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Volumn 3, Issue , 2012, Pages

The allosteric vestibule of a seven transmembrane helical receptor controls G-protein coupling

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; MUSCARINIC M2 RECEPTOR; PILOCARPINE; RECEPTOR; TRANSMEMBRANE HELICAL RECEPTOR; UNCLASSIFIED DRUG;

EID: 84867010308     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms2028     Document Type: Article
Times cited : (116)

References (55)
  • 2
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G protein-coupled receptors and significance for drug discovery
    • Lagerstrom, M. C. & Schioth, H. B. Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat. Rev. Drug Discov. 7, 339-357 (2008).
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 339-357
    • Lagerstrom, M.C.1    Schioth, H.B.2
  • 4
    • 0025834532 scopus 로고
    • Diversity of G proteins in signal transduction
    • Simon, M. I., Strathmann, M. P. & Gautam, N. Diversity of G proteins in signal transduction. Science 252, 802-808 (1991). (Pubitemid 121000516)
    • (1991) Science , vol.252 , Issue.5007 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 5
    • 77952354490 scopus 로고    scopus 로고
    • Seven transmembrane receptors as shapeshifting proteins: The impact of allosteric modulation and functional selectivity on new drug discovery
    • Kenakin, T. & Miller, L. J. Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery. Pharmacol. Rev. 62, 265-304 (2010).
    • (2010) Pharmacol. Rev. , vol.62 , pp. 265-304
    • Kenakin, T.1    Miller, L.J.2
  • 6
    • 77951844975 scopus 로고    scopus 로고
    • Teaching old receptors new tricks: Biasing seven-transmembrane receptors
    • Rajagopal, S., Rajagopal, K. & Lefkowitz, R. J. Teaching old receptors new tricks: biasing seven-transmembrane receptors. Nat. Rev. Drug Discov. 9, 373-386 (2010).
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 373-386
    • Rajagopal, S.1    Rajagopal, K.2    Lefkowitz, R.J.3
  • 8
    • 77958039571 scopus 로고    scopus 로고
    • Energy landscapes as a tool to integrate GPCR structure, dynamics, and function
    • Deupi, X. & Kobilka, B. K. Energy landscapes as a tool to integrate GPCR structure, dynamics, and function. Physiology (Bethesda) 25, 293-303 (2010).
    • (2010) Physiology (Bethesda) , vol.25 , pp. 293-303
    • Deupi, X.1    Kobilka, B.K.2
  • 9
    • 52949102889 scopus 로고    scopus 로고
    • Crystal structure of opsin in its G-protein-interacting conformation
    • Scheerer, P. et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 455, 497-502 (2008).
    • (2008) Nature , vol.455 , pp. 497-502
    • Scheerer, P.1
  • 10
    • 78651411166 scopus 로고    scopus 로고
    • Structure of a nanobody-stabilized active state of the β2 adrenoceptor
    • Rasmussen, S. G. F. et al. Structure of a nanobody-stabilized active state of the β2 adrenoceptor. Nature 469, 175-180 (2011).
    • (2011) Nature , vol.469 , pp. 175-180
    • Rasmussen, S.G.F.1
  • 11
    • 79959564813 scopus 로고    scopus 로고
    • Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation
    • Lebon, G. et al. Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation. Nature 474, 521-525 (2011).
    • (2011) Nature , vol.474 , pp. 521-525
    • Lebon, G.1
  • 12
    • 84855901533 scopus 로고    scopus 로고
    • Molecular mechanism of β-arrestin-biased agonism at seven-transmembrane receptors
    • Reiter, E., Ahn, S., Shukla, A. K. & Lefkowitz, R. J. Molecular mechanism of β-arrestin-biased agonism at seven-transmembrane receptors. Annu. Rev. Pharmacol. Toxicol. 52, 179-197 (2012).
    • (2012) Annu. Rev. Pharmacol. Toxicol. , vol.52 , pp. 179-197
    • Reiter, E.1    Ahn, S.2    Shukla, A.K.3    Lefkowitz, R.J.4
  • 13
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the β2 adrenergic receptor-Gs protein complex
    • Rasmussen, S. G. F. et al. Crystal structure of the β2 adrenergic receptor-Gs protein complex. Nature 477, 549-555 (2011).
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.F.1
  • 14
    • 37549016836 scopus 로고    scopus 로고
    • Heterotrimeric G protein activation by G-protein-coupled receptors
    • Oldham, W. M. & Hamm, H. E. Heterotrimeric G protein activation by G-protein-coupled receptors. Nat. Rev. Mol. Cell. Biol. 9, 60-71 (2008).
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , pp. 60-71
    • Oldham, W.M.1    Hamm, H.E.2
  • 15
    • 73849149844 scopus 로고    scopus 로고
    • Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor
    • Bokoch, M. P. et al. Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor. Nature 463, 108-112 (2010).
    • (2010) Nature , vol.463 , pp. 108-112
    • Bokoch, M.P.1
  • 16
    • 0036258990 scopus 로고    scopus 로고
    • G protein-coupled receptor allosterism and complexing
    • DOI 10.1124/pr.54.2.323
    • Christopoulos, A. & Kenakin, T. G protein-coupled receptor allosterism and complexing. Pharmacol. Rev. 54, 323-374 (2002). (Pubitemid 34575719)
    • (2002) Pharmacological Reviews , vol.54 , Issue.2 , pp. 323-374
    • Christopoulos, A.1    Kenakin, T.2
  • 17
    • 34548362105 scopus 로고    scopus 로고
    • Muscarinic acetylcholine receptors: Mutant mice provide new insights for drug development
    • DOI 10.1038/nrd2379, PII NRD2379
    • Wess, J., Eglen, R. M. & Gautam, D. Muscarinic acetylcholine receptors: mutant mice provide new insights for drug development. Nat. Rev. Drug Discov. 6, 721-733 (2007). (Pubitemid 47342315)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.9 , pp. 721-733
    • Wess, J.1    Eglen, R.M.2    Gautam, D.3
  • 18
    • 0014449606 scopus 로고
    • Inhibition of the actions of carbachol and DFP on guinea pig isolated atria by alkane-bis-ammonium compounds
    • Lüllmann, H., Ohnesorge, F. K., Schauwecker, G. C. & Wassermann, O. R. Inhibition of the actions of carbachol and DFP on guinea pig isolated atria by alkane-bis-ammonium compounds. Eur. J. Pharmacol. 6, 241-247 (1969).
    • (1969) Eur. J. Pharmacol. , vol.6 , pp. 241-247
    • Lüllmann, H.1    Ohnesorge, F.K.2    Schauwecker, G.C.3    Wassermann, O.R.4
  • 19
    • 0020533362 scopus 로고
    • Modification of the binding properties of muscarinic receptors by gallamine
    • Stockton, J. M., Birdsall, N. J., Burgen, A. S. & Hulme, E. C. Modification of the binding properties of muscarinic receptors by gallamine. Mol. Pharmacol. 23, 551-557 (1982).
    • (1982) Mol. Pharmacol. , vol.23 , pp. 551-557
    • Stockton, J.M.1    Birdsall, N.J.2    Burgen, A.S.3    Hulme, E.C.4
  • 21
    • 0038237079 scopus 로고    scopus 로고
    • 5 subtype selectivities of some structurally diverse allosteric ligands in N-methylscopolamine-occupied receptors
    • DOI 10.1124/mol.64.1.21
    • Voigtländer, U. et al. Allosteric site on muscarinic acetylcholine receptors: identification of two amino acids in the muscarinic M2 receptor that account entirely for the M2/M5 subtype selectivities of some structurally diverse allosteric ligands in N-methylscopolamine-occupied receptors. Mol. Pharmacol. 64, 21-31 (2003). (Pubitemid 36759814)
    • (2003) Molecular Pharmacology , vol.64 , Issue.1 , pp. 21-31
    • Voigtlander, U.1    Johren, K.2    Mohr, M.3    Raasch, A.4    Trankle, C.5    Buller, S.6    Ellis, J.7    Holtje, H.-D.8    Mohr, K.9
  • 22
    • 23944472444 scopus 로고    scopus 로고
    • 2 muscarinic acetylcholine receptor: More similarities than differences between the structurally divergent agents gallamine and bis(ammonio)alkane-type hexamethylene-bis-[dimethyl-(3-phthalimidopropyl) ammonium]dibromide
    • DOI 10.1124/mol.105.014043
    • Huang, X.-P., Prilla, S., Mohr, K. & Ellis, J. Critical amino acid residues of the common allosteric site on the M2 muscarinic acetylcholine receptor: more similarities than differences between the structurally divergent agents gallamine and bis(ammonio)alkane-type hexamethylene-bis-[dimethyl-(3- phthalimidopropyl)ammonium]dibromide. Mol. Pharmacol. 68, 769-778 (2005). (Pubitemid 41206031)
    • (2005) Molecular Pharmacology , vol.68 , Issue.3 , pp. 769-778
    • Huang, X.-P.1    Prilla, S.2    Mohr, K.3    Ellis, J.4
  • 23
    • 33745282128 scopus 로고    scopus 로고
    • Allosteric interactions with muscarinic acetylcholine receptors: Complex role of the conserved tryptophan M2 422Trp in a critical cluster of amino acids for baseline affinity, subtype selectivity, and cooperativity
    • Prilla, S., Schrobang, J., Ellis, J., Höltje, H.-D. & Mohr, K. Allosteric interactions with muscarinic acetylcholine receptors: complex role of the conserved tryptophan M2 422Trp in a critical cluster of amino acids for baseline affinity, subtype selectivity, and cooperativity. Mol. Pharmacol. 70, 181-193 (2006).
    • (2006) Mol. Pharmacol. , vol.70 , pp. 181-193
    • Prilla, S.1    Schrobang, J.2    Ellis, J.3    Höltje, H.-D.4    Mohr, K.5
  • 24
    • 59649112659 scopus 로고    scopus 로고
    • Dualsteric GPCR targeting: A novel route to binding and signaling pathway selectivity
    • Antony, J. et al. Dualsteric GPCR targeting: a novel route to binding and signaling pathway selectivity. FASEB J. 23, 442-450 (2009).
    • (2009) FASEB J. , vol.23 , pp. 442-450
    • Antony, J.1
  • 25
    • 84862777405 scopus 로고    scopus 로고
    • Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist
    • Haga, K. et al. Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist. Nature 482, 547-551 (2012).
    • (2012) Nature , vol.482 , pp. 547-551
    • Haga, K.1
  • 26
    • 0041411237 scopus 로고    scopus 로고
    • 1 muscarinic acetylcholine receptor
    • DOI 10.1080/10606820308261
    • Hulme, E. C., Lu, Z. L. & Bee, M. S. Scanning mutagenesis studies of the M1 muscarinic acetylcholine receptor. Receptors Channels 9, 215-228 (2003). (Pubitemid 37069444)
    • (2003) Receptors and Channels , vol.9 , Issue.4 , pp. 215-228
    • Hulme, E.C.1    Lu, Z.L.2    Bee, M.S.3
  • 27
    • 0036169280 scopus 로고    scopus 로고
    • The binding site of aminergic G protein-coupled receptors: The transmembrane segments and second extracellular loop
    • DOI 10.1146/annurev.pharmtox.42.091101.144224
    • Shi, L. & Javitch, J. A. The binding site of aminergic G protein-coupled receptors: the transmembrane segments and second extracellular loop. Annu. Rev. Pharmacol. Toxicol. 42, 437-467 (2002). (Pubitemid 34162546)
    • (2002) Annual Review of Pharmacology and Toxicology , vol.42 , pp. 437-467
    • Shi, L.1    Javitch, J.A.2
  • 28
    • 77954243052 scopus 로고    scopus 로고
    • Short synthesis of the muscarinic superagonist iperoxo
    • Kloeckner, J., Schmitz, J. & Holzgrabe, U. Convergent, short synthesis of the muscarinic superagonist iperoxo. Tetrahedron Lett. 51, 3470-3472 (2010).
    • (2010) Tetrahedron Lett. , vol.51 , pp. 3470-3472
    • Kloeckner, J.1    Schmitz, J.2    Convergent, H.U.3
  • 30
    • 0022367080 scopus 로고
    • Functional reconstitution of purified muscarinic receptors and inhibitory guanine nucleotide regulatory protein
    • DOI 10.1038/316731a0
    • Haga, K. et al. Functional reconstitution of purified muscarinic receptors and inhibitory guanine nucleotide regulatory protein. Nature 316, 731-733 (1985). (Pubitemid 16239349)
    • (1985) Nature , vol.316 , Issue.6030 , pp. 731-733
    • Haga, K.1    Haga, T.2    Ichiyama, A.3
  • 31
    • 0035079910 scopus 로고    scopus 로고
    • 2 acetylcholine receptors on the synthesis of cyclic amp in CHO cells: Dependence on time, receptor density and receptor agonists
    • Michal, P., Lysíková, M. & Tuc?ek, S. Dual effects of muscarinic M(2) acetylcholine receptors on the synthesis of cyclic AMP in CHO cells: dependence on time, receptor density and receptor agonists. Br. J. Pharmacol. 132, 1217-1228 (2001). (Pubitemid 32234705)
    • (2001) British Journal of Pharmacology , vol.132 , Issue.6 , pp. 1217-1228
    • Michal, P.1    Lysikova, M.2    Tucek, S.3
  • 32
    • 77956657852 scopus 로고    scopus 로고
    • Deconvolution of complex G protein-coupled receptor signaling in live cells using dynamic mass redistribution measurements
    • Schröder, R. et al. Deconvolution of complex G protein-coupled receptor signaling in live cells using dynamic mass redistribution measurements. Nat. Biotech. 28, 943-949 (2010).
    • (2010) Nat. Biotech. , vol.28 , pp. 943-949
    • Schröder, R.1
  • 33
    • 80054807491 scopus 로고    scopus 로고
    • Applying label-free dynamic mass redistribution technology to frame signaling of G protein-coupled receptors noninvasively in living cells
    • Schröder, R. et al. Applying label-free dynamic mass redistribution technology to frame signaling of G protein-coupled receptors noninvasively in living cells. Nat. Protoc. 6, 1748-1760 (2011).
    • (2011) Nat. Protoc. , vol.6 , pp. 1748-1760
    • Schröder, R.1
  • 34
    • 0029126526 scopus 로고
    • Detection quantitation, and verification of allosteric interactions of agents with labeled and unlabeled ligands at G protein-coupled receptors: Interactions of strychnine and acetylcholine at muscarinic receptors
    • Lazareno, S. & Birdsall, N. J. Detection, quantitation, and verification of allosteric interactions of agents with labeled and unlabeled ligands at G protein-coupled receptors: interactions of strychnine and acetylcholine at muscarinic receptors. Mol. Pharmacol. 48, 362-378 (1995).
    • (1995) Mol. Pharmacol. , vol.48 , pp. 362-378
    • Lazareno, S.1    Birdsall, N.J.2
  • 35
    • 0037305047 scopus 로고    scopus 로고
    • 35S]GTPγS binding assays
    • DOI 10.1016/S0165-6147(02)00027-5, PII S0165614702000275
    • Milligan, G. Principles: extending the utility of [35S]GTPγS binding assays. Trends Pharmacol. Sci. 24, 87-90 (2003). (Pubitemid 36135882)
    • (2003) Trends in Pharmacological Sciences , vol.24 , Issue.2 , pp. 87-90
    • Milligan, G.1
  • 36
    • 77951223981 scopus 로고    scopus 로고
    • Identification of orthosteric and allosteric site mutations in M2 muscarinic acetylcholine receptors that contribute to ligand-selective signaling bias
    • Gregory, K. J., Hall, N. E., Tobin, A. B., Sexton, P. M. & Christopoulos, A. Identification of orthosteric and allosteric site mutations in M2 muscarinic acetylcholine receptors that contribute to ligand-selective signaling bias. J. Biol. Chem. 285, 7459-7474 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 7459-7474
    • Gregory, K.J.1    Hall, N.E.2    Tobin, A.B.3    Sexton, P.M.4    Christopoulos, A.5
  • 39
    • 34447642715 scopus 로고    scopus 로고
    • The evasive nature of drug efficacy: Implications for drug discovery
    • DOI 10.1016/j.tips.2007.06.005, PII S0165614707001502, Allosterism and Collateral Efficacy
    • Galandrin, S., Oligny-Longpré, G. & Bouvier, M. The evasive nature of drug efficacy: implications for drug discovery. Trends Pharmacol. Sci. 28, 423-430 (2007). (Pubitemid 47087968)
    • (2007) Trends in Pharmacological Sciences , vol.28 , Issue.8 , pp. 423-430
    • Galandrin, S.1    Oligny-Longpre, G.2    Bouvier, M.3
  • 40
    • 34447624153 scopus 로고    scopus 로고
    • Collateral efficacy in drug discovery: Taking advantage of the good (allosteric) nature of 7TM receptors
    • DOI 10.1016/j.tips.2007.06.009, PII S0165614707001551, Allosterism and Collateral Efficacy
    • Kenakin, T. Collateral efficacy in drug discovery: taking advantage of the good (allosteric) nature of 7TM receptors. Trends Pharmacol. Sci. 28, 407-415 (2007). (Pubitemid 47087972)
    • (2007) Trends in Pharmacological Sciences , vol.28 , Issue.8 , pp. 407-415
    • Kenakin, T.1
  • 41
    • 77950588803 scopus 로고    scopus 로고
    • A fluorescence resonance energy transfer-based M2 muscarinic receptor sensor reveals rapid kinetics of allosteric modulation
    • Maier-Peuschel, M. et al. A fluorescence resonance energy transfer-based M2 muscarinic receptor sensor reveals rapid kinetics of allosteric modulation. J. Biol. Chem. 285, 8793-8800 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 8793-8800
    • Maier-Peuschel, M.1
  • 43
    • 77957573768 scopus 로고    scopus 로고
    • Fluorescent labeling of tetracysteine-tagged proteins in intact cells
    • Hoffmann, C. et al. Fluorescent labeling of tetracysteine-tagged proteins in intact cells. Nat. Protoc. 5, 1666-1677 (2010).
    • (2010) Nat. Protoc. , vol.5 , pp. 1666-1677
    • Hoffmann, C.1
  • 44
    • 0038729670 scopus 로고    scopus 로고
    • Measurement of the millisecond activation switch of G protein-coupled receptors in living cells
    • DOI 10.1038/nbt838
    • Vilardaga, J.-P., Bünemann, M., Krasel, C., Castro, M. & Lohse, M. J. Measurement of the millisecond activation switch of G protein-coupled receptors in living cells. Nat. Biotech. 21, 807-812 (2003). (Pubitemid 36791401)
    • (2003) Nature Biotechnology , vol.21 , Issue.7 , pp. 807-812
    • Vilardaga, J.-P.1    Bunemann, M.2    Krasell, C.3    Castro, M.4    Lohse, M.J.5
  • 46
    • 0028240869 scopus 로고
    • Ras-dependent activation of MAP kinase pathway mediated by G-protein βγ subunits
    • DOI 10.1038/369418a0
    • Crespo, P., Xu, N., Simonds, W. F. & Gutkind, J. S. Ras-dependent activation of MAP kinase pathway mediated by G-protein beta gamma subunits. Nature 369, 418-420 (1994). (Pubitemid 24184058)
    • (1994) Nature , vol.369 , Issue.6479 , pp. 418-420
    • Crespo, P.1    Xu, N.2    Simonds, W.F.3    Gutkind, J.S.4
  • 47
    • 0031037296 scopus 로고    scopus 로고
    • Linkage of g protein-coupled receptors to the MAPK signaling pathway through Pl 3-kinase γ
    • DOI 10.1126/science.275.5298.394
    • Lopez-Ilasaca, M., Crespo, P., Pellici, P. G., Gutkind, J. S. & Wetzker, R. Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase γ. Science 275, 394-397 (1997). (Pubitemid 27051618)
    • (1997) Science , vol.275 , Issue.5298 , pp. 394-397
    • Lopez-Ilasaca, M.1    Crespo, P.2    Pellici, P.G.3    Gutkind, J.S.4    Wetzker, R.5
  • 48
    • 57649170953 scopus 로고    scopus 로고
    • A novel mechanism of G protein-coupled receptor functional selectivity
    • Valant, C. et al. A novel mechanism of G protein-coupled receptor functional selectivity. J. Biol. Chem. 283, 29312-29321 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 29312-29321
    • Valant, C.1
  • 49
    • 78650919353 scopus 로고    scopus 로고
    • Importance of the extracellular loops in G protein-coupled receptors for ligand recognition and receptor activation
    • Peeters, M. C., van Westen, G. J. P., Li, Q. & IJzerman, A. P. Importance of the extracellular loops in G protein-coupled receptors for ligand recognition and receptor activation. Trends Pharmacol. Sci. 32, 35-42 (2011).
    • (2011) Trends Pharmacol. Sci. , vol.32 , pp. 35-42
    • Peeters, M.C.1    Van Westen, G.J.P.2    Li, Q.3    Ijzerman, A.P.4
  • 50
    • 80052001378 scopus 로고    scopus 로고
    • Pathway and mechanism of drug binding to G-protein-coupled receptors
    • Dror, R. O. et al. Pathway and mechanism of drug binding to G-protein-coupled receptors. Proc. Natl Acad. Sci. USA 108, 13118-13123 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 13118-13123
    • Dror, R.O.1
  • 51
    • 84857093891 scopus 로고    scopus 로고
    • Molecular basis of ligand dissociation in β-adrenergic receptors
    • González, A., Perez-Acle, T., Pardo, L. & Deupi, X. Molecular basis of ligand dissociation in β-adrenergic receptors. PLoS ONE 6, e23815 (2011).
    • (2011) PLoS ONE , vol.6
    • González, A.1    Perez-Acle, T.2    Pardo, L.3    Deupi, X.4
  • 52
    • 84855879360 scopus 로고    scopus 로고
    • The best of both worlds? Bitopic orthosteric/allosteric ligands of G protein-coupled receptors
    • Valant, C., Robert Lane, J., Sexton, P. M. & Christopoulos, A. The best of both worlds? Bitopic orthosteric/allosteric ligands of G protein-coupled receptors. Annu. Rev. Pharmacol. Toxicol. 52, 153-178 (2012).
    • (2012) Annu. Rev. Pharmacol. Toxicol. , vol.52 , pp. 153-178
    • Valant, C.1    Robert Lane, J.2    Sexton, P.M.3    Christopoulos, A.4
  • 53
    • 0026509982 scopus 로고
    • Agonist-independent inhibition of G protein activation by muscarinic acetylcholine receptor antagonists in cardiac membranes
    • Hilf, G. & Jakobs, K. H. Agonist-independent inhibition of G protein activation by muscarinic acetylcholine receptor antagonists in cardiac membranes. Eur. J. Pharmacol. 225, 245-252 (1992).
    • (1992) Eur. J. Pharmacol. , vol.225 , pp. 245-252
    • Hilf, G.1    Jakobs, K.H.2
  • 54
    • 59449089513 scopus 로고    scopus 로고
    • The C-terminal tail of CRTH2 is a key molecular determinant that constrains Gαi and downstream signaling cascade activation
    • Schröder, R. et al. The C-terminal tail of CRTH2 is a key molecular determinant that constrains Gαi and downstream signaling cascade activation. J. Biol. Chem. 284, 1324-1336 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 1324-1336
    • Schröder, R.1


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