메뉴 건너뛰기




Volumn 395, Issue 4, 2010, Pages 769-784

Activation of the Ghrelin Receptor is Described by a Privileged Collective Motion: A Model for Constitutive and Agonist-induced Activation of a Sub-class A G-Protein Coupled Receptor (GPCR)

Author keywords

activation; ghrelin; GPCR; NMA; receptor

Indexed keywords

1,2,4 TRIAZOLE DERIVATIVE; G PROTEIN COUPLED RECEPTOR; GHRELIN RECEPTOR;

EID: 73649109875     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.09.051     Document Type: Article
Times cited : (33)

References (68)
  • 1
    • 0034677966 scopus 로고    scopus 로고
    • Drug discovery: a historical perspective
    • Drews J. Drug discovery: a historical perspective. Science 287 (2000) 1960-1964
    • (2000) Science , vol.287 , pp. 1960-1964
    • Drews, J.1
  • 4
    • 35648985567 scopus 로고    scopus 로고
    • The growth hormone secretagogue receptor
    • Young Cruz C.R., and Smith R.G. The growth hormone secretagogue receptor. Vitam. Horm. 77 (2008) 47-88
    • (2008) Vitam. Horm. , vol.77 , pp. 47-88
    • Young Cruz, C.R.1    Smith, R.G.2
  • 5
    • 0033540056 scopus 로고    scopus 로고
    • Ghrelin is a growth-hormone-releasing acylated peptide from stomach
    • Kojima M., Hosoda H., Date Y., Nakazato M., Matsuo H., and Kangawa K. Ghrelin is a growth-hormone-releasing acylated peptide from stomach. Nature 402 (1999) 656-660
    • (1999) Nature , vol.402 , pp. 656-660
    • Kojima, M.1    Hosoda, H.2    Date, Y.3    Nakazato, M.4    Matsuo, H.5    Kangawa, K.6
  • 6
    • 38849090670 scopus 로고    scopus 로고
    • Identification of the acyltransferase that octanoylates ghrelin, an appetite-stimulating peptide hormone
    • Yang J., Brown M.S., Liang G., Grishin N.V., and Goldstein J.L. Identification of the acyltransferase that octanoylates ghrelin, an appetite-stimulating peptide hormone. Cell 132 (2008) 387-396
    • (2008) Cell , vol.132 , pp. 387-396
    • Yang, J.1    Brown, M.S.2    Liang, G.3    Grishin, N.V.4    Goldstein, J.L.5
  • 7
    • 0034676324 scopus 로고    scopus 로고
    • Structure-function studies on the new growth hormone-releasing peptide, ghrelin: minimal sequence of ghrelin necessary for activation of growth hormone secretagogue receptor 1a
    • Bednarek M.A., Feighner S.D., Pong S.S., McKee K.K., Hreniuk D.L., Silva M.V., et al. Structure-function studies on the new growth hormone-releasing peptide, ghrelin: minimal sequence of ghrelin necessary for activation of growth hormone secretagogue receptor 1a. J. Med. Chem. 43 (2000) 4370-4376
    • (2000) J. Med. Chem. , vol.43 , pp. 4370-4376
    • Bednarek, M.A.1    Feighner, S.D.2    Pong, S.S.3    McKee, K.K.4    Hreniuk, D.L.5    Silva, M.V.6
  • 8
    • 0035217073 scopus 로고    scopus 로고
    • 1H NMR structural analysis of human ghrelin and its six truncated analogs
    • Silva Elipe M.V., Bednarek M.A., and Gao Y.D. 1H NMR structural analysis of human ghrelin and its six truncated analogs. Biopolymers 59 (2001) 489-501
    • (2001) Biopolymers , vol.59 , pp. 489-501
    • Silva Elipe, M.V.1    Bednarek, M.A.2    Gao, Y.D.3
  • 9
    • 30744470385 scopus 로고    scopus 로고
    • Conformational flexibility of the peptide hormone ghrelin in solution and lipid membrane bound: a molecular dynamics study
    • Beevers A.J., and Kukol A. Conformational flexibility of the peptide hormone ghrelin in solution and lipid membrane bound: a molecular dynamics study. J. Biomol. Struct. Dynam. 23 (2006) 357-364
    • (2006) J. Biomol. Struct. Dynam. , vol.23 , pp. 357-364
    • Beevers, A.J.1    Kukol, A.2
  • 10
    • 36749006143 scopus 로고    scopus 로고
    • Structure and dynamics of the full-length M1 muscarinic acetylcholine receptor studied by molecular dynamics simulations
    • Espinoza-Fonseca L.M., Pedretti A., and Vistoli G. Structure and dynamics of the full-length M1 muscarinic acetylcholine receptor studied by molecular dynamics simulations. Arch. Biochem. Biophys. 469 (2008) 142-150
    • (2008) Arch. Biochem. Biophys. , vol.469 , pp. 142-150
    • Espinoza-Fonseca, L.M.1    Pedretti, A.2    Vistoli, G.3
  • 11
    • 50149116588 scopus 로고    scopus 로고
    • Agonist-induced conformational changes in bovine rhodopsin: insight into activation of G-protein-coupled receptors
    • Bhattacharya S., Hall S.E., and Vaidehi N. Agonist-induced conformational changes in bovine rhodopsin: insight into activation of G-protein-coupled receptors. J. Mol. Biol. 382 (2008) 539-555
    • (2008) J. Mol. Biol. , vol.382 , pp. 539-555
    • Bhattacharya, S.1    Hall, S.E.2    Vaidehi, N.3
  • 12
    • 35348983347 scopus 로고    scopus 로고
    • Mechanism of activation of a G protein-coupled receptor, the human cholecystokinin-2 receptor
    • Marco E., Foucaud M., Langer I., Escrieut C., Tikhonova I.G., and Fourmy D. Mechanism of activation of a G protein-coupled receptor, the human cholecystokinin-2 receptor. J. Biol. Chem 282 (2007) 28779-28790
    • (2007) J. Biol. Chem , vol.282 , pp. 28779-28790
    • Marco, E.1    Foucaud, M.2    Langer, I.3    Escrieut, C.4    Tikhonova, I.G.5    Fourmy, D.6
  • 13
    • 33645783040 scopus 로고    scopus 로고
    • Probing a model of a GPCR/ligand complex in an explicit membrane environment: the human cholecystokinin-1 receptor
    • Henin J., Maigret B., Tarek M., Escrieut C., Fourmy D., and Chipot C. Probing a model of a GPCR/ligand complex in an explicit membrane environment: the human cholecystokinin-1 receptor. Biophys. J. 90 (2006) 1232-1240
    • (2006) Biophys. J. , vol.90 , pp. 1232-1240
    • Henin, J.1    Maigret, B.2    Tarek, M.3    Escrieut, C.4    Fourmy, D.5    Chipot, C.6
  • 17
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park J.H., Scheerer P., Hofmann K.P., Choe H.W., and Ernst O.P. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454 (2008) 183-187
    • (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
  • 18
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum D.M., Rasmussen S.G., and Kobilka B.K. The structure and function of G-protein-coupled receptors. Nature 459 (2009) 356-363
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 19
    • 51249115387 scopus 로고    scopus 로고
    • Human thrombospondin's (TSP-1) C-terminal domain opens to interact with the CD-47 receptor: a molecular modeling study
    • Floquet N., Dedieu S., Martiny L., Dauchez M., and Perahia D. Human thrombospondin's (TSP-1) C-terminal domain opens to interact with the CD-47 receptor: a molecular modeling study. Arch. Biochem. Biophys. 478 (2008) 103-109
    • (2008) Arch. Biochem. Biophys. , vol.478 , pp. 103-109
    • Floquet, N.1    Dedieu, S.2    Martiny, L.3    Dauchez, M.4    Perahia, D.5
  • 20
    • 58149103168 scopus 로고    scopus 로고
    • Collective motions in glucosamine-6-phosphate synthase: influence of ligand binding and their role in ammonia channelling and opening of the fructose-6P binding site
    • Floquet N., Durand P., Maigret B., Badet B., Badet-Denisot M.A., and Perahia D. Collective motions in glucosamine-6-phosphate synthase: influence of ligand binding and their role in ammonia channelling and opening of the fructose-6P binding site. J. Mol. Biol. 385 (2009) 653-664
    • (2009) J. Mol. Biol. , vol.385 , pp. 653-664
    • Floquet, N.1    Durand, P.2    Maigret, B.3    Badet, B.4    Badet-Denisot, M.A.5    Perahia, D.6
  • 21
    • 33748759844 scopus 로고    scopus 로고
    • Normal mode analysis as a prerequisite for drug design: application to matrix metalloproteinases inhibitors
    • Floquet N., Marechal J.D., Badet-Denisot M.A., Robert C.H., Dauchez M., and Perahia D. Normal mode analysis as a prerequisite for drug design: application to matrix metalloproteinases inhibitors. FEBS Lett. 580 (2006) 5130-5136
    • (2006) FEBS Lett. , vol.580 , pp. 5130-5136
    • Floquet, N.1    Marechal, J.D.2    Badet-Denisot, M.A.3    Robert, C.H.4    Dauchez, M.5    Perahia, D.6
  • 22
    • 33751534910 scopus 로고    scopus 로고
    • Conformational heterogeneity and low-frequency vibrational modes of proteins
    • Balog E., Smith J.C., and Perahia D. Conformational heterogeneity and low-frequency vibrational modes of proteins. Phys. Chem. Chem. Phys. 8 (2006) 5543-5548
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , pp. 5543-5548
    • Balog, E.1    Smith, J.C.2    Perahia, D.3
  • 24
    • 0033594988 scopus 로고    scopus 로고
    • Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: a site-directed spin-labeling study
    • Altenbach C., Cai K., Khorana H.G., and Hubbell W.L. Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: a site-directed spin-labeling study. Biochemistry 38 (1999) 7931-7937
    • (1999) Biochemistry , vol.38 , pp. 7931-7937
    • Altenbach, C.1    Cai, K.2    Khorana, H.G.3    Hubbell, W.L.4
  • 25
    • 0035951062 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1
    • Altenbach C., Klein-Seetharaman J., Cai K., Khorana H.G., and Hubbell W.L. Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1. Biochemistry 40 (2001) 15493-15500
    • (2001) Biochemistry , vol.40 , pp. 15493-15500
    • Altenbach, C.1    Klein-Seetharaman, J.2    Cai, K.3    Khorana, H.G.4    Hubbell, W.L.5
  • 26
    • 0033594981 scopus 로고    scopus 로고
    • Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: a site-directed spin-labeling study
    • Altenbach C., Klein-Seetharaman J., Hwa J., Khorana H.G., and Hubbell W.L. Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: a site-directed spin-labeling study. Biochemistry 38 (1999) 7945-7949
    • (1999) Biochemistry , vol.38 , pp. 7945-7949
    • Altenbach, C.1    Klein-Seetharaman, J.2    Hwa, J.3    Khorana, H.G.4    Hubbell, W.L.5
  • 27
    • 33644772378 scopus 로고    scopus 로고
    • Location of Trp265 in metarhodopsin II: implications for the activation mechanism of the visual receptor rhodopsin
    • Crocker E., Eilers M., Ahuja S., Hornak V., Hirshfeld A., Sheves M., and Smith S.O. Location of Trp265 in metarhodopsin II: implications for the activation mechanism of the visual receptor rhodopsin. J. Mol. Biol. 357 (2006) 163-172
    • (2006) J. Mol. Biol. , vol.357 , pp. 163-172
    • Crocker, E.1    Eilers, M.2    Ahuja, S.3    Hornak, V.4    Hirshfeld, A.5    Sheves, M.6    Smith, S.O.7
  • 29
    • 0033555936 scopus 로고    scopus 로고
    • Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy
    • Dunham T.D., and Farrens D.L. Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy. J. Biol. Chem. 274 (1999) 1683-1690
    • (1999) J. Biol. Chem. , vol.274 , pp. 1683-1690
    • Dunham, T.D.1    Farrens, D.L.2
  • 30
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens D.L., Altenbach C., Yang K., Hubbell W.L., and Khorana H.G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274 (1996) 768-770
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 31
    • 0033546197 scopus 로고    scopus 로고
    • Nissenson, R. A.; Bourne, H. R. Similar structures and shared switch mechanisms of the beta2-adrenoceptor and the parathyroid hormone receptor. Zn(II) bridges between helices III and VI block activation
    • Sheikh S.P., Vilardarga J.P., Baranski T.J., Lichtarge O., Iiri T., Meng E.C., et al. Nissenson, R. A.; Bourne, H. R. Similar structures and shared switch mechanisms of the beta2-adrenoceptor and the parathyroid hormone receptor. Zn(II) bridges between helices III and VI block activation. J. Biol. Chem. 274 (1999) 17033-17041
    • (1999) J. Biol. Chem. , vol.274 , pp. 17033-17041
    • Sheikh, S.P.1    Vilardarga, J.P.2    Baranski, T.J.3    Lichtarge, O.4    Iiri, T.5    Meng, E.C.6
  • 32
    • 0034636820 scopus 로고    scopus 로고
    • G protein-coupled receptor activation: analysis of a highly constrained, "straitjacketed" rhodopsin
    • Struthers M., Yu H., and Oprian D.D. G protein-coupled receptor activation: analysis of a highly constrained, "straitjacketed" rhodopsin. Biochemistry 39 (2000) 7938-7942
    • (2000) Biochemistry , vol.39 , pp. 7938-7942
    • Struthers, M.1    Yu, H.2    Oprian, D.D.3
  • 33
    • 0033554440 scopus 로고    scopus 로고
    • Tertiary interactions between transmembrane segments 3 and 5 near the cytoplasmic side of rhodopsin
    • Yu H., and Oprian D.D. Tertiary interactions between transmembrane segments 3 and 5 near the cytoplasmic side of rhodopsin. Biochemistry 38 (1999) 12033-12040
    • (1999) Biochemistry , vol.38 , pp. 12033-12040
    • Yu, H.1    Oprian, D.D.2
  • 34
    • 0037174606 scopus 로고    scopus 로고
    • Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch
    • Shi L., Liapakis G., Xu R., Guarnieri F., Ballesteros J.A., and Javitch J.A. Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch. J. Biol. Chem. 277 (2002) 40989-40996
    • (2002) J. Biol. Chem. , vol.277 , pp. 40989-40996
    • Shi, L.1    Liapakis, G.2    Xu, R.3    Guarnieri, F.4    Ballesteros, J.A.5    Javitch, J.A.6
  • 35
    • 0035856560 scopus 로고    scopus 로고
    • Functional role of a conserved motif in TM6 of the rat mu opioid receptor: constitutively active and inactive receptors result from substitutions of Thr6.34(279) with Lys and Asp
    • Huang P., Li J., Chen C., Visiers I., Weinstein H., and Liu-Chen L.Y. Functional role of a conserved motif in TM6 of the rat mu opioid receptor: constitutively active and inactive receptors result from substitutions of Thr6.34(279) with Lys and Asp. Biochemistry 40 (2001) 13501-13509
    • (2001) Biochemistry , vol.40 , pp. 13501-13509
    • Huang, P.1    Li, J.2    Chen, C.3    Visiers, I.4    Weinstein, H.5    Liu-Chen, L.Y.6
  • 36
    • 0037044308 scopus 로고    scopus 로고
    • The local environment at the cytoplasmic end of TM6 of the mu opioid receptor differs from those of rhodopsin and monoamine receptors: introduction of an ionic lock between the cytoplasmic ends of helices 3 and 6 by a L6.30(275)E mutation inactivates the mu opioid receptor and reduces the constitutive activity of its T6.34(279)K mutant
    • Huang P., Visiers I., Weinstein H., and Liu-Chen L.Y. The local environment at the cytoplasmic end of TM6 of the mu opioid receptor differs from those of rhodopsin and monoamine receptors: introduction of an ionic lock between the cytoplasmic ends of helices 3 and 6 by a L6.30(275)E mutation inactivates the mu opioid receptor and reduces the constitutive activity of its T6.34(279)K mutant. Biochemistry 41 (2002) 11972-11980
    • (2002) Biochemistry , vol.41 , pp. 11972-11980
    • Huang, P.1    Visiers, I.2    Weinstein, H.3    Liu-Chen, L.Y.4
  • 37
    • 45649083187 scopus 로고    scopus 로고
    • Functional role of the "ionic lock"-an interhelical hydrogen-bond network in family A heptahelical receptors
    • Vogel R., Mahalingam M., Ludeke S., Huber T., Siebert F., and Sakmar T.P. Functional role of the "ionic lock"-an interhelical hydrogen-bond network in family A heptahelical receptors. J. Mol. Biol. 380 (2008) 648-655
    • (2008) J. Mol. Biol. , vol.380 , pp. 648-655
    • Vogel, R.1    Mahalingam, M.2    Ludeke, S.3    Huber, T.4    Siebert, F.5    Sakmar, T.P.6
  • 38
    • 0029756165 scopus 로고    scopus 로고
    • Specific tryptophan UV-absorbance changes are probes of the transition of rhodopsin to its active state
    • Lin S.W., and Sakmar T.P. Specific tryptophan UV-absorbance changes are probes of the transition of rhodopsin to its active state. Biochemistry 35 (1996) 11149-11159
    • (1996) Biochemistry , vol.35 , pp. 11149-11159
    • Lin, S.W.1    Sakmar, T.P.2
  • 39
    • 11144225093 scopus 로고    scopus 로고
    • Common structural basis for constitutive activity of the ghrelin receptor family
    • Holst B., Holliday N.D., Bach A., Elling C.E., Cox H.M., and Schwartz T.W. Common structural basis for constitutive activity of the ghrelin receptor family. J. Biol. Chem. 279 (2004) 53806-53817
    • (2004) J. Biol. Chem. , vol.279 , pp. 53806-53817
    • Holst, B.1    Holliday, N.D.2    Bach, A.3    Elling, C.E.4    Cox, H.M.5    Schwartz, T.W.6
  • 40
    • 15444361604 scopus 로고    scopus 로고
    • Structural requirements for the activation of the human growth hormone secretagogue receptor by peptide and nonpeptide secretagogues
    • Feighner S.D., Howard A.D., Prendergast K., Palyha O.C., Hreniuk D.L., Nargund R., et al. Structural requirements for the activation of the human growth hormone secretagogue receptor by peptide and nonpeptide secretagogues. Mol. Endocrinol. 12 (1998) 137-145
    • (1998) Mol. Endocrinol. , vol.12 , pp. 137-145
    • Feighner, S.D.1    Howard, A.D.2    Prendergast, K.3    Palyha, O.C.4    Hreniuk, D.L.5    Nargund, R.6
  • 41
    • 34447530948 scopus 로고    scopus 로고
    • Identification of an efficacy switch region in the ghrelin receptor responsible for interchange between agonism and inverse agonism
    • Holst B., Mokrosinski J., Lang M., Brandt E., Nygaard R., Frimurer T.M., et al. Identification of an efficacy switch region in the ghrelin receptor responsible for interchange between agonism and inverse agonism. J. Biol. Chem. 282 (2007) 15799-15811
    • (2007) J. Biol. Chem. , vol.282 , pp. 15799-15811
    • Holst, B.1    Mokrosinski, J.2    Lang, M.3    Brandt, E.4    Nygaard, R.5    Frimurer, T.M.6
  • 42
    • 34548093246 scopus 로고    scopus 로고
    • Four missense mutations in the ghrelin receptor result in distinct pharmacological abnormalities
    • Liu G., Fortin J.P., Beinborn M., and Kopin A.S. Four missense mutations in the ghrelin receptor result in distinct pharmacological abnormalities. J. Pharmacol. Exp. Ther. 322 (2007) 1036-1043
    • (2007) J. Pharmacol. Exp. Ther. , vol.322 , pp. 1036-1043
    • Liu, G.1    Fortin, J.P.2    Beinborn, M.3    Kopin, A.S.4
  • 43
    • 33644653308 scopus 로고    scopus 로고
    • Loss of constitutive activity of the growth hormone secretagogue receptor in familial short stature
    • Pantel J., Legendre M., Cabrol S., Hilal L., Hajaji Y., Morisset S., et al. Loss of constitutive activity of the growth hormone secretagogue receptor in familial short stature. J. Clin. Invest. 116 (2006) 760-768
    • (2006) J. Clin. Invest. , vol.116 , pp. 760-768
    • Pantel, J.1    Legendre, M.2    Cabrol, S.3    Hilal, L.4    Hajaji, Y.5    Morisset, S.6
  • 44
    • 36148975300 scopus 로고    scopus 로고
    • Toward potent ghrelin receptor ligands based on trisubstituted 1,2,4-triazole structure. 2. Synthesis and pharmacological in vitro and in vivo evaluations
    • Moulin A., Demange L., Berge G., Gagne D., Ryan J., Mousseaux D., et al. Toward potent ghrelin receptor ligands based on trisubstituted 1,2,4-triazole structure. 2. Synthesis and pharmacological in vitro and in vivo evaluations. J. Med. Chem. 50 (2007) 5790-5806
    • (2007) J. Med. Chem. , vol.50 , pp. 5790-5806
    • Moulin, A.1    Demange, L.2    Berge, G.3    Gagne, D.4    Ryan, J.5    Mousseaux, D.6
  • 45
    • 37649022059 scopus 로고    scopus 로고
    • Trisubstituted 1,2,4-triazoles as ligands for the ghrelin receptor: on the significance of the orientation and substitution at position 3
    • Moulin A., Demange L., Ryan J., M'Kadmi C., Galleyrand J.C., Martinez J., and Fehrentz J.A. Trisubstituted 1,2,4-triazoles as ligands for the ghrelin receptor: on the significance of the orientation and substitution at position 3. Bioorg. Med. Chem. Lett. 18 (2008) 164-168
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 164-168
    • Moulin, A.1    Demange, L.2    Ryan, J.3    M'Kadmi, C.4    Galleyrand, J.C.5    Martinez, J.6    Fehrentz, J.A.7
  • 46
    • 39149128278 scopus 로고    scopus 로고
    • New trisubstituted 1,2,4-triazole derivatives as potent ghrelin receptor antagonists. 3. Synthesis and pharmacological in vitro and in vivo evaluations
    • Moulin A., Demange L., Ryan J., Mousseaux D., Sanchez P., Berge G., et al. New trisubstituted 1,2,4-triazole derivatives as potent ghrelin receptor antagonists. 3. Synthesis and pharmacological in vitro and in vivo evaluations. J. Med. Chem. 51 (2008) 689-693
    • (2008) J. Med. Chem. , vol.51 , pp. 689-693
    • Moulin, A.1    Demange, L.2    Ryan, J.3    Mousseaux, D.4    Sanchez, P.5    Berge, G.6
  • 47
    • 33749242759 scopus 로고    scopus 로고
    • Contribution of conformer focusing to the uncertainty in predicting free energies for protein-ligand binding
    • Tirado-Rives J., and Jorgensen W.L. Contribution of conformer focusing to the uncertainty in predicting free energies for protein-ligand binding. J. Med. Chem. 49 (2006) 5880-5884
    • (2006) J. Med. Chem. , vol.49 , pp. 5880-5884
    • Tirado-Rives, J.1    Jorgensen, W.L.2
  • 48
    • 39149107126 scopus 로고    scopus 로고
    • Discovery of novel chemotypes to a G-Protein-Coupled Receptor through ligand-steered homology modeling and structure-based virtual screening
    • Cavasotto C.N., Orry A.J.W., Murgolo N.J., Czarniecki M.F., Kocsi S.A., Hawes B.E., et al. Discovery of novel chemotypes to a G-Protein-Coupled Receptor through ligand-steered homology modeling and structure-based virtual screening. J. Med. Chem. 51 (2008) 581-588
    • (2008) J. Med. Chem. , vol.51 , pp. 581-588
    • Cavasotto, C.N.1    Orry, A.J.W.2    Murgolo, N.J.3    Czarniecki, M.F.4    Kocsi, S.A.5    Hawes, B.E.6
  • 49
    • 0033002410 scopus 로고    scopus 로고
    • Tryptophan rotamer distributions in amphipathic peptides at a lipid surface
    • Clayton A.H., and Sawyer W.H. Tryptophan rotamer distributions in amphipathic peptides at a lipid surface. Biophys. J. 76 (1999) 3235-3242
    • (1999) Biophys. J. , vol.76 , pp. 3235-3242
    • Clayton, A.H.1    Sawyer, W.H.2
  • 50
    • 1442351132 scopus 로고    scopus 로고
    • Protein flexibility in ligand docking and virtual screening to protein kinases
    • Cavasotto C.N., and Abagyan R.A. Protein flexibility in ligand docking and virtual screening to protein kinases. J. Mol. Biol. 337 (2004) 209-225
    • (2004) J. Mol. Biol. , vol.337 , pp. 209-225
    • Cavasotto, C.N.1    Abagyan, R.A.2
  • 51
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • Kobilka B.K., and Deupi X. Conformational complexity of G-protein-coupled receptors. Trends Pharmacol. Sci. 28 (2007) 397-406
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 52
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 53
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 54
    • 0014054519 scopus 로고
    • The detection of disease clustering and a generalized regression approach
    • Mantel N. The detection of disease clustering and a generalized regression approach. Cancer Res 27 (1967) 209-220
    • (1967) Cancer Res , vol.27 , pp. 209-220
    • Mantel, N.1
  • 58
    • 33846823909 scopus 로고
    • Particle mesh Ewald. An N.log(N) method for Ewald sums in large systems
    • Darden T.A., York D.M., and Pedersen L.G. Particle mesh Ewald. An N.log(N) method for Ewald sums in large systems. J. Chem. Phys. 98 (1993) 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.A.1    York, D.M.2    Pedersen, L.G.3
  • 59
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen W.L., Chandrasekhar J., and Madura J.D. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79 (1983) 926-935
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3
  • 61
    • 0029374782 scopus 로고
    • Computation of low-frequency normal modes in macromolecules: improvements to the method of diagonalization in a mixed basis and application to hemoglobin
    • Perahia D., and Mouawad L. Computation of low-frequency normal modes in macromolecules: improvements to the method of diagonalization in a mixed basis and application to hemoglobin. Comput. Chem. 19 (1995) 241-246
    • (1995) Comput. Chem. , vol.19 , pp. 241-246
    • Perahia, D.1    Mouawad, L.2
  • 62
    • 0343471377 scopus 로고    scopus 로고
    • Modification of a PCR-based site-directed mutagenesis method
    • Fisher C.L., and Pei G.K. Modification of a PCR-based site-directed mutagenesis method. Biotechniques 23 (1997) 570-574
    • (1997) Biotechniques , vol.23 , pp. 570-574
    • Fisher, C.L.1    Pei, G.K.2
  • 64
    • 33744485247 scopus 로고    scopus 로고
    • Regulation of ERK1/2 activity by ghrelin-activated growth hormone secretagogue receptor 1A involves a PLC/PKCvarepsilon pathway
    • Mousseaux D., Le Gallic L., Ryan J., Oiry C., Gagne D., Fehrentz J.A., et al. Regulation of ERK1/2 activity by ghrelin-activated growth hormone secretagogue receptor 1A involves a PLC/PKCvarepsilon pathway. Br. J. Pharmacol. 148 (2006) 350-365
    • (2006) Br. J. Pharmacol. , vol.148 , pp. 350-365
    • Mousseaux, D.1    Le Gallic, L.2    Ryan, J.3    Oiry, C.4    Gagne, D.5    Fehrentz, J.A.6
  • 65
    • 0028800721 scopus 로고
    • Prolonged treatment of breast cancer cells with antiestrogens increases the activating protein-1-mediated response: involvement of the estrogen receptor
    • Astruc M.E., Chabret C., Bali P., Gagne D., and Pons M. Prolonged treatment of breast cancer cells with antiestrogens increases the activating protein-1-mediated response: involvement of the estrogen receptor. Endocrinology 136 (1995) 824-832
    • (1995) Endocrinology , vol.136 , pp. 824-832
    • Astruc, M.E.1    Chabret, C.2    Bali, P.3    Gagne, D.4    Pons, M.5
  • 67
    • 73649136911 scopus 로고    scopus 로고
    • The R project for statistical computing (http://www.r-project.org/).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.