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Volumn 55, Issue 6, 2009, Pages 355-361

Molecular modelling of subtypes (α2A, α2B and α2C) of α2-adrenoceptors: A comparative study

Author keywords

2 Adrenoceptor; AutoDock; Binding free energy; Docking; Homology modelling; Subtype selectivity

Indexed keywords

ALPHA 2 ADRENERGIC RECEPTOR; ALPHA 2A ADRENERGIC RECEPTOR; ALPHA 2B ADRENERGIC RECEPTOR; ALPHA 2C ADRENERGIC RECEPTOR;

EID: 67650096635     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2009.05.004     Document Type: Article
Times cited : (19)

References (39)
  • 2
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three dimensional models and computational probing of structure-function relationships in G-protein coupled receptors
    • Ballesteros J.A., and Weinstein H. Integrated methods for the construction of three dimensional models and computational probing of structure-function relationships in G-protein coupled receptors. Methods Neurosci. 25 (1995) 366-428
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 5
    • 33846053644 scopus 로고    scopus 로고
    • The in silico insights of α-adrenergic receptors over the last decade: methodological approaches and structural features of the 3D models
    • Carrieri A., and Fano A. The in silico insights of α-adrenergic receptors over the last decade: methodological approaches and structural features of the 3D models. Curr. Top. Med. Chem. 7 (2007) 195-205
    • (2007) Curr. Top. Med. Chem. , vol.7 , pp. 195-205
    • Carrieri, A.1    Fano, A.2
  • 7
    • 33846105981 scopus 로고    scopus 로고
    • Interest of α2-adrenergic agonists and antagonists in clinical practice: background, facts and perspectives
    • Crassous P.-A., Denis C., Paris H., and Senard J.M. Interest of α2-adrenergic agonists and antagonists in clinical practice: background, facts and perspectives. Curr. Top. Med. Chem. 7 (2007) 187-194
    • (2007) Curr. Top. Med. Chem. , vol.7 , pp. 187-194
    • Crassous, P.-A.1    Denis, C.2    Paris, H.3    Senard, J.M.4
  • 9
    • 3242879177 scopus 로고    scopus 로고
    • iMolTalk: an interactive, internet-based protein structure analysis server
    • Diemand A.V., and Scheib H. iMolTalk: an interactive, internet-based protein structure analysis server. Nucleic Acids Res. 32 (2004) 512-516
    • (2004) Nucleic Acids Res. , vol.32 , pp. 512-516
    • Diemand, A.V.1    Scheib, H.2
  • 11
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity-a rapid access to atomic charges
    • Gasteiger J., and Marsili M. Iterative partial equalization of orbital electronegativity-a rapid access to atomic charges. Tetrahedron 36 (1980) 3219-3228
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 14
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Proceedings of the Nucleic Acids Symposium Series, vol. 41 (1999) 95-98
    • (1999) Proceedings of the Nucleic Acids Symposium Series, vol. 41 , pp. 95-98
    • Hall, T.A.1
  • 15
    • 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., Backmann E., and Downing K.H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213 (1990) 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    Backmann, E.5    Downing, K.H.6
  • 16
    • 0031370977 scopus 로고    scopus 로고
    • LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins
    • Hendlich M., Rippmann F., and Barnickel G. LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins. J. Mol. Graph. Model. 15 (1997) 359-363
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 359-363
    • Hendlich, M.1    Rippmann, F.2    Barnickel, G.3
  • 17
    • 31944434856 scopus 로고    scopus 로고
    • Combination of a modified scoring function with two-dimensional descriptors for calculation of binding affinities of bulky, flexible ligands to proteins
    • Hetenyi C., Paragi G., Maran U., Timar Z., Karelson M., and Penke B. Combination of a modified scoring function with two-dimensional descriptors for calculation of binding affinities of bulky, flexible ligands to proteins. J. Am. Chem. Soc. 128 (2006) 1233-1239
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1233-1239
    • Hetenyi, C.1    Paragi, G.2    Maran, U.3    Timar, Z.4    Karelson, M.5    Penke, B.6
  • 20
    • 11244309572 scopus 로고    scopus 로고
    • Direct measurement of thermodynamic parameters of amyloid formation by isothermal titration calorimetry
    • Kardos J., Yamamoto K., Hasegawa K., Naiki H., and Goto Y. Direct measurement of thermodynamic parameters of amyloid formation by isothermal titration calorimetry. J. Biol. Chem. 279 (2004) 55308-55314
    • (2004) J. Biol. Chem. , vol.279 , pp. 55308-55314
    • Kardos, J.1    Yamamoto, K.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 21
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • Leavitt S., and Freire E. Direct measurement of protein binding energetics by isothermal titration calorimetry. Curr. Opin. Struct. Biol. 11 (2001) 560-566
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 22
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E., Hess B., and van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7 (2001) 306-317
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 23
    • 0026332547 scopus 로고
    • Electrostatic effects in protein: comparison of dielectric and charges model
    • Mehler E.L., and Solmayer T. Electrostatic effects in protein: comparison of dielectric and charges model. Prot. Eng. 4 (1991) 903-910
    • (1991) Prot. Eng. , vol.4 , pp. 903-910
    • Mehler, E.L.1    Solmayer, T.2
  • 24
  • 26
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • Okada T., Sugihara M., Bondar N., Elstner M., Entel P., and Buss V. The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. J. Mol. Biol. 342 (2004) 571-583
    • (2004) J. Mol. Biol. , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 27
    • 4043162793 scopus 로고    scopus 로고
    • Vega-an open platform to develop chemo-bio-informatics application, using plug-in architecture and script programming
    • Pedretti A., Villa L., and Vistoli G. Vega-an open platform to develop chemo-bio-informatics application, using plug-in architecture and script programming. J. Comput. Aided Mol. Des. 18 (2004) 167-173
    • (2004) J. Comput. Aided Mol. Des. , vol.18 , pp. 167-173
    • Pedretti, A.1    Villa, L.2    Vistoli, G.3
  • 31
    • 0035111158 scopus 로고    scopus 로고
    • Molecular structure and gas-phase reactivity of clonidine and rilmenidine: two-layered ONIOM calculations
    • Remko M., Walsh O.A., and Graham R.W. Molecular structure and gas-phase reactivity of clonidine and rilmenidine: two-layered ONIOM calculations. Phys. Chem. Chem. Phys. 3 (2001) 901-907
    • (2001) Phys. Chem. Chem. Phys. , vol.3 , pp. 901-907
    • Remko, M.1    Walsh, O.A.2    Graham, R.W.3
  • 32
    • 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
  • 34
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler G.F.X., Villa C., and Henderson R. Projection structure of rhodopsin. Nature 362 (1993) 770-772
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.X.1    Villa, C.2    Henderson, R.3
  • 35
    • 67650017508 scopus 로고    scopus 로고
    • SYBYL 7.2, Tripos Inc., 1699 South Hanley Rd., St. Louis, MO, USA.
    • SYBYL 7.2, Tripos Inc., 1699 South Hanley Rd., St. Louis, MO, USA.
  • 36
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)
    • Teller D.C., Okada T., Behnke C.A., Palczewski K., and Stenkamp R.E. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry 40 (2001) 7761-7772
    • (2001) Biochemistry , vol.40 , pp. 7761-7772
    • Teller, D.C.1    Okada, T.2    Behnke, C.A.3    Palczewski, K.4    Stenkamp, R.E.5
  • 38
    • 0026006986 scopus 로고
    • 2A-adrenergic receptors: identification of amino acids involved in ligand binding and receptor activation by agonists
    • 2A-adrenergic receptors: identification of amino acids involved in ligand binding and receptor activation by agonists. Mol. Pharmacol. 40 (1991) 168-179
    • (1991) Mol. Pharmacol. , vol.40 , pp. 168-179
    • Wang, C.D.1    Buck, M.A.2    Fraser, C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.