메뉴 건너뛰기




Volumn 10, Issue 11, 2015, Pages

Role of structural dynamics at the receptor G protein interface for signal transduction

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; WATER; BETA 2 ADRENERGIC RECEPTOR; G PROTEIN COUPLED RECEPTOR; GUANOSINE DIPHOSPHATE; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN BINDING;

EID: 84960077614     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0143399     Document Type: Article
Times cited : (10)

References (41)
  • 1
    • 84855799592 scopus 로고    scopus 로고
    • Diversity and modularity of G protein-coupled receptor structures
    • Elsevier Ltd
    • Katritch V, Cherezov V, Stevens RC. Diversity and modularity of G protein-coupled receptor structures. Trends Pharmacol Sci. Elsevier Ltd; 2012; 33: 17-27. doi: 10.1016/j.tips.2011.09.003
    • (2012) Trends Pharmacol Sci. , vol.33 , pp. 17-27
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 2
    • 37549016836 scopus 로고    scopus 로고
    • Heterotrimeric G protein activation by G-protein-coupled receptors
    • PMID: 18043707
    • Oldham WM, Hamm HE. Heterotrimeric G protein activation by G-protein-coupled receptors. Nat Rev Mol Cell Biol. 2008; 9: 60-71. doi: 10.1038/nrm2299 PMID: 18043707
    • (2008) Nat Rev Mol Cell Biol. , vol.9 , pp. 60-71
    • Oldham, W.M.1    Hamm, H.E.2
  • 3
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the ?2 adrenergic receptor-Gs protein complex
    • 2011/07/21 ed. PMID: 21772288
    • Rasmussen SGF, DeVree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, et al. Crystal structure of the ?2 adrenergic receptor-Gs protein complex. Nature. 2011/07/21 ed. 2011; 477: 549-55. doi: 10.1038/nature10361 PMID: 21772288
    • (2011) Nature. , vol.477 , pp. 549-555
    • Rasmussen, S.G.F.1    DeVree, B.T.2    Zou, Y.3    Kruse, A.C.4    Chung, K.Y.5    Kobilka, T.S.6
  • 4
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Department of Biology Massachusetts Institute of Technology Cambridge MA 02139 USA. Available
    • Farrens DL, Altenbach C, Yang K, Hubbell WL, Khorana HG. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science (80-). Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.; 1996; 274: 768-770. Available: Http://www.ncbi.nlm.nih.gov/pubmed/8864113
    • (1996) Science (80-) , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 5
    • 52949102889 scopus 로고    scopus 로고
    • Crystal structure of opsin in its G-protein-interacting conformation
    • Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.: Nature Publishing Group Available
    • Scheerer P, Park JH, Hildebrand PW, Kim YJ, Krauss N, Choe H-W, et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature. Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.: Nature Publishing Group; 2008; 455: 497-502. Available: Http://www.nature.com/nature/journal/v455/n7212/abs/nature07330.html
    • (2008) Nature , vol.455 , pp. 497-502
    • Scheerer, P.1    Park, J.H.2    Hildebrand, P.W.3    Kim, Y.J.4    Krauss, N.5    Choe, H.-W.6
  • 6
    • 84889564886 scopus 로고    scopus 로고
    • Activation and allosteric modulation of a muscarinic acetylcholine receptor
    • Nature Publishing Group
    • Kruse AC, Ring AM, Manglik A, Hu J, Hu K, Eitel K, et al. Activation and allosteric modulation of a muscarinic acetylcholine receptor. Nature. Nature Publishing Group; 2013; 504: 101-6. doi: 10.1038/nature12735
    • (2013) Nature , vol.504 , pp. 101-106
    • Kruse, A.C.1    Ring, A.M.2    Manglik, A.3    Hu, J.4    Hu, K.5    Eitel, K.6
  • 8
    • 70350362562 scopus 로고    scopus 로고
    • A G protein-coupled receptor at work: The rhodopsin model
    • Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany. klaus-peter. hofmann@charite.de
    • Hofmann KP, Scheerer P, Hildebrand PW, Choe H-W, Park JH, Heck M, et al. A G protein-coupled receptor at work: The rhodopsin model. Trends Biochem Sci. Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany. klaus-peter. hofmann@charite.de; 2009; 34: 540-52. doi: 10.1016/j.tibs.2009.07.005
    • (2009) Trends Biochem Sci , vol.34 , pp. 540-552
    • Hofmann, K.P.1    Scheerer, P.2    Hildebrand, P.W.3    Choe, H.-W.4    Park, J.H.5    Heck, M.6
  • 9
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the ?(2) adrenergic receptor-Gs protein complex
    • 1] Department of Molecular and Cellular Physiology Stanford University School of Medicine, Stanford, California 94305, USA [2] , 2200 Copenhagen N, Denmark [3].: Nature Publishing Group Available
    • Rasmussen SGF, Devree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, et al. Crystal structure of the ? (2) adrenergic receptor-Gs protein complex. Nature. 1] Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305, USA [2] , 2200 Copenhagen N, Denmark [3].: Nature Publishing Group; 2011; 450: 383-387. Available: Http://eutils.ncbi.nlm.nih. gov/entrez/eutils/elink.fcgi?dbfrom = pubmed&id=21772288&retmode = ref&cmd = prlinks
    • (2011) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.F.1    Devree, B.T.2    Zou, Y.3    Kruse, A.C.4    Chung, K.Y.5    Kobilka, T.S.6
  • 10
    • 84932647495 scopus 로고    scopus 로고
    • Structural basis for nucleotide exchange in heterotrimeric G proteins
    • Dror RO, Mildorf TJ, Hilger D, Manglik A, Borhani DW, Arlow DH, et al. Structural basis for nucleotide exchange in heterotrimeric G proteins. Science (80-). 2015; 348: 1361-1365. doi: 10.1126/science. aaa5264
    • (2015) Science (80-). , vol.348 , pp. 1361-1365
    • Dror, R.O.1    Mildorf, T.J.2    Hilger, D.3    Manglik, A.4    Borhani, D.W.5    Arlow, D.H.6
  • 11
    • 84887443683 scopus 로고    scopus 로고
    • Molecular basis of cannabinoid CB1 receptor coupling to the G protein heterotrimer G?i: Identification of key CB1 contacts with the C-terminal helix ?5 of G?i
    • PMID: 24092756
    • Shim J-Y, Ahn KH, Kendall D a. Molecular basis of cannabinoid CB1 receptor coupling to the G protein heterotrimer G?i: Identification of key CB1 contacts with the C-terminal helix ?5 of G?i. J Biol Chem. 2013; 288: 32449-65. doi: 10.1074/jbc.M113.489153 PMID: 24092756
    • (2013) J Biol Chem. , vol.288 , pp. 32449-32465
    • Shim, J.-Y.1    Ahn, K.H.2    Kendall, D.A.3
  • 12
    • 84904488770 scopus 로고    scopus 로고
    • Structural basis of g protein-coupled receptor-gi protein interaction: Formation of the cannabinoid cb2 receptor/gi protein complex
    • Mnpotra JS, Qiao Z, Cai J, Lynch DL, Grossfield A, Leioatts N, et al. Structural Basis of G Protein-Coupled Receptor-Gi Protein Interaction: Formation of the Cannabinoid CB2 Receptor/Gi Protein Complex. J Biol Chem. 2014; 0-31. doi: 10.1074/jbc.M113.539916
    • (2014) J Biol Chem. , pp. 0-31
    • Mnpotra, J.S.1    Qiao, Z.2    Cai, J.3    Lynch, D.L.4    Grossfield, A.5    Leioatts, N.6
  • 13
    • 0035971240 scopus 로고    scopus 로고
    • Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: Initial rate analysis based on a double displacement mechanism
    • PMID: 11116153
    • Heck M, Hofmann KP. Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: Initial rate analysis based on a double displacement mechanism. J Biol Chem. 2001; 276: 10000-9. doi: 10.1074/jbc.M009475200 PMID: 11116153
    • (2001) J Biol Chem. , vol.276 , pp. 10000-10009
    • Heck, M.1    Hofmann, K.P.2
  • 14
    • 67649743779 scopus 로고    scopus 로고
    • Structural and kinetic modeling of an activating helix switch in the rhodopsin-transducin interface
    • Institut für Medizinische Physik und Biophysik (CC2) and. Available
    • Scheerer P, Heck M, Goede A, Park J, Choe H, Ernst OP, et al. Structural and kinetic modeling of an activating helix switch in the rhodopsin-transducin interface. Proc Natl Acad Sci U S A. Institut für Medizinische Physik und Biophysik (CC2) and.; 2009; 106: 10660-10665. Available: Http://www.pnas.org/content/106/26/10660.abstract
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 10660-10665
    • Scheerer, P.1    Heck, M.2    Goede, A.3    Park, J.4    Choe, H.5    Ernst, O.P.6
  • 15
    • 80053357815 scopus 로고    scopus 로고
    • Conformational changes in the G protein Gs induced by the ?2 adrenergic receptor
    • Nature Publishing Group Available
    • Chung KY, Rasmussen SGF, Liu T, Li S, Devree BT, Chae PS, et al. Conformational changes in the G protein Gs induced by the ?2 adrenergic receptor. Nature. Nature Publishing Group; 2011; 477: 611-615. Available: Http://www.nature.com/doifinder/10.1038/nature10488
    • (2011) Nature , vol.477 , pp. 611-615
    • Chung, K.Y.1    Rasmussen, S.G.F.2    Liu, T.3    Li, S.4    Devree, B.T.5    Chae, P.S.6
  • 16
    • 84922309763 scopus 로고    scopus 로고
    • Ghrelin receptor conformational dynamics regulate the transition from a preassembled to an active receptor:Gq complex
    • PMID: 25605885
    • Damian M, Mary S, Maingot M, M'Kadmi C, Gagne D, Leyris J-P, et al. Ghrelin receptor conformational dynamics regulate the transition from a preassembled to an active receptor:Gq complex. Proc Natl Acad Sci. 2015; 112: 1601-1606. doi: 10.1073/pnas.1414618112 PMID: 25605885
    • (2015) Proc Natl Acad Sci. , vol.112 , pp. 1601-1606
    • Damian, M.1    Mary, S.2    Maingot, M.3    M'Kadmi, C.4    Gagne, D.5    Leyris, J.-P.6
  • 17
    • 77956635542 scopus 로고    scopus 로고
    • Differential association modes of the thrombin receptor PAR1 with Galphai1 Galpha12 and beta-arrestin 1
    • PMID 20410441
    • Ayoub MA, Trinquet E, Pfleger KDG, Pin J-P. Differential association modes of the thrombin receptor PAR1 with Galphai1, Galpha12, and beta-arrestin 1. FASEB J. 2010; 24: 3522-3535. doi: 10.1096/fj. 10-154997 PMID: 20410441
    • (2010) FASEB J. , vol.24 , pp. 3522-3535
    • Ayoub, M.A.1    Trinquet, E.2    Pfleger, K.D.G.3    Pin, J.-P.4
  • 18
    • 0032516098 scopus 로고    scopus 로고
    • Light-activated rhodopsin induces structural binding motif in G protein alpha subunit
    • Institute for Biomedical Computing, Washington University Medical School, St. Louis, MO 63110, USA. Available
    • Kisselev OG, Kao J, Ponder JW, Fann YC, Gautam N, Marshall GR. Light-activated rhodopsin induces structural binding motif in G protein alpha subunit. Proc Natl Acad Sci U S A. Institute for Biomedical Computing, Washington University Medical School, St. Louis, MO 63110, USA.; 1998; 95: 4270-4275. Available: Http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom = pubmed&id= 9539726&retmode = ref&cmd = prlinks
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 4270-4275
    • Kisselev, O.G.1    Kao, J.2    Ponder, J.W.3    Fann, Y.C.4    Gautam, N.5    Marshall, G.R.6
  • 19
    • 0036385914 scopus 로고    scopus 로고
    • Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings
    • 2002/09/10 ed. S0022283602007453 [pii] PMID: 12217702
    • Koenig BW, Kontaxis G, Mitchell DC, Louis JM, Litman BJ, Bax A. Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings. J Mol Biol. 2002/09/10 ed. 2002; 322: 441-461. S0022283602007453 [pii] PMID: 12217702
    • (2002) J Mol Biol. , vol.322 , pp. 441-461
    • Koenig, B.W.1    Kontaxis, G.2    Mitchell, D.C.3    Louis, J.M.4    Litman, B.J.5    Bax, A.6
  • 20
    • 79953234218 scopus 로고    scopus 로고
    • Crystal structure of metarhodopsin II
    • Nature Publishing Group a division of Macmillan Publishers Limited. All Rights Reserved.
    • Choe H-W, Kim YJ, Park JH, Morizumi T, Pai EF, Krauss N, et al. Crystal structure of metarhodopsin II. Nature. Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.; 2011; 471: 651-5.
    • (2011) Nature , vol.471 , pp. 651-655
    • Choe, H.-W.1    Kim, Y.J.2    Park, J.H.3    Morizumi, T.4    Pai, E.F.5    Krauss, N.6
  • 21
    • 84855990615 scopus 로고    scopus 로고
    • Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II
    • Paul Scherrer Institut Villigen PSI 5232, Switzerland. Available
    • Deupi X, Edwards P, Singhal A, Nickle B, Oprian D, Schertler G, et al. Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II. Proc Natl Acad Sci U S A. Paul Scherrer Institut, Villigen PSI, 5232, Switzerland.; 2012; 109: 119-24. Available: Http://www.pnas.org/cgi/content/abstract/109/1/119
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 119-124
    • Deupi, X.1    Edwards, P.2    Singhal, A.3    Nickle, B.4    Oprian, D.5    Schertler, G.6
  • 22
    • 79953242234 scopus 로고    scopus 로고
    • The structural basis of agonist-induced activation in constitutively active rhodopsin
    • Standfuss J, Edwards PC, D'Antona A, Fransen M, Xie G, Oprian DD, et al. The structural basis of agonist-induced activation in constitutively active rhodopsin. Nature. 2011; 471: 656-60.
    • (2011) Nature. , vol.471 , pp. 656-660
    • Standfuss, J.1    Edwards, P.C.2    D'Antona, A.3    Fransen, M.4    Xie, G.5    Oprian, D.D.6
  • 23
    • 84879548723 scopus 로고    scopus 로고
    • The Role of Ligands on the Equilibria between Functional States of a
    • American Chemical Society
    • Kim TH, Chung KY, Manglik A, Hansen AL, Dror RO, Mildorf TJ, et al. The Role of Ligands on the Equilibria Between Functional States of a. J Am Chem Soc. American Chemical Society; 2013; 135: 9465-74. doi: 10.1021/ja404305k
    • (2013) J Am Chem Soc. , vol.135 , pp. 9465-9474
    • Kim, T.H.1    Chung, K.Y.2    Manglik, A.3    Hansen, A.L.4    Dror, R.O.5    Mildorf, T.J.6
  • 25
    • 84906088654 scopus 로고    scopus 로고
    • Position of transmembrane helix 6 determines receptor g protein coupling specificity
    • PMID: 25046433
    • Rose AS, Elgeti M, Zachariae U, Grubmüller H, Hofmann KP, Scheerer P, et al. Position of transmembrane helix 6 determines receptor g protein coupling specificity. J Am Chem Soc. 2014; 136: 11244-7. doi: 10.1021/ja5055109 PMID: 25046433
    • (2014) J Am Chem Soc. , vol.136 , pp. 11244-11247
    • Rose, A.S.1    Elgeti, M.2    Zachariae, U.3    Grubmüller, H.4    Hofmann, K.P.5    Scheerer, P.6
  • 26
    • 84893790121 scopus 로고    scopus 로고
    • Energetic analysis of the rhodopsin-G-protein complex links the ?5 helix to GDP release
    • PMID: 24292645
    • Alexander NS, Preininger AM, Kaya AI, Stein RA, Hamm HE, Meiler J. Energetic analysis of the rhodopsin-G-protein complex links the ?5 helix to GDP release. Nat Struct Mol Biol. 2014; 21: 56-63. doi: 10.1038/nsmb.2705 PMID: 24292645
    • (2014) Nat Struct Mol Biol. , vol.21 , pp. 56-63
    • Alexander, N.S.1    Preininger, A.M.2    Kaya, A.I.3    Stein, R.A.4    Hamm, H.E.5    Meiler, J.6
  • 27
    • 0036468995 scopus 로고    scopus 로고
    • Kinetic studies of protein-protein interactions
    • Available PMID: 11839488
    • Schreiber G. Kinetic studies of protein-protein interactions. Curr Opin Struct Biol. 2002; 12: 41-7. Available: Http://www.ncbi.nlm.nih.gov/pubmed/11839488 PMID: 11839488
    • (2002) Curr Opin Struct Biol. , vol.12 , pp. 41-47
    • Schreiber, G.1
  • 28
    • 0025036350 scopus 로고
    • Rhodopsin mutants that bind but fail to activate transducin
    • Department of Biology Massachusetts Institute of Technology Cambridge 02139.
    • Franke R, Konig B, Sakmar T, Khorana H, Hofmann K. Rhodopsin mutants that bind but fail to activate transducin. Science (80-). Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.; 1990; 250: 123-125. doi: 10.1126/science.2218504
    • (1990) Science (80-) , vol.250 , pp. 123-125
    • Franke, R.1    Konig, B.2    Sakmar, T.3    Khorana, H.4    Hofmann, K.5
  • 29
    • 0028946950 scopus 로고
    • Characterization of rhodopsin mutants that bind transducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release, and flash-induced light-scattering assays
    • Howard Hughes Medical Institute, Laboratory of Molecular Biology and Biochemistry, Rockefeller University, New York, New York 10021, USA. Available
    • Ernst OP, Hofmann KP, Sakmar TP. Characterization of rhodopsin mutants that bind transducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release, and flash-induced light-scattering assays. J Biol Chem. Howard Hughes Medical Institute, Laboratory of Molecular Biology and Biochemistry, Rockefeller University, New York, New York 10021, USA.; 1995; 270: 10580-10586. Available: Http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi? dbfrom = pubmed&id=7737995&retmode = ref&cmd = prlinks
    • (1995) J Biol Chem , vol.270 , pp. 10580-10586
    • Ernst, O.P.1    Hofmann, K.P.2    Sakmar, T.P.3
  • 30
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H, Sligar S, Wolynes P. The energy landscapes and motions of proteins. Science (80-). 1991; 254: 1598-1603. doi: 10.1126/science.1749933
    • (1991) Science (80-). , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.2    Wolynes, P.3
  • 31
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-proteincoupled receptor opsin
    • Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.: Nature Publishing Group Available
    • Park JH, Scheerer P, Hofmann KP, Choe H-W, Ernst OP. Crystal structure of the ligand-free G-proteincoupled receptor opsin. Nature. Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.: Nature Publishing Group; 2008; 454: 183-187. Available: Http://www.nature.com/nature/journal/v454/n7201/abs/nature07063.html
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.-W.4    Ernst, O.P.5
  • 32
    • 0034723294 scopus 로고    scopus 로고
    • Rhodopsin recognition by mutant gs containing c-terminal residues of transducin
    • PMID 10644728
    • Natochin M, Muradov KG, McEntaffer RL, Artemyev NO. Rhodopsin Recognition by Mutant Gs Containing C-terminal Residues of Transducin. J Biol Chem. 2000; 275: 2669-2675. doi: 10.1074/jbc.275. 4.2669 PMID: 10644728
    • (2000) J Biol Chem. , vol.275 , pp. 2669-2675
    • Natochin, M.1    Muradov, K.G.2    McEntaffer, R.L.3    Artemyev, N.O.4
  • 33
    • 0023518498 scopus 로고
    • The hydrophobic tryptic core of the beta-adrenergic receptor retains Gs regulatory activity in response to agonists and thiols
    • Available PMID: 2890639
    • Rubenstein RC, Wong SK, Ross EM. The hydrophobic tryptic core of the beta-adrenergic receptor retains Gs regulatory activity in response to agonists and thiols. J Biol Chem. 1987; 262: 16655-16662. Available: Http://www.jbc.org/cgi/content/abstract/262/34/16655 PMID: 2890639
    • (1987) J Biol Chem. , vol.262 , pp. 16655-16662
    • Rubenstein, R.C.1    Wong, S.K.2    Ross, E.M.3
  • 34
    • 67649755549 scopus 로고    scopus 로고
    • SuperLooper-a prediction server for the modeling of loops in globular and membrane proteins
    • Institute of Medical Physics and Biophysics Charité, University of Medicine, Berlin, Germany. peter.hildebrand@-charite.de: Oxford University Press
    • Hildebrand PW, Goede A, Bauer RA, Gruening B, Ismer J, Michalsky E, et al. SuperLooper-a prediction server for the modeling of loops in globular and membrane proteins. Nucleic Acids Res. Institute of Medical Physics and Biophysics, Charité, University of Medicine, Berlin, Germany. peter.hildebrand@-charite.de: Oxford University Press; 2009; 37: W571-4. doi: 10.1093/nar/gkp338
    • (2009) Nucleic Acids Res , vol.37 , pp. 571-574
    • Hildebrand, P.W.1    Goede, A.2    Bauer, R.A.3    Gruening, B.4    Ismer, J.5    Michalsky, E.6
  • 35
    • 0041919542 scopus 로고    scopus 로고
    • Improved protein-ligand docking using GOLD
    • Available PMID: 12910460
    • Verdonk ML, Cole JC, Hartshorn MJ, Murray CW, Taylor RD. Improved protein-ligand docking using GOLD. Proteins. 2003; 52: 609-23. Available: Http://www.ncbi.nlm.nih.gov/pubmed/12910460 PMID: 12910460
    • (2003) Proteins. , vol.52 , pp. 609-623
    • Verdonk, M.L.1    Cole, J.C.2    Hartshorn, M.J.3    Murray, C.W.4    Taylor, R.D.5
  • 36
    • 46249092554 scopus 로고    scopus 로고
    • Gromacs 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • American Chemical Society
    • Hess B, Kutzner C, Van Der Spoel D, Lindahl E. GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. J Chem Theory Comput. American Chemical Society; 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
  • 37
    • 77954256616 scopus 로고    scopus 로고
    • G-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation
    • PMID: 20336801
    • Wolf MG, 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: 2169-74. doi: 10.1002/jcc.21507 PMID: 20336801
    • (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
  • 38
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Available PMID: 9129804
    • Berger O, Edholm O. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys J. 1997; 72: 2002-2013. Available: Http://www.sciencedirect.com/science/article/pii/S0006349597788453 PMID: 9129804
    • (1997) Biophys J. , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2
  • 39
    • 1242346370 scopus 로고
    • The missing term in effective pair potentials
    • Inst Fis Liquidos & Sistemas Biol,Ra-1900 La Plata Argentina Available
    • Berendsen HJC, Grigera JR, Straatsma TP. The Missing Term in Effective Pair Potentials. J Phys Chem. Inst Fis Liquidos & Sistemas Biol,Ra-1900 La Plata,Argentina; 1987; 91: 6269-6271. Available: Http://links.isiglobalnet2.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth = mekentosj&SrcApp= Papers&DestLinkType=FullRecord&DestApp=WOS&KeyUT=A1987K994100038
    • (1987) J Phys Chem , vol.91 , pp. 6269-6271
    • Berendsen, H.J.C.1    Grigera, J.R.2    Straatsma, T.P.3
  • 40
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the Amber ff99SB protein force field
    • Shaw Research, New York, New York 10036, USA. Available
    • Lindorff-Larsen K, Piana S, Palmo K, Maragakis P, Klepeis JL, Dror RO, et al. Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins. D. E. Shaw Research, New York, New York 10036, USA.; 2010; 78: 1950-1958. Available: Http://sfx.mpg.de/sfx-local?id = doi:10.1002/prot. 22711
    • (2010) Proteins. D. E. , vol.78 , pp. 1950-1958
    • Lindorff-Larsen, K.1    Piana, S.2    Palmo, K.3    Maragakis, P.4    Klepeis, J.L.5    Dror, R.O.6
  • 41
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of proteinligand complexes
    • Division of Biological Chemistry and Molecular Microbiology, Wellcome Trust Biocentre, School of Life Sciences, University of Dundee, Dow Street, DD1 5EH, Scotland.
    • Schüttelkopf AW, Van Aalten DMF. PRODRG: A ToOl fOr hIgH-ThRoUgHpUt cRyStAlLoGrApHy oF Proteinligand complexes. Acta Crystallogr D Biol Crystallogr. Division of Biological Chemistry and Molecular Microbiology, Wellcome Trust Biocentre, School of Life Sciences, University of Dundee, Dow Street, DD1 5EH, Scotland.; 2004; 60: 1355-63. doi: 10.1107/S0907444904011679
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1355-1363
    • Schüttelkopf, A.W.1    Van Aalten, D.M.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.