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Volumn 1813, Issue 2, 2011, Pages 346-357

Modulation of α2C adrenergic receptor temperature-sensitive trafficking by HSP90

Author keywords

2C AR; Heat shock proteins; HSP90; Intracellular traffic; Low temperature; Molecular chaperones; Raynaud Phenomenon

Indexed keywords

ALPHA 2C ADRENERGIC RECEPTOR; ALVESPIMYCIN; ANTINEOPLASTIC ANTIBIOTIC; BETA ACTIN; BIOCHEMICAL MARKER; CELL SURFACE RECEPTOR; DIMETHYL SULFOXIDE; GLYCEROL; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; MACBECIN; RADICICOL; RADIOLIGAND; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 78650943372     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.11.020     Document Type: Article
Times cited : (25)

References (55)
  • 1
    • 0041506933 scopus 로고    scopus 로고
    • Pharmacology and physiology of human adrenergic receptor polymorphisms
    • Small K.M., McGraw D.W., Liggett S.B. Pharmacology and physiology of human adrenergic receptor polymorphisms. Annu. Rev. Pharmacol. Toxicol. 2003, 43:381-411.
    • (2003) Annu. Rev. Pharmacol. Toxicol. , vol.43 , pp. 381-411
    • Small, K.M.1    McGraw, D.W.2    Liggett, S.B.3
  • 2
    • 0032586029 scopus 로고    scopus 로고
    • Localization and trafficking of alpha2-adrenergic receptor subtypes in cells and tissues
    • Saunders Test C. Localization and trafficking of alpha2-adrenergic receptor subtypes in cells and tissues. Pharmacol. Ther. 1999, 84:193-205.
    • (1999) Pharmacol. Ther. , vol.84 , pp. 193-205
    • Saunders Test, C.1
  • 3
    • 0030844448 scopus 로고    scopus 로고
    • Gene targeting-homing in on alpha 2-adrenoceptor subtype function
    • MacDonald E., Kobilka B.K., Scheinin M. Gene targeting-homing in on alpha 2-adrenoceptor subtype function. Trends Pharmacol. Sci. 1997, 18:211-219.
    • (1997) Trends Pharmacol. Sci. , vol.18 , pp. 211-219
    • MacDonald, E.1    Kobilka, B.K.2    Scheinin, M.3
  • 4
    • 3042616560 scopus 로고    scopus 로고
    • Alpha2-adrenergic receptor subtypes - novel functions uncovered in gene-targeted mouse models
    • Brede M., Philipp M., Knaus A., Muthig V., Hein L. Alpha2-adrenergic receptor subtypes - novel functions uncovered in gene-targeted mouse models. Biol. Cell 2004, 96:343-348.
    • (2004) Biol. Cell , vol.96 , pp. 343-348
    • Brede, M.1    Philipp, M.2    Knaus, A.3    Muthig, V.4    Hein, L.5
  • 5
    • 34548509009 scopus 로고    scopus 로고
    • Alpha2-adrenoceptor subtypes - unexpected functions for receptors and ligands derived from gene-targeted mouse models
    • Knaus A.E., Muthig V., Schickinger S., Moura E., Beetz N., Gilsbach R., Hein L. Alpha2-adrenoceptor subtypes - unexpected functions for receptors and ligands derived from gene-targeted mouse models. Neurochem. Int. 2007, 51:277-281.
    • (2007) Neurochem. Int. , vol.51 , pp. 277-281
    • Knaus, A.E.1    Muthig, V.2    Schickinger, S.3    Moura, E.4    Beetz, N.5    Gilsbach, R.6    Hein, L.7
  • 6
    • 0028973233 scopus 로고
    • Identification of a Gs coupling domain in the amino terminus of the third intracellular loop of the alpha 2A-adrenergic receptor. Evidence for distinct structural determinants that confer Gs versus Gi coupling
    • Eason M.G., Liggett S.B. Identification of a Gs coupling domain in the amino terminus of the third intracellular loop of the alpha 2A-adrenergic receptor. Evidence for distinct structural determinants that confer Gs versus Gi coupling. J. Biol. Chem. 1995, 270:24753-24760.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24753-24760
    • Eason, M.G.1    Liggett, S.B.2
  • 7
    • 0032705301 scopus 로고    scopus 로고
    • G(i) activator region of alpha(2A)-adrenergic receptors: distinct basic residues mediate G(i) versus G(s) activation
    • Wade S.M., Lim W.K., Lan K.L., Chung D.A., Nanamori M., Neubig R.R. G(i) activator region of alpha(2A)-adrenergic receptors: distinct basic residues mediate G(i) versus G(s) activation. Mol. Pharmacol. 1999, 56:1005-1013.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 1005-1013
    • Wade, S.M.1    Lim, W.K.2    Lan, K.L.3    Chung, D.A.4    Nanamori, M.5    Neubig, R.R.6
  • 8
    • 0030908655 scopus 로고    scopus 로고
    • Subtype-specific intracellular trafficking of alpha2-adrenergic receptors
    • Daunt D.A., Hurt C., Hein L., Kallio J., Feng F., Kobilka B.K. Subtype-specific intracellular trafficking of alpha2-adrenergic receptors. Mol. Pharmacol. 1997, 51:711-720.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 711-720
    • Daunt, D.A.1    Hurt, C.2    Hein, L.3    Kallio, J.4    Feng, F.5    Kobilka, B.K.6
  • 9
    • 0034634587 scopus 로고    scopus 로고
    • Cell-type specific targeting of the alpha 2c-adrenoceptor. Evidence for the organization of receptor microdomains during neuronal differentiation of PC12 cells
    • Hurt C.M., Feng F.Y., Kobilka B. Cell-type specific targeting of the alpha 2c-adrenoceptor. Evidence for the organization of receptor microdomains during neuronal differentiation of PC12 cells. J. Biol. Chem. 2000, 275:35424-35431.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35424-35431
    • Hurt, C.M.1    Feng, F.Y.2    Kobilka, B.3
  • 10
    • 0037179578 scopus 로고    scopus 로고
    • Raynaud's Phenomenon
    • Wigley F.M. Raynaud's Phenomenon. N. Engl. J. Med. 2002, 347:1001-1008.
    • (2002) N. Engl. J. Med. , vol.347 , pp. 1001-1008
    • Wigley, F.M.1
  • 11
    • 40149105688 scopus 로고    scopus 로고
    • Regulation of vascular reactivity in scleroderma: new insights into Raynaud's phenomenon
    • Flavahan N.A. Regulation of vascular reactivity in scleroderma: new insights into Raynaud's phenomenon. Rheum. Dis. Clin. North Am. 2008, 34:81-87.
    • (2008) Rheum. Dis. Clin. North Am. , vol.34 , pp. 81-87
    • Flavahan, N.A.1
  • 13
    • 0029128890 scopus 로고
    • Blockade of vasospastic attacks by alpha 2-adrenergic but not alpha 1-adrenergic antagonists in idiopathic Raynaud's disease
    • Freedman R.R., Baer R.P., Mayes M.D. Blockade of vasospastic attacks by alpha 2-adrenergic but not alpha 1-adrenergic antagonists in idiopathic Raynaud's disease. Circulation 1995, 92:1448-1451.
    • (1995) Circulation , vol.92 , pp. 1448-1451
    • Freedman, R.R.1    Baer, R.P.2    Mayes, M.D.3
  • 15
    • 2642569161 scopus 로고    scopus 로고
    • Rho kinase mediates cold-induced constriction of cutaneous arteries: role of alpha2C-adrenoceptor translocation
    • Bailey S.R., Eid A.H., Mitra S., Flavahan S., Flavahan N.A. Rho kinase mediates cold-induced constriction of cutaneous arteries: role of alpha2C-adrenoceptor translocation. Circ. Res. 2004, 94:1367-1374.
    • (2004) Circ. Res. , vol.94 , pp. 1367-1374
    • Bailey, S.R.1    Eid, A.H.2    Mitra, S.3    Flavahan, S.4    Flavahan, N.A.5
  • 16
    • 24344487961 scopus 로고    scopus 로고
    • The regulatory mechanisms of export trafficking of G protein-coupled receptors
    • Duvernay M.T., Filipeanu C.M., Wu G. The regulatory mechanisms of export trafficking of G protein-coupled receptors. Cell. Signal. 2005, 17:1457-1465.
    • (2005) Cell. Signal. , vol.17 , pp. 1457-1465
    • Duvernay, M.T.1    Filipeanu, C.M.2    Wu, G.3
  • 18
    • 33746730393 scopus 로고    scopus 로고
    • 'Effective inefficiency': cellular control of protein trafficking as a mechanism of post-translational regulation
    • Conn P.M., Janovick J.A., Brothers S.P., Knollman P.E. 'Effective inefficiency': cellular control of protein trafficking as a mechanism of post-translational regulation. J. Endocrinol. 2006, 190:13-16.
    • (2006) J. Endocrinol. , vol.190 , pp. 13-16
    • Conn, P.M.1    Janovick, J.A.2    Brothers, S.P.3    Knollman, P.E.4
  • 19
    • 70450263435 scopus 로고    scopus 로고
    • Fine-tuning of GPCR activity by receptor-interacting proteins
    • Ritter S.L., Hall R.A. Fine-tuning of GPCR activity by receptor-interacting proteins. Nat. Rev. Mol. Cell Biol. 2009, 10:819-830.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 819-830
    • Ritter, S.L.1    Hall, R.A.2
  • 20
    • 0034607918 scopus 로고    scopus 로고
    • Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor
    • Petaja-Repo U.E., Hogue M., Laperriere A., Walker P., Bouvier M. Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor. J. Biol. Chem. 2000, 275:13727-13736.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13727-13736
    • Petaja-Repo, U.E.1    Hogue, M.2    Laperriere, A.3    Walker, P.4    Bouvier, M.5
  • 22
    • 34547523029 scopus 로고    scopus 로고
    • Calreticulin and Hsp90 stabilize the human insulin receptor and promote its mobility in the endoplasmic reticulum
    • Ramos R.R., Swanson A.J., Bass J. Calreticulin and Hsp90 stabilize the human insulin receptor and promote its mobility in the endoplasmic reticulum. Proc. Natl Acad. Sci. USA 2007, 104:10470-10475.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 10470-10475
    • Ramos, R.R.1    Swanson, A.J.2    Bass, J.3
  • 23
    • 53049109653 scopus 로고    scopus 로고
    • HSP90 beta regulates rapsyn turnover and subsequent AChR cluster formation and maintenance
    • Luo S., Zhang B., Dong X.P., Tao Y., Ting A., Zhou Test Z. HSP90 beta regulates rapsyn turnover and subsequent AChR cluster formation and maintenance. Neuron 2008, 60:97-110.
    • (2008) Neuron , vol.60 , pp. 97-110
    • Luo, S.1    Zhang, B.2    Dong, X.P.3    Tao, Y.4    Ting, A.5    Zhou Test, Z.6
  • 24
    • 34249712933 scopus 로고    scopus 로고
    • Pharmacological chaperones in nephrogenic diabetes insipidus: possibilities for clinical application
    • Robben J.H., Deen P.M. Pharmacological chaperones in nephrogenic diabetes insipidus: possibilities for clinical application. BioDrugs 2007, 21:157-166.
    • (2007) BioDrugs , vol.21 , pp. 157-166
    • Robben, J.H.1    Deen, P.M.2
  • 25
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities
    • Kim I., Xu W., Reed J.C. Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities. Nat. Rev. Drug Discov. 2008, 7:1013-1030.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 26
    • 33745240417 scopus 로고    scopus 로고
    • F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive
    • Hegedus T., Aleksandrov A., Cui L., Gentzsch M., Chang X.B., Riordan J.R. F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive. Biochim. Biophys. Acta 2006, 1758:565-572.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 565-572
    • Hegedus, T.1    Aleksandrov, A.2    Cui, L.3    Gentzsch, M.4    Chang, X.B.5    Riordan, J.R.6
  • 27
    • 63849242843 scopus 로고    scopus 로고
    • Intracellular potassium stabilizes human ether-à-go-go-related gene channels for export from endoplasmic reticulum
    • Wang L., Dennis A.T., Trieu P., Charron F., Ethier N., Hebert T.E., Wan X., Ficker E. Intracellular potassium stabilizes human ether-à-go-go-related gene channels for export from endoplasmic reticulum. Mol. Pharmacol. 2009, 75:927-937.
    • (2009) Mol. Pharmacol. , vol.75 , pp. 927-937
    • Wang, L.1    Dennis, A.T.2    Trieu, P.3    Charron, F.4    Ethier, N.5    Hebert, T.E.6    Wan, X.7    Ficker, E.8
  • 28
    • 33746079244 scopus 로고    scopus 로고
    • Control and regulation of the cellular responses to cold shock: the responses in yeast and mammalian systems
    • Al-Fageeh M.B., Smales C.M. Control and regulation of the cellular responses to cold shock: the responses in yeast and mammalian systems. Biochem. J. 2006, 397:247-259.
    • (2006) Biochem. J. , vol.397 , pp. 247-259
    • Al-Fageeh, M.B.1    Smales, C.M.2
  • 29
    • 27844457541 scopus 로고    scopus 로고
    • Cell-surface targeting of alpha2-adrenergic receptors - inhibition by a transport deficient mutant through dimerization
    • Zhou F., Filipeanu C.M., Duvernay M.T., Wu G. Cell-surface targeting of alpha2-adrenergic receptors - inhibition by a transport deficient mutant through dimerization. Cell. Signal. 2006, 18:318-327.
    • (2006) Cell. Signal. , vol.18 , pp. 318-327
    • Zhou, F.1    Filipeanu, C.M.2    Duvernay, M.T.3    Wu, G.4
  • 30
    • 4644275035 scopus 로고    scopus 로고
    • Regulation of the cell surface expression and function of angiotensin II type 1 receptor by Rab1-mediated endoplasmic reticulum-to-Golgi transport in cardiac myocytes
    • Filipeanu C.M., Zhou F., Claycomb W.C., Wu G. Regulation of the cell surface expression and function of angiotensin II type 1 receptor by Rab1-mediated endoplasmic reticulum-to-Golgi transport in cardiac myocytes. J. Biol. Chem. 2004, 279:41077-41084.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41077-41084
    • Filipeanu, C.M.1    Zhou, F.2    Claycomb, W.C.3    Wu, G.4
  • 31
    • 33645816540 scopus 로고    scopus 로고
    • G Wu, Differential regulation of the cell-surface targeting and function of beta- and alpha1-adrenergic receptors by Rab1 GTPase in cardiac myocytes
    • Filipeanu C.M., Zhou F., Fugetta E.K. G Wu, Differential regulation of the cell-surface targeting and function of beta- and alpha1-adrenergic receptors by Rab1 GTPase in cardiac myocytes. Mol. Pharmacol. 2006, 69:1571-1578.
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1571-1578
    • Filipeanu, C.M.1    Zhou, F.2    Fugetta, E.K.3
  • 32
    • 33744965473 scopus 로고    scopus 로고
    • Enhancement of the recycling and activation of beta-adrenergic receptor by Rab4 GTPase in cardiac myocytes
    • Filipeanu C.M., Zhou F., Lam M.L., Kerut K.E., Claycomb W.C., Wu G. Enhancement of the recycling and activation of beta-adrenergic receptor by Rab4 GTPase in cardiac myocytes. J. Biol. Chem. 2006, 281:11097-11103.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11097-11103
    • Filipeanu, C.M.1    Zhou, F.2    Lam, M.L.3    Kerut, K.E.4    Claycomb, W.C.5    Wu, G.6
  • 33
    • 0017702173 scopus 로고
    • Contractile properties of small arterial resistance vessels in spontaneously hypertensive and normotensive rats
    • Mulvany M.J., Halpern W. Contractile properties of small arterial resistance vessels in spontaneously hypertensive and normotensive rats. Circ. Res. 1977, 41:19-26.
    • (1977) Circ. Res. , vol.41 , pp. 19-26
    • Mulvany, M.J.1    Halpern, W.2
  • 34
    • 0034725616 scopus 로고    scopus 로고
    • A four amino acid deletion polymorphism in the third intracellular loop of the human alpha 2C-adrenergic receptor confers impaired coupling to multiple effectors
    • Small K.M., Forbes S.L., Rahman F.F., Bridges K.M., Liggett S.B. A four amino acid deletion polymorphism in the third intracellular loop of the human alpha 2C-adrenergic receptor confers impaired coupling to multiple effectors. J. Biol. Chem. 2000, 275:23059-23064.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23059-23064
    • Small, K.M.1    Forbes, S.L.2    Rahman, F.F.3    Bridges, K.M.4    Liggett, S.B.5
  • 36
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard D. Heat-shock protein 90, a chaperone for folding and regulation. Cell. Mol. Life Sci. 2002, 59:1640-1648.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 37
    • 39049138736 scopus 로고    scopus 로고
    • A comparison of Hsp90alpha and Hsp90beta interactions with cochaperones and substrates
    • Taherian A., Krone P.H., Ovsenek N. A comparison of Hsp90alpha and Hsp90beta interactions with cochaperones and substrates. Biochem. Cell Biol. 2008, 86:37-45.
    • (2008) Biochem. Cell Biol. , vol.86 , pp. 37-45
    • Taherian, A.1    Krone, P.H.2    Ovsenek, N.3
  • 39
    • 0035206445 scopus 로고    scopus 로고
    • Cooling evokes redistribution of alpha2C-adrenoceptors from Golgi to plasma membrane in transfected human embryonic kidney 293 cells
    • Jeyaraj S.C., Chotani M.A., Mitra S., Gregg H.E., Flavahan N.A., Morrison K.J. Cooling evokes redistribution of alpha2C-adrenoceptors from Golgi to plasma membrane in transfected human embryonic kidney 293 cells. Mol. Pharmacol. 2001, 60:1195-1200.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1195-1200
    • Jeyaraj, S.C.1    Chotani, M.A.2    Mitra, S.3    Gregg, H.E.4    Flavahan, N.A.5    Morrison, K.J.6
  • 40
    • 77951731676 scopus 로고    scopus 로고
    • Regulation of G-protein coupled receptor traffic by an evolutionary conserved hydrophobic signal
    • Angelotti T., Daunt D., Shcherbakova O.G., Kobilka B., Hurt C.M. Regulation of G-protein coupled receptor traffic by an evolutionary conserved hydrophobic signal. Traffic 2010, 11:560-578.
    • (2010) Traffic , vol.11 , pp. 560-578
    • Angelotti, T.1    Daunt, D.2    Shcherbakova, O.G.3    Kobilka, B.4    Hurt, C.M.5
  • 41
    • 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., Qiao Z.H., Cai J., Pierce W., He D.C., Song Z.H. 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. 2007, 72:1289-1300.
    • (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
  • 42
    • 0035793546 scopus 로고    scopus 로고
    • Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90
    • Xu W., Mimnaugh E., Rosser M.F., Nicchitta C., Marcu M., Yarden Y., Neckers L. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J. Biol. Chem. 2001, 276:3702-3708.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3702-3708
    • Xu, W.1    Mimnaugh, E.2    Rosser, M.F.3    Nicchitta, C.4    Marcu, M.5    Yarden, Y.6    Neckers, L.7
  • 43
    • 0033210210 scopus 로고    scopus 로고
    • GRP94, an ER chaperone with protein and peptide binding properties
    • Argon Y., Simen B.B. GRP94, an ER chaperone with protein and peptide binding properties. Semin. Cell Dev. Biol. 1999, 10:495-505.
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 495-505
    • Argon, Y.1    Simen, B.B.2
  • 45
    • 0041344550 scopus 로고    scopus 로고
    • Activation of metabotropic glutamate receptor mGlu5 on nuclear membranes mediates intranuclear Ca2+ changes in heterologous cell types and neurons
    • O'Malley K.L., Jong Y.J., Gonchar Y., Burkhalter A., Romano C. Activation of metabotropic glutamate receptor mGlu5 on nuclear membranes mediates intranuclear Ca2+ changes in heterologous cell types and neurons. J. Biol. Chem. 2003, 278:28210-28219.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28210-28219
    • O'Malley, K.L.1    Jong, Y.J.2    Gonchar, Y.3    Burkhalter, A.4    Romano, C.5
  • 46
    • 46749113793 scopus 로고    scopus 로고
    • Regulation of CB1 cannabinoid receptor trafficking by the adaptor protein AP-3
    • Rozenfeld R., Devi L.A. Regulation of CB1 cannabinoid receptor trafficking by the adaptor protein AP-3. FASEB J. 2008, 22:2311-2322.
    • (2008) FASEB J. , vol.22 , pp. 2311-2322
    • Rozenfeld, R.1    Devi, L.A.2
  • 47
    • 33845926059 scopus 로고    scopus 로고
    • Seven transmembrane receptor core signaling complexes are assembled prior to plasma membrane trafficking
    • Dupré D.J., Robitaille M., Ethier N., Villeneuve L.R., Mamarbachi A.M., Hébert T.E. Seven transmembrane receptor core signaling complexes are assembled prior to plasma membrane trafficking. J. Biol. Chem. 2006, 281:34561-34573.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34561-34573
    • Dupré, D.J.1    Robitaille, M.2    Ethier, N.3    Villeneuve, L.R.4    Mamarbachi, A.M.5    Hébert, T.E.6
  • 48
    • 0029120998 scopus 로고
    • Expression of heat shock protein 90 (hsp90) in neural and nonneural tissues of the control and hyperthermic rabbit
    • Quraishi H., Brown I.R. Expression of heat shock protein 90 (hsp90) in neural and nonneural tissues of the control and hyperthermic rabbit. Exp. Cell Res. 1995, 219:358-363.
    • (1995) Exp. Cell Res. , vol.219 , pp. 358-363
    • Quraishi, H.1    Brown, I.R.2
  • 50
    • 66749168924 scopus 로고    scopus 로고
    • Essential role of the 90-kilodalton heat shock protein in mediating nongenomic estrogen signaling in coronary artery smooth muscle
    • Han G., Ma H., Chintala R., Fulton D.J., Barman S.A., White R.E. Essential role of the 90-kilodalton heat shock protein in mediating nongenomic estrogen signaling in coronary artery smooth muscle. J. Pharmacol. Exp. Ther. 2009, 329:850-855.
    • (2009) J. Pharmacol. Exp. Ther. , vol.329 , pp. 850-855
    • Han, G.1    Ma, H.2    Chintala, R.3    Fulton, D.J.4    Barman, S.A.5    White, R.E.6
  • 51
    • 64949083563 scopus 로고    scopus 로고
    • Inhibition of cancer invasion and metastasis by targeting the molecular chaperone heat-shock protein 90
    • Koga F., Kihara K., Necker L. Inhibition of cancer invasion and metastasis by targeting the molecular chaperone heat-shock protein 90. Anticancer Res. 2009, 29:797-807.
    • (2009) Anticancer Res. , vol.29 , pp. 797-807
    • Koga, F.1    Kihara, K.2    Necker, L.3
  • 52
    • 51449093764 scopus 로고    scopus 로고
    • Targeting Hsp90: small-molecule inhibitors and their clinical development
    • Taldone T., Gozman A., Maharaj R., Chiosis G. Targeting Hsp90: small-molecule inhibitors and their clinical development. Curr. Opin. Pharmacol. 2008, 8:370-374.
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 370-374
    • Taldone, T.1    Gozman, A.2    Maharaj, R.3    Chiosis, G.4
  • 54
    • 49849106317 scopus 로고    scopus 로고
    • Cyclic AMP acts through Rap1 and JNK signaling to increase expression of cutaneous smooth muscle alpha2C-adrenoceptors
    • Eid A.H., Chotani M.A., Mitra S., Miller T.J., Flavahan N.A. Cyclic AMP acts through Rap1 and JNK signaling to increase expression of cutaneous smooth muscle alpha2C-adrenoceptors. Am. J. Physiol. Heart Circ. Physiol. 2008, 295:H266-H272.
    • (2008) Am. J. Physiol. Heart Circ. Physiol. , vol.295
    • Eid, A.H.1    Chotani, M.A.2    Mitra, S.3    Miller, T.J.4    Flavahan, N.A.5
  • 55
    • 58149500610 scopus 로고    scopus 로고
    • Cold stability of intrinsically disordered proteins
    • Tantos A., Friedrich P., Tompa P. Cold stability of intrinsically disordered proteins. FEBS Lett. 2009, 583:465-469.
    • (2009) FEBS Lett. , vol.583 , pp. 465-469
    • Tantos, A.1    Friedrich, P.2    Tompa, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.