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Volumn 4, Issue 8, 2009, Pages

Lipid raft-mediated regulation of G-protein coupled receptor signaling by ligands which influence receptor dimerization: A computational study

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; LIGAND;

EID: 68749103465     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0006604     Document Type: Article
Times cited : (79)

References (77)
  • 1
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • George SR, O'Dowd BF, Lee SP (2002) G-protein-coupled receptor oligomerization and its potential for drug discovery. Nat Rev Drug Discov 1(10): 808-820.
    • (2002) Nat Rev Drug Discov , vol.1 , Issue.10 , pp. 808-820
    • George, S.R.1    O'Dowd, B.F.2    Lee, S.P.3
  • 2
    • 0033850756 scopus 로고    scopus 로고
    • Molecular manipulation of G-protein-coupled receptors: A new avenue into drug discovery
    • Sautel M, Milligan G (2000) Molecular manipulation of G-protein-coupled receptors: A new avenue into drug discovery. Curr Med Chem 7(9): 889-896.
    • (2000) Curr Med Chem , vol.7 , Issue.9 , pp. 889-896
    • Sautel, M.1    Milligan, G.2
  • 3
    • 35748932049 scopus 로고    scopus 로고
    • Functional membrane diffusion of G-protein coupled receptors
    • Baker A, Sauliere A, Dumas F, Millot C, Mazeres S, et al. (2007) Functional membrane diffusion of G-protein coupled receptors. Eur Biophys J 36(8): 849-860.
    • (2007) Eur Biophys J , vol.36 , Issue.8 , pp. 849-860
    • Baker, A.1    Sauliere, A.2    Dumas, F.3    Millot, C.4    Mazeres, S.5
  • 4
    • 0035726693 scopus 로고    scopus 로고
    • G-protein-coupled receptor dimerization: Modulation of receptor function
    • Rios CD, Jordan BA, Gomes I, Devi LA (2001) G-protein-coupled receptor dimerization: Modulation of receptor function. Pharmacol Ther 92(2-3): 71-87.
    • (2001) Pharmacol Ther , vol.92 , Issue.2-3 , pp. 71-87
    • Rios, C.D.1    Jordan, B.A.2    Gomes, I.3    Devi, L.A.4
  • 5
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
    • Whorton MR, Bokoch MP, Rasmussen SG, Huang B, Zare RN, et al. (2007) A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein. Proc Natl Acad Sci U S A 104(18): 7682-7687.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.18 , pp. 7682-7687
    • Whorton, M.R.1    Bokoch, M.P.2    Rasmussen, S.G.3    Huang, B.4    Zare, R.N.5
  • 6
    • 42949164679 scopus 로고    scopus 로고
    • Efficient coupling of transducin to monomeric rhodopsin in a phospholipid bilayer
    • Whorton MR, Jastrzebska B, Park PS, Fotiadis D, Engel A, et al. (2008) Efficient coupling of transducin to monomeric rhodopsin in a phospholipid bilayer. J Biol Chem 283(7): 4387-4394.
    • (2008) J Biol Chem , vol.283 , Issue.7 , pp. 4387-4394
    • Whorton, M.R.1    Jastrzebska, B.2    Park, P.S.3    Fotiadis, D.4    Engel, A.5
  • 7
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G-protein-coupled receptor as a functional unit
    • Chabre M, le Maire M (2005) Monomeric G-protein-coupled receptor as a functional unit. Biochemistry 44(27): 9395-9403.
    • (2005) Biochemistry , vol.44 , Issue.27 , pp. 9395-9403
    • Chabre, M.1    le Maire, M.2
  • 8
    • 0037426865 scopus 로고    scopus 로고
    • Atomic-force microscopy: Rhodopsin dimers in native disc membranes
    • Fotiadis D, Liang Y, Filipek S, Saperstein DA, Engel A, et al. (2003) Atomic-force microscopy: Rhodopsin dimers in native disc membranes. Nature 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
  • 9
    • 33845505655 scopus 로고    scopus 로고
    • Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes
    • Botelho AV, Huber T, Sakmar TP, Brown MF (2006) Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes. Biophys J 91(12): 4464-4477.
    • (2006) Biophys J , vol.91 , Issue.12 , pp. 4464-4477
    • Botelho, A.V.1    Huber, T.2    Sakmar, T.P.3    Brown, M.F.4
  • 10
    • 0037678455 scopus 로고    scopus 로고
    • Self organization of membrane proteins via dimerization
    • Woolf PJ, Linderman JJ (2003) Self organization of membrane proteins via dimerization. Biophys Chem 104(1): 217-227.
    • (2003) Biophys Chem , vol.104 , Issue.1 , pp. 217-227
    • Woolf, P.J.1    Linderman, J.J.2
  • 11
    • 0034937698 scopus 로고    scopus 로고
    • G protein coupled receptor dimerization: Implications in modulating receptor function
    • Gomes I, Jordan BA, Gupta A, Rios C, Trapaidze N, et al. (2001) G protein coupled receptor dimerization: Implications in modulating receptor function. J Mol Med 79(5-6): 226-242.
    • (2001) J Mol Med , vol.79 , Issue.5-6 , pp. 226-242
    • Gomes, I.1    Jordan, B.A.2    Gupta, A.3    Rios, C.4    Trapaidze, N.5
  • 12
    • 0041494100 scopus 로고    scopus 로고
    • Lipid rafts: Bringing order to chaos
    • Pike LJ (2003) Lipid rafts: Bringing order to chaos. J Lipid Res 44(4): 655-667.
    • (2003) J Lipid Res , vol.44 , Issue.4 , pp. 655-667
    • Pike, L.J.1
  • 13
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster LJ, De Hoog CL, Mann M (2003) Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc Natl Acad Sci U S A 100(10): 5813-5818.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.10 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 14
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • Pralle A, Keller P, Florin EL, Simons K, Horber JK (2000) Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J Cell Biol 148(5): 997-1008.
    • (2000) J Cell Biol , vol.148 , Issue.5 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.L.3    Simons, K.4    Horber, J.K.5
  • 15
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D (2000) Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1(1): 31-39.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , Issue.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 16
    • 0032492636 scopus 로고    scopus 로고
    • Compartmentalization of receptors and enzymes affects activation for a collision coupling mechanism
    • Shea LD, Linderman JJ (1998) Compartmentalization of receptors and enzymes affects activation for a collision coupling mechanism. J Theor Biol 191(3): 249-258.
    • (1998) J Theor Biol , vol.191 , Issue.3 , pp. 249-258
    • Shea, L.D.1    Linderman, J.J.2
  • 17
    • 55649085958 scopus 로고    scopus 로고
    • Collision coupling, crosstalk, and compartmentalization in G-protein coupled receptor systems: Can a single model explain disparate results?
    • Brinkerhoff CJ, Traynor JR, Linderman JJ (2008) Collision coupling, crosstalk, and compartmentalization in G-protein coupled receptor systems: Can a single model explain disparate results? J Theor Biol 255: 278-286.
    • (2008) J Theor Biol , vol.255 , pp. 278-286
    • Brinkerhoff, C.J.1    Traynor, J.R.2    Linderman, J.J.3
  • 18
    • 0344442849 scopus 로고    scopus 로고
    • Dimerization controls the lipid raft partitioning of uPAR/CD87 and regulates its biological functions
    • Cunningham O, Andolfo A, Santovito ML, Iuzzolino L, Blasi F, et al. (2003) Dimerization controls the lipid raft partitioning of uPAR/CD87 and regulates its biological functions. EMBO J 22(22): 5994-6003.
    • (2003) EMBO J , vol.22 , Issue.22 , pp. 5994-6003
    • Cunningham, O.1    Andolfo, A.2    Santovito, M.L.3    Iuzzolino, L.4    Blasi, F.5
  • 19
    • 33746659807 scopus 로고    scopus 로고
    • The active metabolite of clopidogrel disrupts P2Y12 receptor oligomers and partitions them out of lipid rafts
    • Savi P, Zachayus JL, Delesque-Touchard N, Labouret C, Herve C, et al. (2006) The active metabolite of clopidogrel disrupts P2Y12 receptor oligomers and partitions them out of lipid rafts. Proc Natl Acad Sci U S A 103(29): 11069-11074.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.29 , pp. 11069-11074
    • Savi, P.1    Zachayus, J.L.2    Delesque-Touchard, N.3    Labouret, C.4    Herve, C.5
  • 20
    • 0030873019 scopus 로고    scopus 로고
    • Dynamic targeting of the agonist-stimulated m2 muscarinic acetylcholine receptor to caveolae in cardiac myocytes
    • Feron O, Smith TW, Michel T, Kelly RA (1997) Dynamic targeting of the agonist-stimulated m2 muscarinic acetylcholine receptor to caveolae in cardiac myocytes. J Biol Chem 272(28): 17744-17748.
    • (1997) J Biol Chem , vol.272 , Issue.28 , pp. 17744-17748
    • Feron, O.1    Smith, T.W.2    Michel, T.3    Kelly, R.A.4
  • 21
    • 0031714513 scopus 로고    scopus 로고
    • Angiotensin II type 1 receptor: Relationship with caveolae and caveolin after initial agonist stimulation
    • Ishizaka N, Griendling KK, Lassegue B, Alexander RW (1998) Angiotensin II type 1 receptor: Relationship with caveolae and caveolin after initial agonist stimulation. Hypertension 32(3): 459-466.
    • (1998) Hypertension , vol.32 , Issue.3 , pp. 459-466
    • Ishizaka, N.1    Griendling, K.K.2    Lassegue, B.3    Alexander, R.W.4
  • 22
    • 7244257487 scopus 로고    scopus 로고
    • N-formyl peptide receptors cluster in an active raft-associated state prior to phosphorylation
    • Xue M, Vines CM, Buranda T, Cimino DF, Bennett TA, et al. (2004) N-formyl peptide receptors cluster in an active raft-associated state prior to phosphorylation. J Biol Chem 279(43): 45175-45184.
    • (2004) J Biol Chem , vol.279 , Issue.43 , pp. 45175-45184
    • Xue, M.1    Vines, C.M.2    Buranda, T.3    Cimino, D.F.4    Bennett, T.A.5
  • 23
    • 0034731376 scopus 로고    scopus 로고
    • Differential targeting of beta-adrenergic receptor subtypes and adenylyl cyclase to cardiomyocyte caveolae. A mechanism to functionally regulate the cAMP signaling pathway
    • Rybin VO, Xu X, Lisanti MP, Steinberg SF (2000) Differential targeting of beta-adrenergic receptor subtypes and adenylyl cyclase to cardiomyocyte caveolae. A mechanism to functionally regulate the cAMP signaling pathway. J Biol Chem 275(52): 41447-41457.
    • (2000) J Biol Chem , vol.275 , Issue.52 , pp. 41447-41457
    • Rybin, V.O.1    Xu, X.2    Lisanti, M.P.3    Steinberg, S.F.4
  • 24
    • 33845938227 scopus 로고    scopus 로고
    • Cholesterol reduction by methyl-beta-cyclodextrin attenuates the delta opioid receptor-mediated signaling in neuronal cells but enhances it in non-neuronal cells
    • Huang P, Xu W, Yoon SI, Chen C, Chong PL, et al. (2007) Cholesterol reduction by methyl-beta-cyclodextrin attenuates the delta opioid receptor-mediated signaling in neuronal cells but enhances it in non-neuronal cells. Biochem Pharmacol 73(4): 534-549.
    • (2007) Biochem Pharmacol , vol.73 , Issue.4 , pp. 534-549
    • Huang, P.1    Xu, W.2    Yoon, S.I.3    Chen, C.4    Chong, P.L.5
  • 25
    • 36348983962 scopus 로고    scopus 로고
    • Agonist treatment did not affect association of mu opioid receptors with lipid rafts and cholesterol reduction had opposite effects on the receptor-mediated signaling in rat brain and CHO cells
    • Huang P, Xu W, Yoon SI, Chen C, Chong PL, et al. (2007) Agonist treatment did not affect association of mu opioid receptors with lipid rafts and cholesterol reduction had opposite effects on the receptor-mediated signaling in rat brain and CHO cells. Brain Res 1184: 46-56.
    • (2007) Brain Res , vol.1184 , pp. 46-56
    • Huang, P.1    Xu, W.2    Yoon, S.I.3    Chen, C.4    Chong, P.L.5
  • 27
    • 64849115345 scopus 로고    scopus 로고
    • Modeling of G-protein-coupled receptor signaling pathways
    • Linderman JJ (2009) Modeling of G-protein-coupled receptor signaling pathways. J Biol Chem 284(9): 5427-5431.
    • (2009) J Biol Chem , vol.284 , Issue.9 , pp. 5427-5431
    • Linderman, J.J.1
  • 28
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma P, Varma R, Sarasij RC, Ira, Gousset K, et al. (2004) Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 116(4): 577-589.
    • (2004) Cell , vol.116 , Issue.4 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Ira, G.K.4
  • 29
    • 33645520326 scopus 로고    scopus 로고
    • Luteinizing hormone receptors translocate to plasma membrane microdomains after binding of human chorionic gonadotropin
    • Smith SM, Lei Y, Liu J, Cahill ME, Hagen GM, et al. (2006) Luteinizing hormone receptors translocate to plasma membrane microdomains after binding of human chorionic gonadotropin. Endocrinology 147(4): 1789-1795.
    • (2006) Endocrinology , vol.147 , Issue.4 , pp. 1789-1795
    • Smith, S.M.1    Lei, Y.2    Liu, J.3    Cahill, M.E.4    Hagen, G.M.5
  • 30
    • 33144473025 scopus 로고    scopus 로고
    • FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells
    • Meyer BH, Segura JM, Martinez KL, Hovius R, George N, et al. (2006) FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells. Proc Natl Acad Sci U S A 103(7): 2138-2143.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.7 , pp. 2138-2143
    • Meyer, B.H.1    Segura, J.M.2    Martinez, K.L.3    Hovius, R.4    George, N.5
  • 31
    • 18544367674 scopus 로고    scopus 로고
    • Recent advances in membrane microdomains: Rafts, caveolae, and intracellular cholesterol trafficking
    • Schroeder F, Gallegos AM, Atshaves BP, Storey SM, McIntosh AL, et al. (2001) Recent advances in membrane microdomains: Rafts, caveolae, and intracellular cholesterol trafficking. Exp Biol Med (Maywood) 226(10): 873-890.
    • (2001) Exp Biol Med (Maywood) , vol.226 , Issue.10 , pp. 873-890
    • Schroeder, F.1    Gallegos, A.M.2    Atshaves, B.P.3    Storey, S.M.4    McIntosh, A.L.5
  • 32
    • 0000282961 scopus 로고
    • Brownian motion in biological membranes
    • Saffman PG, Delbruck M (1975) Brownian motion in biological membranes. Proc Natl Acad Sci U S A 72(8): 3111-3113.
    • (1975) Proc Natl Acad Sci U S A , vol.72 , Issue.8 , pp. 3111-3113
    • Saffman, P.G.1    Delbruck, M.2
  • 33
    • 0028105976 scopus 로고
    • A monte carlo study of the dynamics of G-protein activation
    • Mahama PA, Linderman JJ (1994) A monte carlo study of the dynamics of G-protein activation. Biophys J 67(3): 1345-1357.
    • (1994) Biophys J , vol.67 , Issue.3 , pp. 1345-1357
    • Mahama, P.A.1    Linderman, J.J.2
  • 34
    • 33747033205 scopus 로고    scopus 로고
    • Spatial modeling of dimerization reaction dynamics in the plasma membrane: Monte carlo vs. continuum differential equations
    • Mayawala K, Vlachos DG, Edwards JS (2006) Spatial modeling of dimerization reaction dynamics in the plasma membrane: Monte carlo vs. continuum differential equations. Biophys Chem 121(3): 194-208.
    • (2006) Biophys Chem , vol.121 , Issue.3 , pp. 194-208
    • Mayawala, K.1    Vlachos, D.G.2    Edwards, J.S.3
  • 35
    • 54049134792 scopus 로고    scopus 로고
    • Stochastic simulations of ErbB homo and heterodimerisation: Potential impacts of receptor conformational state and spatial segregation. IET
    • Hsieh MY, Yang S, Raymond-Stinz MA, Steinberg S, Vlachos DG, et al. (2008) Stochastic simulations of ErbB homo and heterodimerisation: Potential impacts of receptor conformational state and spatial segregation. IET Syst Biol 2(5): 256-272.
    • (2008) Syst Biol , vol.2 , Issue.5 , pp. 256-272
    • Hsieh, M.Y.1    Yang, S.2    Raymond-Stinz, M.A.3    Steinberg, S.4    Vlachos, D.G.5
  • 37
    • 0027504198 scopus 로고
    • Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). effects of calcium-induced differentiation in cultured epithelial cells
    • Kusumi A, Sako Y, Yamamoto M (1993) Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). effects of calcium-induced differentiation in cultured epithelial cells. Biophys J 65(5): 2021-2040.
    • (1993) Biophys J , vol.65 , Issue.5 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 38
    • 12444289530 scopus 로고    scopus 로고
    • Direct observation of ligand binding to membrane proteins in living cells by a saturation transfer double difference (STDD) NMR spectroscopy method shows a significantly higher affinity of integrin alpha(IIb)beta3 in native platelets than in liposomes
    • Claasen B, Axmann M, Meinecke R, Meyer B (2005) Direct observation of ligand binding to membrane proteins in living cells by a saturation transfer double difference (STDD) NMR spectroscopy method shows a significantly higher affinity of integrin alpha(IIb)beta3 in native platelets than in liposomes. J Am Chem Soc 127(3): 916-919.
    • (2005) J Am Chem Soc , vol.127 , Issue.3 , pp. 916-919
    • Claasen, B.1    Axmann, M.2    Meinecke, R.3    Meyer, B.4
  • 39
    • 0035164003 scopus 로고    scopus 로고
    • Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default
    • Oh P, Schnitzer JE (2001) Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default. Mol Biol Cell 12(3): 685-698.
    • (2001) Mol Biol Cell , vol.12 , Issue.3 , pp. 685-698
    • Oh, P.1    Schnitzer, J.E.2
  • 40
    • 0028820041 scopus 로고
    • A detergent-free method for purifying caveolae membrane from tissue culture cells
    • Smart EJ, Ying YS, Mineo C, Anderson RG (1995) A detergent-free method for purifying caveolae membrane from tissue culture cells. Proc Natl Acad Sci U S A 92(22): 10104-10108.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , Issue.22 , pp. 10104-10108
    • Smart, E.J.1    Ying, Y.S.2    Mineo, C.3    Anderson, R.G.4
  • 41
    • 0035877768 scopus 로고    scopus 로고
    • Light- and guanosine 5′-3-O-(thio)triphosphate-sensitive localization of a G protein and its effector on detergent-resistant membrane rafts in rod photoreceptor outer segments
    • Seno K, Kishimoto M, Abe M, Higuchi Y, Mieda M, et al. (2001) Light- and guanosine 5′-3-O-(thio)triphosphate-sensitive localization of a G protein and its effector on detergent-resistant membrane rafts in rod photoreceptor outer segments. J Biol Chem 276(24): 20813-20816.
    • (2001) J Biol Chem , vol.276 , Issue.24 , pp. 20813-20816
    • Seno, K.1    Kishimoto, M.2    Abe, M.3    Higuchi, Y.4    Mieda, M.5
  • 42
    • 37549047211 scopus 로고    scopus 로고
    • Disruption of the plasma membrane integrity by cholesterol depletion impairs effectiveness of TRH receptor-mediated signal transduction via G(q)/ G(11)alpha proteins
    • Ostasov P, Bourova L, Hejnova L, Novotny J, Svoboda P (2007) Disruption of the plasma membrane integrity by cholesterol depletion impairs effectiveness of TRH receptor-mediated signal transduction via G(q)/ G(11)alpha proteins. J Recept Signal Transduct Res 27(5-6): 335-352.
    • (2007) J Recept Signal Transduct Res , vol.27 , Issue.5-6 , pp. 335-352
    • Ostasov, P.1    Bourova, L.2    Hejnova, L.3    Novotny, J.4    Svoboda, P.5
  • 43
    • 0030668748 scopus 로고    scopus 로고
    • Organization of G proteins and adenylyl cyclase at the plasma membrane
    • Huang C, Hepler JR, Chen LT, Gilman AG, Anderson RG, et al. (1997) Organization of G proteins and adenylyl cyclase at the plasma membrane. Mol Biol Cell 8(12): 2365-2378.
    • (1997) Mol Biol Cell , vol.8 , Issue.12 , pp. 2365-2378
    • Huang, C.1    Hepler, J.R.2    Chen, L.T.3    Gilman, A.G.4    Anderson, R.G.5
  • 44
    • 0029075372 scopus 로고
    • Evidence for a regulated interaction between heterotrimeric G proteins and caveolin
    • Li S, Okamoto T, Chun M, Sargiacomo M, Casanova JE, et al. (1995) Evidence for a regulated interaction between heterotrimeric G proteins and caveolin. J Biol Chem 270(26): 15693-15701.
    • (1995) J Biol Chem , vol.270 , Issue.26 , pp. 15693-15701
    • Li, S.1    Okamoto, T.2    Chun, M.3    Sargiacomo, M.4    Casanova, J.E.5
  • 45
    • 41049090774 scopus 로고    scopus 로고
    • Diffusion-limited reactions in G-protein activation: Unexpected consequences of antagonist and agonist competition
    • Brinkerhoff CJ, Choi JS, Linderman JJ (2008) Diffusion-limited reactions in G-protein activation: Unexpected consequences of antagonist and agonist competition. J Theor Biol 251(4): 561-569.
    • (2008) J Theor Biol , vol.251 , Issue.4 , pp. 561-569
    • Brinkerhoff, C.J.1    Choi, J.S.2    Linderman, J.J.3
  • 46
    • 0030834849 scopus 로고    scopus 로고
    • Calculation of diffusion-limited kinetics for the reactions in collision coupling and receptor cross-linking
    • Shea LD, Omann GM, Linderman JJ (1997) Calculation of diffusion-limited kinetics for the reactions in collision coupling and receptor cross-linking. Biophys J 73(6): 2949-2959.
    • (1997) Biophys J , vol.73 , Issue.6 , pp. 2949-2959
    • Shea, L.D.1    Omann, G.M.2    Linderman, J.J.3
  • 47
    • 21344476293 scopus 로고
    • Sensitivity and uncertainty analysis of complex models of disease transmission: An HIV model, as an example
    • Blower SM, Dowlatabadi H (1994) Sensitivity and uncertainty analysis of complex models of disease transmission: An HIV model, as an example. Int Stat Rev 62(2): 229-243.
    • (1994) Int Stat Rev , vol.62 , Issue.2 , pp. 229-243
    • Blower, S.M.1    Dowlatabadi, H.2
  • 48
    • 45449094504 scopus 로고    scopus 로고
    • A methodology for performing global uncertainty and sensitivity analysis in systems biology
    • Marino S, Hogue IB, Ray CJ, Kirschner DE (2008) A methodology for performing global uncertainty and sensitivity analysis in systems biology. J Theor Biol 254(1): 178-196.
    • (2008) J Theor Biol , vol.254 , Issue.1 , pp. 178-196
    • Marino, S.1    Hogue, I.B.2    Ray, C.J.3    Kirschner, D.E.4
  • 49
    • 33645241165 scopus 로고    scopus 로고
    • Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane
    • Nicolau DV Jr, Burrage K, Parton RG, Hancock JF (2006) Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane. Mol Cell Biol 26(1): 313-323.
    • (2006) Mol Cell Biol , vol.26 , Issue.1 , pp. 313-323
    • Nicolau Jr, D.V.1    Burrage, K.2    Parton, R.G.3    Hancock, J.F.4
  • 50
    • 33947647996 scopus 로고    scopus 로고
    • Sources of anomalous diffusion on cell membranes: A monte carlo study
    • Nicolau DV Jr, Hancock JF, Burrage K (2007) Sources of anomalous diffusion on cell membranes: A monte carlo study. Biophys J 92(6): 1975-1987.
    • (2007) Biophys J , vol.92 , Issue.6 , pp. 1975-1987
    • Nicolau Jr, D.V.1    Hancock, J.F.2    Burrage, K.3
  • 51
    • 0037316973 scopus 로고    scopus 로고
    • Caveolae-from ultrastructure to molecular mechanisms
    • Parton RG (2003) Caveolae-from ultrastructure to molecular mechanisms. Nat Rev Mol Cell Biol 4(2): 162-167.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , Issue.2 , pp. 162-167
    • Parton, R.G.1
  • 52
    • 34547673135 scopus 로고    scopus 로고
    • A kinetic model for calcium dynamics in RAW 264.7 cells: 1. mechanisms, parameters, and subpopulational variability
    • Maurya MR, Subramaniam S (2007) A kinetic model for calcium dynamics in RAW 264.7 cells: 1. mechanisms, parameters, and subpopulational variability. Biophys J 93(3): 709-728.
    • (2007) Biophys J , vol.93 , Issue.3 , pp. 709-728
    • Maurya, M.R.1    Subramaniam, S.2
  • 53
    • 0141703270 scopus 로고    scopus 로고
    • A quantitative characterization of the yeast heterotrimeric G protein cycle
    • Yi TM, Kitano H, Simon MI (2003) A quantitative characterization of the yeast heterotrimeric G protein cycle. Proc Natl Acad Sci U S A 100(19): 10764-10769.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.19 , pp. 10764-10769
    • Yi, T.M.1    Kitano, H.2    Simon, M.I.3
  • 54
    • 20744433934 scopus 로고    scopus 로고
    • Ligand-induced partitioning of human CXCR1 chemokine receptors with lipid raft microenvironments facilitates G-protein-dependent signaling
    • Jiao X, Zhang N, Xu X, Oppenheim JJ, Jin T (2005) Ligand-induced partitioning of human CXCR1 chemokine receptors with lipid raft microenvironments facilitates G-protein-dependent signaling. Mol Cell Biol 25(13): 5752-5762.
    • (2005) Mol Cell Biol , vol.25 , Issue.13 , pp. 5752-5762
    • Jiao, X.1    Zhang, N.2    Xu, X.3    Oppenheim, J.J.4    Jin, T.5
  • 55
    • 33751566959 scopus 로고    scopus 로고
    • Selective localization of recognition complexes for leukotriene B4 and formyl-met-leu-phe within lipid raft microdomains of human polymorphonuclear neutrophils
    • Sitrin RG, Emery SL, Sassanella TM, Blackwood RA, Petty HR (2006) Selective localization of recognition complexes for leukotriene B4 and formyl-met-leu-phe within lipid raft microdomains of human polymorphonuclear neutrophils. J Immunol 177(11): 8177-8184.
    • (2006) J Immunol , vol.177 , Issue.11 , pp. 8177-8184
    • Sitrin, R.G.1    Emery, S.L.2    Sassanella, T.M.3    Blackwood, R.A.4    Petty, H.R.5
  • 56
    • 0037072884 scopus 로고    scopus 로고
    • Caveolar localization dictates physiologic signaling of beta 2-adrenoceptors in neonatal cardiac myocytes
    • Xiang Y, Rybin VO, Steinberg SF, Kobilka B (2002) Caveolar localization dictates physiologic signaling of beta 2-adrenoceptors in neonatal cardiac myocytes. J Biol Chem 277(37): 34280-34286.
    • (2002) J Biol Chem , vol.277 , Issue.37 , pp. 34280-34286
    • Xiang, Y.1    Rybin, V.O.2    Steinberg, S.F.3    Kobilka, B.4
  • 57
    • 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
    • Pontier SM, Percherancier Y, Galandrin S, Breit A, Gales C, et al. (2008) Cholesterol-dependent separation of the beta2-adrenergic receptor from its partners determines signaling efficacy: Insight into nanoscale organization of signal transduction. J Biol Chem 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
  • 59
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the delta opioid receptor: Implication for a role in receptor internalization
    • Cvejic S, Devi LA (1997) Dimerization of the delta opioid receptor: Implication for a role in receptor internalization. The Journal of Biological Chemistry 272(43): 26959.
    • (1997) The Journal of Biological Chemistry , vol.272 , Issue.43 , pp. 26959
    • Cvejic, S.1    Devi, L.A.2
  • 60
    • 0029666267 scopus 로고    scopus 로고
    • A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation
    • Hebert TE, Moffett S, Morello JP, Loisel TP, Bichet DG, et al. (1996) A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation. J Biol Chem 271(27): 16384-16392.
    • (1996) J Biol Chem , vol.271 , Issue.27 , pp. 16384-16392
    • Hebert, T.E.1    Moffett, S.2    Morello, J.P.3    Loisel, T.P.4    Bichet, D.G.5
  • 61
    • 0033543572 scopus 로고    scopus 로고
    • Involvement of the amino terminus of the B(2) receptor in agonist-induced receptor dimerization
    • AbdAlla S, Zaki E, Lother H, Quitterer U (1999) Involvement of the amino terminus of the B(2) receptor in agonist-induced receptor dimerization. J Biol Chem 274(37): 26079-26084.
    • (1999) J Biol Chem , vol.274 , Issue.37 , pp. 26079-26084
    • AbdAlla, S.1    Zaki, E.2    Lother, H.3    Quitterer, U.4
  • 62
    • 0031466385 scopus 로고    scopus 로고
    • Identification of caveolin and caveolin-related proteins in the brain
    • Cameron PL, Ruffin JW, Bollag R, Rasmussen H, Cameron RS (1997) Identification of caveolin and caveolin-related proteins in the brain. J Neurosci 17(24): 9520-9535.
    • (1997) J Neurosci , vol.17 , Issue.24 , pp. 9520-9535
    • Cameron, P.L.1    Ruffin, J.W.2    Bollag, R.3    Rasmussen, H.4    Cameron, R.S.5
  • 63
    • 14844290891 scopus 로고    scopus 로고
    • The NK1 receptor localizes to the plasma membrane microdomains, and its activation is dependent on lipid raft integrity
    • Monastyrskaya K, Hostettler A, Buergi S, Draeger A (2005) The NK1 receptor localizes to the plasma membrane microdomains, and its activation is dependent on lipid raft integrity. J Biol Chem 280(8): 7135-7146.
    • (2005) J Biol Chem , vol.280 , Issue.8 , pp. 7135-7146
    • Monastyrskaya, K.1    Hostettler, A.2    Buergi, S.3    Draeger, A.4
  • 64
    • 33646783322 scopus 로고    scopus 로고
    • Localization of the kappa opioid receptor in lipid rafts
    • Xu W, Yoon SI, Huang P, Wang Y, Chen C, et al. (2006) Localization of the kappa opioid receptor in lipid rafts. J Pharmacol Exp Ther 317(3): 1295-1306.
    • (2006) J Pharmacol Exp Ther , vol.317 , Issue.3 , pp. 1295-1306
    • Xu, W.1    Yoon, S.I.2    Huang, P.3    Wang, Y.4    Chen, C.5
  • 65
    • 0037077208 scopus 로고    scopus 로고
    • Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer
    • Ayoub MA, Couturier C, Lucas-Meunier E, Angers S, Fossier P, et al. (2002) Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. J Biol Chem 277(24): 21522-21528.
    • (2002) J Biol Chem , vol.277 , Issue.24 , pp. 21522-21528
    • Ayoub, M.A.1    Couturier, C.2    Lucas-Meunier, E.3    Angers, S.4    Fossier, P.5
  • 66
    • 0037160105 scopus 로고    scopus 로고
    • Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • Mercier JF, Salahpour A, Angers S, Breit A, Bouvier M (2002) Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer. J Biol Chem 277(47): 44925-44931.
    • (2002) J Biol Chem , vol.277 , Issue.47 , pp. 44925-44931
    • Mercier, J.F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5
  • 67
    • 61549138107 scopus 로고    scopus 로고
    • Constitutive dimerization of the G-protein coupled receptor, neurotensin receptor 1, reconstituted into phospholipid bilayers
    • Harding PJ, Attrill H, Boehringer J, Ross S, Wadhams GH, et al. (2009) Constitutive dimerization of the G-protein coupled receptor, neurotensin receptor 1, reconstituted into phospholipid bilayers. Biophys J 96(3): 964-973.
    • (2009) Biophys J , vol.96 , Issue.3 , pp. 964-973
    • Harding, P.J.1    Attrill, H.2    Boehringer, J.3    Ross, S.4    Wadhams, G.H.5
  • 68
    • 3042663287 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerization: Function and ligand pharmacology
    • Milligan G (2004) G protein-coupled receptor dimerization: Function and ligand pharmacology. Mol Pharmacol 66(1): 1-7.
    • (2004) Mol Pharmacol , vol.66 , Issue.1 , pp. 1-7
    • Milligan, G.1
  • 69
    • 2942683015 scopus 로고    scopus 로고
    • An algebra of dimerization and its implications for G-protein coupled receptor signaling
    • Woolf PJ, Linderman JJ (2004) An algebra of dimerization and its implications for G-protein coupled receptor signaling. J Theor Biol 229(2): 157-168.
    • (2004) J Theor Biol , vol.229 , Issue.2 , pp. 157-168
    • Woolf, P.J.1    Linderman, J.J.2
  • 70
    • 50849086372 scopus 로고    scopus 로고
    • Turcotte M, Tang W, Ross EM (2008) Coordinate regulation of G protein signaling via dynamic interactions of receptor and GAP. PLoS Comput Biol 4(8): e1000148.
    • Turcotte M, Tang W, Ross EM (2008) Coordinate regulation of G protein signaling via dynamic interactions of receptor and GAP. PLoS Comput Biol 4(8): e1000148.
  • 71
    • 52949139072 scopus 로고    scopus 로고
    • Flaherty P, Radhakrishnan ML, Dinh T, Rebres RA, Roach TI, et al. (2008) A dual receptor crosstalk model of G-protein-coupled signal transduction. PLoS Comput Biol 4(9): e1000185.
    • Flaherty P, Radhakrishnan ML, Dinh T, Rebres RA, Roach TI, et al. (2008) A dual receptor crosstalk model of G-protein-coupled signal transduction. PLoS Comput Biol 4(9): e1000185.
  • 72
    • 33645288264 scopus 로고    scopus 로고
    • Lipid rafts in lymphocyte activation and migration
    • Manes S, Viola A (2006) Lipid rafts in lymphocyte activation and migration. Mol Membr Biol 23(1): 59-69.
    • (2006) Mol Membr Biol , vol.23 , Issue.1 , pp. 59-69
    • Manes, S.1    Viola, A.2
  • 73
    • 2342451911 scopus 로고    scopus 로고
    • G-protein coupled receptors in lipid rafts and caveolae: How, when and why do they go there?
    • Chini B, Parenti M (2004) G-protein coupled receptors in lipid rafts and caveolae: How, when and why do they go there? J Mol Endocrinol 32(2): 325-338.
    • (2004) J Mol Endocrinol , vol.32 , Issue.2 , pp. 325-338
    • Chini, B.1    Parenti, M.2
  • 74
    • 0033592303 scopus 로고    scopus 로고
    • Modeling activation and desensitization of G-protein coupled receptors provides insight into ligand efficacy
    • Riccobene TA, Omann GM, Linderman JJ (1999) Modeling activation and desensitization of G-protein coupled receptors provides insight into ligand efficacy. J Theor Biol 200(2): 207-222.
    • (1999) J Theor Biol , vol.200 , Issue.2 , pp. 207-222
    • Riccobene, T.A.1    Omann, G.M.2    Linderman, J.J.3
  • 75
    • 0033578385 scopus 로고    scopus 로고
    • Rapid GTP binding and hydrolysis by G(q) promoted by receptor and GTPase-activating proteins
    • Mukhopadhyay S, Ross EM (1999) Rapid GTP binding and hydrolysis by G(q) promoted by receptor and GTPase-activating proteins. Proc Natl Acad Sci U S A 96(17): 9539-9544.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.17 , pp. 9539-9544
    • Mukhopadhyay, S.1    Ross, E.M.2
  • 76
    • 0037470041 scopus 로고    scopus 로고
    • A spatial focusing model for G protein signals. regulator of G protein signaling (RGS) protien-mediated kinetic scaffolding
    • Zhong H, Wade SM, Woolf PJ, Linderman JJ, Traynor JR, et al. (2003) A spatial focusing model for G protein signals. regulator of G protein signaling (RGS) protien-mediated kinetic scaffolding. J Biol Chem 278(9): 7278-7284.
    • (2003) J Biol Chem , vol.278 , Issue.9 , pp. 7278-7284
    • Zhong, H.1    Wade, S.M.2    Woolf, P.J.3    Linderman, J.J.4    Traynor, J.R.5
  • 77
    • 33846503153 scopus 로고    scopus 로고
    • Both ligand- and cell-specific parameters control ligand agonism in a kinetic model of g protein-coupled receptor signaling
    • Kinzer-Ursem TL, Linderman JJ (2007) Both ligand- and cell-specific parameters control ligand agonism in a kinetic model of g protein-coupled receptor signaling. PLoS Comput Biol 3(1): e6.
    • (2007) PLoS Comput Biol , vol.3 , Issue.1
    • Kinzer-Ursem, T.L.1    Linderman, J.J.2


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