메뉴 건너뛰기




Volumn 8, Issue 6, 2012, Pages 1853-1864

Insights on P-glycoproteins efflux mechanism obtained by molecular dynamics simulations

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84862203273     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/ct300083m     Document Type: Article
Times cited : (110)

References (102)
  • 1
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants
    • Juliano, R. L.; Ling, V. A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants Biochim. Biophys. Acta 1976, 455, 152
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 152
    • Juliano, R.L.1    Ling, V.2
  • 2
    • 0031455482 scopus 로고    scopus 로고
    • The P-glycoprotein Efflux Pump: How Does it Transport Drugs?
    • Sharom, F. J. The P-glycoprotein Efflux Pump: How Does it Transport Drugs? J. Membr. Biol. 1997, 160, 161-175
    • (1997) J. Membr. Biol. , vol.160 , pp. 161-175
    • Sharom, F.J.1
  • 4
    • 0346887115 scopus 로고    scopus 로고
    • Structure and function of efflux pumps that confer resistance to drugs
    • Borges-Walmsley, M. I.; McKeegan, K. S.; Walmsley, A. R. Structure and function of efflux pumps that confer resistance to drugs Biochem. J. 2003, 376, 313-338
    • (2003) Biochem. J. , vol.376 , pp. 313-338
    • Borges-Walmsley, M.I.1    McKeegan, K.S.2    Walmsley, A.R.3
  • 5
    • 0028342805 scopus 로고
    • Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: Evidence against direct drug extrusion from the plasma membrane
    • Altenberg, G. A.; Vanoye, C. G.; Horton, J. K.; Reuss, L.; Julie, K. Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: evidence against direct drug extrusion from the plasma membrane Proc. Natl. Acad. Sci. U. S. A. 1994, 91, 4654-4657
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 4654-4657
    • Altenberg, G.A.1    Vanoye, C.G.2    Horton, J.K.3    Reuss, L.4    Julie, K.5
  • 7
    • 0025193531 scopus 로고
    • Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells
    • Raviv, Y.; Pollard, H. B.; Bruggemann, E. P.; Pastan, I.; Gottesman, M. M. Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells J. Biol. Chem. 1990, 265, 3975-3980
    • (1990) J. Biol. Chem. , vol.265 , pp. 3975-3980
    • Raviv, Y.1    Pollard, H.B.2    Bruggemann, E.P.3    Pastan, I.4    Gottesman, M.M.5
  • 8
    • 0033602840 scopus 로고    scopus 로고
    • The membrane lipid environment modulates drug interactions with the P-glycoprotein multidrug transporter
    • Romsicki, Y.; Sharom, F. J. The membrane lipid environment modulates drug interactions with the P-glycoprotein multidrug transporter Biochemistry 1999, 38, 6887-6896
    • (1999) Biochemistry , vol.38 , pp. 6887-6896
    • Romsicki, Y.1    Sharom, F.J.2
  • 9
    • 66149139241 scopus 로고    scopus 로고
    • 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
    • Jones, P. M.; George, A. M. 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 Proteins 2009, 75, 387-396
    • (2009) Proteins , vol.75 , pp. 387-396
    • Jones, P.M.1    George, A.M.2
  • 10
    • 31844448665 scopus 로고    scopus 로고
    • The translocation mechanism of P-glycoprotein
    • Callaghan, R.; Ford, R. C.; Kerr, I. D. The translocation mechanism of P-glycoprotein FEBS Lett. 2006, 580, 1056-1063
    • (2006) FEBS Lett. , vol.580 , pp. 1056-1063
    • Callaghan, R.1    Ford, R.C.2    Kerr, I.D.3
  • 11
    • 0034601776 scopus 로고    scopus 로고
    • Drug Binding Sites on P-Glycoprotein Are Altered by ATP Binding Prior to Nucleotide Hydrolysis
    • Martin, C.; Berridge, G.; Mistry, P.; Higgins, C.; Charlton, P.; Callaghan, R. Drug Binding Sites on P-Glycoprotein Are Altered by ATP Binding Prior to Nucleotide Hydrolysis Biochemistry 2000, 39, 11901-11906
    • (2000) Biochemistry , vol.39 , pp. 11901-11906
    • Martin, C.1    Berridge, G.2    Mistry, P.3    Higgins, C.4    Charlton, P.5    Callaghan, R.6
  • 12
    • 17544365536 scopus 로고
    • The role of passive transbilayer drug movement in multidrug resistance and its modulation
    • Eytan, G. D.; Regev, R.; Oren, G.; Assaraf, Y. G. The role of passive transbilayer drug movement in multidrug resistance and its modulation J. Biol. Chem. 1995, 271, 12897-12902
    • (1995) J. Biol. Chem. , vol.271 , pp. 12897-12902
    • Eytan, G.D.1    Regev, R.2    Oren, G.3    Assaraf, Y.G.4
  • 13
    • 0028831929 scopus 로고
    • Effects of lipids on ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch, I. L.; Senior, A. E. Effects of lipids on ATPase activity of purified Chinese hamster P-glycoprotein Arch. Biochem. Biophys. 1995, 316, 135-140
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 135-140
    • Urbatsch, I.L.1    Senior, A.E.2
  • 14
    • 33744483102 scopus 로고    scopus 로고
    • P-glycoprotein and lipid rafts: Some ambiguous mutual relationships (floating on them, building them or meeting them by chance?)
    • Orlowski, S.; Martin, S.; Escargueil, A. P-glycoprotein and lipid rafts: some ambiguous mutual relationships (floating on them, building them or meeting them by chance?) Cell. Mol. Life Sci. 2006, 63, 1038-1059
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 1038-1059
    • Orlowski, S.1    Martin, S.2    Escargueil, A.3
  • 15
    • 0032956955 scopus 로고    scopus 로고
    • Mechanism of Action of P-Glycoprotein in Relation to Passive Membrane Permeation
    • Eytan, G.; Kuchel, P. Mechanism of Action of P-Glycoprotein in Relation to Passive Membrane Permeation Int. Rev. Cytol. 1999, 190, 175-250
    • (1999) Int. Rev. Cytol. , vol.190 , pp. 175-250
    • Eytan, G.1    Kuchel, P.2
  • 16
    • 36249004263 scopus 로고    scopus 로고
    • Modulation of P-glycoprotein-mediated multidrug resistance by acceleration of passive drug permeation across the plasma membrane
    • Regev, R.; Katzir, H.; Yeheskely-Hayon, D.; Eytan, G. D. Modulation of P-glycoprotein-mediated multidrug resistance by acceleration of passive drug permeation across the plasma membrane FEBS Lett. 2007, 274, 6204-6214
    • (2007) FEBS Lett. , vol.274 , pp. 6204-6214
    • Regev, R.1    Katzir, H.2    Yeheskely-Hayon, D.3    Eytan, G.D.4
  • 17
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. G. Lipid-protein interactions in biological membranes: a structural perspective Biochim. Biophys. Acta 2003, 1612, 1-40
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 18
    • 69849099831 scopus 로고    scopus 로고
    • Lipid dependence of ABC transporter localization and function
    • Klappe, K.; Hummel, I.; Hoekstra, D.; Kok, J. W. Lipid dependence of ABC transporter localization and function Chem. Phys. Lipids. 2009, 161, 57-64
    • (2009) Chem. Phys. Lipids. , vol.161 , pp. 57-64
    • Klappe, K.1    Hummel, I.2    Hoekstra, D.3    Kok, J.W.4
  • 19
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P.; Lee, A. T.; Rees, D. C. The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism Science 2002, 296, 1091-1098
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 24
    • 4544284056 scopus 로고    scopus 로고
    • The coupling mechanism of P-glycoprotein involves residue L339 in the sixth membrane spanning segment
    • Rothnie, A.; Storm, J.; Campbell, J.; Linton, K. J.; Kerr, I. D.; Callaghan, R. The coupling mechanism of P-glycoprotein involves residue L339 in the sixth membrane spanning segment J. Biol. Chem. 2004, 279, 34913-34990
    • (2004) J. Biol. Chem. , vol.279 , pp. 34913-34990
    • Rothnie, A.1    Storm, J.2    Campbell, J.3    Linton, K.J.4    Kerr, I.D.5    Callaghan, R.6
  • 25
    • 41549102797 scopus 로고    scopus 로고
    • Computational models for prediction of interactions with ABC-transporters
    • Ecker, G. F.; Stockner, T.; Chiba, P. Computational models for prediction of interactions with ABC-transporters Drug Discovery Today 2008, 13, 311-317
    • (2008) Drug Discovery Today , vol.13 , pp. 311-317
    • Ecker, G.F.1    Stockner, T.2    Chiba, P.3
  • 26
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J.; Locher, K. P. Structure of a bacterial multidrug ABC transporter Nature 2006, 443, 180-185
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 27
    • 34548133239 scopus 로고    scopus 로고
    • P-glycoprotein models of the apo and ATP-bound states based on homology with Sav1866 and MalK
    • OMara, M. L.; Tieleman, D. P. P-glycoprotein models of the apo and ATP-bound states based on homology with Sav1866 and MalK FEBS Lett. 2007, 581, 4217-4222
    • (2007) FEBS Lett. , vol.581 , pp. 4217-4222
    • Omara, M.L.1    Tieleman, D.P.2
  • 28
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • Ward, A.; Reyes, C. L.; Yu, J.; Roth, C. B.; Chang, G. Flexibility in the ABC transporter MsbA: Alternating access with a twist Proc. Natl. Acad. Sci. U. S. A. 2007, 104, 19005-19010
    • (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
  • 29
    • 75149147634 scopus 로고    scopus 로고
    • Multidrug efflux pumps: Drug binding - Gates or cavity?
    • Crowley, E.; Callaghan, R. Multidrug efflux pumps: drug binding - gates or cavity? FEBS J. 2010, 277, 530-539
    • (2010) FEBS J. , vol.277 , pp. 530-539
    • Crowley, E.1    Callaghan, R.2
  • 30
    • 34247571894 scopus 로고    scopus 로고
    • Retraction of "structure of MsbA from Vibrio cholera: A Multidrug Resistance ABC Transporter Homolog in a Closed Conformation" [J. Mol. Biol. (2003) 330 419-430]
    • Chang, G. Retraction of "Structure of MsbA from Vibrio cholera: A Multidrug Resistance ABC Transporter Homolog in a Closed Conformation" [J. Mol. Biol. (2003) 330 419-430] J. Mol. Biol. 2007, 369, 596
    • (2007) J. Mol. Biol. , vol.369 , pp. 596
    • Chang, G.1
  • 31
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson, R. J.; Locher, K. P. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP FEBS Lett. 2007, 581, 935-938
    • (2007) FEBS Lett. , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 32
    • 18644362391 scopus 로고    scopus 로고
    • Structural basis of energy transduction in the transport cycle of MsbA
    • Dong, J.; Yang, G.; McHaourab, H. S. Structural basis of energy transduction in the transport cycle of MsbA Science 2005, 308, 1023-1028
    • (2005) Science , vol.308 , pp. 1023-1028
    • Dong, J.1    Yang, G.2    McHaourab, H.S.3
  • 34
    • 13244292479 scopus 로고    scopus 로고
    • Three-dimensional structure of P-glycoprotein: The transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state
    • Rosenberg, M. F.; Callaghan, R.; Modok, S.; Higgins, C. F.; Ford, R. C. Three-dimensional structure of P-glycoprotein: the transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state J. Biol. Chem. 2005, 280, 2857-2862
    • (2005) J. Biol. Chem. , vol.280 , pp. 2857-2862
    • Rosenberg, M.F.1    Callaghan, R.2    Modok, S.3    Higgins, C.F.4    Ford, R.C.5
  • 35
    • 79955741987 scopus 로고    scopus 로고
    • Conformational changes induced by ATP-hydrolysis in an ABC transporter: A molecular dynamics study of the Sav1866 exporter
    • Oliveira, A. S.; Baptista, A. M.; Soares, C. M. Conformational changes induced by ATP-hydrolysis in an ABC transporter: a molecular dynamics study of the Sav1866 exporter Proteins 2011, 79, 1977-1990
    • (2011) Proteins , vol.79 , pp. 1977-1990
    • Oliveira, A.S.1    Baptista, A.M.2    Soares, C.M.3
  • 36
    • 79959352522 scopus 로고    scopus 로고
    • Structural consequences of ATP hydrolysis on the ABC transporter NBD dimer: Molecular dynamics studies of HlyB
    • Damas, J. M.; Oliveira, A. S.; Baptista, A. M.; Soares, C. M. Structural consequences of ATP hydrolysis on the ABC transporter NBD dimer: Molecular dynamics studies of HlyB Protein Sci. 2011, 20, 1220-1230
    • (2011) Protein Sci. , vol.20 , pp. 1220-1230
    • Damas, J.M.1    Oliveira, A.S.2    Baptista, A.M.3    Soares, C.M.4
  • 38
    • 79959833862 scopus 로고    scopus 로고
    • Predicting binding to P-Glycoprotein by Flexible Receptor Docking
    • 10.1371/journal.pcbi.1002083
    • Dolghih, E.; Bryant, C.; Renslo, A. R.; Jacobson, M. P. Predicting binding to P-Glycoprotein by Flexible Receptor Docking PLoS Comput. Biol. 2011, 7, e1002083 10.1371/journal.pcbi.1002083
    • (2011) PLoS Comput. Biol. , vol.7 , pp. 1002083
    • Dolghih, E.1    Bryant, C.2    Renslo, A.R.3    Jacobson, M.P.4
  • 39
    • 79952272763 scopus 로고    scopus 로고
    • Probing the stereoselectivity of P-glycoprotein-synthesis, biological activity and ligand docking studies of a set of enantiopure benzopyrano[3,4-b] [1,4]oxazines
    • Jabeen, I.; Wetwitayaklung, P.; Klepsch, F.; Parveen, Z.; Chiba, P.; Ecker, G. F. Probing the stereoselectivity of P-glycoprotein-synthesis, biological activity and ligand docking studies of a set of enantiopure benzopyrano[3,4-b][1,4]oxazines Chem. Commun. (Camb.) 2011, 47, 2586-2588
    • (2011) Chem. Commun. (Camb.) , vol.47 , pp. 2586-2588
    • Jabeen, I.1    Wetwitayaklung, P.2    Klepsch, F.3    Parveen, Z.4    Chiba, P.5    Ecker, G.F.6
  • 40
    • 0019430432 scopus 로고
    • Overcoming of Vincristine Resistance in P388 Leukemia in Vivo and in Vitro through Enhanced Cytotoxicity of Vincristine and Vinblastine by Verapamil
    • Tsuruo, T.; Lida, H.; Tsukagoshi, S.; Sakurai, Y. Overcoming of Vincristine Resistance in P388 Leukemia in Vivo and in Vitro through Enhanced Cytotoxicity of Vincristine and Vinblastine by Verapamil Cancer Res. 1981, 41, 1967-1972
    • (1981) Cancer Res. , vol.41 , pp. 1967-1972
    • Tsuruo, T.1    Lida, H.2    Tsukagoshi, S.3    Sakurai, Y.4
  • 42
    • 0032578434 scopus 로고    scopus 로고
    • Structural flexibility of the linker region of human P-glycoprotein permits ATP hydrolysis and drug transport
    • Hrycyna, C. A.; Airan, L. E.; Germann, U. A.; Ambudkar, S. V.; Pastan, I.; Gottesman, M. M. Structural flexibility of the linker region of human P-glycoprotein permits ATP hydrolysis and drug transport Biochemistry 1998, 37, 13660-13673
    • (1998) Biochemistry , vol.37 , pp. 13660-13673
    • Hrycyna, C.A.1    Airan, L.E.2    Germann, U.A.3    Ambudkar, S.V.4    Pastan, I.5    Gottesman, M.M.6
  • 43
    • 67650498383 scopus 로고    scopus 로고
    • Functional role of the linker region in purified human P-glycoprotein
    • Sato, T.; Kodan, A.; Kimura, Y.; Ueda, K.; Nakatsu, T.; Kato, H. Functional role of the linker region in purified human P-glycoprotein FEBS J. 2009, 276, 3504-3516
    • (2009) FEBS J. , vol.276 , pp. 3504-3516
    • Sato, T.1    Kodan, A.2    Kimura, Y.3    Ueda, K.4    Nakatsu, T.5    Kato, H.6
  • 46
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink, C.; Villa, A.; Mark, A. E.; van Gunsteren, W. F. A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6 J.Comput. Chem. 2004, 25, 1656-1676
    • (2004) J.Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 47
    • 77950101403 scopus 로고    scopus 로고
    • On the Validation of Molecular Dynamics Simulations of Saturated and cis-Monounsaturated Phosphatidylcholine Lipid Bilayers: A Comparison with Experiment
    • Poger, D.; Mark, A. E. On the Validation of Molecular Dynamics Simulations of Saturated and cis-Monounsaturated Phosphatidylcholine Lipid Bilayers: A Comparison with Experiment J. Chem. Theory Comput. 2010, 6, 325-336
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 325-336
    • Poger, D.1    Mark, A.E.2
  • 48
    • 77950590441 scopus 로고    scopus 로고
    • A new force field for simulating phosphatidylcholine bilayers
    • Poger, D.; Van Gunsteren, W. F.; Mark, A. E. A new force field for simulating phosphatidylcholine bilayers J. Comput. Chem. 2010, 31, 1117-1125
    • (2010) J. Comput. Chem. , vol.31 , pp. 1117-1125
    • Poger, D.1    Van Gunsteren, W.F.2    Mark, A.E.3
  • 49
    • 0030999097 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of a Fluid Bilayer of Dipalmitoylphosphatidylcholine at Full Hydration, Constant Pressure, and Constant Temperature
    • Berger, O.; Edholm, O.; Jahnig, F. Molecular Dynamics Simulations of a Fluid Bilayer of Dipalmitoylphosphatidylcholine at Full Hydration, Constant Pressure, and Constant Temperature Biophys. J. 1997, 72, 2002-2013
    • (1997) Biophys. J. , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 50
    • 0029099308 scopus 로고
    • Incorporation of Surface Tension into Molecular Dynamics Simulation of Interface: A Fluid Phase Lipid Bilayer Membrane
    • Chiu, S.-W.; Clark, M. A.; Balaji, V.; Subramaniam, S.; Scott, H. L.; Jakobsson, E. Incorporation of Surface Tension into Molecular Dynamics Simulation of Interface: A Fluid Phase Lipid Bilayer Membrane Biophys. J. 1995, 69, 1230-1245
    • (1995) Biophys. J. , vol.69 , pp. 1230-1245
    • Chiu, S.-W.1    Clark, M.A.2    Balaji, V.3    Subramaniam, S.4    Scott, H.L.5    Jakobsson, E.6
  • 51
    • 65249151900 scopus 로고    scopus 로고
    • Lipid models for United-atom Molecular Dynamics Simulations of Proteins
    • Kukol, A. Lipid models for United-atom Molecular Dynamics Simulations of Proteins J. Chem. Theory Comput. 2009, 5, 615-626
    • (2009) J. Chem. Theory Comput. , vol.5 , pp. 615-626
    • Kukol, A.1
  • 52
  • 53
    • 3042772967 scopus 로고    scopus 로고
    • Simulating the physiological phase of hydrated DPPC bilayers: The Ester Moiety
    • Chandrasekhar, I.; Oostenbrink, C.; van Gunsteren, W. F. Simulating the physiological phase of hydrated DPPC bilayers: The Ester Moiety Soft Mater. 2004, 2, 27-45
    • (2004) Soft Mater. , vol.2 , pp. 27-45
    • Chandrasekhar, I.1    Oostenbrink, C.2    Van Gunsteren, W.F.3
  • 54
    • 84855757480 scopus 로고    scopus 로고
    • 2009.10; Chemical Computing Group Inc. Montreal, QC, Canada
    • Molecular Operating Environment (MOE), 2009.10; Chemical Computing Group Inc.: Montreal, QC, Canada, 2010.
    • (2010) Molecular Operating Environment (MOE)
  • 55
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen, H. GROMACS: A message-passing parallel molecular dynamics implementation Comput. Phys. Commun. 1995, 91, 43-56
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 43-56
    • Berendsen, H.1
  • 56
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E.; Hess, B.; van der Spoel, D. GROMACS 3.0: a package for molecular simulation and trajectory analysis J. Mol. Model. 2001, 7, 306-317
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 58
    • 33947139278 scopus 로고    scopus 로고
    • Setting up and running molecular dynamics simulations of membrane proteins
    • Kandt, C.; Ash, W. L.; Tieleman, D. P. Setting up and running molecular dynamics simulations of membrane proteins Methods 2007, 41, 475-488
    • (2007) Methods , vol.41 , pp. 475-488
    • Kandt, C.1    Ash, W.L.2    Tieleman, D.P.3
  • 59
    • 77954256616 scopus 로고    scopus 로고
    • G-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation
    • Wolf, M. G.; Hoefling, M.; Aponte-Santamaría, C.; Grubmüller, H.; Groenhof, G. g-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation J.Comput. Chem. 2010, 31, 2169-2174
    • (2010) J.Comput. Chem. , vol.31 , pp. 2169-2174
    • Wolf, M.G.1    Hoefling, M.2    Aponte-Santamaría, C.3    Grubmüller, H.4    Groenhof, G.5
  • 60
    • 65549083717 scopus 로고    scopus 로고
    • GridMAT-MD: A grid-based membrane analysis tool for use with molecular dynamics
    • Allen, W. J.; Lemkul, J. A.; Bevan, D. R. GridMAT-MD: a grid-based membrane analysis tool for use with molecular dynamics J.Comput. Chem. 2009, 30, 1952-1958
    • (2009) J.Comput. Chem. , vol.30 , pp. 1952-1958
    • Allen, W.J.1    Lemkul, J.A.2    Bevan, D.R.3
  • 61
    • 70049114950 scopus 로고    scopus 로고
    • Detection of functional modes in protein dynamics
    • 10.1371/journal.pcbi.1000480
    • Hub, J. S.; de Groot, B. L. Detection of functional modes in protein dynamics PLoS Comput. Biol. 2009, 5, e1000480 10.1371/journal.pcbi.1000480
    • (2009) PLoS Comput. Biol. , vol.5 , pp. 1000480
    • Hub, J.S.1    De Groot, B.L.2
  • 63
    • 79957788878 scopus 로고    scopus 로고
    • ProDy: Protein dynamics inferred from theory and experiments
    • Bakan, A.; Meireles, L. M.; Bahar, I. ProDy: protein dynamics inferred from theory and experiments Bioinformatics 2011, 27, 1575-1577
    • (2011) Bioinformatics , vol.27 , pp. 1575-1577
    • Bakan, A.1    Meireles, L.M.2    Bahar, I.3
  • 64
    • 77949634796 scopus 로고    scopus 로고
    • Normal mode analysis of biomolecular structures: Functional mechanisms of membrane proteins
    • Bahar, I.; Lezon, T. R.; Bakan, A.; Shrivastava, I. H. Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins Chem. Rev. 2010, 110, 1463-1497
    • (2010) Chem. Rev. , vol.110 , pp. 1463-1497
    • Bahar, I.1    Lezon, T.R.2    Bakan, A.3    Shrivastava, I.H.4
  • 70
    • 68949213019 scopus 로고    scopus 로고
    • A generic method for assignment of reliability scores applied to solvent accessibility predictions
    • Petersen, B.; Petersen, T. N.; Andersen, P.; Nielsen, M.; Lundegaard, C. A generic method for assignment of reliability scores applied to solvent accessibility predictions BMC Struct. Biol. 2009, 9, 51
    • (2009) BMC Struct. Biol. , vol.9 , pp. 51
    • Petersen, B.1    Petersen, T.N.2    Andersen, P.3    Nielsen, M.4    Lundegaard, C.5
  • 71
    • 34547759752 scopus 로고    scopus 로고
    • APSSP2: A combination method for protein secondary structure prediction based on neural network and example based learning
    • Raghava, G. P. S. APSSP2: A combination method for protein secondary structure prediction based on neural network and example based learning. CASP5 2002, A-132.
    • (2002) CASP5 , vol.132
    • Raghava, G.P.S.1
  • 72
    • 0033933636 scopus 로고    scopus 로고
    • Cascaded multiple classifiers for secondary structure prediction
    • Ouali, M.; King, R. D. Cascaded multiple classifiers for secondary structure prediction Protein Sci. 2000, 9, 1162-1176
    • (2000) Protein Sci. , vol.9 , pp. 1162-1176
    • Ouali, M.1    King, R.D.2
  • 73
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P. Y.; Fasman, G. D. Prediction of protein conformation Biochemistry 1974, 13, 222-245
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 75
    • 34250315776 scopus 로고    scopus 로고
    • Molecular Characterization of Gel and Liquid-Crystalline Structures of Fully Hydrated POPC and POPE Bilayers
    • Leekumjorn, S.; Sum, A. K. Molecular Characterization of Gel and Liquid-Crystalline Structures of Fully Hydrated POPC and POPE Bilayers J. Phys. Chem. B 2007, 111, 6026-6033
    • (2007) J. Phys. Chem. B , vol.111 , pp. 6026-6033
    • Leekumjorn, S.1    Sum, A.K.2
  • 76
    • 33644534548 scopus 로고    scopus 로고
    • New macrocyclic lathyrane diterpenes, from Euphorbia lagascae, as inhibitors of multidrug resistance of tumour cells
    • Duarte, N.; Gyémánt, N.; Abreu, P. M.; Molnár, J.; Ferreira, M.-J. U. New macrocyclic lathyrane diterpenes, from Euphorbia lagascae, as inhibitors of multidrug resistance of tumour cells Planta Med. 2006, 72, 162-168
    • (2006) Planta Med. , vol.72 , pp. 162-168
    • Duarte, N.1    Gyémánt, N.2    Abreu, P.M.3    Molnár, J.4    Ferreira, M.-J.U.5
  • 77
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C.; Laskowski, R. A.; Thornton, J. M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions Protein Eng. 1995, 8, 127-134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 78
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I. K.; Thornton, J. M. Satisfying hydrogen bonding potential in proteins J. Mol. Biol. 1994, 238, 777-793
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 79
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi, G.; Donadio, D.; Parrinello, M. Canonical sampling through velocity rescaling J. Chem. Phys. 2007, 126, 14101-14107
    • (2007) J. Chem. Phys. , vol.126 , pp. 14101-14107
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 80
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W. Canonical dynamics: Equilibrium phase-space distributions Phys. Rev. A 1985, 31, 1695-1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.1
  • 81
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • Nosé, S.; Klein, M. L. Constant pressure molecular dynamics for molecular systems Mol. Phys. 1983, 50, 1055-1076
    • (1983) Mol. Phys. , vol.50 , pp. 1055-1076
    • Nosé, S.1    Klein, M.L.2
  • 82
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • Parrinello, M.; Rahman, A. Polymorphic transitions in single crystals: A new molecular dynamics method J. Appl. Phys. 1981, 52, 7182-7190
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 83
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems
    • Darden, T.; York, D.; Pedersen, L. Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems J. Chem. Phys. 1993, 98, 10089
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 85
    • 84986440341 scopus 로고
    • Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • Miyamoto, S.; Kollman, P. A. Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models J. Comput. Chem. 1992, 13, 952-962
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 87
    • 0037162259 scopus 로고    scopus 로고
    • Molecular theory of hydrophobic mismatch between lipids and peptides
    • Duque, D.; Li, X.-jun; Katsov, K.; Schick, M. Molecular theory of hydrophobic mismatch between lipids and peptides J. Chem. Phys. 2002, 116, 10478-10481
    • (2002) J. Chem. Phys. , vol.116 , pp. 10478-10481
    • Duque, D.1    Li, X.-J.2    Katsov, K.3    Schick, M.4
  • 88
    • 77953699035 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the transmembrane subunit of BtuCD in the lipid bilayer
    • Sun, T.; Liu, M.; Chen, W.; Wang, C. Molecular dynamics simulation of the transmembrane subunit of BtuCD in the lipid bilayer Sci. China Life Sci. 2010, 53, 620-630
    • (2010) Sci. China Life Sci. , vol.53 , pp. 620-630
    • Sun, T.1    Liu, M.2    Chen, W.3    Wang, C.4
  • 89
    • 3242885293 scopus 로고    scopus 로고
    • The PredictProtein server
    • 10.1093/nar/gkh377
    • Rost, B.; Yachdav, G.; Liu, J. The PredictProtein server Nucleic Acids Res. 2004, 32, W321 10.1093/nar/gkh377
    • (2004) Nucleic Acids Res. , vol.32 , pp. 321
    • Rost, B.1    Yachdav, G.2    Liu, J.3
  • 90
    • 0034013435 scopus 로고    scopus 로고
    • Validation of protein crystal structures
    • Kleywegt, G. J. Validation of protein crystal structures Acta Crystallogr. 2000, D56, 249-265
    • (2000) Acta Crystallogr. , vol.56 , pp. 249-265
    • Kleywegt, G.J.1
  • 92
    • 32044453808 scopus 로고    scopus 로고
    • Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux
    • Loo, T. W.; Clarke, D. M. Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux J. Membr. Biol. 2005, 206, 173-185
    • (2005) J. Membr. Biol. , vol.206 , pp. 173-185
    • Loo, T.W.1    Clarke, D.M.2
  • 93
    • 0023836456 scopus 로고
    • Most drugs that reverse multidrug resistance also inhibit photoaffinity labeling of P-glycoprotein by a vinblastine analog
    • Akiyama, S.; Cornwell, M. M.; Kuwano, M.; Pastan, I.; Gottesman, M. M. Most drugs that reverse multidrug resistance also inhibit photoaffinity labeling of P-glycoprotein by a vinblastine analog Mol. Pharmacol. 1988, 33, 144-147
    • (1988) Mol. Pharmacol. , vol.33 , pp. 144-147
    • Akiyama, S.1    Cornwell, M.M.2    Kuwano, M.3    Pastan, I.4    Gottesman, M.M.5
  • 94
    • 79959764016 scopus 로고    scopus 로고
    • Toward a better pharmacophore description of P-glycoprotein modulators, based on macrocyclic diterpenes from Euphorbia species
    • Ferreira, R. J.; dos Santos, D. J.; Ferreira, M.-J.; Guedes, R. C. Toward a better pharmacophore description of P-glycoprotein modulators, based on macrocyclic diterpenes from Euphorbia species J. Chem. Inf. Model 2011, 51, 1315-1324
    • (2011) J. Chem. Inf. Model , vol.51 , pp. 1315-1324
    • Ferreira, R.J.1    Dos Santos, D.J.2    Ferreira, M.-J.3    Guedes, R.C.4
  • 95
    • 0035047222 scopus 로고    scopus 로고
    • Structure-activity relationships of multidrug resistance reversers
    • Wiese, M.; Pajeva, I. K. Structure-activity relationships of multidrug resistance reversers Curr. Med. Chem. 2001, 8, 685-713
    • (2001) Curr. Med. Chem. , vol.8 , pp. 685-713
    • Wiese, M.1    Pajeva, I.K.2
  • 96
    • 73349111250 scopus 로고    scopus 로고
    • Structure-activity relationships of tariquidar analogs as multidrug resistance modulators
    • Pajeva, I. K.; Wiese, M. Structure-activity relationships of tariquidar analogs as multidrug resistance modulators AAPS J. 2009, 11, 435-444
    • (2009) AAPS J. , vol.11 , pp. 435-444
    • Pajeva, I.K.1    Wiese, M.2
  • 98
    • 78650108564 scopus 로고    scopus 로고
    • Dynamics and structural changes induced by ATP binding in SAV1866, a bacterial ABC exporter
    • Becker, J. P.; van Bambeke, F.; Tulkens, P. M.; Prévost, M. Dynamics and structural changes induced by ATP binding in SAV1866, a bacterial ABC exporter J. Phys. Chem. B 2010, 114, 15948-15957
    • (2010) J. Phys. Chem. B , vol.114 , pp. 15948-15957
    • Becker, J.P.1    Van Bambeke, F.2    Tulkens, P.M.3    Prévost, M.4
  • 99
    • 0032492724 scopus 로고    scopus 로고
    • Human P-Glycoprotein Exhibits Reduced Affinity for Substrates during a Catalytic Transition State
    • Ramachandra, M.; Ambudkar, S. V.; Chen, D.; Hrycyna, C. A.; Dey, S.; Gottesman, M. M.; Pastan, I. Human P-Glycoprotein Exhibits Reduced Affinity for Substrates during a Catalytic Transition State Biochemistry 1998, 37, 4693-5038
    • (1998) Biochemistry , vol.37 , pp. 4693-5038
    • Ramachandra, M.1    Ambudkar, S.V.2    Chen, D.3    Hrycyna, C.A.4    Dey, S.5    Gottesman, M.M.6    Pastan, I.7
  • 100
    • 73649111071 scopus 로고    scopus 로고
    • Understanding polyspecificity of multidrug ABC transporters: Closing in on the gaps in ABCB1
    • Gutmann, D. A. P.; Ward, A.; Urbatsch, I. L.; Chang, G.; van Veen, H. W. Understanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1 Trends Biochem. Sci. 2010, 35, 36-42
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 36-42
    • Gutmann, D.A.P.1    Ward, A.2    Urbatsch, I.L.3    Chang, G.4    Van Veen, H.W.5
  • 101
    • 84860417445 scopus 로고    scopus 로고
    • ATP hydrolysis at one of the two sites in ABC transporters initiates transport related conformational transitions
    • Gyimesi, G.; Ramachandran, S.; Kota, P.; Dokholyan, N. V.; Sarkadi, B.; Hegedus, T. ATP hydrolysis at one of the two sites in ABC transporters initiates transport related conformational transitions Biochim. Biophys. Acta 2011, 1808, 2954-2964
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2954-2964
    • Gyimesi, G.1    Ramachandran, S.2    Kota, P.3    Dokholyan, N.V.4    Sarkadi, B.5    Hegedus, T.6
  • 102
    • 77951241376 scopus 로고    scopus 로고
    • Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: Implications for catalysis
    • Siarheyva, A.; Liu, R.; Sharom, F. Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: implications for catalysis J. Biol. Chem. 2010, 285, 7575-7586
    • (2010) J. Biol. Chem. , vol.285 , pp. 7575-7586
    • Siarheyva, A.1    Liu, R.2    Sharom, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.