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Volumn 81, Issue 9, 2013, Pages 1653-1668

Substrate versus inhibitor dynamics of P-glycoprotein

Author keywords

Computational; Drug; Molecular dynamics; Multi drug resistance; Recognition; Simulation

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE; DAUNORUBICIN; MULTIDRUG RESISTANCE PROTEIN;

EID: 84882882457     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24324     Document Type: Article
Times cited : (30)

References (67)
  • 2
    • 34147214716 scopus 로고    scopus 로고
    • Multiple molecular mechanisms for multidrug resistance transporters
    • Higgins CF. Multiple molecular mechanisms for multidrug resistance transporters. Nature 2007;446:749-757.
    • (2007) Nature , vol.446 , pp. 749-757
    • Higgins, C.F.1
  • 3
    • 84870245295 scopus 로고    scopus 로고
    • Mammalian drug efflux transporters of the ATP binding cassette (ABC) family: An overview
    • Schinkel AH, Jonker JW. Mammalian drug efflux transporters of the ATP binding cassette (ABC) family: An overview. Adv Drug Deliv Rev 2012;64:138-153.
    • (2012) Adv Drug Deliv Rev , vol.64 , pp. 138-153
    • Schinkel, A.H.1    Jonker, J.W.2
  • 4
    • 64649090980 scopus 로고    scopus 로고
    • Molecular basis of multidrug transport by ABC transporters
    • Seeger MA, van Veen HW. Molecular basis of multidrug transport by ABC transporters. Biochim Biophys Acta 2009;1794:725-737.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 725-737
    • Seeger, M.A.1    van Veen, H.W.2
  • 7
    • 84861310612 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation
    • Hohl M, Briand C, Gr√otter MG, Seeger MA. Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation. Nat Struct Mol Biol 2012;19:395-402.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 395-402
    • Hohl, M.1    Briand, C.2    Gr√otter, M.G.3    Seeger, M.A.4
  • 8
    • 79960308124 scopus 로고    scopus 로고
    • Molecular-Dynamics simulations of the ATP/apo state of a multidrug ATP-Binding Cassette transporter provide a structural and mechanistic basis for the asymmetric occluded state
    • Jones PM, George AM. Molecular-Dynamics simulations of the ATP/apo state of a multidrug ATP-Binding Cassette transporter provide a structural and mechanistic basis for the asymmetric occluded state. Biophys J 2011;100:3025-3034.
    • (2011) Biophys J , vol.100 , pp. 3025-3034
    • Jones, P.M.1    George, A.M.2
  • 10
    • 33846794508 scopus 로고    scopus 로고
    • About a switch: how P-glycoprotein (ABCB1) harnesses the energy of ATP binding and hydrolysis to do mechanical work
    • Sauna ZE, Ambudker SV. About a switch: how P-glycoprotein (ABCB1) harnesses the energy of ATP binding and hydrolysis to do mechanical work. Molec Canc Therap 2007;6:13-23.
    • (2007) Molec Canc Therap , vol.6 , pp. 13-23
    • Sauna, Z.E.1    Ambudker, S.V.2
  • 11
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide-binding sites are catalytically active
    • Urbatsch IL, Sankaran B, Bhagat S, Senior AE. Both P-glycoprotein nucleotide-binding sites are catalytically active. J Biol Chem 1995;270:26956-26961.
    • (1995) J Biol Chem , vol.270 , pp. 26956-26961
    • Urbatsch, I.L.1    Sankaran, B.2    Bhagat, S.3    Senior, A.E.4
  • 12
    • 84864564117 scopus 로고    scopus 로고
    • Perspectives on the structure-function of ABC transporters: the switch and constant contact models
    • George AM, Jones PM. Perspectives on the structure-function of ABC transporters: the switch and constant contact models. Prog Biophys Mol Biol 2012;109:95-107.
    • (2012) Prog Biophys Mol Biol , vol.109 , pp. 95-107
    • George, A.M.1    Jones, P.M.2
  • 13
    • 73649111071 scopus 로고    scopus 로고
    • Understanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1
    • Gutmann DAP, Ward A, Urbatsch IL, Chang G, van Veen HW. 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
  • 15
    • 84867883248 scopus 로고    scopus 로고
    • Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans
    • Jin MS, Oldham ML, Zhang Q, Chen J. Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans. Nature 2012;490:566-569.
    • (2012) Nature , vol.490 , pp. 566-569
    • Jin, M.S.1    Oldham, M.L.2    Zhang, Q.3    Chen, J.4
  • 16
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen J, Lu G, Lin J, Davidson AL, Quicho FA. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol Cell 2003;12:651-661.
    • (2003) Mol Cell , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quicho, F.A.5
  • 17
    • 0037131184 scopus 로고    scopus 로고
    • Projection structure of P-glycoprotein by electron microscopy
    • Lee J-Y, Urbatsch IL, Senior AE, Wilkens S. Projection structure of P-glycoprotein by electron microscopy. J Biol Chem 2002;277:40125-40131.
    • (2002) J Biol Chem , vol.277 , pp. 40125-40131
    • Lee, J.-Y.1    Urbatsch, I.L.2    Senior, A.E.3    Wilkens, S.4
  • 18
    • 29144502288 scopus 로고    scopus 로고
    • ATP-hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation
    • Lu G, Westbrooks MJ, Davidson AL, Chen J. ATP-hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation. Proc Natl Acad Sci USA 2005;102:17969-17974.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17969-17974
    • Lu, G.1    Westbrooks, M.J.2    Davidson, A.L.3    Chen, J.4
  • 20
    • 77951877993 scopus 로고    scopus 로고
    • Human P-glycoprotein is active when the two halves are clamped together in the closed conformation
    • Loo TW, Bartlett MC, Clarke DM. Human P-glycoprotein is active when the two halves are clamped together in the closed conformation. Biochem Biophys Res Comms 2010;395:436-440.
    • (2010) Biochem Biophys Res Comms , vol.395 , pp. 436-440
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 21
    • 75149135645 scopus 로고    scopus 로고
    • Multidrug efflux pumps: the structures of prokaryotic ATP-binding cassette transporter efflux pumps and implications for our understanding of eukaryotic P-glycoproteins and homologues
    • Kerr ID, Jones PM, George AM. Multidrug efflux pumps: the structures of prokaryotic ATP-binding cassette transporter efflux pumps and implications for our understanding of eukaryotic P-glycoproteins and homologues. FEBS J 2009;277:550-563.
    • (2009) FEBS J , vol.277 , pp. 550-563
    • Kerr, I.D.1    Jones, P.M.2    George, A.M.3
  • 23
    • 77952667227 scopus 로고    scopus 로고
    • Impact of the recent mouse P-glycoprotein structure for structure-based ligand design
    • Klepsch F, Ecker GF. Impact of the recent mouse P-glycoprotein structure for structure-based ligand design. Mol Inf 2010;29:276-286.
    • (2010) Mol Inf , vol.29 , pp. 276-286
    • Klepsch, F.1    Ecker, G.F.2
  • 24
    • 69949167524 scopus 로고    scopus 로고
    • Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis
    • Loo TW, Bartlett MC, Clarke DM. Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis. J Biol Chem 2009;284:24074-24087.
    • (2009) J Biol Chem , vol.284 , pp. 24074-24087
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 25
    • 58849086773 scopus 로고    scopus 로고
    • Data-driven homology modelling of P-glycoprotein in the ATP-bound state indicates flexibility of the transmembrane domains
    • Stockner T, de Vries SJ, Bonvin AMJJ, Ecker GF, Chiba P. Data-driven homology modelling of P-glycoprotein in the ATP-bound state indicates flexibility of the transmembrane domains. FEBS Letts 2009;276:964-972.
    • (2009) FEBS Letts , vol.276 , pp. 964-972
    • Stockner, T.1    de Vries, S.J.2    Bonvin, A.M.J.J.3    Ecker, G.F.4    Chiba, P.5
  • 26
    • 84862203273 scopus 로고    scopus 로고
    • Insights on P-Glycoprotein's efflux mechanism obtained by molecular dynamics simulations
    • Ferreira RJ, Ferreira M-JU, dos Santos DJVA. Insights on P-Glycoprotein's efflux mechanism obtained by molecular dynamics simulations. J Chem Theory Comput 2011;8:1853-1864.
    • (2011) J Chem Theory Comput , vol.8 , pp. 1853-1864
    • Ferreira, R.J.1    Ferreira, M.-J.2    dos Santos, D.J.V.A.3
  • 27
    • 84877783750 scopus 로고    scopus 로고
    • The flexibility of P-glycoprotein for its poly-specific drug binding from molecular dynamics simulations
    • epub:
    • Liu M, Hou T, Feng Z, Li Y. The flexibility of P-glycoprotein for its poly-specific drug binding from molecular dynamics simulations. J Biomolec Struc Dyn 2012;epub:1-18.
    • (2012) J Biomolec Struc Dyn , pp. 1-18
    • Liu, M.1    Hou, T.2    Feng, Z.3    Li, Y.4
  • 28
    • 84867347202 scopus 로고    scopus 로고
    • The effect of environment on the structure of a membrane protein: P-glycoprotein under physiological conditions
    • O'Mara ML, Mark AE. The effect of environment on the structure of a membrane protein: P-glycoprotein under physiological conditions. J Chem Theory Comput 2012;8:3964-3976.
    • (2012) J Chem Theory Comput , vol.8 , pp. 3964-3976
    • O'Mara, M.L.1    Mark, A.E.2
  • 29
    • 84862890003 scopus 로고    scopus 로고
    • Catalytic transitions in the human MDR1 P-glycoprotein drug binding sites
    • Wise JG. Catalytic transitions in the human MDR1 P-glycoprotein drug binding sites. Biochemistry 2012;51:5125-5141.
    • (2012) Biochemistry , vol.51 , pp. 5125-5141
    • Wise, J.G.1
  • 30
    • 34250885126 scopus 로고    scopus 로고
    • The P-glycoprotein (ABCB1) linker domain encodes high-affinity binding sequences to alpha- and beta-tubulins
    • Georges E. The P-glycoprotein (ABCB1) linker domain encodes high-affinity binding sequences to alpha- and beta-tubulins. Biochemistry 2007;46:7337-7342.
    • (2007) Biochemistry , vol.46 , pp. 7337-7342
    • Georges, E.1
  • 31
    • 0032578434 scopus 로고    scopus 로고
    • Structural flexibility of the linker region of human P-glycoprotein permits ATP hydrolysis and drug transport
    • Hrycyna CA, Airan LE, Germann UA, Ambudkar SV, Pastan I, Gottesman MM. 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
  • 33
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 1999;292:195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 34
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole C, Barber JD, Barton GJ. The Jpred 3 secondary structure prediction server. Nucl Acids Res 2008;36:197-201.
    • (2008) Nucl Acids Res , vol.36 , pp. 197-201
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 38
    • 79954524314 scopus 로고    scopus 로고
    • From coarse grained to atomistic: a serial multiscale approach to membrane protein simulations
    • Stansfeld PJ, Sansom MSP. From coarse grained to atomistic: a serial multiscale approach to membrane protein simulations. J Chem Theory Comput 2011;7:1157-1166.
    • (2011) J Chem Theory Comput , vol.7 , pp. 1157-1166
    • Stansfeld, P.J.1    Sansom, M.S.P.2
  • 40
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simuation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simuation. J Chem Theory Comput 2008;4:435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 41
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen WL, Maxwell DS, Tirado-Rives J. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J Am Chem Soc 1996;118:11225-11236.
    • (1996) J Am Chem Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 42
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidycholine at full hydration, constant pressure and constant temperature
    • Berger O, Edholm O, Jahnig F. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidycholine 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
  • 43
    • 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;98:10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 46
    • 77954262905 scopus 로고    scopus 로고
    • 3V: cavity, channel and cleft volume calculator and extractor
    • Voss NR, Gerstein M. 3V: cavity, channel and cleft volume calculator and extractor. Nucleic Acids Research 2010;38(Suppl 2):W555-W562.
    • (2010) Nucleic Acids Research , vol.38 , Issue.SUPPL 2
    • Voss, N.R.1    Gerstein, M.2
  • 47
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott O, Olson AJ. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 2010;31:455-461.
    • (2010) J Comput Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 48
    • 84867537628 scopus 로고    scopus 로고
    • Exploring PHD fingers and H3K4me0 interactions with molecular dynamics simulations and binding free energy calculations: AIRE-PHD1, a comparative study
    • Spiliotopoulos D, Spitaleri A, Musco G. Exploring PHD fingers and H3K4me0 interactions with molecular dynamics simulations and binding free energy calculations: AIRE-PHD1, a comparative study. PLoS ONE 2012;7:e46902.
    • (2012) PLoS ONE , vol.7
    • Spiliotopoulos, D.1    Spitaleri, A.2    Musco, G.3
  • 49
    • 65349114255 scopus 로고    scopus 로고
    • ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments
    • Bond CS, Schuttelkopf AW. ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments. Acta Cryst D 2009;65:510-512.
    • (2009) Acta Cryst D , vol.65 , pp. 510-512
    • Bond, C.S.1    Schuttelkopf, A.W.2
  • 50
    • 47049101437 scopus 로고    scopus 로고
    • Mutational analysis of ABC proteins
    • Loo TW, Clarke DM. Mutational analysis of ABC proteins. Arch Biochem Biophys 2008;476:51-64.
    • (2008) Arch Biochem Biophys , vol.476 , pp. 51-64
    • Loo, T.W.1    Clarke, D.M.2
  • 51
    • 0036176213 scopus 로고    scopus 로고
    • Identification of ligand-binding regions of P-glycoprotein by activated-pharmacophore photoaffinity labeling and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Ecker GF, Csaszar E, Kopp S, Plagens B, Holzer W, Ernst W, Chiba P. Identification of ligand-binding regions of P-glycoprotein by activated-pharmacophore photoaffinity labeling and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Mol Pharmacol 2002;61:637-648.
    • (2002) Mol Pharmacol , vol.61 , pp. 637-648
    • Ecker, G.F.1    Csaszar, E.2    Kopp, S.3    Plagens, B.4    Holzer, W.5    Ernst, W.6    Chiba, P.7
  • 53
    • 33947284958 scopus 로고    scopus 로고
    • Dynamics and function in a bacterial ABC transporter: simulation studies of the BtuCDF system and its components
    • Ivetac A, Campbell JD, Sansom MSP. Dynamics and function in a bacterial ABC transporter: simulation studies of the BtuCDF system and its components. Biochemistry 2007;46:2767-2778.
    • (2007) Biochemistry , vol.46 , pp. 2767-2778
    • Ivetac, A.1    Campbell, J.D.2    Sansom, M.S.P.3
  • 54
    • 79955741987 scopus 로고    scopus 로고
    • Conformational changes induced by ATP-hydrolysis in an ABC transporter: a molecular dynamics study of the Sav1866 exporter
    • Oliveira AS, Baptista AM, Soares CM. Conformational changes induced by ATP-hydrolysis in an ABC transporter: a molecular dynamics study of the Sav1866 exporter. Proteins: Struct Func Bioinf 2011;79:1977-1990.
    • (2011) Proteins: Struct Func Bioinf , vol.79 , pp. 1977-1990
    • Oliveira, A.S.1    Baptista, A.M.2    Soares, C.M.3
  • 55
    • 77951241376 scopus 로고    scopus 로고
    • Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: implications for catalysis
    • Siarheyeva A, Liu R, Sharom FJ. 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
    • Siarheyeva, A.1    Liu, R.2    Sharom, F.J.3
  • 57
    • 4744358624 scopus 로고    scopus 로고
    • The ATP switch model for ABC transporters
    • Higgins CF, Linton KJ. The ATP switch model for ABC transporters. Nat Struct Mol Biol 2004;11:918-926.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2
  • 58
    • 80052436005 scopus 로고    scopus 로고
    • Conformational coupling of the nucleotide-binding and the transmembrane domains in ABC transporters
    • Wen P-C, Tajkhorshid E. Conformational coupling of the nucleotide-binding and the transmembrane domains in ABC transporters. Biophys J 2011;101:680-690.
    • (2011) Biophys J , vol.101 , pp. 680-690
    • Wen, P.-C.1    Tajkhorshid, E.2
  • 59
    • 79959352522 scopus 로고    scopus 로고
    • Structural consequences of ATP hydrolysis on the ABC transporter NBD dimer: molecular dynamics studies of HlyB
    • Damas JM, Oliveira ASF, Baptista AM, Soares CM. Structural consequences of ATP hydrolysis on the ABC transporter NBD dimer: molecular dynamics studies of HlyB. Prot Sci 2011;20:1220-1230.
    • (2011) Prot Sci , vol.20 , pp. 1220-1230
    • Damas, J.M.1    Oliveira, A.S.F.2    Baptista, A.M.3    Soares, C.M.4
  • 60
    • 84855476209 scopus 로고    scopus 로고
    • Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy
    • Verhalen B, Ernst S, Börsch M, Wilkens S. Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy. J Biol Chem 2012;287:1112-1127.
    • (2012) J Biol Chem , vol.287 , pp. 1112-1127
    • Verhalen, B.1    Ernst, S.2    Börsch, M.3    Wilkens, S.4
  • 61
    • 79953173207 scopus 로고    scopus 로고
    • P-glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide binding domains at their C-terminal ends
    • Verhalen B, Wilkens S. P-glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide binding domains at their C-terminal ends. J Biol Chem 2011;286:10476-10482.
    • (2011) J Biol Chem , vol.286 , pp. 10476-10482
    • Verhalen, B.1    Wilkens, S.2
  • 62
    • 84859708410 scopus 로고    scopus 로고
    • Investigational ABC transporter inhibitors
    • Falasca M, Linton KJ. Investigational ABC transporter inhibitors. Expert Opin Invest Drugs 2012;21:657-666.
    • (2012) Expert Opin Invest Drugs , vol.21 , pp. 657-666
    • Falasca, M.1    Linton, K.J.2
  • 63
    • 0032518454 scopus 로고    scopus 로고
    • A general pattern for substrate recognition by P-glycoprotein
    • Seelig A. A general pattern for substrate recognition by P-glycoprotein. Eur J Biochem 1998;251(1-2):252-261.
    • (1998) Eur J Biochem , vol.251 , Issue.1-2 , pp. 252-261
    • Seelig, A.1
  • 65
    • 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 PM, George AM. 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
  • 66
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham ML, Khare D, Quiocho FA, Davidson AL, Chen J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 2007;450:515-521.
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 67
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Prot Eng 1995;8:127-134.
    • (1995) Prot Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


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