메뉴 건너뛰기




Volumn 288, Issue 46, 2013, Pages 33226-33240

Carboxypeptidase M is a positive allosteric modulator of the kinin B1 receptor

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC MODULATION; BIOLUMINESCENCE RESONANCE ENERGY TRANSFER; CONFORMATIONAL CHANGE; EXTRACELLULAR DOMAINS; EXTRACELLULAR LOOP 2; G PROTEIN COUPLED RECEPTORS; POSITIVE ALLOSTERIC MODULATOR; PROTEIN-PROTEIN INTERACTIONS;

EID: 84887829502     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.520791     Document Type: Article
Times cited : (26)

References (74)
  • 1
    • 84884856960 scopus 로고    scopus 로고
    • Rawlings, N. D., and Salvesen, G. S., eds, 3rd Ed., Academic Press, Oxford
    • Zhang, X., and Skidgel, R. (2013) in Handbook of Proteolytic Enzyme (Rawlings, N. D., and Salvesen, G. S., eds) pp. 1357-1366, 3rd Ed., Academic Press, Oxford
    • (2013) Handbook of Proteolytic Enzyme , pp. 1357-1366
    • Zhang, X.1    Skidgel, R.2
  • 2
    • 54249136672 scopus 로고    scopus 로고
    • Structure and mechanism of metallocarboxypeptidases
    • Gomis-Rüth, F. X. (2008) Structure and mechanism of metallocarboxypeptidases. Crit. Rev. Biochem. Mol. Biol. 43, 319-345
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 319-345
    • Gomis-Rüth, F.X.1
  • 3
    • 0037028497 scopus 로고    scopus 로고
    • Structure of the human carboxypeptidase M gene. Identification of a proximal GC-rich promoter and a unique distal promoter that consists of repetitive elements
    • Li, J., Rehli, M., Timblin, B., Tan, F., Krause, S. W., and Skidgel, R. A. (2002) Structure of the human carboxypeptidase M gene. Identification of a proximal GC-rich promoter and a unique distal promoter that consists of repetitive elements. Gene 284, 189-202
    • (2002) Gene , vol.284 , pp. 189-202
    • Li, J.1    Rehli, M.2    Timblin, B.3    Tan, F.4    Krause, S.W.5    Skidgel, R.A.6
  • 4
    • 0024372894 scopus 로고
    • Molecular cloning and sequencing of the cDNA for human membranebound carboxypeptidase M. Comparison with carboxypeptidases A, B, H
    • Tan, F., Chan, S. J., Steiner, D. F., Schilling, J. W., and Skidgel, R. A. (1989) Molecular cloning and sequencing of the cDNA for human membranebound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N. J. Biol. Chem. 264, 13165-13170
    • (1989) N. J. Biol. Chem. , vol.264 , pp. 13165-13170
    • Tan, F.1    Chan, S.J.2    Steiner, D.F.3    Schilling, J.W.4    Skidgel, R.A.5
  • 5
    • 1842557330 scopus 로고    scopus 로고
    • Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity
    • Reverter, D., Maskos, K., Tan, F., Skidgel, R. A., and Bode, W. (2004) Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity. J. Mol. Biol. 338, 257-269
    • (2004) J. Mol. Biol. , vol.338 , pp. 257-269
    • Reverter, D.1    Maskos, K.2    Tan, F.3    Skidgel, R.A.4    Bode, W.5
  • 6
    • 0031886603 scopus 로고    scopus 로고
    • Cellular carboxypeptidases
    • Skidgel, R. A., and Erdös, E. G. (1998) Cellular carboxypeptidases. Immunol. Rev. 161, 129-141
    • (1998) Immunol. Rev. , vol.161 , pp. 129-141
    • Skidgel, R.A.1    Erdös, E.G.2
  • 7
    • 0035200832 scopus 로고    scopus 로고
    • Carboxypeptidases from A to Z. Implications in embryonic development and Wnt binding
    • Reznik, S. E., and Fricker, L. D. (2001) Carboxypeptidases from A to Z. Implications in embryonic development and Wnt binding. Cell. Mol. Life Sci. 58, 1790-1804
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1790-1804
    • Reznik, S.E.1    Fricker, L.D.2
  • 8
    • 0025024253 scopus 로고
    • Carboxypeptidase M in Madin-Darby canine kidney cells. Evidence that carboxypeptidase M has a phosphatidylinositol glycan anchor
    • Deddish, P. A., Skidgel, R. A., Kriho, V. B., Li, X. Y., Becker, R. P., and Erdös, E. G. (1990) Carboxypeptidase M in Madin-Darby canine kidney cells. Evidence that carboxypeptidase M has a phosphatidylinositol glycan anchor. J. Biol. Chem. 265, 15083-15089
    • (1990) J. Biol. Chem. , vol.265 , pp. 15083-15089
    • Deddish, P.A.1    Skidgel, R.A.2    Kriho, V.B.3    Li, X.Y.4    Becker, R.P.5    Erdös, E.G.6
  • 9
    • 0033614445 scopus 로고    scopus 로고
    • Release of glycosylphosphatidylinositolanchored carboxypeptidaseMby phosphatidylinositol-specific phospholipase C up-regulates enzyme synthesis
    • Li, X. Y., and Skidgel, R. A. (1999) Release of glycosylphosphatidylinositolanchored carboxypeptidaseMby phosphatidylinositol- specific phospholipase C up-regulates enzyme synthesis. Biochem. Biophys. Res. Commun. 258, 204-210
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 204-210
    • Li, X.Y.1    Skidgel, R.A.2
  • 10
  • 11
    • 0023690624 scopus 로고
    • Basic carboxypeptidases. Regulators of peptide hormone activity
    • Skidgel, R. A. (1988) Basic carboxypeptidases. Regulators of peptide hormone activity. Trends Pharmacol. Sci. 9, 299-304
    • (1988) Trends Pharmacol. Sci. , vol.9 , pp. 299-304
    • Skidgel, R.A.1
  • 12
    • 0024552834 scopus 로고
    • Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones
    • Skidgel, R. A., Davis, R. M., and Tan, F. (1989) Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones. J. Biol. Chem. 264, 2236-2241
    • (1989) J. Biol. Chem. , vol.264 , pp. 2236-2241
    • Skidgel, R.A.1    Davis, R.M.2    Tan, F.3
  • 13
    • 77049085479 scopus 로고    scopus 로고
    • Differential regulation of inducible and endothelial nitric oxide synthase by kinin B1 and B2 receptors
    • Kuhr, F., Lowry, J., Zhang, Y., Brovkovych, V., and Skidgel, R. A. (2010) Differential regulation of inducible and endothelial nitric oxide synthase by kinin B1 and B2 receptors. Neuropeptides 44, 145-154
    • (2010) Neuropeptides , vol.44 , pp. 145-154
    • Kuhr, F.1    Lowry, J.2    Zhang, Y.3    Brovkovych, V.4    Skidgel, R.A.5
  • 14
    • 14144251086 scopus 로고    scopus 로고
    • International union of pharmacology. XLV. Classification of the kinin receptor family. from molecular mechanisms to pathophysiological consequences
    • Leeb-Lundberg, L. M., Marceau, F., Müller-Esterl, W., Pettibone, D. J., and Zuraw, B. L. (2005) International union of pharmacology. XLV. Classification of the kinin receptor family. From molecular mechanisms to pathophysiological consequences. Pharmacol. Rev. 57, 27-77
    • (2005) Pharmacol. Rev. , vol.57 , pp. 27-77
    • Leeb-Lundberg, L.M.1    Marceau, F.2    Müller-Esterl, W.3    Pettibone, D.J.4    Zuraw, B.L.5
  • 15
    • 77953951240 scopus 로고    scopus 로고
    • Key role for spinal dorsal horn microglial kinin B1 receptor in early diabetic pain neuropathy
    • Talbot, S., Chahmi, E., Dias, J. P., and Couture, R. (2010) Key role for spinal dorsal horn microglial kinin B1 receptor in early diabetic pain neuropathy. J. Neuroinflammation 7, 36
    • (2010) J. Neuroinflammation , vol.7 , pp. 36
    • Talbot, S.1    Chahmi, E.2    Dias, J.P.3    Couture, R.4
  • 16
    • 33748533791 scopus 로고    scopus 로고
    • Kinins and cardiovascular diseases
    • Su, J. B. (2006) Kinins and cardiovascular diseases. Curr. Pharm. Des. 12, 3423-3435
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 3423-3435
    • Su, J.B.1
  • 17
    • 0242441478 scopus 로고    scopus 로고
    • Mechanisms mediating the vasoactive effects of the B1 receptors of bradykinin
    • Duka, I., Duka, A., Kintsurashvili, E., Johns, C., Gavras, I., and Gavras, H. (2003) Mechanisms mediating the vasoactive effects of the B1 receptors of bradykinin. Hypertension 42, 1021-1025
    • (2003) Hypertension , vol.42 , pp. 1021-1025
    • Duka, I.1    Duka, A.2    Kintsurashvili, E.3    Johns, C.4    Gavras, I.5    Gavras, H.6
  • 19
    • 46149110502 scopus 로고    scopus 로고
    • Increased susceptibility to endotoxic shock in transgenic rats with endothelial overexpression of kinin B (1) receptors
    • Merino, V. F., Todiras, M., Campos, L. A., Saul, V., Popova, E., Baltatu, O. C., Pesquero, J. B., and Bader, M. (2008) Increased susceptibility to endotoxic shock in transgenic rats with endothelial overexpression of kinin B(1) receptors. J. Mol. Med. 86, 791-798
    • (2008) J. Mol. Med. , vol.86 , pp. 791-798
    • Merino, V.F.1    Todiras, M.2    Campos, L.A.3    Saul, V.4    Popova, E.5    Baltatu, O.C.6    Pesquero, J.B.7    Bader, M.8
  • 24
    • 74949129329 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitors are allosteric enhancers of kinin B1 and B2 receptor function
    • Erdös, E. G., Tan, F., and Skidgel, R. A. (2010) Angiotensin I-converting enzyme inhibitors are allosteric enhancers of kinin B1 and B2 receptor function. Hypertension 55, 214-220
    • (2010) Hypertension , vol.55 , pp. 214-220
    • Erdös, E.G.1    Tan, F.2    Skidgel, R.A.3
  • 26
    • 78751635214 scopus 로고    scopus 로고
    • Renin-angiotensin-aldosterone blockade for cardiovascular disease prevention
    • Vijayaraghavan, K., and Deedwania, P. (2011) Renin-angiotensin- aldosterone blockade for cardiovascular disease prevention. Cardiol. Clin. 29, 137-156
    • (2011) Cardiol. Clin. , vol.29 , pp. 137-156
    • Vijayaraghavan, K.1    Deedwania, P.2
  • 29
    • 84876578009 scopus 로고    scopus 로고
    • CarboxypeptidaseMaugments kinin B1 receptor signaling by conformational crosstalk and enhances endothelial nitric oxide output
    • Zhang, X., Tan, F., Brovkovych, V., Zhang, Y., Lowry, J. L., and Skidgel, R. A. (2013) CarboxypeptidaseMaugments kinin B1 receptor signaling by conformational crosstalk and enhances endothelial nitric oxide output. Biol. Chem. 394, 335-345
    • (2013) Biol. Chem. , vol.394 , pp. 335-345
    • Zhang, X.1    Tan, F.2    Brovkovych, V.3    Zhang, Y.4    Lowry, J.L.5    Skidgel, R.A.6
  • 30
    • 0029083169 scopus 로고
    • Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M
    • McGwire, G. B., and Skidgel, R. A. (1995) Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M. J. Biol. Chem. 270, 17154-17158
    • (1995) J. Biol. Chem. , vol.270 , pp. 17154-17158
    • McGwire, G.B.1    Skidgel, R.A.2
  • 31
  • 32
    • 0037686694 scopus 로고    scopus 로고
    • Kininase I-type carboxypeptidases enhance nitric oxide production in endothelial cells by generating bradykinin B1 receptor agonists
    • Sangsree, S., Brovkovych, V., Minshall, R. D., and Skidgel, R. A. (2003) Kininase I-type carboxypeptidases enhance nitric oxide production in endothelial cells by generating bradykinin B1 receptor agonists. Am. J. Physiol. Heart Circ. Physiol. 284, H1959-H1968
    • (2003) Am. J. Physiol. Heart Circ. Physiol. , vol.284
    • Sangsree, S.1    Brovkovych, V.2    Minshall, R.D.3    Skidgel, R.A.4
  • 33
    • 0032481259 scopus 로고    scopus 로고
    • B1 bradykinin receptors and carboxypeptidase M are both upregulated in the aorta of pigs after LPS infusion
    • Schremmer-Danninger, E., Offner, A., Siebeck, M., and Roscher, A. A. (1998) B1 bradykinin receptors and carboxypeptidase M are both upregulated in the aorta of pigs after LPS infusion. Biochem. Biophys. Res. Commun. 243, 246-252
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 246-252
    • Schremmer-Danninger, E.1    Offner, A.2    Siebeck, M.3    Roscher, A.A.4
  • 34
    • 43149085551 scopus 로고    scopus 로고
    • Carboxypeptidase M and kinin B1 receptors interact to facilitate efficient B1 signaling from B2 agonists
    • Zhang, X., Tan, F., Zhang, Y., and Skidgel, R. A. (2008) Carboxypeptidase M and kinin B1 receptors interact to facilitate efficient B1 signaling from B2 agonists. J. Biol. Chem. 283, 7994-8004
    • (2008) J. Biol. Chem. , vol.283 , pp. 7994-8004
    • Zhang, X.1    Tan, F.2    Zhang, Y.3    Skidgel, R.A.4
  • 35
    • 79956318380 scopus 로고    scopus 로고
    • Cross-talk between carboxypeptidaseMand the kinin B1 receptor mediates a new mode of G protein-coupled receptor signaling
    • Zhang, X., Tan, F., Brovkovych, V., Zhang, Y., and Skidgel, R. A. (2011) Cross-talk between carboxypeptidaseMand the kinin B1 receptor mediates a new mode of G protein-coupled receptor signaling. J. Biol. Chem. 286, 18547-18561
    • (2011) J. Biol. Chem. , vol.286 , pp. 18547-18561
    • Zhang, X.1    Tan, F.2    Brovkovych, V.3    Zhang, Y.4    Skidgel, R.A.5
  • 36
    • 84872024032 scopus 로고    scopus 로고
    • Emerging opportunities for allosteric modulation of G-protein coupled receptors
    • Wang, C. I., and Lewis, R. J. (2013) Emerging opportunities for allosteric modulation of G-protein coupled receptors. Biochem. Pharmacol. 85, 153-162
    • (2013) Biochem. Pharmacol. , vol.85 , pp. 153-162
    • Wang, C.I.1    Lewis, R.J.2
  • 37
    • 69649097791 scopus 로고    scopus 로고
    • 7TM receptor allostery. Putting numbers to shapeshifting proteins
    • Kenakin, T. P. (2009) 7TM receptor allostery. Putting numbers to shapeshifting proteins. Trends Pharmacol. Sci. 30, 460-469
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 460-469
    • Kenakin, T.P.1
  • 39
    • 0037335653 scopus 로고    scopus 로고
    • Effect of mutation of two critical glutamic acid residues on the activity and stability of human carboxypeptidase M and characterization of its signal for glycosylphosphatidylinositol anchoring
    • Tan, F., Balsitis, S., Black, J. K., Blöchl, A., Mao, J. F., Becker, R. P., Schacht, D., and Skidgel, R. A. (2003) Effect of mutation of two critical glutamic acid residues on the activity and stability of human carboxypeptidase M and characterization of its signal for glycosylphosphatidylinositol anchoring. Biochem. J. 370, 567-578
    • (2003) Biochem. J. , vol.370 , pp. 567-578
    • Tan, F.1    Balsitis, S.2    Black, J.K.3    Blöchl, A.4    Mao, J.F.5    Becker, R.P.6    Schacht, D.7    Skidgel, R.A.8
  • 40
    • 0034717151 scopus 로고    scopus 로고
    • Replacement of the transmembrane anchor in angiotensin I-converting enzyme (ACE) with a glycosylphosphatidylinositol tail affects activation of the B2 bradykinin receptor by ACE inhibitors
    • Marcic, B., Deddish, P. A., Skidgel, R. A., Erdös, E. G., Minshall, R. D., and Tan, F. (2000) Replacement of the transmembrane anchor in angiotensin I-converting enzyme (ACE) with a glycosylphosphatidylinositol tail affects activation of the B2 bradykinin receptor by ACE inhibitors. J. Biol. Chem. 275, 16110-16118
    • (2000) J. Biol. Chem. , vol.275 , pp. 16110-16118
    • Marcic, B.1    Deddish, P.A.2    Skidgel, R.A.3    Erdös, E.G.4    Minshall, R.D.5    Tan, F.6
  • 41
    • 3843130785 scopus 로고    scopus 로고
    • Mutation of tyrosine in the conserved NPXXY sequence leads to constitutive phosphorylation and internalization, but not signaling, of the human B2 bradykinin receptor
    • Kalatskaya, I., Schüssler, S., Blaukat, A., Müller-Esterl, W., Jochum, M., Proud, D., and Faussner, A. (2004) Mutation of tyrosine in the conserved NPXXY sequence leads to constitutive phosphorylation and internalization, but not signaling, of the human B2 bradykinin receptor. J. Biol. Chem. 279, 31268-31276
    • (2004) J. Biol. Chem. , vol.279 , pp. 31268-31276
    • Kalatskaya, I.1    Schüssler, S.2    Blaukat, A.3    Müller-Esterl, W.4    Jochum, M.5    Proud, D.6    Faussner, A.7
  • 42
    • 34250637175 scopus 로고    scopus 로고
    • Bioluminescence resonance energy transfer (BRET) for the real-time detection of proteinprotein interactions
    • Pfleger, K. D., Seeber, R. M., and Eidne, K. A. (2006) Bioluminescence resonance energy transfer (BRET) for the real-time detection of proteinprotein interactions. Nat. Protoc. 1, 337-345
    • (2006) Nat. Protoc. , vol.1 , pp. 337-345
    • Pfleger, K.D.1    Seeber, R.M.2    Eidne, K.A.3
  • 43
    • 0024473762 scopus 로고
    • Enhanced Co2 activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase)
    • Deddish, P. A., Skidgel, R. A., and Erdös, E. G. (1989) Enhanced Co2 activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase). Biochem. J. 261, 289-291
    • (1989) Biochem. J. , vol.261 , pp. 289-291
    • Deddish, P.A.1    Skidgel, R.A.2    Erdös, E.G.3
  • 44
    • 0035937808 scopus 로고    scopus 로고
    • The human B1 bradykinin receptor exhibits high ligand-independent, constitutive activity. Roles of residues in the fourth intracellular and third transmembrane domains
    • Leeb-Lundberg, L. M., Kang, D. S., Lamb, M. E., and Fathy, D. B. (2001) The human B1 bradykinin receptor exhibits high ligand-independent, constitutive activity. Roles of residues in the fourth intracellular and third transmembrane domains. J. Biol. Chem. 276, 8785-8792
    • (2001) J. Biol. Chem. , vol.276 , pp. 8785-8792
    • Leeb-Lundberg, L.M.1    Kang, D.S.2    Lamb, M.E.3    Fathy, D.B.4
  • 45
    • 0030713420 scopus 로고    scopus 로고
    • Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains
    • Tan, F., Rehli, M., Krause, S. W., and Skidgel, R. A. (1997) Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains. Biochem. J. 327, 81-87
    • (1997) Biochem. J. , vol.327 , pp. 81-87
    • Tan, F.1    Rehli, M.2    Krause, S.W.3    Skidgel, R.A.4
  • 46
    • 0035844274 scopus 로고    scopus 로고
    • The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases
    • Aloy, P., Companys, V., Vendrell, J., Aviles, F. X., Fricker, L. D., Coll, M., and Gomis-Rüth, F. X. (2001) The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases. J. Biol. Chem. 276, 16177-16184
    • (2001) J. Biol. Chem. , vol.276 , pp. 16177-16184
    • Aloy, P.1    Companys, V.2    Vendrell, J.3    Aviles, F.X.4    Fricker, L.D.5    Coll, M.6    Gomis-Rüth, F.X.7
  • 47
    • 0032478636 scopus 로고    scopus 로고
    • Gp180, a protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activity
    • Eng, F. J., Novikova, E. G., Kuroki, K., Ganem, D., and Fricker, L. D. (1998) gp180, a protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activity. J. Biol. Chem. 273, 8382-8388
    • (1998) J. Biol. Chem. , vol.273 , pp. 8382-8388
    • Eng, F.J.1    Novikova, E.G.2    Kuroki, K.3    Ganem, D.4    Fricker, L.D.5
  • 50
    • 34548476934 scopus 로고    scopus 로고
    • Critical role for the second extracellular loop in the binding of both orthosteric and allosteric G protein-coupled receptor ligands
    • Avlani, V. A., Gregory, K. J., Morton, C. J., Parker, M. W., Sexton, P. M., and Christopoulos, A. (2007) Critical role for the second extracellular loop in the binding of both orthosteric and allosteric G protein-coupled receptor ligands. J. Biol. Chem. 282, 25677-25686
    • (2007) J. Biol. Chem. , vol.282 , pp. 25677-25686
    • Avlani, V.A.1    Gregory, K.J.2    Morton, C.J.3    Parker, M.W.4    Sexton, P.M.5    Christopoulos, A.6
  • 51
    • 84856511452 scopus 로고    scopus 로고
    • Domain coupling in GPCRs. The engine for induced conformational changes
    • Unal, H., and Karnik, S. S. (2012) Domain coupling in GPCRs. The engine for induced conformational changes. Trends Pharmacol. Sci. 33, 79-88
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 79-88
    • Unal, H.1    Karnik, S.S.2
  • 52
    • 0021683271 scopus 로고
    • Hydrolysis of opioid hexapeptides by carboxypeptidase N. Presence of carboxypeptidase in cell membranes
    • Skidgel, R. A., Johnson, A. R., and Erdös, E. G. (1984) Hydrolysis of opioid hexapeptides by carboxypeptidase N. Presence of carboxypeptidase in cell membranes. Biochem. Pharmacol. 33, 3471-3478
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 3471-3478
    • Skidgel, R.A.1    Johnson, A.R.2    Erdös, E.G.3
  • 53
    • 79951958713 scopus 로고    scopus 로고
    • Strategies for the identification of allosteric modulators of G-protein-coupled receptors
    • Burford, N. T., Watson, J., Bertekap, R., and Alt, A. (2011) Strategies for the identification of allosteric modulators of G-protein-coupled receptors. Biochem. Pharmacol. 81, 691-702
    • (2011) Biochem. Pharmacol. , vol.81 , pp. 691-702
    • Burford, N.T.1    Watson, J.2    Bertekap, R.3    Alt, A.4
  • 56
    • 33646052569 scopus 로고    scopus 로고
    • FRET-based monitoring of conformational change of the β2 adrenergic receptor in living cells
    • Nakanishi, J., Takarada, T., Yunoki, S., Kikuchi, Y., and Maeda, M. (2006) FRET-based monitoring of conformational change of the β2 adrenergic receptor in living cells. Biochem. Biophys. Res. Commun. 343, 1191-1196
    • (2006) Biochem. Biophys. Res. Commun. , vol.343 , pp. 1191-1196
    • Nakanishi, J.1    Takarada, T.2    Yunoki, S.3    Kikuchi, Y.4    Maeda, M.5
  • 59
    • 78650147139 scopus 로고    scopus 로고
    • Allostery at G protein-coupled receptor homo- and heteromers. Uncharted pharmacological landscapes
    • Smith, N. J., and Milligan, G. (2010) Allostery at G protein-coupled receptor homo- and heteromers. Uncharted pharmacological landscapes. Pharmacol. Rev. 62, 701-725
    • (2010) Pharmacol. Rev. , vol.62 , pp. 701-725
    • Smith, N.J.1    Milligan, G.2
  • 60
    • 58149193205 scopus 로고    scopus 로고
    • Allosteric modulators of GPCRs. A novel approach for the treatment of CNS disorders
    • Conn, P. J., Christopoulos, A., and Lindsley, C. W. (2009) Allosteric modulators of GPCRs. A novel approach for the treatment of CNS disorders. Nat. Rev. Drug Discov. 8, 41-54
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 41-54
    • Conn, P.J.1    Christopoulos, A.2    Lindsley, C.W.3
  • 61
    • 70450263435 scopus 로고    scopus 로고
    • Fine-tuning of GPCR activity by receptor- interacting proteins
    • Ritter, S. L., and Hall, R. A. (2009) Fine-tuning of GPCR activity by receptor- interacting proteins. Nat. Rev. Mol. Cell Biol. 10, 819-830
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 819-830
    • Ritter, S.L.1    Hall, R.A.2
  • 64
    • 84863740185 scopus 로고    scopus 로고
    • Mechanism of GPCRdirected autoantibodies in diseases
    • Unal, H., Jagannathan, R., and Karnik, S. S. (2012) Mechanism of GPCRdirected autoantibodies in diseases. Adv. Exp. Med. Biol. 749, 187-199
    • (2012) Adv. Exp. Med. Biol. , vol.749 , pp. 187-199
    • Unal, H.1    Jagannathan, R.2    Karnik, S.S.3
  • 65
    • 18744402177 scopus 로고    scopus 로고
    • Essential role for the second extracellular loop in C5a receptor activation
    • Klco, J. M., Wiegand, C. B., Narzinski, K., and Baranski, T. J. (2005) Essential role for the second extracellular loop in C5a receptor activation. Nat. Struct. Mol. Biol. 12, 320-326
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 320-326
    • Klco, J.M.1    Wiegand, C.B.2    Narzinski, K.3    Baranski, T.J.4
  • 66
    • 66649088302 scopus 로고    scopus 로고
    • Gene deletion of the kinin receptor B1 attenuates cardiac inflammation and fibrosis during the development of experimental diabetic cardiomyopathy
    • Westermann, D., Walther, T., Savvatis, K., Escher, F., Sobirey, M., Riad, A., Bader, M., Schultheiss, H. P., and Tschöpe, C. (2009) Gene deletion of the kinin receptor B1 attenuates cardiac inflammation and fibrosis during the development of experimental diabetic cardiomyopathy. Diabetes 58, 1373-1381
    • (2009) Diabetes , vol.58 , pp. 1373-1381
    • Westermann, D.1    Walther, T.2    Savvatis, K.3    Escher, F.4    Sobirey, M.5    Riad, A.6    Bader, M.7    Schultheiss, H.P.8    Tschöpe, C.9
  • 67
    • 32344447153 scopus 로고    scopus 로고
    • Genetically altered animal models in the kallikrein-kinin system
    • Pesquero, J. B., and Bader, M. (2006) Genetically altered animal models in the kallikrein-kinin system. Biol. Chem. 387, 119-126
    • (2006) Biol. Chem. , vol.387 , pp. 119-126
    • Pesquero, J.B.1    Bader, M.2
  • 68
    • 34250654947 scopus 로고    scopus 로고
    • Bradykinin B1 and B2 receptors both have protective roles in renal ischemia/ reperfusion injury
    • Kakoki, M., McGarrah, R. W., Kim, H. S., and Smithies, O. (2007) Bradykinin B1 and B2 receptors both have protective roles in renal ischemia/ reperfusion injury. Proc. Natl. Acad. Sci. U.S.A. 104, 7576-7581
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7576-7581
    • Kakoki, M.1    McGarrah, R.W.2    Kim, H.S.3    Smithies, O.4
  • 69
    • 32344438274 scopus 로고    scopus 로고
    • The role of bradykinin B1 receptor on cardiac remodeling in stroke-prone spontaneously hypertensive rats (SHR-SP)
    • Moniwa, N., Agata, J., Hagiwara, M., Ura, N., and Shimamoto, K. (2006) The role of bradykinin B1 receptor on cardiac remodeling in stroke-prone spontaneously hypertensive rats (SHR-SP). Biol. Chem. 387, 203-209
    • (2006) Biol. Chem. , vol.387 , pp. 203-209
    • Moniwa, N.1    Agata, J.2    Hagiwara, M.3    Ura, N.4    Shimamoto, K.5
  • 70
  • 72
    • 42349110618 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme inhibition after experimental myocardial infarct. Role of the kinin B1 and B2 receptors
    • Duka, A., Kintsurashvili, E., Duka, I., Ona, D., Hopkins, T. A., Bader, M., Gavras, I., and Gavras, H. (2008) Angiotensin-converting enzyme inhibition after experimental myocardial infarct. Role of the kinin B1 and B2 receptors. Hypertension 51, 1352-1357
    • (2008) Hypertension , vol.51 , pp. 1352-1357
    • Duka, A.1    Kintsurashvili, E.2    Duka, I.3    Ona, D.4    Hopkins, T.A.5    Bader, M.6    Gavras, I.7    Gavras, H.8
  • 73
    • 60349086455 scopus 로고    scopus 로고
    • The kinin B1 receptor contributes to the cardioprotective effect of angiotensin-converting enzyme inhibitors and angiotensin receptor blockers in mice
    • Xu, J., Carretero, O. A., Shesely, E. G., Rhaleb, N. E., Yang, J. J., Bader, M., and Yang, X. P. (2009) The kinin B1 receptor contributes to the cardioprotective effect of angiotensin-converting enzyme inhibitors and angiotensin receptor blockers in mice. Exp. Physiol. 94, 322-329
    • (2009) Exp. Physiol. , vol.94 , pp. 322-329
    • Xu, J.1    Carretero, O.A.2    Shesely, E.G.3    Rhaleb, N.E.4    Yang, J.J.5    Bader, M.6    Yang, X.P.7
  • 74
    • 0037053405 scopus 로고    scopus 로고
    • Novel mode of action of angiotensin i converting enzyme inhibitors. Direct activation of bradykinin B1 receptor
    • Ignjatovic, T., Tan, F., Brovkovych, V., Skidgel, R. A., and Erdös, E. G. (2002) Novel mode of action of angiotensin I converting enzyme inhibitors. Direct activation of bradykinin B1 receptor. J. Biol. Chem. 277, 16847-16852
    • (2002) J. Biol. Chem. , vol.277 , pp. 16847-16852
    • Ignjatovic, T.1    Tan, F.2    Brovkovych, V.3    Skidgel, R.A.4    Erdös, E.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.