메뉴 건너뛰기




Volumn 47, Issue 2, 2006, Pages 700-708

Heat shock protein 90 is an essential molecular chaperone for nuclear transport of glucocorticoid receptor β

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GLUCOCORTICOID RECEPTOR BETA; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; LACTACYSTIN; 17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; 17-(ALLYLAMINO)-17-DEMETHOXYGELDANAMYCIN; ACETYLCYSTEINE; BENZOQUINONE DERIVATIVE; DRUG DERIVATIVE; GLUCOCORTICOID RECEPTOR; MACROCYCLIC LACTAM; PROTEIN SERINE THREONINE KINASE; RIFABUTIN;

EID: 33644856017     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.05-0697     Document Type: Article
Times cited : (30)

References (64)
  • 1
    • 12844283112 scopus 로고    scopus 로고
    • Corticosteroid glaucoma
    • Morrison JC, Pollack IP, eds. New York: Thieme Medical Publishers, Inc
    • Clark A, Morrison JM. Corticosteroid glaucoma. In: Glaucoma: Science and Practice. Morrison JC, Pollack IP, eds. New York: Thieme Medical Publishers, Inc.; 2002:197-206.
    • (2002) Glaucoma: Science and Practice , pp. 197-206
    • Clark, A.1    Morrison, J.M.2
  • 2
    • 0013815909 scopus 로고
    • Intraocular pressure response to topical corticosteroids
    • Armaly MF, Becker B. Intraocular pressure response to topical corticosteroids. Fed Proc. 1965;24:1274-1278.
    • (1965) Fed Proc , vol.24 , pp. 1274-1278
    • Armaly, M.F.1    Becker, B.2
  • 3
    • 84873771930 scopus 로고
    • Effect of corticosteroids on intraocular pressure and fluid dynamics, I: The effect of dexamethasone in the normal eye
    • Armaly MF. Effect of corticosteroids on intraocular pressure and fluid dynamics, I: the effect of dexamethasone in the normal eye. Arch Ophthalmol. 1963;70:482-491.
    • (1963) Arch Ophthalmol , vol.70 , pp. 482-491
    • Armaly, M.F.1
  • 4
    • 0000776312 scopus 로고
    • Topical corticosteroids and heredity in primary open-angle glaucoma
    • Becker B, Hahn KA. Topical corticosteroids and heredity in primary open-angle glaucoma. Am J Ophthalmol. 1964;57:543-551.
    • (1964) Am J Ophthalmol , vol.57 , pp. 543-551
    • Becker, B.1    Hahn, K.A.2
  • 5
    • 0023816683 scopus 로고
    • Intraocular pressure response to topical dexamethasone as a predictor for the development of primary open-angle glaucoma
    • Lewis JM, Priddy T, Judd J, et al. Intraocular pressure response to topical dexamethasone as a predictor for the development of primary open-angle glaucoma. Am J Ophthalmol. 1988;106:607-612.
    • (1988) Am J Ophthalmol , vol.106 , pp. 607-612
    • Lewis, J.M.1    Priddy, T.2    Judd, J.3
  • 6
    • 0033036990 scopus 로고    scopus 로고
    • Effects of glucocorticoids on the trabecular meshwork: Towards a better understanding of glaucoma
    • Wordinger RJ, Clark AF. Effects of glucocorticoids on the trabecular meshwork: towards a better understanding of glaucoma. Prog Retin Eye Res. 1999;18:629-667.
    • (1999) Prog Retin Eye Res , vol.18 , pp. 629-667
    • Wordinger, R.J.1    Clark, A.F.2
  • 7
    • 33644811218 scopus 로고    scopus 로고
    • Regulation of glucocorticoid responsiveness in glaucomatous trabecular meshwork cells by glucocorticoid receptor beta
    • Zhang X, Clark A, Yorio T. Regulation of glucocorticoid responsiveness in glaucomatous trabecular meshwork cells by glucocorticoid receptor beta. Invest Ophthalmol Vis Sci. 2005;46:4607-4616.
    • (2005) Invest Ophthalmol Vis Sci , vol.46 , pp. 4607-4616
    • Zhang, X.1    Clark, A.2    Yorio, T.3
  • 8
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans RM. The steroid and thyroid hormone receptor superfamily. Science. 1988;240:889-895.
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 10
    • 0022393794 scopus 로고
    • Primary structure and expression of a functional human glucocorticoid receptor cDNA
    • Hollenberg SM, Weinberger C, Ong ES, et al. Primary structure and expression of a functional human glucocorticoid receptor cDNA. Nature. 1985;318:635-641.
    • (1985) Nature , vol.318 , pp. 635-641
    • Hollenberg, S.M.1    Weinberger, C.2    Ong, E.S.3
  • 11
    • 0025895395 scopus 로고
    • The genomic structure of the human glucocorticoid receptor
    • Encio IJ, Detera-Wadleigh SD. The genomic structure of the human glucocorticoid receptor. J Biol Chem. 1991;266:7182-7188.
    • (1991) J Biol Chem , vol.266 , pp. 7182-7188
    • Encio, I.J.1    Detera-Wadleigh, S.D.2
  • 12
    • 0012473279 scopus 로고
    • The nuclear receptor superfamily: The second decade
    • Mangelsdorf DJ, Thummel C, Beato M, et al. The nuclear receptor superfamily: the second decade. Cell. 1995;83:835-839.
    • (1995) Cell , vol.83 , pp. 835-839
    • Mangelsdorf, D.J.1    Thummel, C.2    Beato, M.3
  • 13
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna NJ, O'Malley BW. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell. 2002;108:465-474.
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 14
    • 0029993518 scopus 로고    scopus 로고
    • The human glucocorticoid receptor beta isoform: Expression, biochemical properties, and putative function
    • Oakley RH, Sar M, Cidlowski JA. The human glucocorticoid receptor beta isoform: expression, biochemical properties, and putative function. J Biol Chem. 1996;271:9550-9559.
    • (1996) J Biol Chem , vol.271 , pp. 9550-9559
    • Oakley, R.H.1    Sar, M.2    Cidlowski, J.A.3
  • 15
    • 0029056558 scopus 로고
    • Glucocorticoid receptor beta, a potential endogenous inhibitor of glucocorticoid action in humans
    • Bamberger CM, Bamberger AM, de Castro M, Chrousos GP. Glucocorticoid receptor beta, a potential endogenous inhibitor of glucocorticoid action in humans. J Clin Invest. 1995;95:2435-2441.
    • (1995) J Clin Invest , vol.95 , pp. 2435-2441
    • Bamberger, C.M.1    Bamberger, A.M.2    de Castro, M.3    Chrousos, G.P.4
  • 16
    • 0033600936 scopus 로고    scopus 로고
    • The dominant negative activity of the human glucocorticoid receptor beta isoform: Specificity and mechanisms of action
    • Oakley RH, Jewell CM, Yudt MR, Bofetiado DM, Cidlowski JA. The dominant negative activity of the human glucocorticoid receptor beta isoform: specificity and mechanisms of action. J Biol Chem. 1999;274:27857-27866.
    • (1999) J Biol Chem , vol.274 , pp. 27857-27866
    • Oakley, R.H.1    Jewell, C.M.2    Yudt, M.R.3    Bofetiado, D.M.4    Cidlowski, J.A.5
  • 17
    • 0037979126 scopus 로고    scopus 로고
    • Molecular origins for the dominant negative function of human glucocorticoid receptor beta
    • Yudt MR, Jewell CM, Bienstock RJ, Cidlowski JA. Molecular origins for the dominant negative function of human glucocorticoid receptor beta. Mol Cell Biol. 2003;23:4319-4330.
    • (2003) Mol Cell Biol , vol.23 , pp. 4319-4330
    • Yudt, M.R.1    Jewell, C.M.2    Bienstock, R.J.3    Cidlowski, J.A.4
  • 18
    • 0033914479 scopus 로고    scopus 로고
    • Is there a role for glucocorticoid receptor beta in glucocorticoid-dependent asthmatics?
    • Leung DY, Chrousos GP. Is there a role for glucocorticoid receptor beta in glucocorticoid-dependent asthmatics? Am J Respir Crit Care Med. 2000;162:1-3.
    • (2000) Am J Respir Crit Care Med , vol.162 , pp. 1-3
    • Leung, D.Y.1    Chrousos, G.P.2
  • 19
    • 0027366385 scopus 로고
    • The hsp56 immunophilin component of steroid receptor heterocomplexes: Could this be the elusive nuclear localization signal-binding protein?
    • Pratt WB, Czar MJ, Stancato LF, Owens JK. The hsp56 immunophilin component of steroid receptor heterocomplexes: could this be the elusive nuclear localization signal-binding protein? J Steroid Biochem Mol Biol. 1993;46:269-279.
    • (1993) J Steroid Biochem Mol Biol , vol.46 , pp. 269-279
    • Pratt, W.B.1    Czar, M.J.2    Stancato, L.F.3    Owens, J.K.4
  • 20
    • 0027484097 scopus 로고
    • Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes
    • Smith DF. Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol Endocrinol. 1993;7:1418-429.
    • (1993) Mol Endocrinol , vol.7 , pp. 1418-1429
    • Smith, D.F.1
  • 21
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt WB, Toft DO. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev. 1997;18:306-360.
    • (1997) Endocr Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 22
    • 0027438228 scopus 로고
    • The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59)
    • Ratajczak T, Carrello A, Mark PJ, et al. The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59). J Biol Chem. 1993;268:13187-13192.
    • (1993) J Biol Chem , vol.268 , pp. 13187-13192
    • Ratajczak, T.1    Carrello, A.2    Mark, P.J.3
  • 24
    • 0026553797 scopus 로고
    • A model of glucocorticoid receptor unfolding and stabilization by a heat shock protein complex
    • Pratt WB, Scherrer LC, Hutchison KA, Dalman FC. A model of glucocorticoid receptor unfolding and stabilization by a heat shock protein complex. J Steroid Biochem Mol Biol. 1992;41:223-229.
    • (1992) J Steroid Biochem Mol Biol , vol.41 , pp. 223-229
    • Pratt, W.B.1    Scherrer, L.C.2    Hutchison, K.A.3    Dalman, F.C.4
  • 25
    • 0028156864 scopus 로고
    • In vivo functional protein-protein interaction: Nuclear targeted hsp90 shifts cytoplasmic steroid receptor mutants into the nucleus
    • Kang KI, Devin J, Cadepond F, et al. In vivo functional protein-protein interaction: nuclear targeted hsp90 shifts cytoplasmic steroid receptor mutants into the nucleus. Proc Natl Acad Sci USA. 1994;91:340-344.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 340-344
    • Kang, K.I.1    Devin, J.2    Cadepond, F.3
  • 26
    • 0030808079 scopus 로고    scopus 로고
    • Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus
    • Czar MJ, Galigniana MD, Silverstein AM, Pratt WB. Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus. Biochemistry. 1997;36:7776-7785.
    • (1997) Biochemistry , vol.36 , pp. 7776-7785
    • Czar, M.J.1    Galigniana, M.D.2    Silverstein, A.M.3    Pratt, W.B.4
  • 27
    • 0027106265 scopus 로고
    • Control of steroid receptor function and cytoplasmic-nuclear transport by heat shock proteins
    • Pratt WB. Control of steroid receptor function and cytoplasmic-nuclear transport by heat shock proteins. Bioessays. 1992;14:841-848.
    • (1992) Bioessays , vol.14 , pp. 841-848
    • Pratt, W.B.1
  • 28
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt WB. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J Biol Chem. 1993;268:21455-458.
    • (1993) J Biol Chem , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 29
    • 0022351390 scopus 로고
    • Effects of molybdate on steroid receptors in intact GHI cells. Evidence for dissociation of an intracellular 10 S receptor oligomer prior to nuclear accumulation
    • Raaka BM, Finnerty M, Sun E, Samuels HH. Effects of molybdate on steroid receptors in intact GHI cells. Evidence for dissociation of an intracellular 10 S receptor oligomer prior to nuclear accumulation. J Biol Chem. 1985;260:14009-4015.
    • (1985) J Biol Chem , vol.260 , pp. 14009-14015
    • Raaka, B.M.1    Finnerty, M.2    Sun, E.3    Samuels, H.H.4
  • 30
    • 0031757167 scopus 로고    scopus 로고
    • Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton
    • Galigniana MD, Scruggs JL, Herrington J, et al. Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton. Mol Endocrinol. 1998;12:1903-1913.
    • (1998) Mol Endocrinol , vol.12 , pp. 1903-1913
    • Galigniana, M.D.1    Scruggs, J.L.2    Herrington, J.3
  • 31
    • 0028862366 scopus 로고
    • Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus
    • Czar MJ, Lyons RH, Welsh MJ, Renoir JM, Pratt WB. Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus. Mol Endocrinol. 1995;9:1549-560.
    • (1995) Mol Endocrinol , vol.9 , pp. 1549-1560
    • Czar, M.J.1    Lyons, R.H.2    Welsh, M.J.3    Renoir, J.M.4    Pratt, W.B.5
  • 32
    • 0026760349 scopus 로고
    • The cytoskeleton and the cellular traffic of the progesterone receptor
    • Perrot-Applanat M, Lescop P, Milgrom E. The cytoskeleton and the cellular traffic of the progesterone receptor. J Cell Biol. 1992;119:337-348.
    • (1992) J Cell Biol , vol.119 , pp. 337-348
    • Perrot-Applanat, M.1    Lescop, P.2    Milgrom, E.3
  • 33
    • 0035805599 scopus 로고    scopus 로고
    • Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus
    • Galigniana MD, Radanyi C, Renoir JM, Housley PR, Pratt WB. Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus. J Biol Chem. 2001;276:14884-14889.
    • (2001) J Biol Chem , vol.276 , pp. 14884-14889
    • Galigniana, M.D.1    Radanyi, C.2    Renoir, J.M.3    Housley, P.R.4    Pratt, W.B.5
  • 34
    • 0037085381 scopus 로고    scopus 로고
    • A new first step in activation of steroid receptors: Hormone-induced switching of FKBP51 and FKBP52 immunophilins
    • Davies TH, Ning YM, Sanchez ER. A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins. J Biol Chem. 2002;277:4597-4600.
    • (2002) J Biol Chem , vol.277 , pp. 4597-4600
    • Davies, T.H.1    Ning, Y.M.2    Sanchez, E.R.3
  • 35
    • 0029807036 scopus 로고    scopus 로고
    • The non-ligand binding beta-isoform of the human glucocorticoid receptor (hGR beta): Tissue levels, mechanism of action, and potential physiologic role
    • de Castro M, Elliot S, Kino T, et al. The non-ligand binding beta-isoform of the human glucocorticoid receptor (hGR beta): tissue levels, mechanism of action, and potential physiologic role. Mol Med. 1996;2:597-607.
    • (1996) Mol Med , vol.2 , pp. 597-607
    • de Castro, M.1    Elliot, S.2    Kino, T.3
  • 36
    • 0030691015 scopus 로고    scopus 로고
    • Evidence that the beta-isoform of the human glucocorticoid receptor does not act as a physiologically significant repressor
    • Hecht K, Carlstedt-Duke J, Stierna P, Gustafsson J, Bronnegard M, Wikstrom AC. Evidence that the beta-isoform of the human glucocorticoid receptor does not act as a physiologically significant repressor. J Biol Chem. 1997;272:26659-26664.
    • (1997) J Biol Chem , vol.272 , pp. 26659-26664
    • Hecht, K.1    Carlstedt-Duke, J.2    Stierna, P.3    Gustafsson, J.4    Bronnegard, M.5    Wikstrom, A.C.6
  • 38
    • 0020383274 scopus 로고
    • Human trabecular endothelium, corneal endothelium, keratocytes, and scleral fibroblasts in primary cell culture: A comparative study of growth characteristics, morphology, and phagocytic activity by light and scanning electron microscopy
    • Tripathi RC, Tripathi BJ. Human trabecular endothelium, corneal endothelium, keratocytes, and scleral fibroblasts in primary cell culture: a comparative study of growth characteristics, morphology, and phagocytic activity by light and scanning electron microscopy. Exp Eye Res. 1982;35:611-624.
    • (1982) Exp Eye Res , vol.35 , pp. 611-624
    • Tripathi, R.C.1    Tripathi, B.J.2
  • 39
    • 0028123512 scopus 로고
    • Preliminary characterization of a transformed cell strain derived from human trabecular meshwork
    • Pang IH, Shade DL, Clark AF, Steely HT, DeSantis L. Preliminary characterization of a transformed cell strain derived from human trabecular meshwork. Curr Eye Res. 1994;13:51-63.
    • (1994) Curr Eye Res , vol.13 , pp. 51-63
    • Pang, I.H.1    Shade, D.L.2    Clark, A.F.3    Steely, H.T.4    DeSantis, L.5
  • 40
    • 0043269344 scopus 로고    scopus 로고
    • Auditing the pharmacological accounts for Hsp90 molecular chaperone inhibitors: Unfolding the relationship between pharmacokinetics and pharmacodynamics
    • Workman P. Auditing the pharmacological accounts for Hsp90 molecular chaperone inhibitors: unfolding the relationship between pharmacokinetics and pharmacodynamics. Mol Cancer Ther. 2003;2:131-138.
    • (2003) Mol Cancer Ther , vol.2 , pp. 131-138
    • Workman, P.1
  • 41
    • 0035900780 scopus 로고    scopus 로고
    • Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids
    • Wallace AD, Cidlowski JA. Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids. J Biol Chem. 2001;276:42714-42721.
    • (2001) J Biol Chem , vol.276 , pp. 42714-42721
    • Wallace, A.D.1    Cidlowski, J.A.2
  • 42
    • 0030926777 scopus 로고    scopus 로고
    • Lactacystin and clastolactacystin beta-lactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation
    • Craiu A, Gaczynska M, Akopian T, et al. Lactacystin and clastolactacystin beta-lactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation. J Biol Chem. 1997;272:13437-13445.
    • (1997) J Biol Chem , vol.272 , pp. 13437-13445
    • Craiu, A.1    Gaczynska, M.2    Akopian, T.3
  • 43
    • 0029870306 scopus 로고    scopus 로고
    • Lactacystin, an inhibitor of the proteasome, blocks the degradation of a mutant precursor of glycosylphosphatidylinositol- linked protein in a pre-Golgi compartment
    • Oda K, Ikehara Y, Omura S. Lactacystin, an inhibitor of the proteasome, blocks the degradation of a mutant precursor of glycosylphosphatidylinositol- linked protein in a pre-Golgi compartment. Biochem Biophys Res Commun. 1996;219:800-805.
    • (1996) Biochem Biophys Res Commun , vol.219 , pp. 800-805
    • Oda, K.1    Ikehara, Y.2    Omura, S.3
  • 44
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
    • Mimnaugh EG, Chavany C, Neckers L. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J Biol Chem. 1996;271:22796-22801.
    • (1996) J Biol Chem , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 45
    • 0033863883 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome
    • An WG, Schulte TW, Neckers LM. The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome. Cell Growth Differ. 2000;11:355-360.
    • (2000) Cell Growth Differ , vol.11 , pp. 355-360
    • An, W.G.1    Schulte, T.W.2    Neckers, L.M.3
  • 46
    • 0028786332 scopus 로고
    • Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association
    • Schulte TW, Blagosklonny MV, Ingui C, Neckers L. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J Biol Chem. 1995;270:24585-24588.
    • (1995) J Biol Chem , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3    Neckers, L.4
  • 47
    • 0031590456 scopus 로고    scopus 로고
    • Geldanamycin-induced destabilization of Raf-1 involves the proteasome
    • Schulte TW, An WG, Neckers LM. Geldanamycin-induced destabilization of Raf-1 involves the proteasome. Biochem Biophys Res Commun. 1997;239:655-659.
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 655-659
    • Schulte, T.W.1    An, W.G.2    Neckers, L.M.3
  • 48
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • Treier M, Staszewski LM, Bohmann D. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell. 1994;78:787-798.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 49
    • 0029916504 scopus 로고    scopus 로고
    • T cell antigen receptor ubiquitination is a consequence of receptor-mediated tyrosine kinase activation
    • Cenciarelli C, Wilhelm KG Jr, Guo A, Weissman AM. T cell antigen receptor ubiquitination is a consequence of receptor-mediated tyrosine kinase activation. J Biol Chem. 1996;271:8709-8713.
    • (1996) J Biol Chem , vol.271 , pp. 8709-8713
    • Cenciarelli, C.1    Wilhelm Jr, K.G.2    Guo, A.3    Weissman, A.M.4
  • 50
    • 0028091174 scopus 로고
    • Glucocorticoid-induced formation of cross-linked actin networks in cultured human trabecular meshwork cells
    • Clark AF, Wilson K, McCartney MD, Miggans ST, Kunkle M, Howe W. Glucocorticoid-induced formation of cross-linked actin networks in cultured human trabecular meshwork cells. Invest Ophthalmol Vis Sci. 1994;35:281-294.
    • (1994) Invest Ophthalmol Vis Sci , vol.35 , pp. 281-294
    • Clark, A.F.1    Wilson, K.2    McCartney, M.D.3    Miggans, S.T.4    Kunkle, M.5    Howe, W.6
  • 51
    • 0028979080 scopus 로고
    • Subcellular distribution of the glucocorticoid receptor and evidence for its association with microtubules
    • Akner G, Wikstrom AC, Gustafsson JA. Subcellular distribution of the glucocorticoid receptor and evidence for its association with microtubules. J Steroid Biochem Mol Biol. 1995;52:1-16.
    • (1995) J Steroid Biochem Mol Biol , vol.52 , pp. 1-16
    • Akner, G.1    Wikstrom, A.C.2    Gustafsson, J.A.3
  • 52
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A, Thao L, Sensintaffar J, et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature. 2003;425:407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3
  • 54
    • 0036091221 scopus 로고    scopus 로고
    • 17-Allylamino-17- demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts
    • Solit DB, Zheng FF, Drobnjak M, et al. 17-Allylamino-17- demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts. Clin Cancer Res. 2002;8:986 -993.
    • (2002) Clin Cancer Res , vol.8 , pp. 986-993
    • Solit, D.B.1    Zheng, F.F.2    Drobnjak, M.3
  • 55
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou B, Prodromou C, Roe SM, et al. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 1998;17:4829-4836.
    • (1998) EMBO J , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3
  • 56
    • 0030863995 scopus 로고    scopus 로고
    • The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation
    • Grenert JP, Sullivan WP, Fadden P, et al. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J Biol Chem. 1997;272:23843-23850.
    • (1997) J Biol Chem , vol.272 , pp. 23843-23850
    • Grenert, J.P.1    Sullivan, W.P.2    Fadden, P.3
  • 57
    • 0030810984 scopus 로고    scopus 로고
    • The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin
    • Segnitz B, Gehring U. The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin. J Biol Chem. 1997;272:18694-18701.
    • (1997) J Biol Chem , vol.272 , pp. 18694-18701
    • Segnitz, B.1    Gehring, U.2
  • 58
    • 0037075232 scopus 로고    scopus 로고
    • Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2
    • Basso AD, Solit DB, Munster PN, Rosen N. Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene. 2002;21:1159-1166.
    • (2002) Oncogene , vol.21 , pp. 1159-1166
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 59
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA. 1994;91:8324-8328.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 60
    • 0025832620 scopus 로고
    • Selective production of specific components of avermectins in Streptomyces avermitilis
    • Omura S, Ikeda H, Tanaka H. Selective production of specific components of avermectins in Streptomyces avermitilis. J Antibiot (Tokyo). 1991;44:560-563.
    • (1991) J Antibiot (Tokyo) , vol.44 , pp. 560-563
    • Omura, S.1    Ikeda, H.2    Tanaka, H.3
  • 61
    • 0036219609 scopus 로고    scopus 로고
    • Neckers L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med. 2002;8:S55-S61.
    • Neckers L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med. 2002;8:S55-S61.
  • 62
    • 0030324952 scopus 로고    scopus 로고
    • A pathway of multi-chaperone interactions common to diverse regulatory proteins: Estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor
    • Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF. A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor. Cell Stress Chaperones. 1996;1:237-250.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 237-250
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hjermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 63
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The hip-hop connection
    • Frydman J, Hohfeld J. Chaperones get in touch: the hip-hop connection. Trends Biochem Sci. 1997;22:87-92.
    • (1997) Trends Biochem Sci , vol.22 , pp. 87-92
    • Frydman, J.1    Hohfeld, J.2
  • 64
    • 0038217763 scopus 로고    scopus 로고
    • Regulation of the heat shock conjugate Hsc70 in the mammalian cell: The characterization of the anti-apoptotic protein BAG-1 provides novel insights
    • Hohfeld J. Regulation of the heat shock conjugate Hsc70 in the mammalian cell: the characterization of the anti-apoptotic protein BAG-1 provides novel insights. Biol Chem. 1998;379:269-274.
    • (1998) Biol Chem , vol.379 , pp. 269-274
    • Hohfeld, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.