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Volumn 16, Issue 4, 2009, Pages 342-350

Molecular dynamics study of the internal water molecules in vasopressin and oxytocin receptors

Author keywords

GPCR; Internal water; Molecular dynamics; Protein hydration; Vasopressin and oxytocin receptors

Indexed keywords

LIGAND; OXYTOCIN; OXYTOCIN RECEPTOR; VASOPRESSIN DERIVATIVE; VASOPRESSIN RECEPTOR; WATER;

EID: 65349166282     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609787848072     Document Type: Article
Times cited : (5)

References (57)
  • 1
    • 0027082924 scopus 로고
    • Internal water molecules and H-bonding in biological macromolecules: A review of structural features with functional implications
    • Meyer, E. Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications. Prot. Sci., 1992, 1, 1543-1562.
    • (1992) Prot. Sci , vol.1 , pp. 1543-1562
    • Meyer, E.1
  • 3
    • 0042868638 scopus 로고    scopus 로고
    • Role of water mediated interactions in protein-protein recognition landscapes
    • Papoian, G.A.; Ulander, J.; Wolynes, P.G. Role of water mediated interactions in protein-protein recognition landscapes. J. Am. Chem. Soc., 2003, 125, 9170-9178.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 9170-9178
    • Papoian, G.A.1    Ulander, J.2    Wolynes, P.G.3
  • 4
    • 0037058894 scopus 로고    scopus 로고
    • Molecular recognition-viewed through the eyes of the solvent
    • Ben-Naim, A. Molecular recognition-viewed through the eyes of the solvent. Biophys. Chem., 2002, 101-102, 309-319.
    • (2002) Biophys. Chem , vol.101-102 , pp. 309-319
    • Ben-Naim, A.1
  • 5
    • 8644234346 scopus 로고    scopus 로고
    • Water-mediated interaction at a protein-protein interface
    • Ikura, T.; Urakubo, Y.; Nobutoshi, I. Water-mediated interaction at a protein-protein interface. Chem. Phys., 2004, 307, 111-119.
    • (2004) Chem. Phys , vol.307 , pp. 111-119
    • Ikura, T.1    Urakubo, Y.2    Nobutoshi, I.3
  • 6
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: An evolutionary success
    • Bockaert, J.; Pin, J.P. Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J., 1999, 18, 1723-1729.
    • (1999) EMBO J , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 8
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether, U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr. Rev., 2000, 21, 90-113.
    • (2000) Endocr. Rev , vol.21 , pp. 90-113
    • Gether, U.1
  • 9
    • 0038458865 scopus 로고    scopus 로고
    • Modeling the 3D structure of GPCRs: Advances and application to drug discovery
    • Becker, O.M.; Shacham, S.; Marantz, Y.; Noiman, S. Modeling the 3D structure of GPCRs: advances and application to drug discovery. Curr. Opin. DrugDiscov. Devel., 2003, 6, 353-361.
    • (2003) Curr. Opin. DrugDiscov. Devel , vol.6 , pp. 353-361
    • Becker, O.M.1    Shacham, S.2    Marantz, Y.3    Noiman, S.4
  • 10
    • 0034801665 scopus 로고    scopus 로고
    • G protein-coupled receptor drug discovery: Implications from the crystal structure of rhodopsin
    • Ballesteros, J.; Palczewski, K. G protein-coupled receptor drug discovery: implications from the crystal structure of rhodopsin. Curr. Opin. DrugDiscov. Devel., 2001, 4, 561-574.
    • (2001) Curr. Opin. DrugDiscov. Devel , vol.4 , pp. 561-574
    • Ballesteros, J.1    Palczewski, K.2
  • 11
    • 0031951116 scopus 로고    scopus 로고
    • Structural bases of vaso-pressin/oxytocin receptor function
    • Barberis, C.; Mouillac, B.; Durroux, T. Structural bases of vaso-pressin/oxytocin receptor function. J. Endocrinol., 1998, 156, 223-229.
    • (1998) J. Endocrinol , vol.156 , pp. 223-229
    • Barberis, C.1    Mouillac, B.2    Durroux, T.3
  • 13
    • 0032452027 scopus 로고    scopus 로고
    • Signal transduction pathways of the human V1-vascular, V2-renal, V3-pituitary vasopressin and oxytocin receptors
    • Thibonnier, M.; Berti-Mattera, L.N.; Dulin, N.; Conarty, D.M.; Mattera, R. Signal transduction pathways of the human V1-vascular, V2-renal, V3-pituitary vasopressin and oxytocin receptors. Prog. Brain. Res., 1998, 119, 147-161.
    • (1998) Prog. Brain. Res , vol.119 , pp. 147-161
    • Thibonnier, M.1    Berti-Mattera, L.N.2    Dulin, N.3    Conarty, D.M.4    Mattera, R.5
  • 15
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros, J.A.; Shi, L.; Javitch, J.A. Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol. Pharmacol., 2001, 60, 1-19.
    • (2001) Mol. Pharmacol , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 16
    • 0037452868 scopus 로고    scopus 로고
    • Sequence analyses of G-protein-coupled receptors: Similarities to rhodopsin
    • Mirzadegan, T.; Benko, G.; Filipek, S.; Palczewski, K. Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin. Biochemistry, 42, 2003, 2759-2767.
    • (2003) Biochemistry , vol.42 , pp. 2759-2767
    • Mirzadegan, T.1    Benko, G.2    Filipek, S.3    Palczewski, K.4
  • 17
    • 0037215651 scopus 로고    scopus 로고
    • Rhodopsin crystal: New template yielding realistic models of G-protein-coupled receptors?
    • Archer, E.; Maigret, B.; Escrieut, C.; Pradayrol, L.; Fourmy, D. Rhodopsin crystal: new template yielding realistic models of G-protein-coupled receptors? Trends Pharmacol. Sci., 2003, 24, 36-40.
    • (2003) Trends Pharmacol. Sci , vol.24 , pp. 36-40
    • Archer, E.1    Maigret, B.2    Escrieut, C.3    Pradayrol, L.4    Fourmy, D.5
  • 20
    • 2442438851 scopus 로고    scopus 로고
    • Homo-and hetero-dimeric complex formations of the human oxytocin receptor
    • Devost, D.; Zingg, H.H. Homo-and hetero-dimeric complex formations of the human oxytocin receptor. J. Neuroendocrinol., 2004, 16 372-377.
    • (2004) J. Neuroendocrinol , vol.16 , pp. 372-377
    • Devost, D.1    Zingg, H.H.2
  • 21
    • 0029837656 scopus 로고    scopus 로고
    • Vasopressin and oxytocin receptors in the central nervous system
    • Barberis, C.; Tribollet, E. Vasopressin and oxytocin receptors in the central nervous system. Crit. Rev. Neurobiol., 1996, 10, 119-154.
    • (1996) Crit. Rev. Neurobiol , vol.10 , pp. 119-154
    • Barberis, C.1    Tribollet, E.2
  • 22
    • 33644764283 scopus 로고    scopus 로고
    • The effect of tightly-bound water molecules on scaffold diversity in computer-aided de novo ligand design of CDK-2 inhibitors
    • Garcia-Sosa, A.T.; Mancera, R.L. The effect of tightly-bound water molecules on scaffold diversity in computer-aided de novo ligand design of CDK-2 inhibitors. J. Mol. Model., 2006, 12, 422-431.
    • (2006) J. Mol. Model , vol.12 , pp. 422-431
    • Garcia-Sosa, A.T.1    Mancera, R.L.2
  • 23
    • 33645783040 scopus 로고    scopus 로고
    • Probing a model of a GPCR/ligand complex in an explicit membrane environment. The human cholecystokinin-1 receptor
    • Hénin, J.; Maigret, B.; Tarek, M.; Escrieut, C.; Fourmy, D.; Chi-pot, C. Probing a model of a GPCR/ligand complex in an explicit membrane environment. The human cholecystokinin-1 receptor. Biophys. J., 2006, 90, 1232-1240.
    • (2006) Biophys. J , vol.90 , pp. 1232-1240
    • Hénin, J.1    Maigret, B.2    Tarek, M.3    Escrieut, C.4    Fourmy, D.5    Chi-pot, C.6
  • 24
    • 1542316348 scopus 로고    scopus 로고
    • Novel approaches for modeling of the Al adenosine receptor and its agonist binding site
    • Gutiérrez-de-Teran, H.; Centeno, N.B.; Pastor, M.; Sanz, F. Novel approaches for modeling of the Al adenosine receptor and its agonist binding site. Proteins, 2004, 54, 705-715.
    • (2004) Proteins , vol.54 , pp. 705-715
    • Gutiérrez-de-Teran, H.1    Centeno, N.B.2    Pastor, M.3    Sanz, F.4
  • 25
    • 29244479584 scopus 로고    scopus 로고
    • Molecular dynamics simulations of bovine rhodopsin: Influence of protonation states and different membrane-mimicking environments
    • Schlegel, B.; Sippl, W.; Höltje, H-D. Molecular dynamics simulations of bovine rhodopsin: influence of protonation states and different membrane-mimicking environments. J. Mol. Model., 2005, 12, 49-64.
    • (2005) J. Mol. Model , vol.12 , pp. 49-64
    • Schlegel, B.1    Sippl, W.2    Höltje, H.-D.3
  • 26
    • 0037015153 scopus 로고    scopus 로고
    • Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations
    • Röhrig, U.F.; Guidoni, L.; Rothlisberger, U. Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations. Biochemistry, 2000, 41, 10799-10809.
    • (2000) Biochemistry , vol.41 , pp. 10799-10809
    • Röhrig, U.F.1    Guidoni, L.2    Rothlisberger, U.3
  • 27
    • 33644679534 scopus 로고    scopus 로고
    • Structural changes in the Schiff base region of squid rhodopsin upon photoisomerization studied by low-temperature FTIR spectroscopy
    • Ota, T.; Furutani, Y.; Terakita, A.; Shichida, Y.; Kandori, H. Structural changes in the Schiff base region of squid rhodopsin upon photoisomerization studied by low-temperature FTIR spectroscopy. Biochemistry, 2006, 45, 2845-2851.
    • (2006) Biochemistry , vol.45 , pp. 2845-2851
    • Ota, T.1    Furutani, Y.2    Terakita, A.3    Shichida, Y.4    Kandori, H.5
  • 28
    • 0037197848 scopus 로고    scopus 로고
    • Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography
    • Okada, T.; Fujiyoshi, Y.; Silow, M.; Navarro, J.; Landau, E.M.; Shichida, Y. Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. Proc. Natl. Acad. Sci., 2002, 99, 5982-5987.
    • (2002) Proc. Natl. Acad. Sci , vol.99 , pp. 5982-5987
    • Okada, T.1    Fujiyoshi, Y.2    Silow, M.3    Navarro, J.4    Landau, E.M.5    Shichida, Y.6
  • 29
    • 33645698998 scopus 로고    scopus 로고
    • Investigation of mechanism of desmopressin binding in vasopressin V2 receptor versus vasopressin Via and oxytocin receptors-molecular dynamics simulation of the agonist-bound state in the membrane-aqueous system
    • Ślusarz, M.J.; Ślusarz, R.; Ciarkowski, J. Investigation of mechanism of desmopressin binding in vasopressin V2 receptor versus vasopressin Via and oxytocin receptors-molecular dynamics simulation of the agonist-bound state in the membrane-aqueous system. Biopolymers, 2006, 81, 321-338.
    • (2006) Biopolymers , vol.81 , pp. 321-338
    • Ślusarz, M.J.1    Ślusarz, R.2    Ciarkowski, J.3
  • 31
    • 4744371035 scopus 로고    scopus 로고
    • Molecular dynamics of complexes of atosiban with neurohypophy-seal receptors in the fully hydrated phospolipid bilayer
    • Ślusarz, M.J.; Ślusarz, R.; Meadows, R.; Trojnar, J.; Ciarkowski, J. Molecular dynamics of complexes of atosiban with neurohypophy-seal receptors in the fully hydrated phospolipid bilayer. QSAR Comb. Sci., 2004, 23, 536-545.
    • (2004) QSAR Comb. Sci , vol.23 , pp. 536-545
    • Ślusarz, M.J.1    Ślusarz, R.2    Meadows, R.3    Trojnar, J.4    Ciarkowski, J.5
  • 32
    • 23044496352 scopus 로고    scopus 로고
    • Study of New Oxytocin Antagonist Barusiban Fe200 440, Affinity Toward Human Oxytocin Receptor Versus Vasopressin V1a and V2 Receptors-Molecular Dynamics Simulation in POPC Bilayer
    • Ślusarz, M.J.; Gieldón, A.; Ślusarz, R.; Meadows, R.; Trojnar, J.; Ciarkowski, J. Study of New Oxytocin Antagonist Barusiban Fe200 440, Affinity Toward Human Oxytocin Receptor Versus Vasopressin V1a and V2 Receptors-Molecular Dynamics Simulation in POPC Bilayer. QSAR Comb. Sci., 2005, 24, 603-610.
    • (2005) QSAR Comb. Sci , vol.24 , pp. 603-610
    • Ślusarz, M.J.1    Gieldón, A.2    Ślusarz, R.3    Meadows, R.4    Trojnar, J.5    Ciarkowski, J.6
  • 33
    • 33644789620 scopus 로고    scopus 로고
    • Molecular dynamics simulation of human neurohypophyseal hormone receptors complexed with oxytocin-modeling of an activated state
    • Ślusarz, M.J.; Ślusarz, R.; Ciarkowski, J. Molecular dynamics simulation of human neurohypophyseal hormone receptors complexed with oxytocin-modeling of an activated state. J. Pept. Sci., 2006, 12, 171-179.
    • (2006) J. Pept. Sci , vol.12 , pp. 171-179
    • Ślusarz, M.J.1    Ślusarz, R.2    Ciarkowski, J.3
  • 34
    • 33644790823 scopus 로고    scopus 로고
    • Analysis of interactions responsible for vasopressin binding to human neurohypophyseal hormone receptors-molecular dynamics study of the activated receptor-vasopressin-Gα systems
    • Ślusarz, M.J.; Gieldoń, A.; Ślusarz, R.; Ciarkowski, J. Analysis of interactions responsible for vasopressin binding to human neurohypophyseal hormone receptors-molecular dynamics study of the activated receptor-vasopressin-Gα systems. J. Pept. Sci., 2006, 12, 180-189.
    • (2006) J. Pept. Sci , vol.12 , pp. 180-189
    • Ślusarz, M.J.1    Gieldoń, A.2    Ślusarz, R.3    Ciarkowski, J.4
  • 35
    • 33646111925 scopus 로고    scopus 로고
    • Molecular docking-based study of vasopressin analogues modified at positions 2 and 3 with N-methylphenylalanine: Influence on receptor-bound conformations and interactions with vasopressin and oxytocin receptors
    • Ślusarz, M.J.; Sikorska, E.; Ślusarz, R.; Ciarkowski, J. Molecular docking-based study of vasopressin analogues modified at positions 2 and 3 with N-methylphenylalanine: influence on receptor-bound conformations and interactions with vasopressin and oxytocin receptors. J. Med. Chem., 2006, 49, 2463-2469.
    • (2006) J. Med. Chem , vol.49 , pp. 2463-2469
    • Ślusarz, M.J.1    Sikorska, E.2    Ślusarz, R.3    Ciarkowski, J.4
  • 36
    • 84986516411 scopus 로고
    • Application of the Multimolecule and Multiconformational RESP Methodology to Biopolymers: Charge Derication for DNA, RNA, and Proteins
    • Cieplak, P.; Cornell, W.D.; Bayly, C.; Kollman, P.A. Application of the Multimolecule and Multiconformational RESP Methodology to Biopolymers: Charge Derication for DNA, RNA, and Proteins. J. Comput. Chem. 1995, 16, 1357-1377.
    • (1995) J. Comput. Chem , vol.16 , pp. 1357-1377
    • Cieplak, P.1    Cornell, W.D.2    Bayly, C.3    Kollman, P.A.4
  • 38
    • 65349095730 scopus 로고    scopus 로고
    • Sybyl 6.8, Tripos Inc. 1699 South Hanley Rd.; St. Louis, MO 63144, U.S.A.
    • Sybyl 6.8, Tripos Inc. 1699 South Hanley Rd.; St. Louis, MO 63144, U.S.A.
  • 40
    • 65349162957 scopus 로고    scopus 로고
    • Case, D.A.; Pearlman, D.A.; Caldwell, J.W.; Cheatham, T.E.; Wang, J.; Ross, W.S.; Simmerling, C.L.; Darden, T.A.; Merz, K.M.; Stanton, R.V.; Cheng, A.; Vincent, J.J.; Crowley, M.; Tsui, V.; Gohlke, H.; Radmer, R.; Duan, Y.; Pitera, J.; Massova, I.; Seibel, G.L.; Singh, U.C.; Weiner, P.; Kollman, P.A. Amber 7. University of California, San Francisco, 2002.
    • Case, D.A.; Pearlman, D.A.; Caldwell, J.W.; Cheatham, T.E.; Wang, J.; Ross, W.S.; Simmerling, C.L.; Darden, T.A.; Merz, K.M.; Stanton, R.V.; Cheng, A.; Vincent, J.J.; Crowley, M.; Tsui, V.; Gohlke, H.; Radmer, R.; Duan, Y.; Pitera, J.; Massova, I.; Seibel, G.L.; Singh, U.C.; Weiner, P.; Kollman, P.A. Amber 7. University of California, San Francisco, 2002.
  • 41
    • 0022446888 scopus 로고
    • Structure of pressinoic acid: The cyclic moiety of vasopressin
    • Langs, D.A.; Smith, G.D.; Stezowski, J.J.; Hughes, R.E. Structure of pressinoic acid: the cyclic moiety of vasopressin. Science, 1986, 232, 1240-1242.
    • (1986) Science , vol.232 , pp. 1240-1242
    • Langs, D.A.1    Smith, G.D.2    Stezowski, J.J.3    Hughes, R.E.4
  • 42
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a La-marckian genetic algorithm and an empirical binding free energy function
    • Morris, G.M.; Goodsell, D.S.; Halliday, R.S.; Huey, R.; Hart, W.E.; Belew, R.K.; Olson, A.J. Automated docking using a La-marckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem., 1998, 19, 1639-1662.
    • (1998) J. Comput. Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 43
    • 0029705324 scopus 로고    scopus 로고
    • Automated docking of flexible ligands: Applications of AutoDock
    • Goodsell, D.S.; Morris, G.M.; Olson, A.J. Automated docking of flexible ligands: applications of AutoDock. J. Mol. Recognition, 1996, 9, 1-5.
    • (1996) J. Mol. Recognition , vol.9 , pp. 1-5
    • Goodsell, D.S.1    Morris, G.M.2    Olson, A.J.3
  • 44
    • 0034950798 scopus 로고    scopus 로고
    • Effects of phospholipid unsaturation on the membrane/water interface: A molecular simulation study
    • Murzyn, K.; Róg, T.; Jezierski, G.; Takaoka, Y.; Pasenkiewicz-Gierula, M. Effects of phospholipid unsaturation on the membrane/water interface: a molecular simulation study. Biophys. J., 2001, 81, 170-183.
    • (2001) Biophys. J , vol.81 , pp. 170-183
    • Murzyn, K.1    Róg, T.2    Jezierski, G.3    Takaoka, Y.4    Pasenkiewicz-Gierula, M.5
  • 47
    • 33645941402 scopus 로고
    • The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen, W.L.; Tirado-Rives, J. The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin. J. Am. Chem. Soc., 1988, 770, 1657-1666.
    • (1988) J. Am. Chem. Soc , vol.770 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 48
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential RESP, model perform in calcluating confor-mational energies of organic and biological molecules?
    • Wang, J.; Cieplak, P.; Kollman, P.A. How well does a restrained electrostatic potential RESP, model perform in calcluating confor-mational energies of organic and biological molecules? J. Comput. Chem., 2000, 21, 1049-1074.
    • (2000) J. Comput. Chem , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 49
    • 0034284122 scopus 로고    scopus 로고
    • Recent changes to RasMol, recombining the variants
    • Bernstein, H.J. Recent changes to RasMol, recombining the variants. TIBS 2000, 2000, 25, 453-455.
    • (2000) TIBS , vol.2000 , Issue.25 , pp. 453-455
    • Bernstein, H.J.1
  • 50
    • 77957055780 scopus 로고
    • Integrated Methods for Modeling G-Protein Coupled Receptors
    • Ballesteros, J.A.; Weinstein, H. Integrated Methods for Modeling G-Protein Coupled Receptors. Methods Neurosci., 1995, 25, 366-428.
    • (1995) Methods Neurosci , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 51
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide crosslinking
    • Hubbell, W.L.; Altenbach, C.; Hubbell, C.M.; Khorana, H.G. Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide crosslinking. Adv. Protein Chem., 2003, 63, 243-290.
    • (2003) Adv. Protein Chem , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 52
    • 0033033914 scopus 로고    scopus 로고
    • Activation Mechanism of Human Oxytocin Receptor: A Combined Study of Experimental and Computer-Simulated Mutagenesis
    • Fanelli, F.; Barbier, P.; Zanchetta, D.; De Benedetti, P.G.; Chini, B. Activation Mechanism of Human Oxytocin Receptor: A Combined Study of Experimental and Computer-Simulated Mutagenesis. Mol. Pharmacol., 1999, 56, 214-225.
    • (1999) Mol. Pharmacol , vol.56 , pp. 214-225
    • Fanelli, F.1    Barbier, P.2    Zanchetta, D.3    De Benedetti, P.G.4    Chini, B.5
  • 53
    • 0031647808 scopus 로고    scopus 로고
    • Structure/function studies on receptors for vasopressin and oxytocin
    • Wheatley, M.; Hawtin, S.R.; Yarwood, N.J. Structure/function studies on receptors for vasopressin and oxytocin. Adv. Exp. Med. Biol., 1998, 449, 363-365.
    • (1998) Adv. Exp. Med. Biol , vol.449 , pp. 363-365
    • Wheatley, M.1    Hawtin, S.R.2    Yarwood, N.J.3
  • 55
    • 0029011757 scopus 로고
    • Related contribution of specific helix 2 and 7 residues to conformational activation of the serotonin 5-HT2A receptor
    • Sealfon, S.C; Chi, L.; Ebersole, B.J.; Rodic, V.; Zhang, D.; Ballesteros, J.A.; Weinstein, H. Related contribution of specific helix 2 and 7 residues to conformational activation of the serotonin 5-HT2A receptor. J. Biol. Chem., 1995, 270, 16683-16688.
    • (1995) J. Biol. Chem , vol.270 , pp. 16683-16688
    • Sealfon, S.C.1    Chi, L.2    Ebersole, B.J.3    Rodic, V.4    Zhang, D.5    Ballesteros, J.A.6    Weinstein, H.7
  • 56
    • 0037329292 scopus 로고    scopus 로고
    • Structure and activation of muscarinic acetylcholine receptors
    • Hulme, E.C.; Lu, Z.L.; Saldanha, J.W.; Bee, M.S. Structure and activation of muscarinic acetylcholine receptors. Biochem. Soc. Trans., 2001, 31, 29-34.
    • (2001) Biochem. Soc. Trans , vol.31 , pp. 29-34
    • Hulme, E.C.1    Lu, Z.L.2    Saldanha, J.W.3    Bee, M.S.4
  • 57
    • 0032819441 scopus 로고    scopus 로고
    • A Mutation in the Second Transmembrane Region of the CB1 Receptor Selectively Disrupts G Protein Signaling and Prevents Receptor Internalization
    • Roche, J.P.; Bounds, S.; Brown, S.; Mackie, K. A Mutation in the Second Transmembrane Region of the CB1 Receptor Selectively Disrupts G Protein Signaling and Prevents Receptor Internalization. Mol. Pharmacol., 1999, 56, 611-618.
    • (1999) Mol. Pharmacol , vol.56 , pp. 611-618
    • Roche, J.P.1    Bounds, S.2    Brown, S.3    Mackie, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.