drugs and modulators
    • Safa AR (2004) Identification and characterization of the binding sites of P-glycoprotein for multidrug resistance-related drugs and modulators. Curr Med Chem Anticancer Agents 4: 1-17. doi: 10.2174/1568011043482142. PubMed: 14754408. (Pubitemid 38081746)
    • (2004) Current Medicinal Chemistry - Anti-Cancer Agents , vol.4 , Issue.1 , pp. 1-17
    • Safa, A.R.1
  • 17
    • 63449139456 scopus 로고    scopus 로고
    • Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding
    • doi:10.1126/science.1168750. PubMed: 19325113
    • Aller SG, Yu J, Ward A, Weng Y, Chittaboina S et al. (2009) Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding. Science 323: 1718-1722. doi:10.1126/science.1168750. PubMed: 19325113.
    • (2009) Science , vol.323 , pp. 1718-1722
    • Aller, S.G.1    Yu, J.2    Ward, A.3    Weng, Y.4    Chittaboina, S.5
  • 18
    • 84879000440 scopus 로고    scopus 로고
    • Mass spectrometry reveals synergistic effects of nucleotides, lipids, and drugs binding to a multidrug resistance efflux pump
    • doi:10.1073/pnas.1303888110. PubMed: 23690617
    • Marcoux J, Wang SC, Politis A, Reading E, Ma J et al. (2013) Mass spectrometry reveals synergistic effects of nucleotides, lipids, and drugs binding to a multidrug resistance efflux pump. Proc Natl Acad Sci U S A 110: 9704-9709. doi:10.1073/pnas.1303888110. PubMed: 23690617.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 9704-9709
    • Marcoux, J.1    Wang, S.C.2    Politis, A.3    Reading, E.4    Ma, J.5
  • 19
    • 79953725116 scopus 로고    scopus 로고
    • Design and synthesis of selenazole-containing peptides for cocrystallization with P-glycoprotein
    • doi:10.1002/cbic. 201100048. PubMed: 21387512
    • Tao HC, Weng Y, Zhuo RP, Chang G, Urbatsch IL et al. (2011) Design and synthesis of selenazole-containing peptides for cocrystallization with P-glycoprotein. Chembiochem 12: 868-873. doi:10.1002/cbic. 201100048. PubMed: 21387512.
    • (2011) Chembiochem , vol.12 , pp. 868-873
    • Tao, H.C.1    Weng, Y.2    Zhuo, R.P.3    Chang, G.4    Urbatsch, I.L.5
  • 20
    • 0032881342 scopus 로고    scopus 로고
    • The molecular interaction of the high affinity reversal agent XR9576 with P-glycoprotein
    • DOI 10.1038/sj.bjp.0702807
    • Martin C, Berridge G, Mistry P, Higgins C, Charlton P et al. (1999) The molecular interaction of the high affinity reversal agent XR9576 with Pglycoprotein. Br J Pharmacol 128: 403-411. doi:10.1038/sj.bjp. 0702807. PubMed: 10510451. (Pubitemid 29458600)
    • (1999) British Journal of Pharmacology , vol.128 , Issue.2 , pp. 403-411
    • Martin, C.1    Berridge, G.2    Mistry, P.3    Higgins, C.4    Charlton, P.5    Callaghan, R.6
  • 21
    • 79955629985 scopus 로고    scopus 로고
    • 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 nucleotidebinding sites
    • doi:10.1021/bi200073f. PubMed: 21452853
    • Ohnuma S, Chufan E, Nandigama K, Jenkins LMM, Durell SR et al. (2011) 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 nucleotidebinding sites. Biochemistry 50: 3724-3735. doi:10.1021/bi200073f. PubMed: 21452853.
    • (2011) Biochemistry , vol.50 , pp. 3724-3735
    • Ohnuma, S.1    Chufan, E.2    Nandigama, K.3    Lmm, J.4    Durell, S.R.5
  • 22
    • 0028928984 scopus 로고
    • Membrane topology of a cysteine-less mutant of human P-glycoprotein
    • doi: 10.1074/jbc.270.2.843. PubMed: 7822320
    • Loo TW, Clarke DM (1995) Membrane topology of a cysteine-less mutant of human P-glycoprotein. J Biol Chem 270: 843-848. doi: 10.1074/jbc.270.2.843. PubMed: 7822320.
    • (1995) J Biol Chem , vol.270 , pp. 843-848
    • Loo, T.W.1    Clarke, D.M.2
  • 23
    • 0025216388 scopus 로고
    • Photoaffinity probes for the alpha 1-adrenergic receptor and the calcium channel bind to a common domain in P-glycoprotein
    • PubMed: 1968459
    • Greenberger LM, Yang CP, Gindin E, Horwitz SB (1990) Photoaffinity probes for the alpha 1-adrenergic receptor and the calcium channel bind to a common domain in P-glycoprotein. J Biol Chem 265: 4394-4401. PubMed: 1968459.
    • (1990) J Biol Chem , vol.265 , pp. 4394-4401
    • Greenberger, L.M.1    Yang, C.P.2    Gindin, E.3    Horwitz, S.B.4
  • 24
    • 47049101437 scopus 로고    scopus 로고
    • Mutational analysis of ABC proteins
    • doi:10.1016/j.abb.2008.02.025. PubMed: 18328253
    • Loo TW, Clarke DM (2008) Mutational analysis of ABC proteins. Arch Biochem Biophys 476: 51-64. doi:10.1016/j.abb.2008.02.025. PubMed: 18328253.
    • (2008) Arch Biochem Biophys , vol.476 , pp. 51-64
    • Loo, T.W.1    Clarke, D.M.2
  • 25
    • 0037113961 scopus 로고    scopus 로고
    • Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein
    • DOI 10.1074/jbc.M208433200
    • Loo TW, Clarke DM (2002) Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein. J Biol Chem 277: 44332-44338. doi:10.1074/jbc.M208433200. PubMed: 12223492. (Pubitemid 36157868)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 44332-44338
    • Loo, T.W.1    Clarke, D.M.2
  • 27
    • 84864535297 scopus 로고    scopus 로고
    • 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
    • doi:10.1074/ jbc.M112.376202. PubMed: 22700974
    • Loo TW, Bartlett MC, Detty MR, Clarke DM (2012) 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. J Biol Chem 287: 26806-26816. doi:10.1074/ jbc.M112.376202. PubMed: 22700974.
    • (2012) J Biol Chem , vol.287 , pp. 26806-26816
    • Loo, T.W.1    Bartlett, M.C.2    Detty, M.R.3    Clarke, D.M.4
  • 28
    • 0035937707 scopus 로고    scopus 로고
    • Correlation between steadystate ATP hydrolysis and vanadate-induced ADP trapping in human Pglycoprotein - Evidence for ADP release as the rate-limiting step in the catalytic cycle and its modulation by substrates
    • doi:10.1074/jbc.M010044200. PubMed: 11121420
    • Kerr KM, Sauna ZE, Ambudkar SV (2001) Correlation between steadystate ATP hydrolysis and vanadate-induced ADP trapping in human Pglycoprotein - Evidence for ADP release as the rate-limiting step in the catalytic cycle and its modulation by substrates. J Biol Chem 276: 8657-8664. doi:10.1074/jbc. M010044200. PubMed: 11121420.
    • (2001) J Biol Chem , vol.276 , pp. 8657-8664
    • Kerr, K.M.1    Sauna, Z.E.2    Ambudkar, S.V.3
  • 29
    • 79951838702 scopus 로고    scopus 로고
    • The "Specific" P-glycoprotein inhibitor tariquidar is also a substrate and an inhibitor for breast cancer resistance protein (BCRP/ABCG2)
    • doi:10.1021/cn100078a. PubMed: 22778859
    • Kannan P, Telu S, Shukla S, Ambudkar SV, Pike VW et al. (2011) The "Specific" P-glycoprotein inhibitor tariquidar is also a substrate and an inhibitor for breast cancer resistance protein (BCRP/ABCG2). ACS Chem Neurosci 2: 82-89. doi:10.1021/cn100078a. PubMed: 22778859.
    • (2011) ACS Chem Neurosci , vol.2 , pp. 82-89
    • Kannan, P.1    Telu, S.2    Shukla, S.3    Ambudkar, S.V.4    Pike, V.W.5
  • 30
    • 84855998504 scopus 로고    scopus 로고
    • Use of Baculovirus BacMam vectors for expression of ABC drug transporters in mammalian cells
    • doi: 10.1124/dmd.111.042721. PubMed: 22041108
    • Shukla S, Schwartz C, Kapoor K, Kouanda A, Ambudkar SV (2012) Use of Baculovirus BacMam vectors for expression of ABC drug transporters in mammalian cells. Drug Metab Dispos 40: 304-312. doi: 10.1124/dmd.111.042721. PubMed: 22041108.
    • (2012) Drug Metab Dispos , vol.40 , pp. 304-312
    • Shukla, S.1    Schwartz, C.2    Kapoor, K.3    Kouanda, A.4    Ambudkar, S.V.5
  • 31
    • 84867883248 scopus 로고    scopus 로고
    • Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans
    • doi:10.1038/nature11448. PubMed: 23000902
    • Jin MS, Oldham ML, Zhang QJ, Chen J (2012) Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans. Nature 490: 566-570. doi:10.1038/nature11448. PubMed: 23000902.
    • (2012) Nature , vol.490 , pp. 566-570
    • Jin, M.S.1    Oldham, M.L.2    Zhang, Q.J.3    Chen, J.4
  • 32
    • 84882338908 scopus 로고    scopus 로고
    • Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain
    • doi:10.1073/pnas.1309275110. PubMed: 23901103
    • Ward AB, Szewczyk P, Grimard V, Lee CW, Martinez L et al. (2013) Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain. Proc Natl Acad Sci U S A 110: 13386-13391. doi:10.1073/pnas.1309275110. PubMed: 23901103.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 13386-13391
    • Ward, A.B.1    Szewczyk, P.2    Grimard, V.3    Lee, C.W.4    Martinez, L.5
  • 33
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • PubMed: 19499576
    • Trott O, Olson AJ (2010) AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 31: 455-461. PubMed: 19499576.
    • (2010) J Comput Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 34
    • 0037687304 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein: Direct evidence for the substrate-induced fit mechanism for drug binding
    • DOI 10.1074/jbc.C300073200
    • Loo TW, Bartlett MC, Clarke DM (2003) Substrate-induced conformational, changes in the transmembrane segments of human Pglycoprotein - Direct evidence for the substrate-induced fit mechanism for drug binding. J Biol Chem 278: 13603-13606. doi:10.1074/ jbc.C300073200. PubMed: 12609990. (Pubitemid 36799891)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 13603-13606
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 35
    • 79959833862 scopus 로고    scopus 로고
    • Predicting Binding to P-glycoprotein by flexible receptor docking
    • PubMed: 21731480
    • Dolghih E, Bryant C, Renslo AR, Jacobson MP (2011) Predicting Binding to P-glycoprotein by flexible receptor docking. PLoS Comput Biol 7 (6): e1002083. PubMed: 21731480.
    • (2011) PLoS Comput Biol , vol.7 , Issue.6
    • Dolghih, E.1    Bryant, C.2    Renslo, A.R.3    Jacobson, M.P.4
  • 36
    • 79958172123 scopus 로고    scopus 로고
    • Exhaustive sampling of docking poses reveals binding hypotheses for propafenone type inhibitors of Pglycoprotein
    • PubMed: 21589945
    • Klepsch F, Chiba P, Ecker GF (2011) Exhaustive sampling of docking poses reveals binding hypotheses for propafenone type inhibitors of Pglycoprotein. PLoS Comput Biol 7 (5): e1002036. PubMed: 21589945.
    • (2011) PLoS Comput Biol , vol.7 , Issue.5
    • Klepsch, F.1    Chiba, P.2    Ecker, G.F.3
  • 37
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • doi:10.1073/pnas.0709388104. PubMed: 18024585
    • Ward A, Reyes CL, Yu J, Roth CB, Chang G (2007) Flexibility in the ABC transporter MsbA: Alternating access with a twist. Proc Natl Acad Sci U S A 104: 19005-19010. doi:10.1073/pnas.0709388104. PubMed: 18024585.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 38
    • 69949167524 scopus 로고    scopus 로고
    • Identification of residues in the drug translocation pathway of the human multidrug resistance Pglycoprotein by Arginine mutagenesis
    • doi:10.1074/jbc.M109.023267. PubMed: 19581304
    • Loo TW, Bartlett MC, Clarke DM (2009) Identification of residues in the drug translocation pathway of the human multidrug resistance Pglycoprotein by Arginine mutagenesis. J Biol Chem 284: 24074-24087. doi:10.1074/jbc.M109.023267. PubMed: 19581304.
    • (2009) J Biol Chem , vol.284 , pp. 24074-24087
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 39
    • 33749985062 scopus 로고    scopus 로고
    • Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket
    • DOI 10.1042/BJ20060715
    • Loo TW, Bartlett MC, Clarke DM (2006) Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket. Biochem J 399: 351-359. doi:10.1042/BJ20060715. PubMed: 16813563. (Pubitemid 44570297)
    • (2006) Biochemical Journal , vol.399 , Issue.2 , pp. 351-359
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 40
    • 0031434236 scopus 로고    scopus 로고
    • Identification of residues in the drug-binding site of human P- glycoprotein using a thiol-reactive substrate
    • DOI 10.1074/jbc.272.51.31945
    • Loo TW, Clarke DM (1997) Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate. J Biol Chem 272: 31945-31948. doi:10.1074/jbc.272.51.31945. PubMed: 9405384. (Pubitemid 28011858)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.51 , pp. 31945-31948
    • Loo, T.W.1    Clarke, D.M.2
  • 41
    • 0347379911 scopus 로고    scopus 로고
    • Methanethiosulfonate Derivatives of Rhodamine and Verapamil Activate Human P-glycoprotein at Different Sites
    • DOI 10.1074/jbc.M310448200
    • Loo TW, Bartlett MC, Clarke DM (2003) Methanethiosulfonate derivatives of rhodamine and verapamil activate human P-glycoprotein at different sites. J Biol Chem 278: 50136-50141. doi:10.1074/ jbc.M310448200. PubMed: 14522974. (Pubitemid 37548851)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50136-50141
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 42
    • 0038419822 scopus 로고    scopus 로고
    • Permanent activation of the human P-glycoprotein by covalent modification of a residue in the drug-binding site
    • DOI 10.1074/jbc.C300154200
    • Loo TW, Bartlett MC, Clarke DM (2003) Permanent activation of the human P-glycoprotein by covalent modification of a residue in the drugbinding site. J Biol Chem 278: 20449-20452. doi:10.1074/ jbc.C300154200. PubMed: 12711602. (Pubitemid 36806339)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.23 , pp. 20449-20452
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 43
    • 84856305229 scopus 로고    scopus 로고
    • Catalytic and transport cycles of ABC exporters
    • doi:10.1042/bse0500063. PubMed: 21967052
    • Al-Shawi MK (2011) Catalytic and transport cycles of ABC exporters. Essays Biochem 50: 63-83. doi:10.1042/bse0500063. PubMed: 21967052.
    • (2011) Essays Biochem , vol.50 , pp. 63-83
    • Al-Shawi, M.K.1
  • 44
    • 84869211870 scopus 로고    scopus 로고
    • A measure of the broad substrate specificity of enzymes based on 'Duplicate' catalytic residues
    • doi:10.1371/journal.pone.0049313. PubMed: 23166637
    • Chakraborty S, Ásgeirsson B, Rao BJ (2012) A measure of the broad substrate specificity of enzymes based on 'Duplicate' catalytic residues. PLOS ONE 7 (11): e49313. doi:10.1371/journal.pone.0049313. PubMed: 23166637.
    • (2012) PLOS ONE , vol.7 , Issue.11
    • Chakraborty, S.1    Ásgeirsson, B.2    Rao, B.J.3
  • 45
    • 0345139075 scopus 로고
    • Functional role for the 170- to 180-kDa glycoprotein specific to drug-resistant tumor cells as revealed by monoclonal antibodies
    • DOI 10.1073/pnas.83.20.7785
    • Hamada H, Tsuruo T (1986) Functional role for the 170- to 180-kDa glycoprotein specific to drug-resistant tumor cells as revealed by monoclonal antibodies. Proc Natl Acad Sci U S A 83: 7785-7789. doi: 10.1073/pnas.83.20. 7785. PubMed: 2429319. (Pubitemid 17183929)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.20 , pp. 7785-7789
    • Hamada, H.1    Tsuruo, T.2
  • 46
    • 0029797074 scopus 로고    scopus 로고
    • Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a vaccinia-based transient expression system
    • Ramachandra M, Ambudkar SV, Gottesman MM, Pastan I, Hrycyna CA (1996) Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a vaccinia-based transient expression system. Mol Biol Cell 7: 1485-1498. doi:10.1091/ mbc.7.10.1485. PubMed: 8898356. (Pubitemid 26339723)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.10 , pp. 1485-1498
    • Ramachandra, M.1    Ambudkar, S.V.2    Gottesman, M.M.3    Pastan, I.4    Hrycyna, C.A.5
  • 47
    • 0034142125 scopus 로고    scopus 로고
    • Functional characterization of glycosylation-deficient human P- glycoprotein using a vaccinia virus expression system
    • DOI 10.1007/s002320001020
    • Gribar JJ, Ramachandra M, Hrycyna CA, Dey S, Ambudkar SV (2000) Functional characterization of glycosylation-deficient human Pglycoprotein using a vaccinia virus expression system. J Membr Biol 173: 203-214. doi:10.1007/s002320001020. PubMed: 10667916. (Pubitemid 30100212)
    • (2000) Journal of Membrane Biology , vol.173 , Issue.3 , pp. 203-214
    • Gribar, J.J.1    Ramachandra, M.2    Hrycyna, C.A.3    Dey, S.4    Ambudkar, S.V.5
  • 48
    • 0037180390 scopus 로고    scopus 로고
    • Importance of the conserved walker B glutamate residues, 556 and 1201, for the completion of the catalytic cycle of ATP hydrolysis by human P-glycoprotein (ABCB1)
    • DOI 10.1021/bi026626e
    • Sauna ZE, Müller M, Peng XH, Ambudkar SV (2002) Importance of the conserved Walker B glutamate residues, 556 and 1201, for the completion of the catalytic cycle of ATP hydrolysis by human Pglycoprotein (ABCB1). Biochemistry 41: 13989-14000. doi:10.1021/ bi026626e. PubMed: 12437356. (Pubitemid 35364871)
    • (2002) Biochemistry , vol.41 , Issue.47 , pp. 13989-14000
    • Sauna, Z.E.1    Muller, M.2    Peng, X.-H.3    Ambudkar, S.V.4
  • 49
    • 0032492724 scopus 로고    scopus 로고
    • Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state
    • DOI 10.1021/bi973045u
    • Ramachandra M, Ambudkar SV, Chen D, Hrycyna CA, Dey S et al. (1998) Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state. Biochemistry 37: 5010-5019. doi: 10.1021/bi973045u. PubMed: 9538020. (Pubitemid 28175983)
    • (1998) Biochemistry , vol.37 , Issue.14 , pp. 5010-5019
    • Ramachandra, M.1    Ambudkar, S.V.2    Chen, D.3    Hrycyna, C.A.4    Dey, S.5    Gottesman, M.M.6    Pastan, I.7
  • 50
    • 0034646468 scopus 로고    scopus 로고
    • Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein
    • DOI 10.1073/pnas.97.6.2515
    • Sauna ZE, Ambudkar SV (2000) Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein. Proc Natl Acad Sci U S A 97: 2515-2520. doi:10.1073/pnas.97.6.2515. PubMed: 10716986. (Pubitemid 30159202)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.6 , pp. 2515-2520
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 51
    • 0032321894 scopus 로고    scopus 로고
    • Drug-stimulatable ATPase activity in crude membranes of human MDR1- transfected mammalian cells
    • DOI 10.1016/S0076-6879(98)92039-0
    • Ambudkar SV (1998) Drug-stimulatable ATPase activity in crude membranes of human MDR1- transfected mammalian cells. Methods Enzymol 292: 504-514. doi:10.1016/S0076-6879(98)92039-0. PubMed: 9711578. (Pubitemid 29343911)
    • (1998) Methods in Enzymology , vol.292 , pp. 504-514
    • Ambudkar, S.V.1
  • 52
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Altschul SF, Madden TL, Schäffer AA, Zhang JH, Zhang Z et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402. doi:10.1093/nar/ 25.17.3389. PubMed: 9254694. (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 53
    • 0000243829 scopus 로고
    • Procheck - A program to check the stereochemical quality of protein structures
    • doi:10.1107/S0021889892009944
    • Laskowski RA, Macarthur MW, Moss DS, Thornton JM (1993) Procheck - a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26: 283-291. doi:10.1107/ S0021889892009944.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 57
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • Sanner MF (1999) Python: A programming language for software integration and development. J Mol Graph Model 17: 57-61. PubMed: 10660911. (Pubitemid 30029318)
    • (1999) Journal of Molecular Graphics and Modelling , vol.17 , Issue.1 , pp. 57-61
    • Sanner, M.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.