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Volumn 204, Issue 3, 2014, Pages 377-393

A G protein-coupled receptor and the intracellular synthase of its agonist functionally cooperate

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; HEAT SHOCK PROTEIN 90; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROSTAGLANDIN D SYNTHASE; PROSTAGLANDIN D2 SYNTHASE; SYNTHETASE; TRANSCRIPTION FACTOR DP1; UNCLASSIFIED DRUG;

EID: 84893490892     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201304015     Document Type: Article
Times cited : (21)

References (64)
  • 1
    • 79961074094 scopus 로고    scopus 로고
    • G protein coupled receptor kinases as therapeutic targets in cardiovascular disease
    • Belmonte, S.L., and B.C. Blaxall. 2011. G protein coupled receptor kinases as therapeutic targets in cardiovascular disease. Circ. Res. 109:309-319. http://dx.doi.org/10.1161/CIRCRESAHA.110.231233
    • (2011) Circ. Res. , vol.109 , pp. 309-319
    • Belmonte, S.L.1    Blaxall, B.C.2
  • 2
    • 0037205411 scopus 로고    scopus 로고
    • Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70. Hop. Hsp90 complexes
    • Brinker, A., C. Scheufler, F. Von Der Mulbe, B. Fleckenstein, C. Herrmann, G. Jung, I. Moarefi, and F.U. Hartl. 2002. Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70. Hop. Hsp90 complexes. J. Biol. Chem. 277:19265-19275. http://dx.doi.org/10.1074/jbc. M109002200
    • (2002) J. Biol. Chem. , vol.277 , pp. 19265-19275
    • Brinker, A.1    Scheufler, C.2    Von Der Mulbe, F.3    Fleckenstein, B.4    Herrmann, C.5    Jung, G.6    Moarefi, I.7    Hartl, F.U.8
  • 3
    • 80054027590 scopus 로고    scopus 로고
    • WDR36 acts as a scaffold protein tethering a G-protein-coupled receptor, Gαq and phospholipase Cβ in a signalling complex
    • Cartier, A., A. Parent, P. Labrecque, G. Laroche, and J.L. Parent. 2011. WDR36 acts as a scaffold protein tethering a G-protein-coupled receptor, Gαq and phospholipase Cβ in a signalling complex. J. Cell Sci. 124:3292-3304. http://dx.doi.org/10.1242/jcs.085795
    • (2011) J. Cell Sci. , vol.124 , pp. 3292-3304
    • Cartier, A.1    Parent, A.2    Labrecque, P.3    Laroche, G.4    Parent, J.L.5
  • 4
    • 33746588172 scopus 로고    scopus 로고
    • The Hsp90 chaperone complex regulates GDI-dependent Rab recycling
    • Chen, C.Y., and W.E. Balch. 2006. The Hsp90 chaperone complex regulates GDI-dependent Rab recycling. Mol. Biol. Cell. 17:3494-3507. http://dx.doi.org/10.1091/mbc. E05-12-1096
    • (2006) Mol. Biol. Cell. , vol.17 , pp. 3494-3507
    • Chen, C.Y.1    Balch, W.E.2
  • 5
  • 6
    • 33644841233 scopus 로고    scopus 로고
    • Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90
    • Cliff, M.J., R. Harris, D. Barford, J.E. Ladbury, and M.A. Williams. 2006. Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90. Structure. 14:415-426. http://dx.doi.org/10.1016/j.str.2005.12.009
    • (2006) Structure. , vol.14 , pp. 415-426
    • Cliff, M.J.1    Harris, R.2    Barford, D.3    Ladbury, J.E.4    Williams, M.A.5
  • 7
    • 34748871331 scopus 로고    scopus 로고
    • G protein-coupled receptor trafficking in health and disease: lessons learned to prepare for therapeutic mutant rescue in vivo
    • Conn, P.M., A. Ulloa-Aguirre, J. Ito, and J.A. Janovick. 2007. G protein-coupled receptor trafficking in health and disease: lessons learned to prepare for therapeutic mutant rescue in vivo. Pharmacol. Rev. 59:225-250. http://dx.doi.org/10.1124/pr.59.3.2
    • (2007) Pharmacol. Rev. , vol.59 , pp. 225-250
    • Conn, P.M.1    Ulloa-Aguirre, A.2    Ito, J.3    Janovick, J.A.4
  • 8
    • 57349129484 scopus 로고    scopus 로고
    • Cell surface targeting of mu-delta opioid receptor heterodimers by RTP4
    • Décaillot, F.M., R. Rozenfeld, A. Gupta, and L.A. Devi. 2008. Cell surface targeting of mu-delta opioid receptor heterodimers by RTP4. Proc. Natl. Acad. Sci. USA. 105:16045-16050. http://dx.doi.org/10.1073/pnas.0804106105
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 16045-16050
    • Décaillot, F.M.1    Rozenfeld, R.2    Gupta, A.3    Devi, L.A.4
  • 9
    • 46249090619 scopus 로고    scopus 로고
    • Prostaglandin D2 receptors control osteoclastogenesis and the activity of human osteoclasts
    • Durand, M., M.A. Gallant, and A.J. de Brum-Fernandes. 2008. Prostaglandin D2 receptors control osteoclastogenesis and the activity of human osteoclasts. J. Bone Miner. Res. 23:1097-1105. http://dx.doi.org/10.1359/jbmr.080228
    • (2008) J. Bone Miner. Res. , vol.23 , pp. 1097-1105
    • Durand, M.1    Gallant, M.A.2    de Brum-Fernandes, A.J.3
  • 10
    • 78650943372 scopus 로고    scopus 로고
    • Modulation of α(2C) adrenergic receptor temperature-sensitive trafficking by HSP90
    • Filipeanu, C.M., R. de Vries, A.H. Danser, and D.R. Kapusta. 2011. Modulation of α(2C) adrenergic receptor temperature-sensitive trafficking by HSP90. Biochim. Biophys. Acta. 1813:346-357. http://dx.doi.org/10.1016/j.bbamcr.2010.11.020
    • (2011) Biochim. Biophys. Acta. , vol.1813 , pp. 346-357
    • Filipeanu, C.M.1    de Vries, R.2    Danser, A.H.3    Kapusta, D.R.4
  • 11
    • 0034704138 scopus 로고    scopus 로고
    • Transcriptional activation of the human hematopoietic prostaglandin D synthase gene in megakaryoblastic cells. Roles of the oct-1 element in the 5'-flanking region and the AP-2 element in the untranslated exon 1
    • Fujimori, K., Y. Kanaoka, Y. Sakaguchi, and Y. Urade. 2000. Transcriptional activation of the human hematopoietic prostaglandin D synthase gene in megakaryoblastic cells. Roles of the oct-1 element in the 5'-flanking region and the AP-2 element in the untranslated exon 1. J. Biol. Chem. 275:40511-40516. http://dx.doi.org/10.1074/jbc. M007688200
    • (2000) J. Biol. Chem. , vol.275 , pp. 40511-40516
    • Fujimori, K.1    Kanaoka, Y.2    Sakaguchi, Y.3    Urade, Y.4
  • 12
    • 15344348453 scopus 로고    scopus 로고
    • Production of prostaglandin D(2) by human osteoblasts and modulation of osteoprotegerin, RANKL, and cellular migration by DP and CRTH2 receptors
    • Gallant, M.A., R. Samadfam, J.A. Hackett, J. Antoniou, J.L. Parent, and A.J. de Brum-Fernandes. 2005. Production of prostaglandin D(2) by human osteoblasts and modulation of osteoprotegerin, RANKL, and cellular migration by DP and CRTH2 receptors. J. Bone Miner. Res. 20:672-681. http://dx.doi.org/10.1359/JBMR.041211
    • (2005) J. Bone Miner. Res. , vol.20 , pp. 672-681
    • Gallant, M.A.1    Samadfam, R.2    Hackett, J.A.3    Antoniou, J.4    Parent, J.L.5    de Brum-Fernandes, A.J.6
  • 13
    • 33846849199 scopus 로고    scopus 로고
    • Differential regulation of the signaling and trafficking of the two prostaglandin D2 receptors, prostanoid DP receptor and CRTH2
    • Gallant, M.A., D. Slipetz, E. Hamelin, M.D. Rochdi, S. Talbot, A.J. de Brum-Fernandes, and J.L. Parent. 2007. Differential regulation of the signaling and trafficking of the two prostaglandin D2 receptors, prostanoid DP receptor and CRTH2. Eur. J. Pharmacol. 557:115-123. http://dx.doi.org/10.1016/j.ejphar.2006.11.058
    • (2007) Eur. J. Pharmacol. , vol.557 , pp. 115-123
    • Gallant, M.A.1    Slipetz, D.2    Hamelin, E.3    Rochdi, M.D.4    Talbot, S.5    de Brum-Fernandes, A.J.6    Parent, J.L.7
  • 17
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F.U., A. Bracher, and M. Hayer-Hartl. 2011. Molecular chaperones in protein folding and proteostasis. Nature. 475:324-332. http://dx.doi.org/10.1038/nature10317
    • (2011) Nature. , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 18
    • 35549009435 scopus 로고    scopus 로고
    • Involvement of the 90-kDa heat shock protein (Hsp-90) in CB2 cannabinoid receptor-mediated cell migration: a new role of Hsp-90 in migration signaling of a G protein-coupled receptor
    • He, F., Z.H. Qiao, J. Cai, W. Pierce, D.C. He, and Z.H. Song. 2007. Involvement of the 90-kDa heat shock protein (Hsp-90) in CB2 cannabinoid receptor-mediated cell migration: a new role of Hsp-90 in migration signaling of a G protein-coupled receptor. Mol. Pharmacol. 72:1289-1300. http://dx.doi.org/10.1124/mol.107.036566
    • (2007) Mol. Pharmacol. , vol.72 , pp. 1289-1300
    • He, F.1    Qiao, Z.H.2    Cai, J.3    Pierce, W.4    He, D.C.5    Song, Z.H.6
  • 19
    • 84867348947 scopus 로고    scopus 로고
    • Prostanoids as regulators of innate and adaptive immunity
    • Hirata, T., and S. Narumiya. 2012. Prostanoids as regulators of innate and adaptive immunity. Adv. Immunol. 116:143-174. http://dx.doi.org/10.1016/B978-0-12-394300-2.00005-3
    • (2012) Adv. Immunol. , vol.116 , pp. 143-174
    • Hirata, T.1    Narumiya, S.2
  • 21
    • 0842299122 scopus 로고    scopus 로고
    • Proteasomes and molecular chaperones: cellular machinery responsible for folding and destruction of unfolded proteins
    • Imai, J., H. Yashiroda, M. Maruya, I. Yahara, and K. Tanaka. 2003. Proteasomes and molecular chaperones: cellular machinery responsible for folding and destruction of unfolded proteins. Cell Cycle. 2:584-590. http://dx.doi.org/10.4161/cc.2.6.586
    • (2003) Cell Cycle. , vol.2 , pp. 584-590
    • Imai, J.1    Yashiroda, H.2    Maruya, M.3    Yahara, I.4    Tanaka, K.5
  • 22
    • 84874506372 scopus 로고    scopus 로고
    • Hsp90: structure and function
    • Jackson, S.E. 2013. Hsp90: structure and function. Top. Curr. Chem. 328: 155-240. http://dx.doi.org/10.1007/128_2012_356
    • (2013) Top. Curr. Chem. , vol.328 , pp. 155-240
    • Jackson, S.E.1
  • 24
    • 84856323688 scopus 로고    scopus 로고
    • Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation
    • Kriegenburg, F., L. Ellgaard, and R. Hartmann-Petersen. 2012. Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation. FEBS J. 279:532-542. http://dx.doi.org/10.1111/j.1742-4658.2011.08456.x
    • (2012) FEBS J. , vol.279 , pp. 532-542
    • Kriegenburg, F.1    Ellgaard, L.2    Hartmann-Petersen, R.3
  • 25
    • 69249089709 scopus 로고    scopus 로고
    • Structural basis of the catalytic mechanism operating in open-closed conformers of lipocalin type prostaglandin D synthase
    • Kumasaka, T., K. Aritake, H. Ago, D. Irikura, T. Tsurumura, M. Yamamoto, M. Miyano, Y. Urade, and O. Hayaishi. 2009. Structural basis of the catalytic mechanism operating in open-closed conformers of lipocalin type prostaglandin D synthase. J. Biol. Chem. 284:22344-22352. http://dx.doi.org/10.1074/jbc. M109.018341
    • (2009) J. Biol. Chem. , vol.284 , pp. 22344-22352
    • Kumasaka, T.1    Aritake, K.2    Ago, H.3    Irikura, D.4    Tsurumura, T.5    Yamamoto, M.6    Miyano, M.7    Urade, Y.8    Hayaishi, O.9
  • 26
    • 84878821413 scopus 로고    scopus 로고
    • Inverse agonist and pharmacochaperone properties of MK-0524 on the prostanoid DP1 receptor
    • Labrecque, P., S.J. Roy, L. Fréchette, C. Iorio-Morin, M.A. Gallant, and J.L. Parent. 2013. Inverse agonist and pharmacochaperone properties of MK-0524 on the prostanoid DP1 receptor. PLoS ONE. 8:e65767. http://dx.doi.org/10.1371/journal.pone.0065767
    • (2013) PLoS ONE. , vol.8
    • Labrecque, P.1    Roy, S.J.2    Fréchette, L.3    Iorio-Morin, C.4    Gallant, M.A.5    Parent, J.L.6
  • 27
    • 81755189074 scopus 로고    scopus 로고
    • Regulation of β2-adrenergic receptor maturation and anterograde trafficking by an interaction with Rab geranylgeranyltransferase: modulation of Rab geranylgeranylation by the receptor
    • Lachance, V., A. Cartier, S. Génier, S. Munger, P. Germain, P. Labrecque, and J.L. Parent. 2011. Regulation of β2-adrenergic receptor maturation and anterograde trafficking by an interaction with Rab geranylgeranyltransferase: modulation of Rab geranylgeranylation by the receptor. J. Biol. Chem. 286:40802-40813. http://dx.doi.org/10.1074/jbc. M111.267815
    • (2011) J. Biol. Chem. , vol.286 , pp. 40802-40813
    • Lachance, V.1    Cartier, A.2    Génier, S.3    Munger, S.4    Germain, P.5    Labrecque, P.6    Parent, J.L.7
  • 28
    • 84858122979 scopus 로고    scopus 로고
    • GPCRs and cancer
    • Lappano, R., and M. Maggiolini. 2012. GPCRs and cancer. Acta Pharmacol. Sin. 33:351-362. http://dx.doi.org/10.1038/aps.2011.183
    • (2012) Acta Pharmacol. Sin. , vol.33 , pp. 351-362
    • Lappano, R.1    Maggiolini, M.2
  • 29
    • 84867710042 scopus 로고    scopus 로고
    • G protein-coupled receptors in the spotlight, [In French.]
    • Lebon, G., and C.G. Tate. 2012. G protein-coupled receptors in the spotlight. [In French.] Med. Sci. (Paris). 28:876-882. http://dx.doi.org/10.1051/medsci/20122810017
    • (2012) Med. Sci. (Paris). , vol.28 , pp. 876-882
    • Lebon, G.1    Tate, C.G.2
  • 30
    • 34548159460 scopus 로고    scopus 로고
    • Opioid receptor pharmacological chaperones act by binding and stabilizing newly synthesized receptors in the endoplasmic reticulum
    • Leskelä, T.T., P.M. Markkanen, E.M. Pietilä, J.T. Tuusa, and U.E. Petäjä-Repo. 2007. Opioid receptor pharmacological chaperones act by binding and stabilizing newly synthesized receptors in the endoplasmic reticulum. J. Biol. Chem. 282:23171-23183. http://dx.doi.org/10.1074/jbc. M610896200
    • (2007) J. Biol. Chem. , vol.282 , pp. 23171-23183
    • Leskelä, T.T.1    Markkanen, P.M.2    Pietilä, E.M.3    Tuusa, J.T.4    Petäjä-Repo, U.E.5
  • 31
    • 0345803950 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase interaction with Hsp90 mediates kinase maturation
    • Luo, J., and J.L. Benovic. 2003. G protein-coupled receptor kinase interaction with Hsp90 mediates kinase maturation. J. Biol. Chem. 278:50908-50914. http://dx.doi.org/10.1074/jbc. M307637200
    • (2003) J. Biol. Chem. , vol.278 , pp. 50908-50914
    • Luo, J.1    Benovic, J.L.2
  • 32
    • 84857471063 scopus 로고    scopus 로고
    • Regulation of GPCR activity, trafficking and localization by GPCR-interacting proteins
    • Magalhaes, A.C., H. Dunn, and S.S. Ferguson. 2012. Regulation of GPCR activity, trafficking and localization by GPCR-interacting proteins. Br. J. Pharmacol. 165:1717-1736. http://dx.doi.org/10.1111/j.1476-5381.2011.01552.x
    • (2012) Br. J. Pharmacol. , vol.165 , pp. 1717-1736
    • Magalhaes, A.C.1    Dunn, H.2    Ferguson, S.S.3
  • 34
    • 34848926209 scopus 로고    scopus 로고
    • Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches
    • McClellan, A.J., Y. Xia, A.M. Deutschbauer, R.W. Davis, M. Gerstein, and J. Frydman. 2007. Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell. 131:121-135. http://dx.doi.org/10.1016/j.cell.2007.07.036
    • (2007) Cell. , vol.131 , pp. 121-135
    • Mcclellan, A.J.1    Xia, Y.2    Deutschbauer, A.M.3    Davis, R.W.4    Gerstein, M.5    Frydman, J.6
  • 35
    • 74449090243 scopus 로고    scopus 로고
    • Structural analysis of lipocalin-type prostaglandin D synthase complexed with biliverdin by small-angle X-ray scattering and multi-dimensional NMR
    • Miyamoto, Y., S. Nishimura, K. Inoue, S. Shimamoto, T. Yoshida, A. Fukuhara, M. Yamada, Y. Urade, N. Yagi, T. Ohkubo, and T. Inui. 2010. Structural analysis of lipocalin-type prostaglandin D synthase complexed with biliverdin by small-angle X-ray scattering and multi-dimensional NMR. J. Struct. Biol. 169:209-218. http://dx.doi.org/10.1016/j.jsb.2009.10.005
    • (2010) J. Struct. Biol. , vol.169 , pp. 209-218
    • Miyamoto, Y.1    Nishimura, S.2    Inoue, K.3    Shimamoto, S.4    Yoshida, T.5    Fukuhara, A.6    Yamada, M.7    Urade, Y.8    Yagi, N.9    Ohkubo, T.10    Inui, T.11
  • 36
    • 0028969527 scopus 로고
    • Different intracellular locations for prostaglandin endoperoxide H synthase-1 and -2
    • Morita, I., M. Schindler, M.K. Regier, J.C. Otto, T. Hori, D.L. DeWitt, and W.L. Smith. 1995. Different intracellular locations for prostaglandin endoperoxide H synthase-1 and -2. J. Biol. Chem. 270:10902-10908. http://dx.doi.org/10.1074/jbc.270.18.10902
    • (1995) J. Biol. Chem. , vol.270 , pp. 10902-10908
    • Morita, I.1    Schindler, M.2    Regier, M.K.3    Otto, J.C.4    Hori, T.5    Dewitt, D.L.6    Smith, W.L.7
  • 37
    • 0032823306 scopus 로고    scopus 로고
    • Prostanoid receptors: structures, properties, and functions
    • Narumiya, S., Y. Sugimoto, and F. Ushikubi. 1999. Prostanoid receptors: structures, properties, and functions. Physiol. Rev. 79:1193-1226.
    • (1999) Physiol. Rev. , vol.79 , pp. 1193-1226
    • Narumiya, S.1    Sugimoto, Y.2    Ushikubi, F.3
  • 38
    • 59549107791 scopus 로고    scopus 로고
    • Role of prostaglandin D(2) and its receptors in the pathophysiology of asthma
    • Oguma, T., K. Asano, and A. Ishizaka. 2008. Role of prostaglandin D(2) and its receptors in the pathophysiology of asthma. Allergol. Int. 57:307-312. http://dx.doi.org/10.2332/allergolint.08-RAI-0033
    • (2008) Allergol. Int. , vol.57 , pp. 307-312
    • Oguma, T.1    Asano, K.2    Ishizaka, A.3
  • 39
    • 0029860102 scopus 로고    scopus 로고
    • Vasopressin V2 receptor mutants that cause X-linked nephrogenic diabetes insipidus: analysis of expression, processing, and function
    • Oksche, A., R. Schülein, C. Rutz, U. Liebenhoff, J. Dickson, H. Müller, M. Birnbaumer, and W. Rosenthal. 1996. Vasopressin V2 receptor mutants that cause X-linked nephrogenic diabetes insipidus: analysis of expression, processing, and function. Mol. Pharmacol. 50:820-828.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 820-828
    • Oksche, A.1    Schülein, R.2    Rutz, C.3    Liebenhoff, U.4    Dickson, J.5    Müller, H.6    Birnbaumer, M.7    Rosenthal, W.8
  • 40
    • 0035980107 scopus 로고    scopus 로고
    • Thrombin receptor signaling to cytoskeleton requires Hsp90
    • Pai, K.S., V.B. Mahajan, A. Lau, and D.D. Cunningham. 2001. Thrombin receptor signaling to cytoskeleton requires Hsp90. J. Biol. Chem. 276:32642-32647. http://dx.doi.org/10.1074/jbc. M104212200
    • (2001) J. Biol. Chem. , vol.276 , pp. 32642-32647
    • Pai, K.S.1    Mahajan, V.B.2    Lau, A.3    Cunningham, D.D.4
  • 41
    • 59849102081 scopus 로고    scopus 로고
    • Rab11 regulates the recycling of the beta2-adrenergic receptor through a direct interaction
    • Parent, A., E. Hamelin, P. Germain, and J.L. Parent. 2009. Rab11 regulates the recycling of the beta2-adrenergic receptor through a direct interaction. Biochem. J. 418:163-172. http://dx.doi.org/10.1042/BJ20080867
    • (2009) Biochem. J. , vol.418 , pp. 163-172
    • Parent, A.1    Hamelin, E.2    Germain, P.3    Parent, J.L.4
  • 43
    • 0037007201 scopus 로고    scopus 로고
    • Ligands act as pharmacological chaperones and increase the efficiency of delta opioid receptor maturation
    • Petäjä-Repo, U.E., M. Hogue, S. Bhalla, A. Laperrière, J.P. Morello, and M. Bouvier. 2002. Ligands act as pharmacological chaperones and increase the efficiency of delta opioid receptor maturation. EMBO J. 21:1628-1637. http://dx.doi.org/10.1093/emboj/21.7.1628
    • (2002) EMBO J. , vol.21 , pp. 1628-1637
    • Petäjä-Repo, U.E.1    Hogue, M.2    Bhalla, S.3    Laperrière, A.4    Morello, J.P.5    Bouvier, M.6
  • 44
    • 84869065405 scopus 로고    scopus 로고
    • Design principles of protein biosynthesis-coupled quality control
    • Rodrigo-Brenni, M.C., and R.S. Hegde. 2012. Design principles of protein biosynthesis-coupled quality control. Dev. Cell. 23:896-907. http://dx.doi.org/10.1016/j.devcel.2012.10.012
    • (2012) Dev. Cell. , vol.23 , pp. 896-907
    • Rodrigo-Brenni, M.C.1    . Hegde, R.2
  • 47
    • 0037110754 scopus 로고    scopus 로고
    • RabalphaGDI activity is regulated by a Hsp90 chaperone complex
    • Sakisaka, T., T. Meerlo, J. Matteson, H. Plutner, and W.E. Balch. 2002. RabalphaGDI activity is regulated by a Hsp90 chaperone complex. EMBO J. 21:6125-6135. http://dx.doi.org/10.1093/emboj/cdf603
    • (2002) EMBO J. , vol.21 , pp. 6125-6135
    • Sakisaka, T.1    Meerlo, T.2    Matteson, J.3    Plutner, H.4    Balch, W.E.5
  • 48
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler, C., A. Brinker, G. Bourenkov, S. Pegoraro, L. Moroder, H. Bartunik, F.U. Hartl, and I. Moarefi. 2000. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell. 101:199-210. http://dx.doi.org/10.1016/S0092-8674(00)80830-2
    • (2000) Cell. , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 50
    • 0025159176 scopus 로고
    • A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis
    • Sikorski, R.S., M.S. Boguski, M. Goebl, and P. Hieter. 1990. A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis. Cell. 60:307-317. http://dx.doi.org/10.1016/0092-8674(90)90745-Z
    • (1990) Cell. , vol.60 , pp. 307-317
    • Sikorski, R.S.1    Boguski, M.S.2    Goebl, M.3    Hieter, P.4
  • 51
    • 84858228729 scopus 로고    scopus 로고
    • G protein-coupled receptor signalling in the cardiac nuclear membrane: evidence and possible roles in physiological and pathophysiological function
    • Tadevosyan, A., G. Vaniotis, B.G. Allen, T.E. Hébert, and S. Nattel. 2012. G protein-coupled receptor signalling in the cardiac nuclear membrane: evidence and possible roles in physiological and pathophysiological function. J. Physiol. 590:1313-1330.
    • (2012) J. Physiol. , vol.590 , pp. 1313-1330
    • Tadevosyan, A.1    Vaniotis, G.2    Allen, B.G.3    Hébert, T.E.4    Nattel, S.5
  • 52
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: emerging mechanistic insights
    • Taipale, M., D.F. Jarosz, and S. Lindquist. 2010. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell Biol. 11:515-528. http://dx.doi.org/10.1038/nrm2918
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 53
    • 0034161713 scopus 로고    scopus 로고
    • Cutting edge: differential production of prostaglandin D2 by human helper T cell subsets
    • Tanaka, K., K. Ogawa, K. Sugamura, M. Nakamura, S. Takano, and K. Nagata. 2000. Cutting edge: differential production of prostaglandin D2 by human helper T cell subsets. J. Immunol. 164:2277-2280.
    • (2000) J. Immunol. , vol.164 , pp. 2277-2280
    • Tanaka, K.1    Ogawa, K.2    Sugamura, K.3    Nakamura, M.4    Takano, S.5    Nagata, K.6
  • 54
    • 79551650386 scopus 로고    scopus 로고
    • Pharmacoperones: a new therapeutic approach for diseases caused by misfolded G protein-coupled receptors
    • Ulloa-Aguirre, A., and P. Michael Conn. 2011. Pharmacoperones: a new therapeutic approach for diseases caused by misfolded G protein-coupled receptors. Recent Pat. Endocr. Metab, Immune Drug Discov. 5:13-24. http://dx.doi.org/10.2174/187221411794351851
    • (2011) Recent Pat. Endocr. Metab, Immune Drug Discov. , vol.5 , pp. 13-24
    • Ulloa-Aguirre, A.1    Michael Conn, P.2
  • 55
    • 0034684216 scopus 로고    scopus 로고
    • Biochemical, structural, genetic, physiological, and pathophysiological features of lipocalin-type prostaglandin D synthase
    • Urade, Y., and O. Hayaishi. 2000. Biochemical, structural, genetic, physiological, and pathophysiological features of lipocalin-type prostaglandin D synthase. Biochim. Biophys. Acta. 1482:259-271. http://dx.doi.org/10.1016/S0167-4838(00)00161-8
    • (2000) Biochim. Biophys. Acta. , vol.1482 , pp. 259-271
    • Urade, Y.1    Hayaishi, O.2
  • 57
    • 80455179690 scopus 로고    scopus 로고
    • Nuclear GPCRs in cardiomyocytes: an insider's view of β-adrenergic receptor signaling
    • Vaniotis, G., B.G. Allen, and T.E. Hébert. 2011. Nuclear GPCRs in cardiomyocytes: an insider's view of β-adrenergic receptor signaling. Am. J. Physiol. Heart Circ. Physiol. 301:H1754-H1764. http://dx.doi.org/10.1152/ajpheart.00657.2011
    • (2011) Am. J. Physiol. Heart Circ. Physiol. , vol.301
    • Vaniotis, G.1    Allen, B.G.2    Hébert, T.E.3
  • 58
    • 79957562543 scopus 로고    scopus 로고
    • G protein-coupled receptors: mutations and endocrine diseases
    • Vassart, G., and S. Costagliola. 2011. G protein-coupled receptors: mutations and endocrine diseases. Nat. Rev. Endocrinol. 7:362-372. http://dx.doi.org/10.1038/nrendo.2011.20
    • (2011) Nat. Rev. Endocrinol. , vol.7 , pp. 362-372
    • Vassart, G.1    Costagliola, S.2
  • 59
    • 84872865382 scopus 로고    scopus 로고
    • Posttranslational modification and quality control
    • Wang, X., J.S. Pattison, and H. Su. 2013. Posttranslational modification and quality control. Circ. Res. 112:367-381. http://dx.doi.org/10.1161/CIRCRESAHA.112.268706
    • (2013) Circ. Res. , vol.112 , pp. 367-381
    • Wang, X.1    Pattison, J.S.2    Su, H.3
  • 60
    • 2942593899 scopus 로고    scopus 로고
    • 3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex
    • Wu, B., P. Li, Y. Liu, Z. Lou, Y. Ding, C. Shu, S. Ye, M. Bartlam, B. Shen, and Z. Rao. 2004. 3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex. Proc. Natl. Acad. Sci. USA. 101:8348-8353. http://dx.doi.org/10.1073/pnas.0305969101
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 8348-8353
    • Wu, B.1    Li, P.2    Liu, Y.3    Lou, Z.4    Ding, Y.5    Shu, C.6    Ye, S.7    Bartlam, M.8    Shen, B.9    Rao, Z.10
  • 61
    • 84934439633 scopus 로고    scopus 로고
    • Molecular interaction network of the Hsp90 chaperone system
    • Zhao, R., and W.A. Houry. 2007. Molecular interaction network of the Hsp90 chaperone system. Adv. Exp. Med. Biol. 594:27-36. http://dx.doi.org/10.1007/978-0-387-39975-1_3
    • (2007) Adv. Exp. Med. Biol. , vol.594 , pp. 27-36
    • Zhao, R.1    Houry, W.A.2
  • 62
    • 78649749070 scopus 로고    scopus 로고
    • Structure-function analysis of human l-prostaglandin D synthase bound with fatty acid molecules
    • Zhou, Y., N. Shaw, Y. Li, Y. Zhao, R. Zhang, and Z.J. Liu. 2010. Structure-function analysis of human l-prostaglandin D synthase bound with fatty acid molecules. FASEB J. 24:4668-4677. http://dx.doi.org/10.1096/fj.10-164863
    • (2010) FASEB J. , vol.24 , pp. 4668-4677
    • Zhou, Y.1    Shaw, N.2    Li, Y.3    Zhao, Y.4    Zhang, R.5    Liu, Z.J.6


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