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Volumn 9, Issue 6, 1998, Pages 238-243

Recent advances in the study of hsp90 structure and mechanism of action

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALUMINUM FLUORIDE; ANSAMYCIN DERIVATIVE; ANTIBODY; BERYLLIUM; BINDING PROTEIN; CELL PROTEIN; CHAPERONE; CYCLOSPORIN; DNA TOPOISOMERASE (ATP HYDROLYSING); GELDANAMYCIN; GLUCOCORTICOID RECEPTOR; HEAT SHOCK PROTEIN 90; HERBIMYCIN A; IMMUNOPHILIN; MYOSIN; MYRISTIC ACID; PHOSPHOPROTEIN PHOSPHATASE; PROGESTERONE RECEPTOR; PROTEIN KINASE; PROTEIN TYROSINE KINASE; STEROID RECEPTOR; TACROLIMUS; TRANSCRIPTION FACTOR;

EID: 0031848850     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1043-2760(98)00060-5     Document Type: Review
Times cited : (73)

References (59)
  • 1
    • 0022574582 scopus 로고
    • src with the cellular proteins pp50 and pp90
    • src with the cellular proteins pp50 and pp90. Curr Top Microbiol Immunol. 123:1986;1-22.
    • (1986) Curr Top Microbiol Immunol , vol.123 , pp. 1-22
    • Brugge, J.1
  • 2
    • 0030027968 scopus 로고    scopus 로고
    • Supervising the fold: Functional principles of molecular chaperones
    • Buchner J Supervising the fold: functional principles of molecular chaperones. FASEB. J 10:1996;10-19.
    • (1996) FASEB , vol.10 , pp. 10-19
    • Buchner, J.1
  • 3
    • 0028331568 scopus 로고
    • Selective deletions in the 90 kDa heat shock protein (hsp90) impede hetero-oligomeric complex formation with the glucocorticosteroid receptor (GR) or hormone binding by GR
    • Cadepond F, Jibard N, Binart N, Schweizer-Groyer G, Segard-Maurel I, Baulieu E-E Selective deletions in the 90 kDa heat shock protein (hsp90) impede hetero-oligomeric complex formation with the glucocorticosteroid receptor (GR) or hormone binding by GR. J Steroid Biochem Mol Biol. 48:1994;361-367.
    • (1994) J Steroid Biochem Mol Biol , vol.48 , pp. 361-367
    • Cadepond, F.1    Jibard, N.2    Binart, N.3    Schweizer-Groyer, G.4    Segard-Maurel, I.5    Baulieu E-E6
  • 4
    • 0031238563 scopus 로고    scopus 로고
    • Yeast molecular chaperones and the mechanism of steroid hormone action
    • Caplan A Yeast molecular chaperones and the mechanism of steroid hormone action. Trends Endocrinol Metab. 8:1997;271-276.
    • (1997) Trends Endocrinol Metab , vol.8 , pp. 271-276
    • Caplan, A.1
  • 5
    • 0030897705 scopus 로고    scopus 로고
    • Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo
    • Carver L, Bradfield C Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo. J Biol Chem. 272:1997;11452-11456.
    • (1997) J Biol Chem , vol.272 , pp. 11452-11456
    • Carver, L.1    Bradfield, C.2
  • 6
    • 0025191377 scopus 로고
    • Aluminofluoride and beryllofluoride complexes: New phosphate analogs in enzymology
    • Chabre M Aluminofluoride and beryllofluoride complexes: new phosphate analogs in enzymology. Trends Biochem Sci. 15:1990;6-10.
    • (1990) Trends Biochem Sci , vol.15 , pp. 6-10
    • Chabre, M.1
  • 7
    • 0029760873 scopus 로고    scopus 로고
    • A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock
    • Chen C-F, Chen Y, Dai Ket al. A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock. Mol Cell Biol. 16:1996;4691-4699.
    • (1996) Mol Cell Biol , vol.16 , pp. 4691-4699
    • Chen C-F1    Chen, Y.2    Dai, K.3
  • 8
    • 0029885423 scopus 로고    scopus 로고
    • Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70
    • Chen S, Prapapanich V, Rimerman RA, Honoré B, Smith D Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70. Mol Endocrinol. 10:1996;682-693.
    • (1996) Mol Endocrinol , vol.10 , pp. 682-693
    • Chen, S.1    Prapapanich, V.2    Rimerman, R.A.3    Honoré, B.4    Smith, D.5
  • 9
    • 0031846768 scopus 로고    scopus 로고
    • Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with hsp90 mutants
    • (in press).
    • Chen S, Sullivan WP, Toft DO, Smith DF: 1998. Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with hsp90 mutants. Cell Stress Chaperones 1998 (in press).
    • (1998) Cell Stress Chaperones 1998
    • Chen, S.1    Sullivan, W.P.2    Toft, D.O.3    Smith, D.F.4
  • 11
    • 0027526899 scopus 로고
    • ATP induces a conformational change of the 90-kDa heat shock protein (hsp90)
    • Csermely P, Kajtár J, Hollósi Met al. ATP induces a conformational change of the 90-kDa heat shock protein (hsp90). J Biol Chem. 268:1993;1901-1907.
    • (1993) J Biol Chem , vol.268 , pp. 1901-1907
    • Csermely, P.1    Kajtár, J.2    Hollósi, M.3
  • 12
    • 0031873752 scopus 로고    scopus 로고
    • The 90 kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review
    • (in press).
    • Csermely P, Schaider T, Sôti C, Prohászka Z, Nardai G: 1998. The 90 kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol Ther 1998 (in press).
    • (1998) Pharmacol Ther 1998
    • Csermely, P.1    Schaider, T.2    Sôti, C.3    Prohászka, Z.4    Nardai, G.5
  • 13
    • 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 M, Lyons R, Welsh M, Renoir J, Pratt W 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. 9:1995;1549-1560.
    • (1995) Mol Endocrinol , vol.9 , pp. 1549-1560
    • Czar, M.1    Lyons, R.2    Welsh, M.3    Renoir, J.4    Pratt, W.5
  • 14
    • 0030869037 scopus 로고    scopus 로고
    • Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery
    • Dittmar K, Demady D, Stancato L, Krishna P, Pratt W Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. J Biol Chem. 272:1997;21213-21220.
    • (1997) J Biol Chem , vol.272 , pp. 21213-21220
    • Dittmar, K.1    Demady, D.2    Stancato, L.3    Krishna, P.4    Pratt, W.5
  • 15
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman B, Morimoto R The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO. J 15:1996;2969-2979.
    • (1996) EMBO , vol.15 , pp. 2969-2979
    • Freeman, B.1    Morimoto, R.2
  • 16
    • 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 J, Sullivan W, Fadden Pet 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. 272:1997;23843-23850.
    • (1997) J Biol Chem , vol.272 , pp. 23843-23850
    • Grenert, J.1    Sullivan, W.2    Fadden, P.3
  • 17
    • 0032478703 scopus 로고    scopus 로고
    • Modular folding and evidence for phosphorylation-induced stabilization of an hsp90-dependent kinase
    • Hartson S, Ottinger E, Huang W, Barany G, Burn P, Matts R Modular folding and evidence for phosphorylation-induced stabilization of an hsp90-dependent kinase. J Biol Chem. 273:1998;8475-8482.
    • (1998) J Biol Chem , vol.273 , pp. 8475-8482
    • Hartson, S.1    Ottinger, E.2    Huang, W.3    Barany, G.4    Burn, P.5    Matts, R.6
  • 18
    • 0028913971 scopus 로고
    • Cyclophilin-40: Evidence for a dimeric complex with hsp90
    • Hoffman K, Handschumacher R Cyclophilin-40: evidence for a dimeric complex with hsp90. Biochem. J 307:1995;5-8.
    • (1995) Biochem , vol.307 , pp. 5-8
    • Hoffman, K.1    Handschumacher, R.2
  • 19
    • 0031018112 scopus 로고    scopus 로고
    • Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids
    • Hu J, Toft D, Seeger C Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids. EMBO. J 16:1997;59-68.
    • (1997) EMBO , vol.16 , pp. 59-68
    • Hu, J.1    Toft, D.2    Seeger, C.3
  • 20
    • 0028940309 scopus 로고
    • Transient interaction of hsp90 with early unfolding intermediates of citrate synthase
    • Jakob U, Lilie H, Meyer I, Buchner J Transient interaction of hsp90 with early unfolding intermediates of citrate synthase. J Biol Chem. 270:1995;7288-7294.
    • (1995) J Biol Chem , vol.270 , pp. 7288-7294
    • Jakob, U.1    Lilie, H.2    Meyer, I.3    Buchner, J.4
  • 22
    • 0032488906 scopus 로고    scopus 로고
    • Hop modulates hsp70/hsp90 interactions in protein folding
    • Johnson B, Schumacher R, Ross E, Toft D Hop modulates hsp70/hsp90 interactions in protein folding. J Biol Chem. 273:1998;3679-3686.
    • (1998) J Biol Chem , vol.273 , pp. 3679-3686
    • Johnson, B.1    Schumacher, R.2    Ross, E.3    Toft, D.4
  • 24
    • 0024548919 scopus 로고
    • Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II
    • Lees-Miller S, Anderson C Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II. J Biol Chem. 264:1989;2431-2437.
    • (1989) J Biol Chem , vol.264 , pp. 2431-2437
    • Lees-Miller, S.1    Anderson, C.2
  • 25
    • 0031615108 scopus 로고    scopus 로고
    • Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism
    • Leverson J, Ness S Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism. Mol Cell. 1:1998;203-211.
    • (1998) Mol Cell , vol.1 , pp. 203-211
    • Leverson, J.1    Ness, S.2
  • 26
    • 0030462612 scopus 로고    scopus 로고
    • Two eukaryote-specific regions of hsp82 are dispensable for its viability and signal transduction functions in yeast
    • Louvion J-F, Warth R, Picard D Two eukaryote-specific regions of hsp82 are dispensable for its viability and signal transduction functions in yeast. Proc Natl Acad Sci USA. 93:1996;13937-13942.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13937-13942
    • Louvion J-F1    Warth, R.2    Picard, D.3
  • 27
    • 0031002895 scopus 로고    scopus 로고
    • A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Ma Q, Whitlock J Jr. A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin. J Biol Chem. 272:1997;8878-8884.
    • (1997) J Biol Chem , vol.272 , pp. 8878-8884
    • Ma, Q.1    Whitlock J., Jr.2
  • 28
    • 0343488499 scopus 로고    scopus 로고
    • Chaperone-assisted protein folding
    • Martin J, Hartl F Chaperone-assisted protein folding. Curr Opin Struct Biol. 7:1997;41-52.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 41-52
    • Martin, J.1    Hartl, F.2
  • 29
    • 0031882767 scopus 로고    scopus 로고
    • Hepatitis B virus X-associated protein 2 is a subunit of the unliganded aryl hydrocarbon receptor core complex and exhibits transcriptional enhancer activity
    • Meyer B, Pray-Grant M, Vanden Heuvel J, Perdew G Hepatitis B virus X-associated protein 2 is a subunit of the unliganded aryl hydrocarbon receptor core complex and exhibits transcriptional enhancer activity. Mol Cell Biol. 18:1998;978-988.
    • (1998) Mol Cell Biol , vol.18 , pp. 978-988
    • Meyer, B.1    Pray-Grant, M.2    Vanden Heuvel, J.3    Perdew, G.4
  • 30
    • 0028012587 scopus 로고
    • The carboxy-terminal region of mammalian hsp90 is required for its dimerization and function in vivo
    • Minami Y, Kimura Y, Kawasaki H, Suzuki K, Yahara I The carboxy-terminal region of mammalian hsp90 is required for its dimerization and function in vivo. Mol Cell Biol. 14:1994;1459-1464.
    • (1994) Mol Cell Biol , vol.14 , pp. 1459-1464
    • Minami, Y.1    Kimura, Y.2    Kawasaki, H.3    Suzuki, K.4    Yahara, I.5
  • 31
    • 13144260667 scopus 로고    scopus 로고
    • Phosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: Regulation of hsp90-binding activity of FKBP52
    • Miyata Y, Chambraud B, Radanyi Cet al. Phosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: regulation of hsp90-binding activity of FKBP52. Proc Natl Acad Sci USA. 94:1997;14500-14505.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14500-14505
    • Miyata, Y.1    Chambraud, B.2    Radanyi, C.3
  • 32
    • 0027475243 scopus 로고
    • Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases
    • Nadeau K, Das A, Walsh C Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases. J Biol Chem. 268:1993;1479-1487.
    • (1993) J Biol Chem , vol.268 , pp. 1479-1487
    • Nadeau, K.1    Das, A.2    Walsh, C.3
  • 33
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae hsp90 chaperone
    • Nathan D, Vos M, Lindquist S In vivo functions of the Saccharomyces cerevisiae hsp90 chaperone. Proc Natl Acad Sci USA. 94:1997;12949-12956.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12949-12956
    • Nathan, D.1    Vos, M.2    Lindquist, S.3
  • 35
    • 0029889955 scopus 로고    scopus 로고
    • A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains
    • Owens-Grillo J, Czar M, Hutchison K, Hoffmann K, Perdew G, Pratt W A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains. J Biol Chem. 271:1996;13468-13475.
    • (1996) J Biol Chem , vol.271 , pp. 13468-13475
    • Owens-Grillo, J.1    Czar, M.2    Hutchison, K.3    Hoffmann, K.4    Perdew, G.5    Pratt, W.6
  • 36
    • 0027135268 scopus 로고
    • Localization and characterization of the 86- And 84-kDa heat shock proteins in Hepa 1c1c7 cells
    • Perdew G, Hord N, Hollenback C, Welsh M Localization and characterization of the 86- and 84-kDa heat shock proteins in Hepa 1c1c7 cells. Exp Cell Res. 209:1993;350-356.
    • (1993) Exp Cell Res , vol.209 , pp. 350-356
    • Perdew, G.1    Hord, N.2    Hollenback, C.3    Welsh, M.4
  • 37
    • 0001951209 scopus 로고    scopus 로고
    • The role of heat shock proteins in the regulation of steroid receptor function
    • In Freedman, LP, ed. Boston, Birkhäuser.
    • Picard D: 1997. The role of heat shock proteins in the regulation of steroid receptor function. In Freedman, LP, ed. The Molecular Biology of Steroid and Nuclear Hormone Receptors, pp 1-18. Boston, Birkhäuser.
    • (1997) The Molecular Biology of Steroid and Nuclear Hormone Receptors , pp. 1-18
    • Picard, D.1
  • 38
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt W, Toft D Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev. 18:1997;306-360.
    • (1997) Endocr Rev , vol.18 , pp. 306-360
    • Pratt, W.1    Toft, D.2
  • 39
    • 0031871101 scopus 로고    scopus 로고
    • Studies with purified chaperones advance understanding of the mechanism of glucocorticoid receptor-hsp90 heterocomplex assembly
    • Pratt W, Dittmar K Studies with purified chaperones advance understanding of the mechanism of glucocorticoid receptor-hsp90 heterocomplex assembly. Trends Endocrinol Metab. 9:1998;244-252.
    • (1998) Trends Endocrinol Metab , vol.9 , pp. 244-252
    • Pratt, W.1    Dittmar, K.2
  • 40
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the hsp90 molecular chaperone
    • Prodromou C, Roe S, O'Brien R, Ladbury J, Piper P, Pearl L Identification and structural characterization of the ATP/ADP-binding site in the hsp90 molecular chaperone. Cell. 90:1997;65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.2    O'Brien, R.3    Ladbury, J.4    Piper, P.5    Pearl, L.6
  • 41
    • 0027962531 scopus 로고
    • The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain
    • Radanyi C, Chambraud B, Baulieu E-E The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain. Proc Natl Acad Sci USA. 91:1994;11197-11201.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11197-11201
    • Radanyi, C.1    Chambraud, B.2    Baulieu E-E3
  • 42
    • 0030752373 scopus 로고    scopus 로고
    • ATP-binding properties of human hsp90
    • Scheibel T, Neuhofen S, Weikl Tet al. ATP-binding properties of human hsp90. J Biol Chem. 272:1997;18608-18613.
    • (1997) J Biol Chem , vol.272 , pp. 18608-18613
    • Scheibel, T.1    Neuhofen, S.2    Weikl, T.3
  • 43
    • 0032539709 scopus 로고    scopus 로고
    • Two chaperone sites in hsp90 differing in substrate specificity and ATP dependence
    • Scheibel T, Weikl T, Buchner J Two chaperone sites in hsp90 differing in substrate specificity and ATP dependence. Proc Natl Acad Sci. 95:1998;1495-1499.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 1495-1499
    • Scheibel, T.1    Weikl, T.2    Buchner, J.3
  • 44
    • 0029963674 scopus 로고    scopus 로고
    • Pharmacologic shifting of a balance between protein refolding and degradation mediated by hsp90
    • Schneider C, Sepp-Lorenzino L, Nimmesgern Eet al. Pharmacologic shifting of a balance between protein refolding and degradation mediated by hsp90. Proc Natl Acad Sci. 93:1996;14536-14541.
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 14536-14541
    • Schneider, C.1    Sepp-Lorenzino, L.2    Nimmesgern, E.3
  • 45
    • 0029813620 scopus 로고    scopus 로고
    • Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway
    • Schulte T, Blagosklonny M, Romanova Let al. Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway. Mol Cell Biol. 16:1996;5839-5845.
    • (1996) Mol Cell Biol , vol.16 , pp. 5839-5845
    • Schulte, T.1    Blagosklonny, M.2    Romanova, L.3
  • 46
    • 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. 272:1997;18694-18701.
    • (1997) J Biol Chem , vol.272 , pp. 18694-18701
    • Segnitz, B.1    Gehring, U.2
  • 47
    • 0030921056 scopus 로고    scopus 로고
    • Protein phosphatase 5 is a major component of glucocorticoid receptor-hsp90 complexes with properties of an FK506-binding immunophilin
    • Silverstein A, Galigniana M, Chen M-S, Owens-Grillo J, Chinkers M, Pratt W Protein phosphatase 5 is a major component of glucocorticoid receptor-hsp90 complexes with properties of an FK506-binding immunophilin. J Biol Chem. 272:1997;16224-16230.
    • (1997) J Biol Chem , vol.272 , pp. 16224-16230
    • Silverstein, A.1    Galigniana, M.2    Chen M-S3    Owens-Grillo, J.4    Chinkers, M.5    Pratt, W.6
  • 48
    • 0027484097 scopus 로고
    • Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes
    • Smith D Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol Endocrinol. 7:1993;1418-1429.
    • (1993) Mol Endocrinol , vol.7 , pp. 1418-1429
    • Smith, D.1
  • 49
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent
    • Smith D, Whitesell L, Naiar S, Chen S, Prapapanich V, Rimerman R Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol Cell Biol. 15:1995;6804-6812.
    • (1995) Mol Cell Biol , vol.15 , pp. 6804-6812
    • Smith, D.1    Whitesell, L.2    Naiar, S.3    Chen, S.4    Prapapanich, V.5    Rimerman, R.6
  • 50
    • 0028954475 scopus 로고
    • Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor
    • Song H, Dunbar J, Zhang Y, Guo D, Donner D Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J Biol Chem. 270:1995;3574-3581.
    • (1995) J Biol Chem , vol.270 , pp. 3574-3581
    • Song, H.1    Dunbar, J.2    Zhang, Y.3    Guo, D.4    Donner, D.5
  • 51
    • 0031054517 scopus 로고    scopus 로고
    • The hsp90-binding antibiotic geldenamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase
    • Stancato L, Silverstein A, Owens-Grillo J, Chow Y-H, Jove R, Pratt W The hsp90-binding antibiotic geldenamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase. J Biol Chem. 272:1997;4013-4020.
    • (1997) J Biol Chem , vol.272 , pp. 4013-4020
    • Stancato, L.1    Silverstein, A.2    Owens-Grillo, J.3    Chow Y-H4    Jove, R.5    Pratt, W.6
  • 52
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins C, Russo A, Schneider C, Rosen N, Hartl F, Pavletich N Crystal structure of an hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell. 89:1997;239-250.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.1    Russo, A.2    Schneider, C.3    Rosen, N.4    Hartl, F.5    Pavletich, N.6
  • 53
    • 0030938717 scopus 로고    scopus 로고
    • Nucleotides and two functional states of hsp90
    • Sullivan W, Stensgard B, Caucutt Get al. Nucleotides and two functional states of hsp90. J Biol Chem. 272:1997;8007-8012.
    • (1997) J Biol Chem , vol.272 , pp. 8007-8012
    • Sullivan, W.1    Stensgard, B.2    Caucutt, G.3
  • 54
    • 0027159830 scopus 로고
    • Biochemical and immunological evidence that an acidic domain of hsp90 is involved in the stabilization of untransformed glucocorticoid receptor complexes
    • Tbarka N, Richard-Mèreau C, Formstecher P, Dautrevaux M Biochemical and immunological evidence that an acidic domain of hsp90 is involved in the stabilization of untransformed glucocorticoid receptor complexes. FEBS Lett. 322:1993;125-128.
    • (1993) FEBS Lett , vol.322 , pp. 125-128
    • Tbarka, N.1    Richard-Mèreau, C.2    Formstecher, P.3    Dautrevaux, M.4
  • 55
    • 0030997120 scopus 로고    scopus 로고
    • Hsp90 is obligatory for the heme-regulated eIF-2α kinase to acquire and maintain an activable conformation
    • Uma S, Hartson S, Chen J-J, Matts R Hsp90 is obligatory for the heme-regulated eIF-2α kinase to acquire and maintain an activable conformation. J Biol Chem. 272:1997;11648-11656.
    • (1997) J Biol Chem , vol.272 , pp. 11648-11656
    • Uma, S.1    Hartson, S.2    Chen J-J3    Matts, R.4
  • 56
    • 0029973294 scopus 로고    scopus 로고
    • Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
    • Whitesell L, Cook P Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol Endocrinol. 10:1996;705-712.
    • (1996) Mol Endocrinol , vol.10 , pp. 705-712
    • Whitesell, L.1    Cook, P.2
  • 57
    • 0028064940 scopus 로고
    • v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA. 91:1994;8324-8328.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.2    Decosta, B.3    Myers, C.4    Neckers, L.5
  • 58
    • 0031438929 scopus 로고    scopus 로고
    • Sequence-specific and phosphorylation-dependent proline isomerization: A potential mitotic regulatory mechanism
    • Yaffe M, Schutkowski M, Shen Met al. Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. Science. 278:1997;1957-1960.
    • (1997) Science , vol.278 , pp. 1957-1960
    • Yaffe, M.1    Schutkowski, M.2    Shen, M.3
  • 59
    • 0030862486 scopus 로고    scopus 로고
    • In vitro evidence that hsp90 contains two independent chaperone sites
    • Young J, Schneider C, Hartl F In vitro evidence that hsp90 contains two independent chaperone sites. FEBS Lett. 418:1997;139-143.
    • (1997) FEBS Lett , vol.418 , pp. 139-143
    • Young, J.1    Schneider, C.2    Hartl, F.3


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