메뉴 건너뛰기




Volumn 15, Issue 10, 2014, Pages 996-1006

Computational approaches for modeling GPCR dimerization

Author keywords

Brownian dynamics simulations; Coarse grained MD simulations; Computer modeling; Membrane protein dimerization; Molecular dynamics simulations; Protein docking

Indexed keywords

ADENOSINE A2A RECEPTOR; BETA 1 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR; CHEMOKINE RECEPTOR CXCR4; G PROTEIN COUPLED RECEPTOR; HISTAMINE H1 RECEPTOR; LUTEINIZING HORMONE RECEPTOR; MEMBRANE PROTEIN; NEUROTENSIN RECEPTOR; OPSIN; RHODOPSIN; THROMBOXANE A2 RECEPTOR; THYROTROPIN RECEPTOR;

EID: 84930983678     PISSN: 13892010     EISSN: 18734316     Source Type: Journal    
DOI: 10.2174/1389201015666141013102515     Document Type: Article
Times cited : (16)

References (95)
  • 1
    • 3543080493 scopus 로고    scopus 로고
    • The state of GPCR research in 2004.
    • 575-577, 626
    • [I] Ellis, C. The state of GPCR research in 2004. Nat. Rev. Drug Discov., 2004, 3(7), 575, 575-577, 626.
    • (2004) Nat. Rev. Drug Discov , vol.3 , Issue.7 , pp. 575
    • Ellis, C.1
  • 2
    • 0033843626 scopus 로고    scopus 로고
    • Towards 3D structures of G protein-coupled receptors: A multidisciplinary approach
    • [2] Muller, G. Towards 3D structures of G protein-coupled receptors: a multidisciplinary approach. Curr. Med. Chem., 2000, 7(9), 861-888.
    • (2000) Curr. Med. Chem. , vol.7 , Issue.9 , pp. 861-888
    • Muller, G.1
  • 3
    • 33847419390 scopus 로고    scopus 로고
    • International union of basic and clinical pharmacology. LXVII. Recommendations for the recognition and nomenclature of G protein-coupled receptor heteromultimers
    • [3] Pin, J.P.; Neubig, R.; Bouvier, M.; Devi, L.; Filizola, M.; Javitch, J.A.; Lohse, M.J.; Milligan, G.; Palczewski, K.; Parmentier, M.; Spedding, M. International union of basic and clinical pharmacology. LXVII. Recommendations for the recognition and nomenclature of G protein-coupled receptor heteromultimers. Pharmacol. Rev., 2007, 59(1), 5-13.
    • (2007) Pharmacol. Rev. , vol.59 , Issue.1 , pp. 5-13
    • Pin, J.P.1    Neubig, R.2    Bouvier, M.3    Devi, L.4    Filizola, M.5    Javitch, J.A.6    Lohse, M.J.7    Milligan, G.8    Palczewski, K.9    Parmentier, M.10    Spedding, M.11
  • 5
    • 85039894030 scopus 로고    scopus 로고
    • Advances in experimental medicine and biology: G protein-coupled receptors - modeling and simulation
    • [5] Filizola, M. Advances in experimental medicine and biology: G protein-coupled receptors - modeling and simulation, Part II GPCRs in motion: insights from simulations. 2014, 796, 37-125.
    • (2014) Part II Gpcrs in Motion: Insights from Simulations , vol.796 , pp. 37-125
    • Filizola, M.1
  • 6
    • 0034724192 scopus 로고    scopus 로고
    • Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • [6] Angers, S.; Salahpour, A.; Joly, E.; Hilairet, S.; Chelsky, D.; Dennis, M.; Bouvier, M. Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci. USA, 2000, 97(7), 3684-3689.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.7 , pp. 3684-3689
    • Angers, S.1    Salahpour, A.2    Joly, E.3    Hilairet, S.4    Chelsky, D.5    Dennis, M.6    Bouvier, M.7
  • 7
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: An emerging concept for G protein-coupled receptor ontogeny and function
    • [7] Angers, S.; Salahpour, A.; Bouvier, M. Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. Annu. Rev. Pharmacol. Toxicol., 2002, 42, 409-435.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 8
    • 0035930602 scopus 로고    scopus 로고
    • Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer
    • [8] Cheng, Z.J.; Miller, L.J. Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer. J. Biol. Chem., 2001, 276(51), 48040-48047.
    • (2001) J. Biol. Chem. , vol.276 , Issue.51 , pp. 48040-48047
    • Cheng, Z.J.1    Miller, L.J.2
  • 9
    • 0035958023 scopus 로고    scopus 로고
    • Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta -opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy
    • [9] McVey, M.; Ramsay, D.; Kellett, E.; Rees, S.; Wilson, S.; Pope, A.J.; Milligan, G. Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta -opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy. J. Biol. Chem., 2001, 276(17), 14092-14099.
    • (2001) J. Biol. Chem. , vol.276 , Issue.17 , pp. 14092-14099
    • Mcvey, M.1    Ramsay, D.2    Kellett, E.3    Rees, S.4    Wilson, S.5    Pope, A.J.6    Milligan, G.7
  • 10
    • 0038237527 scopus 로고    scopus 로고
    • Homodimerization of neuropeptide y receptors investigated by fluorescence resonance energy transfer in living cells
    • [10] Dinger, M.C.; Bader, J.E.; Kobor, A.D.; Kretzschmar, A.K.; Beck-Sickinger, A.G. Homodimerization of neuropeptide y receptors investigated by fluorescence resonance energy transfer in living cells. J. Biol. Chem., 2003, 278(12), 10562-10571.
    • (2003) J. Biol. Chem. , vol.278 , Issue.12 , pp. 10562-10571
    • Dinger, M.C.1    Bader, J.E.2    Kobor, A.D.3    Kretzschmar, A.K.4    Beck-Sickinger, A.G.5
  • 11
    • 28444493656 scopus 로고    scopus 로고
    • Crosstalk in G protein-coupled receptors: Changes at the transmembrane homodimer interface determine activation
    • 11[] Guo, W.; Shi, L.; Filizola, M.; Weinstein, H.; Javitch, J.A. Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation. Proc. Natl. Acad. Sci. USA, 2005, 102(48), 17495-17500.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.48 , pp. 17495-17500
    • Guo, W.1    Shi, L.2    Filizola, M.3    Weinstein, H.4    Javitch, J.A.5
  • 12
    • 0029556994 scopus 로고
    • Projection structure of frog rhodopsin in two crystal forms
    • [12] Schertler, G.F.; Hargrave, P.A. Projection structure of frog rhodopsin in two crystal forms. Proc. Natl. Acad. Sci. USA, 1995, 92(25), 11578-11582.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , Issue.25 , pp. 11578-11582
    • Schertler, G.F.1    Hargrave, P.A.2
  • 14
    • 0035976714 scopus 로고    scopus 로고
    • Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane
    • [14] Davies, A.; Gowen, B.E.; Krebs, A.M.; Schertler, G.F.; Saibil, H.R. Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane. J. Mol. Biol., 2001, 314(3), 455-463.
    • (2001) J. Mol. Biol. , vol.314 , Issue.3 , pp. 455-463
    • Davies, A.1    Gowen, B.E.2    Krebs, A.M.3    Schertler, G.F.4    Saibil, H.R.5
  • 15
    • 0037426865 scopus 로고    scopus 로고
    • Atomic-force microscopy: Rhodopsin dimers in native disc membranes
    • [15] Fotiadis, D.; Liang, Y.; Filipek, S.; Saperstein, D.A.; Engel, A.; Palczewski, K. Atomic-force microscopy: Rhodopsin dimers in native disc membranes. Nature, 2003, 421(6919), 127-128.
    • (2003) Nature , vol.421 , Issue.6919 , pp. 127-128
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5    Palczewski, K.6
  • 16
    • 1942468189 scopus 로고    scopus 로고
    • The G protein-coupled receptor rhodopsin in the native membrane. FEBS
    • [16] Fotiadis, D.; Liang, Y.; Filipek, S.; Saperstein, D.A.; Engel, A.; Palczewski, K. The G protein-coupled receptor rhodopsin in the native membrane. FEBS. Lett., 2004, 564(3), 281-288.
    • (2004) Lett. , vol.564 , Issue.3 , pp. 281-288
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5    Palczewski, K.6
  • 17
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • [17] Liang, Y.; Fotiadis, D.; Filipek, S.; Saperstein, D.A.; Palczewski, K.; Engel, A. Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J. Biol. Chem., 2003, 278(24), 21655-21662.
    • (2003) J. Biol. Chem. , vol.278 , Issue.24 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 18
    • 84884683292 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy analysis of serotonin, adrenergic, muscarinic, and dopamine receptor dimerization: The oligomer number puzzle. Mol
    • [18] Herrick-Davis, K.; Grinde, E.; Cowan, A.; Mazurkiewicz, J.E. Fluorescence correlation spectroscopy analysis of serotonin, adrenergic, muscarinic, and dopamine receptor dimerization: the oligomer number puzzle. Mol. Pharmacol., 2013, 84(4), 630-642.
    • (2013) Pharmacol. , vol.84 , Issue.4 , pp. 630-642
    • Herrick-Davis, K.1    Grinde, E.2    Cowan, A.3    Mazurkiewicz, J.E.4
  • 19
    • 84890612981 scopus 로고    scopus 로고
    • Single-molecule imaging revealed dynamic GPCR dimerization
    • [19] Kasai, R.S.; Kusumi, A. Single-molecule imaging revealed dynamic GPCR dimerization. Curr. Opin. Cell Biol., 2014, 27, 78-86.
    • (2014) Curr. Opin. Cell Biol. , vol.27 , pp. 78-86
    • Kasai, R.S.1    Kusumi, A.2
  • 20
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • [20] Park, J.H.; Scheerer, P.; Hofmann, K.P.; Choe, H.W.; Ernst, O.P. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nat., 2008, 454(7201), 183-187.
    • (2008) Nat. , vol.454 , Issue.7201 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 25
    • 84876197291 scopus 로고    scopus 로고
    • Crystal structure of oligomeric beta1-adrenergic G protein-coupled receptors in ligand-free basal state
    • [25] Huang, J.; Chen, S.; Zhang, J.J.; Huang, X.Y. Crystal structure of oligomeric beta1-adrenergic G protein-coupled receptors in ligand-free basal state. Nat. Struct. Mol. Biol., 2013, 20(4), 419-425.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , Issue.4 , pp. 419-425
    • Huang, J.1    Chen, S.2    Zhang, J.J.3    Huang, X.Y.4
  • 26
    • 72449150733 scopus 로고    scopus 로고
    • Bioinformatics and molecular modelling approaches to GPCR oligomerization
    • [26] Simpson, L.M.; Taddese, B.; Wall, I.D.; Reynolds, C.A. Bioinformatics and molecular modelling approaches to GPCR oligomerization. Curr. Opin. Pharmacol., 2010, 10(1), 30-37.
    • (2010) Curr. Opin. Pharmacol. , vol.10 , Issue.1 , pp. 30-37
    • Simpson, L.M.1    Taddese, B.2    Wall, I.D.3    Reynolds, C.A.4
  • 27
    • 80053487319 scopus 로고    scopus 로고
    • Oligomerization of G protein-coupled receptors: Computational methods
    • [27] Selent, J.; Kaczor, A.A. Oligomerization of G protein-coupled receptors: computational methods. Curr. Med. Chem., 2011, 18(30), 4588-4605.
    • (2011) Curr. Med. Chem. , vol.18 , Issue.30 , pp. 4588-4605
    • Selent, J.1    Kaczor, A.A.2
  • 28
    • 85039879766 scopus 로고    scopus 로고
    • Receptor-Receptor interactions. Chapter 4 Simulating G Protein-coupled receptors in native-like membranes: From monomers to oligomers
    • [28] Conn, P.M. Receptor-Receptor interactions. Chapter 4 Simulating G Protein-coupled receptors in native-like membranes: from monomers to oligomers. Methods Cell Biol., 2013, 117, 63-90.
    • (2013) Methods Cell Biol. , vol.117 , pp. 63-90
    • Conn, P.M.1
  • 31
    • 84863535732 scopus 로고    scopus 로고
    • Structural determinants of the supramolecular organization of G protein-coupled receptors in bilayers
    • [31] Periole, X.; Knepp, A.M.; Sakmar, T.P.; Marrink, S.J.; Huber, T. Structural determinants of the supramolecular organization of G protein-coupled receptors in bilayers. J. Am. Chem. Soc., 2012, 134(26), 10959-10965.
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.26 , pp. 10959-10965
    • Periole, X.1    Knepp, A.M.2    Sakmar, T.P.3    Marrink, S.J.4    Huber, T.5
  • 32
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • [32] Murakami, M.; Kouyama, T. Crystal structure of squid rhodopsin. Nature, 2008, 453(7193), 363-367.
    • (2008) Nature , vol.453 , Issue.7193 , pp. 363-367
    • Murakami, M.1    Kouyama, T.2
  • 34
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • [34] Lichtarge, O.; Bourne, H.R.; Cohen, F.E. An evolutionary trace method defines binding surfaces common to protein families. J. Mol. Biol., 1996, 257(2), 342-358.
    • (1996) J. Mol. Biol. , vol.257 , Issue.2 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 35
    • 0028295169 scopus 로고
    • Correlated mutations and residue contacts in proteins
    • [35] Gobel, U.; Sander, C.; Schneider, R.; Valencia, A. Correlated mutations and residue contacts in proteins. Proteins, 1994, 18(4), 309-317.
    • (1994) Proteins , vol.18 , Issue.4 , pp. 309-317
    • Gobel, U.1    Sander, C.2    Schneider, R.3    Valencia, A.4
  • 36
    • 0035664761 scopus 로고    scopus 로고
    • Lipid-facing correlated mutations and dimerization in G-protein coupled receptors
    • [36] Gouldson, P.R.; Dean, M.K.; Snell, C.R.; Bywater, R.P.; Gkoutos, G.; Reynolds, C.A. Lipid-facing correlated mutations and dimerization in G-protein coupled receptors. Prot. Eng., 2001, 14(10), 759-767.
    • (2001) Prot. Eng. , vol.14 , Issue.10 , pp. 759-767
    • Gouldson, P.R.1    Dean, M.K.2    Snell, C.R.3    Bywater, R.P.4    Gkoutos, G.5    Reynolds, C.A.6
  • 37
    • 0346220017 scopus 로고    scopus 로고
    • Dimerization in aminergic G-protein-coupled receptors: Application of a hidden-site class model of evolution
    • [37] Soyer, O.S.; Dimmic, M.W.; Neubig, R.R.; Goldstein, R.A. Dimerization in aminergic G-protein-coupled receptors: Application of a hidden-site class model of evolution. Biochem., 2003, 42(49), 14522-14531.
    • (2003) Biochem. , vol.42 , Issue.49 , pp. 14522-14531
    • Soyer, O.S.1    Dimmic, M.W.2    Neubig, R.R.3    Goldstein, R.A.4
  • 38
    • 21344467203 scopus 로고    scopus 로고
    • The study of G-protein coupled receptor oligomerization with computational modeling and bioinformatics
    • [38] Filizola, M.; Weinstein, H. The study of G-protein coupled receptor oligomerization with computational modeling and bioinformatics. FEBS. J., 2005, 272(12), 2926-2938.
    • (2005) FEBS. J. , vol.272 , Issue.12 , pp. 2926-2938
    • Filizola, M.1    Weinstein, H.2
  • 40
    • 33646934650 scopus 로고    scopus 로고
    • Computational methods in drug design: Modeling G protein-coupled receptor monomers, dimers, and oligomers
    • [40] Reggio, P.H. Computational methods in drug design: modeling G protein-coupled receptor monomers, dimers, and oligomers. AAPS. J., 2006, 8(2), E322-E336.
    • (2006) AAPS. J. , vol.8 , Issue.2 , pp. E322-E336
    • Reggio, P.H.1
  • 41
    • 84858225002 scopus 로고    scopus 로고
    • Protein coupled receptor activation: X-ray crystallography and long-scale moleculardynamics simulations
    • [41] Vanni, S.; Rothlisberger, U. A closer look into G protein coupled receptor activation: X-ray crystallography and long-scale molecular dynamics simulations. Curr. Med. Chem., 2012, 19(8), 1135-1145.
    • (2012) Curr. Med. Chem. , vol.19 , Issue.8 , pp. 1135-1145
    • Vanni, S.1    Rothlisberger, U.A.2    Closer Look Into, G.3
  • 42
    • 84873182166 scopus 로고    scopus 로고
    • Characterization of the dynamic events of GPCRs by automated computational simulations
    • [42] Gutierrez-de-Teran, H.; Bello, X.; Rodriguez, D. Characterization of the dynamic events of GPCRs by automated computational simulations. Biochem. Soc. Trans., 2013, 41(1), 205-212.
    • (2013) Biochem. Soc. Trans. , vol.41 , Issue.1 , pp. 205-212
    • Gutierrez-De-teran, H.1    Bello, X.2    Rodriguez, D.3
  • 43
    • 77953281763 scopus 로고    scopus 로고
    • Role of aggregation in rhodopsin signal transduction
    • [43] Neri, M.; Vanni, S.; Tavernelli, I.; Rothlisberger, U. Role of aggregation in rhodopsin signal transduction. Biochem., 2010, 49(23), 4827-4832.
    • (2010) Biochem. , vol.49 , Issue.23 , pp. 4827-4832
    • Neri, M.1    Vanni, S.2    Tavernelli, I.3    Rothlisberger, U.4
  • 44
    • 84863780022 scopus 로고    scopus 로고
    • Characterization of the homodimerization interface and functional hotspots of the CXCR4 chemokine receptor
    • [44] Rodriguez, D.; Gutierrez-de-Teran, H. Characterization of the homodimerization interface and functional hotspots of the CXCR4 chemokine receptor. Proteins, 2012, 80(8), 1919-1928.
    • (2012) Proteins , vol.80 , Issue.8 , pp. 1919-1928
    • Rodriguez, D.1    Gutierrez-De-teran, H.2
  • 45
    • 84881112796 scopus 로고    scopus 로고
    • Structure-based studies of chemokine receptors
    • [45] Zhu, L.; Zhao, Q.; Wu, B. Structure-based studies of chemokine receptors. Curr. Opin. Struct. Biol., 2013, 23(4), 539-546.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , Issue.4 , pp. 539-546
    • Zhu, L.1    Zhao, Q.2    Wu, B.3
  • 48
    • 67650089750 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the heterodimeric mGluR2/5HT(2A) complex. An atomistic resolution study of a potential new target in psychiatric conditions
    • [48] Bruno, A.; Guadix, A.E.; Costantino, G. Molecular dynamics simulation of the heterodimeric mGluR2/5HT(2A) complex. An atomistic resolution study of a potential new target in psychiatric conditions. J. Chem. Inf. Model., 2009, 49(6), 1602-1616.
    • (2009) J. Chem. Inf. Model. , vol.49 , Issue.6 , pp. 1602-1616
    • Bruno, A.1    Guadix, A.E.2    Costantino, G.3
  • 50
    • 84888984921 scopus 로고    scopus 로고
    • Multiscale modelling to understand the self-assembly mechanism of human beta2-adrenergic receptor in lipid bilayer
    • [50] Ghosh, A.; Sonavane, U.; Joshi, R. Multiscale modelling to understand the self-assembly mechanism of human beta2-adrenergic receptor in lipid bilayer. Comput. Biol. Chem., 2014, 48, 29-39.
    • (2014) Comput. Biol. Chem. , vol.48 , pp. 29-39
    • Ghosh, A.1    Sonavane, U.2    Joshi, R.3
  • 51
    • 84896539831 scopus 로고    scopus 로고
    • Cholesterol modulates the dimer interface of the beta(2)-adrenergic receptor via cholesterol occupancy sites
    • [51] Prasanna, X.; Chattopadhyay, A.; Sengupta, D. Cholesterol modulates the dimer interface of the beta(2)-adrenergic receptor via cholesterol occupancy sites. Biophys. J., 2014, 106(6), 1290-1300.
    • (2014) Biophys. J. , vol.106 , Issue.6 , pp. 1290-1300
    • Prasanna, X.1    Chattopadhyay, A.2    Sengupta, D.3
  • 52
    • 84855452967 scopus 로고    scopus 로고
    • The role of the lipid matrix for structure and function of the GPCR rhodopsin
    • [52] Soubias, O.; Gawrisch, K. The role of the lipid matrix for structure and function of the GPCR rhodopsin. Biochim. Biophys. Acta., 2012, 1818(2), 234-240.
    • (2012) Biochim. Biophys. Acta. , vol.1818 , Issue.2 , pp. 234-240
    • Soubias, O.1    Gawrisch, K.2
  • 53
    • 23044445764 scopus 로고    scopus 로고
    • Using synthetic lipids to stabilize purified beta2 adrenoceptor in detergent micelles
    • [53] Yao, Z.; Kobilka, B. Using synthetic lipids to stabilize purified beta2 adrenoceptor in detergent micelles. Anal. Biochem., 2005, 343(2), 344-346.
    • (2005) Anal. Biochem. , vol.343 , Issue.2 , pp. 344-346
    • Yao, Z.1    Kobilka, B.2
  • 54
    • 78649803915 scopus 로고    scopus 로고
    • Cholesterol depletion enhances adrenergic signaling in cardiac myocytes
    • [54] Paila, Y.D.; Jindal, E.; Goswami, S.K.; Chattopadhyay, A. Cholesterol depletion enhances adrenergic signaling in cardiac myocytes. Biochim. Biophys. Acta., 2011, 1808(1), 461-465.
    • (2011) Biochim. Biophys. Acta. , vol.1808 , Issue.1 , pp. 461-465
    • Paila, Y.D.1    Jindal, E.2    Goswami, S.K.3    Chattopadhyay, A.4
  • 55
    • 54049106162 scopus 로고    scopus 로고
    • Cholesterol-dependent separation of the beta2-adrenergic receptor from its partners determines signaling efficacy: Insight into nanoscale organization of signal transduction
    • [55] Pontier, S.M.; Percherancier, Y.; Galandrin, S.; Breit, A.; Gales, C.; Bouvier, M. Cholesterol-dependent separation of the beta2-adrenergic receptor from its partners determines signaling efficacy: insight into nanoscale organization of signal transduction. J. Biol. Chem., 2008, 283(36), 24659-24672.
    • (2008) J. Biol. Chem. , vol.283 , Issue.36 , pp. 24659-24672
    • Pontier, S.M.1    Percherancier, Y.2    Galandrin, S.3    Breit, A.4    Gales, C.5    Bouvier, M.6
  • 56
    • 2442509293 scopus 로고    scopus 로고
    • Cholesterol modulates ligand binding and G-protein coupling to serotonin(1A) receptors from bovine hippocampus. Biochim. Biophys
    • [56] Pucadyil, T.J.; Chattopadhyay, A. Cholesterol modulates ligand binding and G-protein coupling to serotonin(1A) receptors from bovine hippocampus. Biochim. Biophys. Acta, 2004, 1663(1-2), 188-200.
    • (2004) Acta , vol.1663 , Issue.1-2 , pp. 188-200
    • Pucadyil, T.J.1    Chattopadhyay, A.2
  • 57
    • 33847037508 scopus 로고    scopus 로고
    • Cholesterol depletion induces dynamic confinement of the G-protein coupled serotonin(1A) receptor in the plasma membrane of living cells
    • [57] Pucadyil, T.J.; Chattopadhyay, A. Cholesterol depletion induces dynamic confinement of the G-protein coupled serotonin(1A) receptor in the plasma membrane of living cells. Biochim. Biophys. Acta, 2007, 1768(3), 655-668.
    • (2007) Biochim. Biophys. Acta , vol.1768 , Issue.3 , pp. 655-668
    • Pucadyil, T.J.1    Chattopadhyay, A.2
  • 58
    • 84865311070 scopus 로고    scopus 로고
    • Membrane cholesterol stabilizes the human serotonin(1A) receptor
    • [58] Saxena, R.; Chattopadhyay, A. Membrane cholesterol stabilizes the human serotonin(1A) receptor. Biochim. Biophys. Acta, 2012, 1818(12), 2936-2942.
    • (2012) Biochim. Biophys. Acta , vol.1818 , Issue.12 , pp. 2936-2942
    • Saxena, R.1    Chattopadhyay, A.2
  • 59
    • 84872965208 scopus 로고    scopus 로고
    • Membrane lipids in the function of serotonin and adrenergic receptors
    • [59] Jafurulla, M.; Chattopadhyay, A. Membrane lipids in the function of serotonin and adrenergic receptors. Curr. Med. Chem., 2013, 20(1), 47-55.
    • (2013) Curr. Med. Chem. , vol.20 , Issue.1 , pp. 47-55
    • Jafurulla, M.1    Chattopadhyay, A.2
  • 60
    • 82955248059 scopus 로고    scopus 로고
    • Uncovering the intimate relationship between lipids, cholesterol and GPCR activation
    • [60] Oates, J.; Watts, A. Uncovering the intimate relationship between lipids, cholesterol and GPCR activation. Curr. Opin. Struct. Biol., 2011, 21(6), 802-807.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , Issue.6 , pp. 802-807
    • Oates, J.1    Watts, A.2
  • 61
    • 77952306521 scopus 로고    scopus 로고
    • Membrane cholesterol in the function and organization of G-protein coupled receptors
    • [61] Paila, Y.D.; Chattopadhyay, A. Membrane cholesterol in the function and organization of G-protein coupled receptors. Subcell. Biochem., 2010, 51, 439-466.
    • (2010) Subcell. Biochem. , vol.51 , pp. 439-466
    • Paila, Y.D.1    Chattopadhyay, A.2
  • 62
    • 84867366833 scopus 로고    scopus 로고
    • Predictions for cholesterol interaction sites on the A2A adenosine receptor
    • [62] Lee, J.Y.; Lyman, E. Predictions for cholesterol interaction sites on the A2A adenosine receptor. J. Am. Chem. Soc., 2012, 134(40), 16512-16515.
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.40 , pp. 16512-16515
    • Lee, J.Y.1    Lyman, E.2
  • 63
    • 84868234553 scopus 로고    scopus 로고
    • Identification of cholesterol binding sites in the serotonin1A receptor
    • [63] Sengupta, D.; Chattopadhyay, A. Identification of cholesterol binding sites in the serotonin1A receptor. J. Phys. Chem. B., 2012, 116(43), 12991-12996.
    • (2012) J. Phys. Chem. B. , vol.116 , Issue.43 , pp. 12991-12996
    • Sengupta, D.1    Chattopadhyay, A.2
  • 64
    • 84874427933 scopus 로고    scopus 로고
    • Mapping the functional binding sites of cholesterol in beta2-adrenergic receptor by long-time molecular dynamics simulations
    • [64] Cang, X.; Du, Y.; Mao, Y.; Wang, Y.; Yang, H.; Jiang, H. Mapping the functional binding sites of cholesterol in beta2-adrenergic receptor by long-time molecular dynamics simulations. J. Phys. Chem. B., 2013, 117(4), 1085-1094.
    • (2013) J. Phys. Chem. B. , vol.117 , Issue.4 , pp. 1085-1094
    • Cang, X.1    Du, Y.2    Mao, Y.3    Wang, Y.4    Yang, H.5    Jiang, H.6
  • 65
    • 77955262698 scopus 로고    scopus 로고
    • Lessons from free energy simulations of delta-opioid receptor homodimers involving the fourthtransmembrane helix
    • [65] Provasi, D.; Johnston, J.M.; Filizola, M. Lessons from free energy simulations of delta-opioid receptor homodimers involving the fourth transmembrane helix. Biochem., 2010, 49(31), 6771-6776.
    • (2010) Biochem. , vol.49 , Issue.31 , pp. 6771-6776
    • Provasi, D.1    Johnston, J.M.2    Filizola, M.3
  • 67
    • 84866056455 scopus 로고    scopus 로고
    • Assessing the relative stability of dimer interfaces in g protein-coupled receptors
    • 67[] Johnston, J.M.; Wang, H.; Provasi, D.; Filizola, M. Assessing the relative stability of dimer interfaces in g protein-coupled receptors. PLoS. Comput. Biol., 2012, 8(8), e1002649.
    • (2012) Plos. Comput. Biol , vol.8 , Issue.8
    • Johnston, J.M.1    Wang, H.2    Provasi, D.3    Filizola, M.4
  • 68
    • 84882454897 scopus 로고    scopus 로고
    • Modeling complexes of transmembrane proteins: Systematic analysis of protein-protein docking tools
    • [68] Kaczor, A.A.; Selent J.; Sanz, F.; Pastor, M. Modeling complexes of transmembrane proteins: systematic analysis of protein-protein docking tools. Mol. Inf., 2013, 32, 717-733.
    • (2013) Mol. Inf. , vol.32 , pp. 717-733
    • Kaczor, A.A.1    Selent, J.2    Sanz, F.3    Pastor, M.4
  • 69
    • 33749578426 scopus 로고    scopus 로고
    • Quaternary structure predictions of transmembrane proteins starting from the monomer: A docking-based approach
    • [69] Casciari, D.; Seeber, M.; Fanelli, F. Quaternary structure predictions of transmembrane proteins starting from the monomer: a docking-based approach. BMC. Bioinfor., 2006, 7, 340.
    • (2006) BMC. Bioinfor. , vol.7 , pp. 340
    • Casciari, D.1    Seeber, M.2    Fanelli, F.3
  • 70
    • 33751203259 scopus 로고    scopus 로고
    • Dimerization of the lutropin receptor: Insights from computational modeling
    • [70] Fanelli, F. Dimerization of the lutropin receptor: insights from computational modeling. Mol. Cell Endocrinol., 2007, 260-262, 59-64.
    • (2007) Mol. Cell Endocrinol. , vol.260-262 , pp. 59-64
    • Fanelli, F.1
  • 71
    • 52049125498 scopus 로고    scopus 로고
    • Homodimerization of neurotensin 1 receptor involves helices 1, 2, and 4: Insights from quaternary structure predictions and dimerization free energy estimations
    • [71] Casciari, D.; Dell'Orco, D.; Fanelli, F. Homodimerization of neurotensin 1 receptor involves helices 1, 2, and 4: Insights from quaternary structure predictions and dimerization free energy estimations. J. Chem. Inf. Model., 2008, 48(8), 1669-1678.
    • (2008) J. Chem. Inf. Model. , vol.48 , Issue.8 , pp. 1669-1678
    • Casciari, D.1    Dell'orco, D.2    Fanelli, F.3
  • 72
    • 79953194763 scopus 로고    scopus 로고
    • Dimerization and ligand binding affect the structure network of A(2A) adenosine receptor
    • [72] Fanelli, F.; Felline, A. Dimerization and ligand binding affect the structure network of A(2A) adenosine receptor. Biochim. Biophys. Acta., 2011, 1808(5), 1256-1266.
    • (2011) Biochim. Biophys. Acta. , vol.1808 , Issue.5 , pp. 1256-1266
    • Fanelli, F.1    Felline, A.2
  • 74
    • 84873729688 scopus 로고    scopus 로고
    • D5 dopamine receptor carboxyl tail involved in D5-D2 heteromer formation
    • [74] O'Dowd, B.F.; Nguyen, T.; Ji, X.; George, S.R. D5 dopamine receptor carboxyl tail involved in D5-D2 heteromer formation. Biochem. Biophys. Res. Commun., 2013, 431(3), 586-589.
    • (2013) Biochem. Biophys. Res. Commun. , vol.431 , Issue.3 , pp. 586-589
    • O'dowd, B.F.1    Nguyen, T.2    Ji, X.3    George, S.R.4
  • 76
    • 0001297162 scopus 로고
    • Brownian dynamics as smart Monte Carlo simulation
    • [76] Rossky, P.J.; Doll, J.D.; Friedman, H.L. Brownian dynamics as smart Monte Carlo simulation. J. Chem. Physics, 1978, 69(10), 14628-14633.
    • (1978) J. Chem. Physics , vol.69 , Issue.10 , pp. 14628-14633
    • Rossky, P.J.1    Doll, J.D.2    Friedman, H.L.3
  • 77
    • 0032905447 scopus 로고    scopus 로고
    • Brownian dynamics simulations of interactions between aldolase and G- or F-actin
    • [77] Ouporov, I.V.; Knull, H.R.; Thomasson, K.A. Brownian dynamics simulations of interactions between aldolase and G- or F-actin. Biophys. J., 1999, 76(1 Pt 1), 17-27.
    • (1999) Biophys. J. , vol.76 , pp. 17-27
    • Ouporov, I.V.1    Knull, H.R.2    Thomasson, K.A.3
  • 78
    • 0344474660 scopus 로고    scopus 로고
    • Brownian dynamics study of the interaction between plastocyanin and cytochrome f
    • [78] Pearson, D.C.; Gross, E.L. Brownian dynamics study of the interaction between plastocyanin and cytochrome f. Biophys. J., 1998, 75(6), 2698-2711.
    • (1998) Biophys. J. , vol.75 , Issue.6 , pp. 2698-2711
    • Pearson, D.C.1    Gross, E.L.2
  • 79
    • 0348111263 scopus 로고    scopus 로고
    • Brownian dynamics simulations of glycolytic enzyme subsets with F-actin
    • [79] Lowe, S.L.; Adrian, C.; Ouporov, I.V.; Waingeh, V.F.; Thomasson, K.A. Brownian dynamics simulations of glycolytic enzyme subsets with F-actin. Biopolym., 2003, 70(4), 456-470.
    • (2003) Biopolym. , vol.70 , Issue.4 , pp. 456-470
    • Lowe, S.L.1    Adrian, C.2    Ouporov, I.V.3    Waingeh, V.F.4    Thomasson, K.A.5
  • 80
    • 44349160733 scopus 로고    scopus 로고
    • Protein-protein docking by simulating the process of association subject to biochemical constraints
    • [80] Motiejunas, D.; Gabdoulline, R.; Wang, T.; Feldman-Salit, A.; Johann, T.; Winn, P.J.; Wade, R.C. Protein-protein docking by simulating the process of association subject to biochemical constraints. Proteins, 2008, 71(4), 1955-1969.
    • (2008) Proteins , vol.71 , Issue.4 , pp. 1955-1969
    • Motiejunas, D.1    Gabdoulline, R.2    Wang, T.3    Feldman-Salit, A.4    Johann, T.5    Winn, P.J.6    Wade, R.C.7
  • 81
    • 0035016038 scopus 로고    scopus 로고
    • Brownian
    • [81] Ouporov, I.V.; Knull, H.R.; Huber, A.; Thomasson, K.A. Brownian dynamics simulations of aldolase binding glyceraldehyde 3- phosphate dehydrogenase and the possibility of substrate channeling. Biophys. J., 2001, 80(6), 2527-2535.
    • (2001) Biophys. J. , vol.80 , Issue.6 , pp. 2527-2535
    • Ouporov, I.V.1    Knull, H.R.2    Huber, A.3    Thomasson, K.A.4
  • 82
    • 0035281357 scopus 로고    scopus 로고
    • Computer simulation of protein-protein interactions
    • [82] Elcock, A.H.; Sept, D.; McCammon, J.A. Computer simulation of protein-protein interactions. J. Physical Chem. B., 2001, 105(8), 1504-1518.
    • (2001) J. Physical Chem. B. , vol.105 , Issue.8 , pp. 1504-1518
    • Elcock, A.H.1    Sept, D.2    Mccammon, J.A.3
  • 83
    • 21244491250 scopus 로고    scopus 로고
    • Brownian dynamics study of cytochrome f interactions with cytochrome c6 and plastocyanin in Chlamydomonas reinhardtii plastocyanin, and cytochrome c6 mutants
    • [83] Haddadian, E.J.; Gross, E.L. Brownian dynamics study of cytochrome f interactions with cytochrome c6 and plastocyanin in Chlamydomonas reinhardtii plastocyanin, and cytochrome c6 mutants. Biophys. J., 2005, 88(3), 2323-2339.
    • (2005) Biophys. J. , vol.88 , Issue.3 , pp. 2323-2339
    • Haddadian, E.J.1    Gross, E.L.2
  • 84
    • 0035066437 scopus 로고    scopus 로고
    • Brownian dynamics simulations of interaction between scorpion toxin Lq2 and potassium ion channel
    • [84] Cui, M.; Shen, J.; Briggs, J.M.; Luo, X.; Tan, X.; Jiang, H.; Chen, K.; Ji, R. Brownian dynamics simulations of interaction between scorpion toxin Lq2 and potassium ion channel. Biophys. J., 2001, 80(4), 1659-1669.
    • (2001) Biophys. J. , vol.80 , Issue.4 , pp. 1659-1669
    • Cui, M.1    Shen, J.2    Briggs, J.M.3    Luo, X.4    Tan, X.5    Jiang, H.6    Chen, K.7    Ji, R.8
  • 85
    • 0036302289 scopus 로고    scopus 로고
    • Brownian dynamics simulations of the recognition of the scorpion toxin P05 with the small-conductance calcium-activated potassium channels
    • [85] Cui, M.; Shen, J.; Briggs, J.M.; Fu, W.; Wu, J.; Zhang, Y.; Luo, X.; Chi, Z.; Ji, R.; Jiang, H.; Chen, K. Brownian dynamics simulations of the recognition of the scorpion toxin P05 with the small-conductance calcium-activated potassium channels. J. Mol. Biol., 2002, 318(2), 417-428.
    • (2002) J. Mol. Biol. , vol.318 , Issue.2 , pp. 417-428
    • Cui, M.1    Shen, J.2    Briggs, J.M.3    Fu, W.4    Wu, J.5    Zhang, Y.6    Luo, X.7    Chi, Z.8    Ji, R.9    Jiang, H.10    Chen, K.11
  • 86
    • 28544434796 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex
    • [86] Yu, L.; Sun, C.; Song, D.; Shen, J.; Xu, N.; Gunasekera, A.; Hajduk, P.J.; Olejniczak, E.T. Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex. Biochemistry, 2005, 44(48), 15834-15841.
    • (2005) Biochemistry , vol.44 , Issue.48 , pp. 15834-15841
    • Yu, L.1    Sun, C.2    Song, D.3    Shen, J.4    Xu, N.5    Gunasekera, A.6    Hajduk, P.J.7    Olejniczak, E.T.8
  • 87
    • 56549099908 scopus 로고    scopus 로고
    • Prediction of protein loop structures using a local move Monte Carlo approach and a grid-based force field
    • [87] Cui, M.; Mezei, M.; Osman, R. Prediction of protein loop structures using a local move Monte Carlo approach and a grid-based force field. Prot. Eng. Des. Sel., 2008, 21(12), 729-735.
    • (2008) Prot. Eng. Des. Sel. , vol.21 , Issue.12 , pp. 729-735
    • Cui, M.1    Mezei, M.2    Osman, R.3
  • 88
    • 84863290577 scopus 로고    scopus 로고
    • Predicting protein interactions by Brownian Dynamics simulations
    • 2012, Article ID 121034
    • 88[] Meng, X.Y.; Zhang, H.X.; Mezei, M.; Cui, M. Predicting protein interactions by Brownian Dynamics simulations. J. Biomed. Biotechnol., 2012, 2012, Article ID 121034.
    • (2012) J. Biomed.
    • Meng, X.Y.1    Zhang, H.X.2    Mezei, M.3    Cui, M.4
  • 89
    • 46049097169 scopus 로고    scopus 로고
    • Modeling dimerizations of transmembrane proteins using Brownian dynamics simulations
    • [89] Cui, M.; Mezei, M.; Osman, R. Modeling dimerizations of transmembrane proteins using Brownian dynamics simulations. J. Comput. Aided Mol. Des., 2008, 22(8), 553-561.
    • (2008) J. Comput. Aided Mol. Des. , vol.22 , Issue.8 , pp. 553-561
    • Cui, M.1    Mezei, M.2    Osman, R.3
  • 91
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • [91] Heldin, C.H. Dimerization of cell surface receptors in signal transduction. Cell, 1995, 80(2), 213-223.
    • (1995) Cell , vol.80 , Issue.2 , pp. 213-223
    • Heldin, C.H.1
  • 92
    • 0035032316 scopus 로고    scopus 로고
    • Oligomerisation of G-protein-coupled receptors
    • [92] Milligan, G. Oligomerisation of G-protein-coupled receptors. J. Cell Sci., 2001, 114(7), 1265-1271.
    • (2001) J. Cell Sci. , vol.114 , Issue.7 , pp. 1265-1271
    • Milligan, G.1
  • 93
    • 0035726693 scopus 로고    scopus 로고
    • G-protein-coupled receptor dimerization: Modulation of receptor function. Pharmacol
    • [93] Rios, C.D.; Jordan, B.A.; Gomes, I.; Devi, L.A. G-protein-coupled receptor dimerization: modulation of receptor function. Pharmacol. Ther., 2001, 92(2-3), 71-87.
    • (2001) Ther. , vol.92 , Issue.2-3 , pp. 71-87
    • Rios, C.D.1    Jordan, B.A.2    Gomes, I.3    Devi, L.A.4
  • 94
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • [94] George, S.R.; O'Dowd, B.F.; Lee, S.P. G-protein-coupled receptor oligomerization and its potential for drug discovery. Nat. Rev. Drug Discov., 2002, 1(10), 808-820.
    • (2002) Nat. Rev. Drug , vol.1 , Issue.10 , pp. 808-820
    • George, S.R.1    O'dowd, B.F.2    Lee, S.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.