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Volumn 36, Issue 7, 1993, Pages 934-938

Signal Transduction by a 5-HT2 Receptor: A Mechanistic Hypothesis from Molecular Dynamics Simulations of the Three-Dimensional Model of the Receptor Complexed to Ligands

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; LIGAND; MEMBRANE PROTEIN; SEROTONIN; SEROTONIN 2 RECEPTOR;

EID: 0027416441     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm00059a021     Document Type: Editorial
Times cited : (98)

References (61)
  • 2
    • 0024519931 scopus 로고
    • Structural basis of β-adrenergic receptor function
    • Strader, C. D.; Sigal, I. S.; Dixon, R. A. F. Structural basis of β-adrenergic receptor function. FASEB J. 1989, 3, 1825–1831.
    • (1989) FASEB J. , vol.3 , pp. 1825-1831
    • Strader, C.D.1    Sigal, I.S.2    Dixon, R.A.F.3
  • 4
    • 0025812324 scopus 로고
    • Model systems for the study of seven-transmembrane-segment receptors
    • Dohlman, H. G.; Thorner, J.; Caron, M. G.; Lefkowitz, R. J. Model systems for the study of seven-transmembrane-segment receptors. Annu. Rev. Biochem. 1991, 60, 653–688.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 653-688
    • Dohlman, H.G.1    Thorner, J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 5
    • 0026071908 scopus 로고
    • Structure/function relationship of proteins belonging to the family of receptors coupled to GTP-binding proteins
    • Strossberg, A. D. Structure/function relationship of proteins belonging to the family of receptors coupled to GTP-binding proteins. Eur. J. Biochem. 1991, 196, 1–10.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 1-10
    • Strossberg, A.D.1
  • 9
    • 0023663097 scopus 로고
    • Computer-aided molecular design
    • McCammon, J. A. Computer-aided molecular design. Science 1987, 238, 486–491.
    • (1987) Science , vol.238 , pp. 486-491
    • McCammon, J.A.1
  • 11
    • 84934421289 scopus 로고
    • Simulations of ligand-receptor interactions as guides for design
    • Munksgaard, Copenhagen
    • Weinstein, H.; Osman, R. Simulations of ligand-receptor interactions as guides for design. In Alfred Benzon Symposium 28; Munksgaard, Copenhagen, 1989; pp 169–182.
    • (1989) Alfred Benzon Symposium , vol.28 , pp. 169-182
    • Weinstein, H.1    Osman, R.2
  • 12
    • 0025695420 scopus 로고
    • On the structural and mechanistic basis of function, classification, and ligand design for 5-HT receptors
    • Weinstein, H.; Osman, R. On the structural and mechanistic basis of function, classification, and ligand design for 5-HT receptors. Neuropsychopharmacology 1990, 3, 397–409.
    • (1990) Neuropsychopharmacology , vol.3 , pp. 397-409
    • Weinstein, H.1    Osman, R.2
  • 13
    • 85022607078 scopus 로고    scopus 로고
    • Receptor mechanisms at atomic resolution: New perspectives for drug design. Submitted for publication in
    • Weinstein, H.; Zhang, D. Receptor mechanisms at atomic resolution: New perspectives for drug design. Submitted for publication in J. Med. Chem.
    • J. Med. Chem.
    • Weinstein, H.1    Zhang, D.2
  • 14
    • 0025868465 scopus 로고
    • Molecular dynamics of dopamine at the D2 receptor. Proc
    • Dahl, S. G.; Edvardsen, O.; Sylte, I. Molecular dynamics of dopamine at the D2 receptor. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 8111–8115.
    • (1991) Natl. Acad. Sci. U.S.A. , vol.88 , pp. 8111-8115
    • Dahl, S.G.1    Edvardsen, O.2    Sylte, I.3
  • 15
    • 0025881062 scopus 로고
    • Three-dimensional models of neurotransmitter G-binding protein-coupled receptors
    • Hibert, M. F.; Trumpp-Kallmeyer, S.; Bruinvels, A.; Hoflack, J. Three-dimensional models of neurotransmitter G-binding protein-coupled receptors. Mol. Pharmacol. 1991, 40, 8–15.
    • (1991) Mol. Pharmacol. , vol.40 , pp. 8-15
    • Hibert, M.F.1    Trumpp-Kallmeyer, S.2    Bruinvels, A.3    Hoflack, J.4
  • 16
    • 0026751715 scopus 로고
    • Molecular dynamics of serotonin and ritanserin interacting with the 5-HT2 receptor
    • Edvardsen, O.; Sylte, I.; Dahl, S. G. Molecular dynamics of serotonin and ritanserin interacting with the 5-HT2 receptor. Mol. Brain Res. 1992, 14, 166–178.
    • (1992) Mol. Brain Res. , vol.14 , pp. 166-178
    • Edvardsen, O.1    Sylte, I.2    Dahl, S.G.3
  • 17
    • 0026457758 scopus 로고
    • A model of the adrenergic beta-2 receptor and binding sites for agonist and antagonist
    • Lewell, X. Q. A model of the adrenergic beta-2 receptor and binding sites for agonist and antagonist. Drug Design Discov. 1992, 9, 29–48.
    • (1992) Drug Design Discov. , vol.9 , pp. 29-48
    • Lewell, X.Q.1
  • 18
    • 0026681102 scopus 로고
    • Three-dimensional structure for the beta2 adrenergic receptor protein based on computer modeling studies
    • MaloneyHuss, K.; Lybrand, T. P. Three-dimensional structure for the beta2 adrenergic receptor protein based on computer modeling studies. J. Mol. Biol. 1992, 225, 859–871.
    • (1992) J. Mol. Biol. , vol.225 , pp. 859-871
    • MaloneyHuss, K.1    Lybrand, T.P.2
  • 19
    • 0026451988 scopus 로고
    • Molecular modeling of adenosine receptors. 1. The ligand binding site on the A1 receptor
    • Ijzerman, A. P.; Van Galen, P. J. M.; Jacobson, K. A. Molecular modeling of adenosine receptors. 1. The ligand binding site on the A1 receptor. Drug Design Discov. 1992, 9, 49–67.
    • (1992) Drug Design Discov. , vol.9 , pp. 49-67
    • Ijzerman, A.P.1    Van Galen, P.J.M.2    Jacobson, K.A.3
  • 20
    • 0025667804 scopus 로고
    • Three-dimensional modelling of G protein-linked receptors
    • Findlay, J.; Eliopoulos, E. Three-dimensional modelling of G protein-linked receptors. Trends Pharmacol. Sci. 1990, 11, 492–499.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 492-499
    • Findlay, J.1    Eliopoulos, E.2
  • 21
    • 0011219025 scopus 로고
    • Three-dimensional models of G-protein coupled receptors
    • Humblet, C.; Mirzadegan, T. Three-dimensional models of G-protein coupled receptors. Annu. Rep. Med. Chem. 1992, 27, 291–300.
    • (1992) Annu. Rep. Med. Chem. , vol.27 , pp. 291-300
    • Humblet, C.1    Mirzadegan, T.2
  • 22
    • 0025292355 scopus 로고
    • Model for the structure of Bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R.; Baldwin, J. M.; Ceska, T. A.; Zemlin, F.; Beckmann, E.; Downing, K. H. Model for the structure of Bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 1990, 213, 899–929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 23
    • 0026517309 scopus 로고
    • On the use of the transmembrane domain of bacteriorhodopsin as a template for modeling the three-dimensional structure of guanine nucleotide-binding regulatory protein-coupled receptors
    • Pardo, L.; Ballesteros, J. A.; Osman, R.; Weinstein, H. On the use of the transmembrane domain of bacteriorhodopsin as a template for modeling the three-dimensional structure of guanine nucleotide-binding regulatory protein-coupled receptors. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 4009–4012.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4009-4012
    • Pardo, L.1    Ballesteros, J.A.2    Osman, R.3    Weinstein, H.4
  • 24
    • 0026755609 scopus 로고
    • Analysis and refinement of criteria for predicting the structure and relative orientations of transmembranal helical domains
    • Ballesteros, J. A.; Weinstein, H. Analysis and refinement of criteria for predicting the structure and relative orientations of transmembranal helical domains. Biophys. J. 1992, 62, 107–109.
    • (1992) Biophys. J. , vol.62 , pp. 107-109
    • Ballesteros, J.A.1    Weinstein, H.2
  • 25
    • 0026660322 scopus 로고
    • Modeling of G-protein-coupled receptors: Application to dopamine, adrenaline, serotonin, acetylcholine, and mammalian opsin receptors
    • Trumpp-Kallmeyer, S.; Hoklack, J.; Bruinvels, A.; Hibert, M. Modeling of G-protein-coupled receptors: Application to dopamine, adrenaline, serotonin, acetylcholine, and mammalian opsin receptors. J. Med. Chem. 1992, 35, 3448–3462.
    • (1992) J. Med. Chem. , vol.35 , pp. 3448-3462
    • Trumpp-Kallmeyer, S.1    Hoklack, J.2    Bruinvels, A.3    Hibert, M.4
  • 26
    • 85022614136 scopus 로고
    • Hallucinogens acting at 5-HT receptors: Towards a mechanistic understanding at atomic resolution
    • Lin, G., Glennon, R. A., Eds.; National Institute on Drug Abuse: Washington, D.C., in press
    • Weinstein, H.; Zhang, D.; Ballesteros, J. A. Hallucinogens acting at 5-HT receptors: Towards a mechanistic understanding at atomic resolution. In NIDA Research Monograph, Hallucinogens: An Update; Lin, G., Glennon, R. A., Eds.; National Institute on Drug Abuse: Washington, D.C., 1992; in press.
    • (1992) NIDA Research Monograph, Hallucinogens: An Update
    • Weinstein, H.1    Zhang, D.2    Ballesteros, J.A.3
  • 27
    • 0026608113 scopus 로고
    • Drug efficacy at guanine nucleotide-binding regulatory protein-linked receptors: Thermodynamic interpretation of negative antagonism and of receptor activity in the absence of ligand
    • Costa, T.; Ogino, Y.; Munson, P. J.; Onaran, H. O.; Rodbard, D. Drug efficacy at guanine nucleotide-binding regulatory protein-linked receptors: Thermodynamic interpretation of negative antagonism and of receptor activity in the absence of ligand. Mol. Pharmacol. 1992, 41, 549–560.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 549-560
    • Costa, T.1    Ogino, Y.2    Munson, P.J.3    Onaran, H.O.4    Rodbard, D.5
  • 29
    • 0025189905 scopus 로고
    • The 5HT2 receptor defines a family of structurally disctinct but functionally conserved serotonin receptors
    • Julius, D.; Huang, K. N.; LiveUi, T. J.; Axel, R.; Jessel, T. M. The 5HT2 receptor defines a family of structurally disctinct but functionally conserved serotonin receptors. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 928–932.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 928-932
    • Julius, D.1    Huang, K.N.2    LiveUi, T.J.3    Axel, R.4    Jessel, T.M.5
  • 30
    • 0024507731 scopus 로고
    • Molecular biology of 5-HT receptors
    • Hartig, P. R. Molecular biology of 5-HT receptors. Trends Pharmacol. Sci. 1989, 10, 64–69.
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 64-69
    • Hartig, P.R.1
  • 32
    • 0026546071 scopus 로고
    • Of mice and flies: Commonalities among 5-HT receptors
    • Hen, R. Of mice and flies: Commonalities among 5-HT receptors. Trends Pharmacol. Sci. 1992, 13, 160–165.
    • (1992) Trends Pharmacol. Sci. , vol.13 , pp. 160-165
    • Hen, R.1
  • 34
    • 84988199995 scopus 로고
    • Simulations of molecular stereoelectronic mechanisms for the interaction of hallucinogens and indole derivatives at 5-HT receptors
    • Naray-Szabo, G., Kaiman, S., Eds.; CRC Press: Boca Raton, FL
    • Weinstein, H.; Osman, R.; Mazurek, A. P. Simulations of molecular stereoelectronic mechanisms for the interaction of hallucinogens and indole derivatives at 5-HT receptors. In Stereoelectronic Aspects of Biomolecular Interactions; Naray-Szabo, G., Kaiman, S., Eds.; CRC Press: Boca Raton, FL, 1987; pp 199–210.
    • (1987) Stereoelectronic Aspects of Biomolecular Interactions , pp. 199-210
    • Weinstein, H.1    Osman, R.2    Mazurek, A.P.3
  • 35
    • 0024164102 scopus 로고
    • US-HHS, NIDA: NIDA Research Monograph 90, Proceedings of the 50th Annual Meeting, Maryland
    • Weinstein, H.; Osman, R.; Mercier, G. In Problems of Drug Dependence; US-HHS, NIDA: NIDA Research Monograph 90, Proceedings of the 50th Annual Meeting, Maryland, 1988; pp 243–255.
    • (1988) Problems of Drug Dependence , pp. 243-255
    • Weinstein, H.1    Osman, R.2    Mercier, G.3
  • 36
    • 0025782832 scopus 로고
    • Proline kinks in transmembrane alpha-helices
    • von Heijne, G. Proline kinks in transmembrane alpha-helices. J. Mol. Biol. 1991, 218, 499–503.
    • (1991) J. Mol. Biol. , vol.218 , pp. 499-503
    • von Heijne, G.1
  • 37
    • 0025945775 scopus 로고
    • Proline residues in transmembrane helices: Structural or dynamic role
    • Williams, K. A.; Deber, C. M. Proline residues in transmembrane helices: Structural or dynamic role? Biochemistry 1991, 30, 8919–8923.
    • (1991) Biochemistry , vol.30 , pp. 8919-8923
    • Williams, K.A.1    Deber, C.M.2
  • 38
    • 0026696183 scopus 로고
    • The role of Pro/Hyp-kinks in determining the transmembrane helix length and gating mechanism of a Leu-zervamicin channel
    • Ballesteros, J. A.; Weinstein, H. The role of Pro/Hyp-kinks in determining the transmembrane helix length and gating mechanism of a Leu-zervamicin channel. Biophys. J. 1992, 62, 110–111.
    • (1992) Biophys. J. , vol.62 , pp. 110-111
    • Ballesteros, J.A.1    Weinstein, H.2
  • 39
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow, D. J.; Thornton, J. M. Helix geometry in proteins. J. Mol. Biol. 1988, 203, 601–619.
    • (1988) J. Mol. Biol. , vol.203 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 41
    • 0023404610 scopus 로고
    • Pro-induced constraints in alpha-helices
    • Piela, L.; Nemethy, G.; Scheraga, H. A. Pro-induced constraints in alpha-helices. Biopolymers 1987, 26, 1587–1600.
    • (1987) Biopolymers , vol.26 , pp. 1587-1600
    • Piela, L.1    Nemethy, G.2    Scheraga, H.A.3
  • 42
    • 0024346677 scopus 로고
    • Hydrophobic organization of membrane proteins
    • Rees, D. C.; DeAntonio, L.; Eisenberg, D. Hydrophobic organization of membrane proteins. Science 1989, 245, 510–513.
    • (1989) Science , vol.245 , pp. 510-513
    • Rees, D.C.1    DeAntonio, L.2    Eisenberg, D.3
  • 43
    • 0025681503 scopus 로고
    • Membrane proteins: from sequence to structure
    • von Heijne, G.; Manoil, C. Membrane proteins: from sequence to structure. Prot. Eng. 1990, 4, 109–112.
    • (1990) Prot. Eng. , vol.4 , pp. 109-112
    • von Heijne, G.1    Manoil, C.2
  • 44
    • 0026716643 scopus 로고
    • Membrane protein structure prediction: Hydrophobicity analysis and the “positive inside” rule
    • von Heijne, G. Membrane protein structure prediction: Hydrophobicity analysis and the “positive inside” rule. J. Mol. Biol. 1992, 225, 487–494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • von Heijne, G.1
  • 45
    • 0026642866 scopus 로고
    • Bacteriorhodopsin can be refolded from two independently stable tranmembrane helices and the complementary five-helix fragment
    • Kahn, T. W.; Engelman, D. M. Bacteriorhodopsin can be refolded from two independently stable tranmembrane helices and the complementary five-helix fragment. Biochemistry 1992, 31, 6144–6151.
    • (1992) Biochemistry , vol.31 , pp. 6144-6151
    • Kahn, T.W.1    Engelman, D.M.2
  • 46
    • 0023646081 scopus 로고
    • Mutations that uncouple the beta-adrenergic receptor from Gs and increase agonist affinity
    • Strader, C. D.; Dixon, R. A. F.; Cheung, A. H.; Candelore, M. R.; Blake, A. D.; Sigal, I. S. Mutations that uncouple the beta-adrenergic receptor from Gs and increase agonist affinity. J. Biol. Chem. 1987, 262, 16439–16443.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16439-16443
    • Strader, C.D.1    Dixon, R.A.F.2    Cheung, A.H.3    Candelore, M.R.4    Blake, A.D.5    Sigal, I.S.6
  • 49
    • 0021994880 scopus 로고
    • Structural analysis of carboxypeptidase A and its complexes with inhibitors as a basis for modeling enzyme recognition and specificity
    • Liebman, M. N.; Venanzi, C. A.; Weinstein, H. Structural analysis of carboxypeptidase A and its complexes with inhibitors as a basis for modeling enzyme recognition and specificity. Biopolymers 1985, 24, 1721–1758.
    • (1985) Biopolymers , vol.24 , pp. 1721-1758
    • Liebman, M.N.1    Venanzi, C.A.2    Weinstein, H.3
  • 50
    • 0026761782 scopus 로고
    • Modeling of the structure of bacteriorhodopsin
    • Jahnig, F.; Endholm, O. Modeling of the structure of bacteriorhodopsin. J. Mol. Biol. 1992, 225, 837–850.
    • (1992) J. Mol. Biol. , vol.225 , pp. 837-850
    • Jahnig, F.1    Endholm, O.2
  • 51
    • 0019729293 scopus 로고
    • Quantum chemical studies on molecular determinants of drug action
    • Weinstein, H.; Osman, R.; Topiol, S.; Green, J. P. Quantum chemical studies on molecular determinants of drug action. Ann. N. Y. Acad. Sci. 1981, 367, 434–451.
    • (1981) Ann. N. Y. Acad. Sci. , vol.367 , pp. 434-451
    • Weinstein, H.1    Osman, R.2    Topiol, S.3    Green, J.P.4
  • 52
    • 84983941884 scopus 로고
    • Molecular determinants for binding of methylenedioxytryptamines at 5-HT/LSD receptors
    • Reggio, P.; Weinstein, H.; Osman, R.; Topiol, S. Molecular determinants for binding of methylenedioxytryptamines at 5-HT/LSD receptors. Int. J. Quantum Chem. 1981, QBS8, 373–384.
    • (1981) Int. J. Quantum Chem. , vol.QBS8 , pp. 373-384
    • Reggio, P.1    Weinstein, H.2    Osman, R.3    Topiol, S.4
  • 53
    • 0003824417 scopus 로고
    • Electrostatic potentials as descriptors of molecular reactivity: The basis for some successful predictions of biological activity
    • Politzer, P., Truhlar, D. G., Eds.; Plenum Press: New York
    • Weinstein, H.; Osman, R.; Green, J. P.; Topiol, S. Electrostatic potentials as descriptors of molecular reactivity: The basis for some successful predictions of biological activity. In Chemical Applications of Atomic and Molecular Electrostatic Potentials; Politzer, P., Truhlar, D. G., Eds.; Plenum Press: New York, 1981; pp 309–323.
    • (1981) Chemical Applications of Atomic and Molecular Electrostatic Potentials , pp. 309-323
    • Weinstein, H.1    Osman, R.2    Green, J.P.3    Topiol, S.4
  • 54
    • 84987112016 scopus 로고
    • Theoretical and experimental studies of drug-receptor interactions: Determinants for recognition of 5-HT analogs
    • Mazurek, A. P.; Weinstein, H.; Osman, R.; Topiol, S.; Ebersole, B. J. Theoretical and experimental studies of drug-receptor interactions: Determinants for recognition of 5-HT analogs. Int. J. Quantum Chem. 1984, QBS11, 183–194.
    • (1984) Int. J. Quantum Chem. , vol.QBS11 , pp. 183-194
    • Mazurek, A.P.1    Weinstein, H.2    Osman, R.3    Topiol, S.4    Ebersole, B.J.5
  • 55
    • 0026630139 scopus 로고
    • Serine mutations in transmembrane V of the dopamine D1 receptor affect ligand interactions and receptor activation
    • Pollock, N. J.; Manelli, A. M.; Hutchins, C. W.; Steffey, M. E.; MacKenzie, R. G.; Frail, D. E. Serine mutations in transmembrane V of the dopamine D1 receptor affect ligand interactions and receptor activation. J. Biol. Chem. 1992, 267, 17780–17786.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17780-17786
    • Pollock, N.J.1    Manelli, A.M.2    Hutchins, C.W.3    Steffey, M.E.4    MacKenzie, R.G.5    Frail, D.E.6
  • 56
    • 0025642404 scopus 로고
    • An aspartate conserved among G-protein receptors confers allosteric regulation of a2-adrenergic receptors by sodium
    • Horstman, D. A.; Brandon, S.; Wilson, A. L.; Guyeer, C. A.; Gragoe, E. J.; Limbird, L. E. An aspartate conserved among G-protein receptors confers allosteric regulation of a2-adrenergic receptors by sodium. J. Biol. Chem. 1990, 265, 21590–21595.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21590-21595
    • Horstman, D.A.1    Brandon, S.2    Wilson, A.L.3    Guyeer, C.A.4    Gragoe, E.J.5    Limbird, L.E.6
  • 57
    • 0025852998 scopus 로고
    • Regulation of dopamine D2 receptors by sodium and pH
    • Neve, K. A. Regulation of dopamine D2 receptors by sodium and pH. Mol. Pharm. 1991, 39, 570–578.
    • (1991) Mol. Pharm. , vol.39 , pp. 570-578
    • Neve, K.A.1
  • 58
    • 0023893314 scopus 로고
    • Site-directed mutagenesis and continuous expression of human β-adrenergic receptors
    • Chung, F.-Z.; Wang, C.-D.; Potter, P. C.; Venter, J. C.; Fraser, C. M. Site-directed mutagenesis and continuous expression of human β-adrenergic receptors. J. Biol. Chem. 1988, 263, 4052–4055.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4052-4055
    • Chung, F.-Z.1    Wang, C.-D.2    Potter, P.C.3    Venter, J.C.4    Fraser, C.M.5
  • 59
    • 0026592357 scopus 로고
    • Constitutive activation of the alpha1B-adrenergic receptor by all amino acid substitutions at a single site
    • Kjelsberg, M. A.; Cotecchia, S.; Ostrowski, J.; Caron, M. G.; Lefkowitz, R. J. Constitutive activation of the alpha1B-adrenergic receptor by all amino acid substitutions at a single site. J. Biol. Chem. 1992, 267, 1430–1433.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1430-1433
    • Kjelsberg, M.A.1    Cotecchia, S.2    Ostrowski, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 60
    • 84946450438 scopus 로고
    • Algorithms for macromolecular dynamics and constraint dynamics
    • van Gunsteren, W. F.; Berendsen, H. J. C. Algorithms for macromolecular dynamics and constraint dynamics. J. Mol. Phys. 1977, 34, 1311–1327.
    • (1977) J. Mol. Phys. , vol.34 , pp. 1311-1327
    • van Gunsteren, W.F.1    Berendsen, H.J.C.2


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