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Volumn 805, Issue , 2014, Pages 441-457

Chemosensorial G-proteins-coupled receptors: A perspective from computational methods

Author keywords

Bioinformatics; G protein coupled receptors; Molecular dynamics; Multi scale modeling; Odor and bitter taste perception

Indexed keywords

ADENYLATE CYCLASE; CALMODULIN; CHLORIDE CHANNEL; CYCLIC NUCLEOTIDE GATED CHANNEL; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 84896915850     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-319-02970-2_18     Document Type: Article
Times cited : (4)

References (105)
  • 4
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human 2-Adrenergic G protein-coupled receptor
    • Cherezov V, Rosenbaum DM, Hanson MA, Rasmussen SGF, Thian FS et al (2007) High-resolution crystal structure of an engineered human 2-Adrenergic G protein-coupled receptor. Science 318:1258-1265
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1    Rosenbaum, D.M.2    Hanson, M.A.3    Rasmussen, S.G.F.4    Thian, F.S.5
  • 5
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the human beta2 adrenergic G-protein-coupled receptor
    • Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS et al (2007) Crystal structure of the human beta2 adrenergic G-protein-coupled receptor. Nature 450:383-387
    • (2007) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.1    Choi, H.J.2    Rosenbaum, D.M.3    Kobilka, T.S.4    Thian, F.S.5
  • 6
    • 0033572358 scopus 로고    scopus 로고
    • The G protein subunit gene families
    • Downes GB, Gautam N (1999) The G protein subunit gene families. Genomics 62:544-552
    • (1999) Genomics , vol.62 , pp. 544-552
    • Downes, G.B.1    Gautam, N.2
  • 7
    • 60149095122 scopus 로고    scopus 로고
    • Structural determinants involved in the formation and activation of G protein betagamma dimers
    • McIntire WE (2009) Structural determinants involved in the formation and activation of G protein betagamma dimers. Neurosignals 17:82-99
    • (2009) Neurosignals , vol.17 , pp. 82-99
    • McIntire, W.E.1
  • 8
    • 0029593456 scopus 로고
    • The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2
    • Wall MA, Coleman DE, Lee E, Iñiguez-Lluhi JA, Posner BA et al (1995) The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2. Cell 83:1047-1058
    • (1995) Cell , vol.83 , pp. 1047-1058
    • Wall, M.A.1    Coleman, D.E.2    Lee, E.3    Iñiguez-Lluhi, J.A.4    Posner, B.A.5
  • 9
    • 84858120018 scopus 로고    scopus 로고
    • Ice breaking in GPCR structural biology
    • Zhao Q, B-l W (2012) Ice breaking in GPCR structural biology. Acta Pharmacol Sin 33:324-334
    • (2012) Acta Pharmacol Sin , vol.33 , pp. 324-334
    • Zhao, Q.1    B-l, W.2
  • 10
    • 84878112106 scopus 로고    scopus 로고
    • Structure of the human smoothened receptor bound to an antitumour agent
    • doi:10.1038/nature12167
    • Wang C, Wu H, Katritch V, Han GW, Huang XP et al (2013) Structure of the human smoothened receptor bound to an antitumour agent. Nature. doi:10.1038/nature12167
    • (2013) Nature
    • Wang, C.1    Wu, H.2    Katritch, V.3    Han, G.W.4    Huang, X.P.5
  • 12
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G protein-coupled receptors and significance for drug discovery
    • Lagerstrom MC, Schioth HB (2008) Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat Rev Drug Discov 7:339-357
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 339-357
    • Lagerstrom, M.C.1    Schioth, H.B.2
  • 13
    • 84856511452 scopus 로고    scopus 로고
    • Domain coupling in GPCRs: The engine for induced conformational changes
    • Unal H, Karnik SS (2012) Domain coupling in GPCRs: The engine for induced conformational changes. Trends Pharmacol Sci 33:79-88
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 79-88
    • Unal, H.1    Karnik, S.S.2
  • 14
    • 84870563233 scopus 로고    scopus 로고
    • GI functions of GPR39: Novel biology
    • Depoortere I (2012) GI functions of GPR39: Novel biology. Curr Opin Pharmacol 12:647-652
    • (2012) Curr Opin Pharmacol , vol.12 , pp. 647-652
    • Depoortere, I.1
  • 15
    • 84867840947 scopus 로고    scopus 로고
    • Structure of the agonist-bound neurotensin receptor
    • White JF, Noinaj N, Shibata Y, Love J, Kloss B et al (2012) Structure of the agonist-bound neurotensin receptor. Nature 490:508-513
    • (2012) Nature , vol.490 , pp. 508-513
    • White, J.F.1    Noinaj, N.2    Shibata, Y.3    Love, J.4    Kloss, B.5
  • 16
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang S (1997) G protein mechanisms: Insights from structural analysis. Annu Rev Biochem 66:639-678
    • (1997) Annu Rev Biochem , vol.66 , pp. 639-678
    • Sprang, S.1
  • 17
    • 77953252509 scopus 로고    scopus 로고
    • The quest to understand heterotrimeric G protein signaling
    • Tesmer JJ (2010) The quest to understand heterotrimeric G protein signaling. Nat Struct Mol Biol 17:650-652
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 650-652
    • Tesmer, J.J.1
  • 18
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: Critical elements in the control of small G proteins
    • Bos JL, Rehmann H, Wittinghofer A (2007) GEFs and GAPs: Critical elements in the control of small G proteins. Cell 129:865-877
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 19
    • 80053357815 scopus 로고    scopus 로고
    • Conformational changes in the G protein Gs induced by the 2 adrenergic receptor
    • Chung KY, Rasmussen SG, Liu T, Li S, DeVree BT et al (2011) Conformational changes in the G protein Gs induced by the 2 adrenergic receptor. Nature 477:611-615
    • (2011) Nature , vol.477 , pp. 611-615
    • Chung, K.Y.1    Rasmussen, S.G.2    Liu, T.3    Li, S.4    DeVree, B.T.5
  • 20
    • 80053141840 scopus 로고    scopus 로고
    • Structural flexibility of the G alpha s alpha-helical domain in the beta2-Adrenoceptor Gs complex
    • Westfield GH, Rasmussen SG, Su M, Dutta S, DeVree BT et al (2011) Structural flexibility of the G alpha s alpha-helical domain in the beta2-Adrenoceptor Gs complex. Proc Natl Acad Sci USA 108:16086-16091
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 16086-16091
    • Westfield, G.H.1    Rasmussen, S.G.2    Su, M.3    Dutta, S.4    DeVree, B.T.5
  • 23
    • 80051811105 scopus 로고    scopus 로고
    • Computational molecular biology approaches to ligand-Target interactions
    • Lupieri P, Nguyen CH, Bafghi ZG, Giorgetti A, Carloni P (2009) Computational molecular biology approaches to ligand-Target interactions. HFSP J 3:228-239
    • (2009) HFSP J , vol.3 , pp. 228-239
    • Lupieri, P.1    Nguyen, C.H.2    Bafghi, Z.G.3    Giorgetti, A.4    Carloni, P.5
  • 24
    • 37549016836 scopus 로고    scopus 로고
    • Heterotrimeric G protein activation by G-protein-coupled receptors
    • Oldham W (2008) Heterotrimeric G protein activation by G-protein-coupled receptors. Nat Rev Mol Cell Biol 9:60-71
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 60-71
    • Oldham, W.1
  • 25
    • 0036301043 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated ion channels
    • Kaupp UB, Seifert R (2002) Cyclic nucleotide-gated ion channels. Physiol Rev 82:769-824
    • (2002) Physiol Rev , vol.82 , pp. 769-824
    • Kaupp, U.B.1    Seifert, R.2
  • 26
    • 33646553933 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated ion channels in sensory transduction
    • Pifferi S, Boccaccio A, Menini A (2006) Cyclic nucleotide-gated ion channels in sensory transduction. FEBS Lett 580:2853-2859
    • (2006) FEBS Lett , vol.580 , pp. 2853-2859
    • Pifferi, S.1    Boccaccio, A.2    Menini, A.3
  • 27
    • 0027500632 scopus 로고
    • The cyclic nucleotide-Activated conductance in olfactory cilia: Effects of cytoplasmic Mg2C and Ca2C
    • Kleene SJ (1993) The cyclic nucleotide-Activated conductance in olfactory cilia: Effects of cytoplasmic Mg2C and Ca2C. J Membr Biol 131:237-243
    • (1993) J Membr Biol , vol.131 , pp. 237-243
    • Kleene, S.J.1
  • 28
    • 0027491955 scopus 로고
    • Nonlinear amplification by calcium-dependent chloride channels in olfactory receptor cells
    • Lowe G, Gold GH (1993) Nonlinear amplification by calcium-dependent chloride channels in olfactory receptor cells. Nature 366:283-286
    • (1993) Nature , vol.366 , pp. 283-286
    • Lowe, G.1    Gold, G.H.2
  • 29
    • 0034005530 scopus 로고    scopus 로고
    • Determination of fractional calcium ion current in cyclic nucleotide-gated channels
    • Frings S, Hackos DH, Dzeja C, Ohyama T, Hagen V et al (2000) Determination of fractional calcium ion current in cyclic nucleotide-gated channels. Methods Enzymol 315:797-817
    • (2000) Methods Enzymol , vol.315 , pp. 797-817
    • Frings, S.1    Hackos, D.H.2    Dzeja, C.3    Ohyama, T.4    Hagen, V.5
  • 30
    • 0033178821 scopus 로고    scopus 로고
    • Calcium signalling and regulation in olfactory neurons
    • Menini A (1999) Calcium signalling and regulation in olfactory neurons. Curr Opin Neurobiol 9:419-426
    • (1999) Curr Opin Neurobiol , vol.9 , pp. 419-426
    • Menini, A.1
  • 31
    • 0035855833 scopus 로고    scopus 로고
    • How the olfactory system makes sense of scents
    • Firestein S (2001) How the olfactory system makes sense of scents. Nature 413:211-218
    • (2001) Nature , vol.413 , pp. 211-218
    • Firestein, S.1
  • 33
    • 0034611738 scopus 로고    scopus 로고
    • A family of candidate taste receptors in human and mouse
    • Matsunami H, Montmayeur J-P, Buck LB (2000) A family of candidate taste receptors in human and mouse. Nature 404:601-604
    • (2000) Nature , vol.404 , pp. 601-604
    • Matsunami, H.1    Montmayeur, J.-P.2    Buck, L.B.3
  • 34
    • 77957871915 scopus 로고    scopus 로고
    • Insights into the binding of phenyltiocarbamide (PTC) agonist to its target human TAS2R38 bitter receptor
    • Biarnes X, Marchiori A, Giorgetti A, Lanzara C, Gasparini P et al (2010) Insights into the binding of phenyltiocarbamide (PTC) agonist to its target human TAS2R38 bitter receptor. PLoS One 5:e12394
    • (2010) PLoS One , vol.5
    • Biarnes, X.1    Marchiori, A.2    Giorgetti, A.3    Lanzara, C.4    Gasparini, P.5
  • 35
    • 30744472932 scopus 로고    scopus 로고
    • Contrasting modes of evolution between vertebrate sweet/umami receptor genes and bitter receptor genes
    • Shi P, Zhang J (2006) Contrasting modes of evolution between vertebrate sweet/umami receptor genes and bitter receptor genes. Mol Biol Evol 23:292-300
    • (2006) Mol Biol Evol , vol.23 , pp. 292-300
    • Shi, P.1    Zhang, J.2
  • 36
    • 13944250257 scopus 로고    scopus 로고
    • The molecular basis of individual differences in phenylthiocarbamide and propylthiouracil bitterness perception
    • Bufe B, Breslin PA, Kuhn C, Reed DR, Tharp CD et al (2005) The molecular basis of individual differences in phenylthiocarbamide and propylthiouracil bitterness perception. Curr Biol 15:322-327
    • (2005) Curr Biol , vol.15 , pp. 322-327
    • Bufe, B.1    Breslin, P.A.2    Kuhn, C.3    Reed, D.R.4    Tharp, C.D.5
  • 37
    • 61449135187 scopus 로고    scopus 로고
    • Real-Time analysis of amyloid fibril formation of alpha-synuclein using a fibrillation-state-specific fluorescent probe of JC-1
    • Lee JH, Lee IH, Choe YJ, Kang S, Kim HY et al (2009) Real-Time analysis of amyloid fibril formation of alpha-synuclein using a fibrillation-state- specific fluorescent probe of JC-1. Biochem J 418:311-323
    • (2009) Biochem J , vol.418 , pp. 311-323
    • Lee, J.H.1    Lee, I.H.2    Choe, Y.J.3    Kang, S.4    Kim, H.Y.5
  • 38
    • 0037016771 scopus 로고    scopus 로고
    • Molecular mechanisms of bitter and sweet taste transduction
    • Margolskee RF (2002) Molecular mechanisms of bitter and sweet taste transduction. J Biol Chem 277:1-4
    • (2002) J Biol Chem , vol.277 , pp. 1-4
    • Margolskee, R.F.1
  • 40
    • 56549111367 scopus 로고    scopus 로고
    • The evolution of animal chemosensory receptor gene repertoires: Roles of chance and necessity
    • Nei M, Niimura Y, Nozawa M (2008) The evolution of animal chemosensory receptor gene repertoires: Roles of chance and necessity. Nat Rev Genet 9:951-963
    • (2008) Nat Rev Genet , vol.9 , pp. 951-963
    • Nei, M.1    Niimura, Y.2    Nozawa, M.3
  • 41
    • 84863242886 scopus 로고    scopus 로고
    • CRDB: Database of chemosensory receptor gene families in vertebrate
    • Dong D, Jin K, Wu X, Zhong Y (2012) CRDB: Database of chemosensory receptor gene families in vertebrate. PLoS One 7:e31540
    • (2012) PLoS One , vol.7
    • Dong, D.1    Jin, K.2    Wu, X.3    Zhong, Y.4
  • 42
    • 79955811328 scopus 로고    scopus 로고
    • Recent progress in the study of G protein-coupled receptors with molecular dynamics computer simulations
    • Grossfield A (2011) Recent progress in the study of G protein-coupled receptors with molecular dynamics computer simulations. Biochim Biophys Acta 1808:1868-1878
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 1868-1878
    • Grossfield, A.1
  • 43
    • 80052077522 scopus 로고    scopus 로고
    • Showcasing modern molecular dynamics simulations of membrane proteins through G protein-coupled receptors
    • Johnston JM, Filizola M (2011) Showcasing modern molecular dynamics simulations of membrane proteins through G protein-coupled receptors. Curr Opin Struct Biol 21:552-558
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 552-558
    • Johnston, J.M.1    Filizola, M.2
  • 44
    • 84859887931 scopus 로고    scopus 로고
    • Molecular dynamics simulations of G protein-coupled receptors
    • Bruno A, Costantino G (2012) Molecular dynamics simulations of G protein-coupled receptors. Mol Inform 31:222-230
    • (2012) Mol Inform , vol.31 , pp. 222-230
    • Bruno, A.1    Costantino, G.2
  • 45
    • 66149189210 scopus 로고    scopus 로고
    • G protein inactive and active forms investigated by simulation methods
    • Khafizov K, Lattanzi G, Carloni P (2009) G protein inactive and active forms investigated by simulation methods. Proteins 75:919-930
    • (2009) Proteins , vol.75 , pp. 919-930
    • Khafizov, K.1    Lattanzi, G.2    Carloni, P.3
  • 46
    • 0034042247 scopus 로고    scopus 로고
    • Analysis of the molecular basis for octanal interactions in the expressed rat 17 olfactory receptor
    • Singer MS (2000) Analysis of the molecular basis for octanal interactions in the expressed rat 17 olfactory receptor. Chem Senses 25:155-165
    • (2000) Chem Senses , vol.25 , pp. 155-165
    • Singer, M.S.1
  • 47
    • 16644373208 scopus 로고    scopus 로고
    • Making sense of olfaction through predictions of the 3-D structure and function of olfactory receptors
    • Floriano WB, Vaidehi N, Goddard WA 3rd (2004) Making sense of olfaction through predictions of the 3-D structure and function of olfactory receptors. Chem Senses 29:269-290
    • (2004) Chem Senses , vol.29 , pp. 269-290
    • Floriano, W.B.1    Vaidehi, N.2    Goddard III, W.A.3
  • 48
    • 34249817116 scopus 로고    scopus 로고
    • 3-Dimensional structures of G protein-coupled receptors and binding sites of agonists and antagonists
    • discussion 1548S
    • Goddard WA 3rd, Abrol R (2007) 3-Dimensional structures of G protein-coupled receptors and binding sites of agonists and antagonists. J Nutr 137:1528S-1538S; discussion 1548S
    • (2007) J Nutr , vol.137
    • Goddard III, W.A.1    Abrol, R.2
  • 49
    • 0028338534 scopus 로고
    • GCRDb: A G-protein-coupled receptor database
    • Kolakowski LF Jr (1994) GCRDb: A G-protein-coupled receptor database. Receptors Channels 2:1-7
    • (1994) Receptors Channels , vol.2 , pp. 1-7
    • Kolakowski Jr., L.F.1
  • 51
    • 56749103466 scopus 로고    scopus 로고
    • The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist
    • Jaakola VP, Griffith MT, Hanson MA, Cherezov V, Chien EY et al (2008) The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322:1211-1217
    • (2008) Science , vol.322 , pp. 1211-1217
    • Jaakola, V.P.1    Griffith, M.T.2    Hanson, M.A.3    Cherezov, V.4    Chien, E.Y.5
  • 52
    • 43949095157 scopus 로고    scopus 로고
    • On the applicability of GPCR homology models to computer-Aided drug discovery: A comparison between in silico and crystal structures of the beta2-Adrenergic receptor
    • Costanzi S (2008) On the applicability of GPCR homology models to computer-Aided drug discovery: A comparison between in silico and crystal structures of the beta2-Adrenergic receptor. J Med Chem 51:2907-2914
    • (2008) J Med Chem , vol.51 , pp. 2907-2914
    • Costanzi, S.1
  • 53
    • 41149147416 scopus 로고    scopus 로고
    • Homology modeling of the serotonin transporter: Insights into the primary escitalopram-binding site
    • Jorgensen AM, Tagmose L, Jorgensen AM, Topiol S, Sabio M et al (2007) Homology modeling of the serotonin transporter: Insights into the primary escitalopram-binding site. ChemMedChem 2:815-826
    • (2007) ChemMedChem , vol.2 , pp. 815-826
    • Jorgensen, A.M.1    Tagmose, L.2    Jorgensen, A.M.3    Topiol, S.4    Sabio, M.5
  • 54
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors
    • Academic Press, San Diego
    • Ballesteros JA, Weinstein H, Stuart CS (1995) Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors. In: Methods in neurosciences. Academic Press, San Diego, pp 366-428
    • (1995) Methods In Neurosciences , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2    Stuart, C.S.3
  • 55
    • 14044270215 scopus 로고    scopus 로고
    • Structural basis for a broad but selective ligand spectrum of a mouse olfactory receptor: Mapping the odorant-binding site
    • Katada S, Hirokawa T, Oka Y, Suwa M, Touhara K (2005) Structural basis for a broad but selective ligand spectrum of a mouse olfactory receptor: Mapping the odorant-binding site. J Neurosci 25:1806-1815
    • (2005) J Neurosci , vol.25 , pp. 1806-1815
    • Katada, S.1    Hirokawa, T.2    Oka, Y.3    Suwa, M.4    Touhara, K.5
  • 57
    • 33748355624 scopus 로고    scopus 로고
    • Probing the activation-promoted structural rearrangements in preassembled receptor-G protein complexes
    • Gales C, Van Durm JJ, Schaak S, Pontier S, Percherancier Y et al (2006) Probing the activation-promoted structural rearrangements in preassembled receptor-G protein complexes. Nat Struct Mol Biol 13:778-786
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 778-786
    • Gales, C.1    Van Durm, J.J.2    Schaak, S.3    Pontier, S.4    Percherancier, Y.5
  • 58
    • 33751119043 scopus 로고    scopus 로고
    • The receptorbound empty pocket' state of the heterotrimeric G-protein alpha-subunit is conformationally dynamic
    • Abdulaev NG, Ngo T, Ramon E, Brabazon DM, Marino JP et al (2006) The receptorbound empty pocket' state of the heterotrimeric G-protein alpha-subunit is conformationally dynamic. Biochemistry 45:12986-12997
    • (2006) Biochemistry , vol.45 , pp. 12986-12997
    • Abdulaev, N.G.1    Ngo, T.2    Ramon, E.3    Brabazon, D.M.4    Marino, J.P.5
  • 59
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function
    • Kristiansen K (2004) Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol Ther 103:21-80
    • (2004) Pharmacol Ther , vol.103 , pp. 21-80
    • Kristiansen, K.1
  • 60
    • 33750702165 scopus 로고    scopus 로고
    • Structural basis of function in heterotrimeric G proteins
    • Oldham WM, Hamm HE (2006) Structural basis of function in heterotrimeric G proteins. Q Rev Biophys 39:117-166
    • (2006) Q Rev Biophys , vol.39 , pp. 117-166
    • Oldham, W.M.1    Hamm, H.E.2
  • 61
    • 34547157646 scopus 로고    scopus 로고
    • Receptor-mediated activation of heterotrimeric Gproteins: Current structural insights
    • Johnston CA, Siderovski DP (2007) Receptor-mediated activation of heterotrimeric Gproteins: Current structural insights. Mol Pharmacol 72:219-230
    • (2007) Mol Pharmacol , vol.72 , pp. 219-230
    • Johnston, C.A.1    Siderovski, D.P.2
  • 62
    • 1842851911 scopus 로고    scopus 로고
    • Molecular dynamics simulations of transducin: Interdomain and front to back communication in activation and nucleotide exchange
    • Ceruso MA, Periole X, Weinstein H (2004) Molecular dynamics simulations of transducin: Interdomain and front to back communication in activation and nucleotide exchange. J Mol Biol 338:469-481
    • (2004) J Mol Biol , vol.338 , pp. 469-481
    • Ceruso, M.A.1    Periole, X.2    Weinstein, H.3
  • 63
    • 0032478195 scopus 로고    scopus 로고
    • Dynamic properties of the guanine nucleotide binding protein alpha subunit and comparison of its guanosine triphosphate hydrolase domain with that of ras p21
    • Mello LV, van Aalten DM, Findlay JB (1998) Dynamic properties of the guanine nucleotide binding protein alpha subunit and comparison of its guanosine triphosphate hydrolase domain with that of ras p21. Biochemistry 37:3137-3142
    • (1998) Biochemistry , vol.37 , pp. 3137-3142
    • Mello, L.V.1    Van Aalten, D.M.2    Findlay, J.B.3
  • 64
    • 0032530652 scopus 로고    scopus 로고
    • Structural basis of activity and subunit recognition in G protein heterotrimers
    • Wall MA, Posner BA, Sprang SR (1998) Structural basis of activity and subunit recognition in G protein heterotrimers. Structure 6:1169-1183
    • (1998) Structure , vol.6 , pp. 1169-1183
    • Wall, M.A.1    Posner, B.A.2    Sprang, S.R.3
  • 65
    • 0035040818 scopus 로고    scopus 로고
    • Regulation and role of adenylyl cyclase isoforms
    • Hanoune J, Defer N (2001) Regulation and role of adenylyl cyclase isoforms. Annu Rev Pharmacol Toxicol 41:145-174
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 145-174
    • Hanoune, J.1    Defer, N.2
  • 66
    • 2642689663 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha
    • Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR (1997) Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha. GTPgammaS. Science 278:1907-1916
    • (1997) GTPgammaS. Science , vol.278 , pp. 1907-1916
    • Tesmer, J.J.1    Sunahara, R.K.2    Gilman, A.G.3    Sprang, S.R.4
  • 67
    • 36248969224 scopus 로고    scopus 로고
    • Function and dysfunction of CNG channels: Insights from channelopathies and mouse models
    • Biel M, Michalakis S (2007) Function and dysfunction of CNG channels: Insights from channelopathies and mouse models. Mol Neurobiol 35:266-277
    • (2007) Mol Neurobiol , vol.35 , pp. 266-277
    • Biel, M.1    Michalakis, S.2
  • 68
    • 33845623303 scopus 로고    scopus 로고
    • Origin of functional diversity among tetrameric voltagegated channels
    • Anselmi C, Carloni P, Torre V (2007) Origin of functional diversity among tetrameric voltagegated channels. Proteins 66:136-146
    • (2007) Proteins , vol.66 , pp. 136-146
    • Anselmi, C.1    Carloni, P.2    Torre, V.3
  • 71
    • 84856431269 scopus 로고    scopus 로고
    • Anoctamin 2/TMEM16B: A calcium-Activated chloride channel in olfactory transduction
    • Pifferi S, Cenedese V, Menini A (2012) Anoctamin 2/TMEM16B: A calcium-Activated chloride channel in olfactory transduction. Exp Physiol 97:193-199
    • (2012) Exp Physiol , vol.97 , pp. 193-199
    • Pifferi, S.1    Cenedese, V.2    Menini, A.3
  • 72
    • 42149185064 scopus 로고    scopus 로고
    • Molecular physiology of bestrophins: Multifunctional membrane proteins linked to best disease and other retinopathies
    • Hartzell HC, Qu Z, Yu K, Xiao Q, Chien LT (2008) Molecular physiology of bestrophins: Multifunctional membrane proteins linked to best disease and other retinopathies. Physiol Rev 88:639-672
    • (2008) Physiol Rev , vol.88 , pp. 639-672
    • Hartzell, H.C.1    Qu, Z.2    Yu, K.3    Xiao, Q.4    Chien, L.T.5
  • 73
    • 33748032396 scopus 로고    scopus 로고
    • Bestrophin-2 is a candidate calcium-Activated chloride channel involved in olfactory transduction
    • Pifferi S, Pascarella G, Boccaccio A, Mazzatenta A, Gustincich S et al (2006) Bestrophin-2 is a candidate calcium-Activated chloride channel involved in olfactory transduction. Proc Natl Acad Sci USA 103:12929-12934
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12929-12934
    • Pifferi, S.1    Pascarella, G.2    Boccaccio, A.3    Mazzatenta, A.4    Gustincich, S.5
  • 74
    • 34447567192 scopus 로고    scopus 로고
    • Temporal development of cyclic nucleotide-gated and Ca2C -Activated Cl currents in isolated mouse olfactory sensory neurons
    • Boccaccio A, Menini A (2007) Temporal development of cyclic nucleotide-gated and Ca2C -Activated Cl-currents in isolated mouse olfactory sensory neurons. J Neurophysiol 98:153-160
    • (2007) J Neurophysiol , vol.98 , pp. 153-160
    • Boccaccio, A.1    Menini, A.2
  • 75
    • 69949085891 scopus 로고    scopus 로고
    • Calciumactivated chloride currents in olfactory sensory neurons from mice lacking bestrophin-2
    • Pifferi S, Dibattista M, Sagheddu C, Boccaccio A, Al Qteishat A et al (2009) Calciumactivated chloride currents in olfactory sensory neurons from mice lacking bestrophin-2. J Physiol 587:4265-4279
    • (2009) J Physiol , vol.587 , pp. 4265-4279
    • Pifferi, S.1    Dibattista, M.2    Sagheddu, C.3    Boccaccio, A.4    Al Qteishat, A.5
  • 76
    • 0036083537 scopus 로고    scopus 로고
    • Molecular structure and physiological function of chloride channels
    • Jentsch TJ, Stein V, Weinreich F, Zdebik AA (2002) Molecular structure and physiological function of chloride channels. Physiol Rev 82:503-568
    • (2002) Physiol Rev , vol.82 , pp. 503-568
    • Jentsch, T.J.1    Stein, V.2    Weinreich, F.3    Zdebik, A.A.4
  • 77
    • 21244486285 scopus 로고    scopus 로고
    • Structure and function of CLCA proteins
    • Loewen ME, Forsyth GW (2005) Structure and function of CLCA proteins. Physiol Rev 85:1061-1092
    • (2005) Physiol Rev , vol.85 , pp. 1061-1092
    • Loewen, M.E.1    Forsyth, G.W.2
  • 78
    • 59649115245 scopus 로고    scopus 로고
    • Regulation of bestrophin Cl channels by calcium: Role of the C terminus
    • Xiao Q, Prussia A, Yu K, Cui YY, Hartzell HC (2008) Regulation of bestrophin Cl channels by calcium: Role of the C terminus. J Gen Physiol 132:681-692
    • (2008) J Gen Physiol , vol.132 , pp. 681-692
    • Xiao, Q.1    Prussia, A.2    Yu, K.3    Cui, Y.Y.4    Hartzell, H.C.5
  • 79
  • 80
    • 33749519366 scopus 로고    scopus 로고
    • Using metadynamics to understand the mechanism of calmodulin/target recognition at atomic detail
    • Fiorin G, Pastore A, Carloni P, Parrinello M (2006) Using metadynamics to understand the mechanism of calmodulin/target recognition at atomic detail. Biophys J 91:2768-2777
    • (2006) Biophys J , vol.91 , pp. 2768-2777
    • Fiorin, G.1    Pastore, A.2    Carloni, P.3    Parrinello, M.4
  • 82
    • 0028956081 scopus 로고
    • The energetics and dynamics of molecular recognition by calmodulin
    • Ehrhardt MR, Urbauer JL, Wand AJ (1995) The energetics and dynamics of molecular recognition by calmodulin. Biochemistry 34:2731-2738
    • (1995) Biochemistry , vol.34 , pp. 2731-2738
    • Ehrhardt, M.R.1    Urbauer, J.L.2    Wand, A.J.3
  • 83
    • 77956243395 scopus 로고    scopus 로고
    • Characterization of the beta-D-glucopyranoside binding site of the human bitter taste receptor hTAS2R16
    • Sakurai T, Misaka T, Ishiguro M, Masuda K, Sugawara T et al (2010) Characterization of the beta-D-glucopyranoside binding site of the human bitter taste receptor hTAS2R16. J Biol Chem 285:28373-28378
    • (2010) J Biol Chem , vol.285 , pp. 28373-28378
    • Sakurai, T.1    Misaka, T.2    Ishiguro, M.3    Masuda, K.4    Sugawara, T.5
  • 84
    • 84988053595 scopus 로고
    • A combined ab initio quantum mechanical and molecular mechanical method for carrying out simulations on complex molecular systems: Applications to the CH3Cl C Cl exchange reaction and gas phase protonation of polyethers
    • Singh UC, Kollman PA (1986) A combined ab initio quantum mechanical and molecular mechanical method for carrying out simulations on complex molecular systems: Applications to the CH3Cl C Cl-exchange reaction and gas phase protonation of polyethers. J Comput Chem 7:718-730
    • (1986) J Comput Chem , vol.7 , pp. 718-730
    • Singh, U.C.1    Kollman, P.A.2
  • 85
    • 0037458815 scopus 로고    scopus 로고
    • Positional cloning of the human quantitative trait locus underlying taste sensitivity to phenylthiocarbamide
    • Kim UK, Jorgenson E, Coon H, Leppert M, Risch N et al (2003) Positional cloning of the human quantitative trait locus underlying taste sensitivity to phenylthiocarbamide. Science 299:1221-1225
    • (2003) Science , vol.299 , pp. 1221-1225
    • Kim, U.K.1    Jorgenson, E.2    Coon, H.3    Leppert, M.4    Risch, N.5
  • 86
    • 36748998784 scopus 로고    scopus 로고
    • Haddock versus haddock: New features and performance of haddock2.0 on the capri targets
    • de Vries SJ, van Dijk AD, Krzeminski M, van Dijk M, Thureau A et al (2007) HADDOCK versus HADDOCK: New features and performance of HADDOCK2.0 on the CAPRI targets. Proteins 69:726-733
    • (2007) Proteins , vol.69 , pp. 726-733
    • De Vries, S.J.1    Van Dijk, A.D.2    Krzeminski, M.3    Van Dijk, M.4    Thureau, A.5
  • 87
    • 0037442962 scopus 로고    scopus 로고
    • Haddock: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C, Boelens R, Bonvin AM (2003) HADDOCK: A protein-protein Docking approach based on biochemical or biophysical information. J Am Chem Soc 125:1731-1737
    • (2003) J Am Chem Soc , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 88
    • 84878530705 scopus 로고    scopus 로고
    • Coarsegrained/ molecular mechanics of the TAS2R38 bitter taste receptor: Experimentally-validated detailed structural prediction of agonist binding
    • Marchiori A, Capece L, Giorgetti A, Gasparini P, Behrens M et al (2013) Coarsegrained/ molecular mechanics of the TAS2R38 bitter taste receptor: Experimentally-validated detailed structural prediction of agonist binding. PLoS One 8(5):e64675
    • (2013) PLoS One , vol.8 , Issue.5
    • Marchiori, A.1    Capece, L.2    Giorgetti, A.3    Gasparini, P.4    Behrens, M.5
  • 89
    • 84865201339 scopus 로고    scopus 로고
    • Homology model-Assisted elucidation of binding sites in GPCRs
    • Vaidehi N, Klein-Seetharaman J (eds Humana Press
    • Levit A, Barak D, Behrens M, Meyerhof W, Niv M (2012) Homology model-Assisted elucidation of binding sites in GPCRs. In: Vaidehi N, Klein-Seetharaman J (eds) Membrane protein structure and dynamics. Humana Press, pp 179-205
    • (2012) Membrane Protein Structure And Dynamics , pp. 179-205
    • Levit, A.1    Barak, D.2    Behrens, M.3    Meyerhof, W.4    Niv, M.5
  • 90
    • 84877730113 scopus 로고    scopus 로고
    • Dynamic modular architecture of protein-protein interaction networks beyond the dichotomy of 'date' and 'party' hubs
    • Chang X, Xu T, Li Y, Wang K (2013) Dynamic modular architecture of protein-protein interaction networks beyond the dichotomy of 'date' and 'party' hubs. Sci Rep 3:1691
    • (2013) Sci Rep , vol.3 , pp. 1691
    • Chang, X.1    Xu, T.2    Li, Y.3    Wang, K.4
  • 91
    • 77649182705 scopus 로고    scopus 로고
    • Unveiling the role of network and systems biology in Drug discovery
    • Pujol A, Mosca R, Farrés J, Aloy P (2010) Unveiling the role of network and systems biology in Drug discovery. Trends Pharmacol Sci 31:115-123
    • (2010) Trends Pharmacol Sci , vol.31 , pp. 115-123
    • Pujol, A.1    Mosca, R.2    Farrés, J.3    Aloy, P.4
  • 92
    • 79951788562 scopus 로고    scopus 로고
    • Towards the prediction of protein interaction partners using physical docking
    • Wass MN, Fuentes G, Pons C, Pazos F, Valencia A (2011) Towards the prediction of protein interaction partners using physical docking. Mol Syst Biol 7:1-8
    • (2011) Mol Syst Biol , vol.7 , pp. 1-8
    • Wass, M.N.1    Fuentes, G.2    Pons, C.3    Pazos, F.4    Valencia, A.5
  • 93
    • 79952674000 scopus 로고    scopus 로고
    • Interactome networks and human Disease
    • Vidal M, Cusick ME, Barabási A-L (2011) Interactome networks and human Disease. Cell 144:986-998
    • (2011) Cell , vol.144 , pp. 986-998
    • Vidal, M.1    Cusick, M.E.2    Barabási, A.-L.3
  • 94
    • 34247098754 scopus 로고    scopus 로고
    • Multiscale modeling of biomolecular systems: In serial and in parallel
    • Ayton GS, Noid WG, Voth GA (2007) Multiscale modeling of biomolecular systems: In serial and in parallel. Curr Opin Struct Biol 17:192-198
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 192-198
    • Ayton, G.S.1    Noid, W.G.2    Voth, G.A.3
  • 95
    • 80053391759 scopus 로고    scopus 로고
    • Capturing the essence of folding and functions of biomolecules using coarse-grained models
    • Hyeon C, Thirumalai D (2011) Capturing the essence of folding and functions of biomolecules using coarse-grained models. Nat Commun 2:487
    • (2011) Nat Commun , vol.2 , pp. 487
    • Hyeon, C.1    Thirumalai, D.2
  • 97
    • 79961038713 scopus 로고    scopus 로고
    • Multiscale simulations suggest a mechanism for integrin inside-out activation
    • Kalli AC, Campbell ID, Sansom MSP (2011) Multiscale simulations suggest a mechanism for integrin inside-out activation. Proc Natl Acad Sci USA 108:11890-11895
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 11890-11895
    • Kalli, A.C.1    Campbell, I.D.2    Sansom, M.S.P.3
  • 98
    • 77951241004 scopus 로고    scopus 로고
    • Multiscale simulations of protein landscapes: Using coarse-grained models as reference potentials to full explicit models
    • Messer BM, Roca M, Chu ZT, Vicatos S, Kilshtain AV et al (2010) Multiscale simulations of protein landscapes: Using coarse-grained models as reference potentials to full explicit models. Proteins 78:1212-1227
    • (2010) Proteins , vol.78 , pp. 1212-1227
    • Messer, B.M.1    Roca, M.2    Chu, Z.T.3    Vicatos, S.4    Kilshtain, A.V.5
  • 99
    • 33748266722 scopus 로고    scopus 로고
    • Mixed atomistic and coarse-grained molecular dynamics: Simulation of a membrane-bound ion channel
    • Shi Q, Izvekov S, Voth GA (2006) Mixed atomistic and coarse-grained molecular dynamics: Simulation of a membrane-bound ion channel. J Phys Chem B 110:15045-15048
    • (2006) J Phys Chem B , vol.110 , pp. 15045-15048
    • Shi, Q.1    Izvekov, S.2    Voth, G.A.3
  • 100
    • 18744391399 scopus 로고    scopus 로고
    • Structural dynamics of the lac repressor-DNA complex revealed by a multiscale simulation
    • Villa E, Balaeff A, Schulten K (2005) Structural dynamics of the lac repressor-DNA complex revealed by a multiscale simulation. Proc Natl Acad Sci USA 102:6783-6788
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6783-6788
    • Villa, E.1    Balaeff, A.2    Schulten, K.3
  • 101
    • 37749005024 scopus 로고    scopus 로고
    • Microseconds dynamics simulations of the outer-membrane protease T
    • Neri M, Baaden M, Carnevale V, Anselmi C, Maritan A et al (2008) Microseconds dynamics simulations of the outer-membrane protease T. Biophys J 94:71-78
    • (2008) Biophys J , vol.94 , pp. 71-78
    • Neri, M.1    Baaden, M.2    Carnevale, V.3    Anselmi, C.4    Maritan, A.5
  • 102
    • 28844494903 scopus 로고    scopus 로고
    • Coarse-grained model of proteins incorporating atomistic detail of the active site
    • Neri M, Anselmi C, Cascella M, Maritan A, Carloni P (2005) Coarse-grained model of proteins incorporating atomistic detail of the active site. Phys Rev Lett 95:218102
    • (2005) Phys Rev Lett , vol.95 , pp. 218102
    • Neri, M.1    Anselmi, C.2    Cascella, M.3    Maritan, A.4    Carloni, P.5
  • 103
    • 84867684737 scopus 로고    scopus 로고
    • Hybrid molecular mechanics/coarse-grained simulations for structural prediction of G-protein coupled receptor/ ligand complexes
    • Leguebe M, Nguyen C, Capece L, Hoang Z, Giorgetti A et al (2012) Hybrid molecular mechanics/coarse-grained simulations for structural prediction of G-protein coupled receptor/ ligand complexes. PLoS One 7:e47332
    • (2012) PLoS One , vol.7
    • Leguebe, M.1    Nguyen, C.2    Capece, L.3    Hoang, Z.4    Giorgetti, A.5
  • 104
    • 79551571786 scopus 로고    scopus 로고
    • Predicting novel binding modes of agonists to B adrenergic receptors using all-Atom molecular dynamics simulations
    • Vanni S, Neri M, Tavernelli I, Rothlisberger U (2011) Predicting novel binding modes of agonists to B adrenergic receptors using all-Atom molecular dynamics simulations. PLoS Comput Biol 7:e1001053
    • (2011) PLoS Comput Biol , vol.7
    • Vanni, S.1    Neri, M.2    Tavernelli, I.3    Rothlisberger, U.4
  • 105
    • 33747754105 scopus 로고    scopus 로고
    • Comprehensive repertoire and phylogenetic analysis of the G protein-coupled receptors in human and mouse
    • Bjarnadottir TK, Gloriam DE, Hellstrand SH, Kristiansson H, Fredriksson R et al (2006) Comprehensive repertoire and phylogenetic analysis of the G protein-coupled receptors in human and mouse. Genomics 88:263-273
    • (2006) Genomics , vol.88 , pp. 263-273
    • Bjarnadottir, T.K.1    Gloriam, D.E.2    Hellstrand, S.H.3    Kristiansson, H.4    Fredriksson, R.5


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