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Volumn 10, Issue 6, 2004, Pages 283-290

Therapeutic and diagnostic implications of Hsp90 activation

Author keywords

[No Author keywords available]

Indexed keywords

17 AMINOGELDANAMYCIN; ANTINEOPLASTIC AGENT; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 2642521990     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molmed.2004.04.006     Document Type: Review
Times cited : (249)

References (70)
  • 1
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • Isaacs J.S., et al. Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell. 3:2003;213-217
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1
  • 2
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt W.B., Toft D.O. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood). 228:2003;111-133
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 3
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte T.W., Neckers L.M. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother. Pharmacol. 42:1998;273-279
    • (1998) Cancer Chemother. Pharmacol. , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 4
    • 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., et al. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J. Biol. Chem. 276:2001;3702-3708
    • (2001) J. Biol. Chem. , vol.276 , pp. 3702-3708
    • Xu, W.1
  • 5
    • 0037075232 scopus 로고    scopus 로고
    • Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2
    • Basso A.D., et al. Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene. 21:2002;1159-1166
    • (2002) Oncogene , vol.21 , pp. 1159-1166
    • Basso, A.D.1
  • 6
    • 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 T.W., et al. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J. Biol. Chem. 270:1995;24585-24588
    • (1995) J. Biol. Chem. , vol.270 , pp. 24585-24588
    • Schulte, T.W.1
  • 7
    • 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 W.G., et al. 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. 11:2000;355-360
    • (2000) Cell Growth Differ. , vol.11 , pp. 355-360
    • An, W.G.1
  • 8
    • 0029145215 scopus 로고
    • Geldanamycin selectively destabilizes and conformationally alters mutated p53
    • Blagosklonny M.V., et al. Geldanamycin selectively destabilizes and conformationally alters mutated p53. Oncogene. 11:1995;933-939
    • (1995) Oncogene , vol.11 , pp. 933-939
    • Blagosklonny, M.V.1
  • 9
    • 0036494113 scopus 로고    scopus 로고
    • + lymphoma cells by the Hsp90 antagonist 17-allylamino,17-demethoxygeldanamycin
    • + lymphoma cells by the Hsp90 antagonist 17-allylamino, 17-demethoxygeldanamycin. Cancer Res. 62:2002;1559-1566
    • (2002) Cancer Res. , vol.62 , pp. 1559-1566
    • Bonvini, P.1
  • 10
    • 0141925960 scopus 로고    scopus 로고
    • FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases
    • Yao Q., et al. FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases. Clin. Cancer Res. 9:2003;4483-4493
    • (2003) Clin. Cancer Res. , vol.9 , pp. 4483-4493
    • Yao, Q.1
  • 11
    • 1642541150 scopus 로고    scopus 로고
    • 17-allylamino-17-demethoxygeldanamycin (17-AAG) is effective in down-regulating mutated, constitutively activated KIT protein in human mast cells
    • Fumo G., et al. 17-allylamino-17-demethoxygeldanamycin (17-AAG) is effective in down-regulating mutated, constitutively activated KIT protein in human mast cells. Blood. 103:2004;1078-1084
    • (2004) Blood , vol.103 , pp. 1078-1084
    • Fumo, G.1
  • 12
    • 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 D.B., 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. 8:2002;986-993
    • (2002) Clin. Cancer Res. , vol.8 , pp. 986-993
    • Solit, D.B.1
  • 13
    • 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
  • 14
    • 0025640051 scopus 로고
    • Reconstitution of progesterone receptor with heat shock proteins
    • Smith D.F., et al. Reconstitution of progesterone receptor with heat shock proteins. Mol. Endocrinol. 4:1990;1704-1711
    • (1990) Mol. Endocrinol. , vol.4 , pp. 1704-1711
    • Smith, D.F.1
  • 15
    • 0032484127 scopus 로고    scopus 로고
    • The assembly of progesterone receptor-hsp90 complexes using purified proteins
    • Kosano H., et al. The assembly of progesterone receptor-hsp90 complexes using purified proteins. J. Biol. Chem. 273:1998;32973-32979
    • (1998) J. Biol. Chem. , vol.273 , pp. 32973-32979
    • Kosano, H.1
  • 16
    • 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., et al. 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. U. S. A. 91:1994;8324-8328
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 8324-8328
    • Whitesell, L.1
  • 17
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C., et al. 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
  • 18
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins C.E., et al. 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.E.1
  • 19
    • 0032538995 scopus 로고    scopus 로고
    • In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis
    • Obermann W.M., et al. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J. Cell Biol. 143:1998;901-910
    • (1998) J. Cell Biol. , vol.143 , pp. 901-910
    • Obermann, W.M.1
  • 20
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou B., et al. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17:1998;4829-4836
    • (1998) EMBO J. , vol.17 , pp. 4829-4836
    • Panaretou, B.1
  • 21
    • 0033581021 scopus 로고    scopus 로고
    • The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes
    • Grenert J.P., et al. The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes. J. Biol. Chem. 274:1999;17525-17533
    • (1999) J. Biol. Chem. , vol.274 , pp. 17525-17533
    • Grenert, J.P.1
  • 22
    • 0028233833 scopus 로고
    • Depletion of the erbB-2 gene product p185 by benzoquinoid ansamycins
    • Miller P., et al. Depletion of the erbB-2 gene product p185 by benzoquinoid ansamycins. Cancer Res. 54:1994;2724-2730
    • (1994) Cancer Res. , vol.54 , pp. 2724-2730
    • Miller, P.1
  • 23
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
    • Mimnaugh E.G., et al. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem. 271:1996;22796-22801
    • (1996) J. Biol. Chem. , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1
  • 24
    • 0029056501 scopus 로고
    • Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent
    • Supko J.G., et al. Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent. Cancer Chemother. Pharmacol. 36:1995;305-315
    • (1995) Cancer Chemother. Pharmacol. , vol.36 , pp. 305-315
    • Supko, J.G.1
  • 25
    • 0038404927 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol
    • Solit D.B., et al. Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol. Cancer Res. 63:2003;2139-2144
    • (2003) Cancer Res. , vol.63 , pp. 2139-2144
    • Solit, D.B.1
  • 26
    • 0141596326 scopus 로고    scopus 로고
    • Clinical development of 17-allylamino, 17-demethoxygeldanamycin
    • Sausville E.A., et al. Clinical development of 17-allylamino, 17-demethoxygeldanamycin. Curr. Cancer Drug Targets. 3:2003;377-383
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 377-383
    • Sausville, E.A.1
  • 27
    • 0035071607 scopus 로고    scopus 로고
    • A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells
    • Chiosis G., et al. A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells. Chem. Biol. 8:2001;289-299
    • (2001) Chem. Biol. , vol.8 , pp. 289-299
    • Chiosis, G.1
  • 28
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumor selectivity on Hsp90 inhibitors
    • Kamal A., et al. A high-affinity conformation of Hsp90 confers tumor selectivity on Hsp90 inhibitors. Nature. 425:2003;407-410
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1
  • 29
    • 0029665779 scopus 로고    scopus 로고
    • Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Stepanova L., et al. Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev. 10:1996;1491-1502
    • (1996) Genes Dev. , vol.10 , pp. 1491-1502
    • Stepanova, L.1
  • 30
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta S.R., et al. Cellular survival: a play in three Akts. Genes Dev. 13:1999;2905-2927
    • (1999) Genes Dev. , vol.13 , pp. 2905-2927
    • Datta, S.R.1
  • 31
    • 0034771555 scopus 로고    scopus 로고
    • The Hsp90 inhibitor geldanamycin selectively sensitizes Bcr-Abl-expressing leukemia cells to cytotoxic chemotherapy
    • Blagosklonny M.V., et al. The Hsp90 inhibitor geldanamycin selectively sensitizes Bcr-Abl-expressing leukemia cells to cytotoxic chemotherapy. Leukemia. 15:2001;1537-1543
    • (2001) Leukemia , vol.15 , pp. 1537-1543
    • Blagosklonny, M.V.1
  • 32
    • 0035266132 scopus 로고    scopus 로고
    • Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lowers Bcr-Abl levels and induces apoptosis and differentiation of Bcr-Abl-positive human leukemic blasts
    • Nimmanapalli R., et al. Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lowers Bcr-Abl levels and induces apoptosis and differentiation of Bcr-Abl-positive human leukemic blasts. Cancer Res. 61:2001;1799-1804
    • (2001) Cancer Res. , vol.61 , pp. 1799-1804
    • Nimmanapalli, R.1
  • 33
    • 0037108448 scopus 로고    scopus 로고
    • BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90
    • Gorre M.E., et al. BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90. Blood. 100:2002;3041-3044
    • (2002) Blood , vol.100 , pp. 3041-3044
    • Gorre, M.E.1
  • 34
    • 0036339108 scopus 로고    scopus 로고
    • ErbB2 overexpression in an ovarian cancer cell line confers sensitivity to the HSP90 inhibitor geldanamycin
    • Smith V., et al. ErbB2 overexpression in an ovarian cancer cell line confers sensitivity to the HSP90 inhibitor geldanamycin. Anticancer Res. 22:2002;1993-1999
    • (2002) Anticancer Res. , vol.22 , pp. 1993-1999
    • Smith, V.1
  • 35
    • 0141729370 scopus 로고    scopus 로고
    • Physiologically-based pharmacokinetics and molecular pharmacodynamics of 17-(allylamino)-17-demethoxygeldanamycin and its active metabolite in tumor-bearing mice
    • Xu L., et al. Physiologically-based pharmacokinetics and molecular pharmacodynamics of 17-(allylamino)-17-demethoxygeldanamycin and its active metabolite in tumor-bearing mice. J. Pharmacokinet. Pharmacodyn. 30:2003;185-219
    • (2003) J. Pharmacokinet. Pharmacodyn. , vol.30 , pp. 185-219
    • Xu, L.1
  • 36
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • Ferrarini M., et al. Unusual expression and localization of heat-shock proteins in human tumor cells. Int. J. Cancer. 51:1992;613-619
    • (1992) Int. J. Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1
  • 37
    • 0028044818 scopus 로고
    • Differential expression of heat shock proteins in pancreatic carcinoma
    • Gress T.M., et al. Differential expression of heat shock proteins in pancreatic carcinoma. Cancer Res. 54:1994;547-551
    • (1994) Cancer Res. , vol.54 , pp. 547-551
    • Gress, T.M.1
  • 38
    • 0029849363 scopus 로고    scopus 로고
    • Expression and roles of heat shock proteins in human breast cancer
    • Yano M., et al. Expression and roles of heat shock proteins in human breast cancer. Jpn. J. Cancer Res. 87:1996;908-915
    • (1996) Jpn. J. Cancer Res. , vol.87 , pp. 908-915
    • Yano, M.1
  • 39
    • 0025287603 scopus 로고
    • Selective over-expression of mRNA coding for 90 KDa stress-protein in human ovarian cancer
    • Mileo A.M., et al. Selective over-expression of mRNA coding for 90 KDa stress-protein in human ovarian cancer. Anticancer Res. 10:1990;903-906
    • (1990) Anticancer Res. , vol.10 , pp. 903-906
    • Mileo, A.M.1
  • 40
    • 0034480623 scopus 로고    scopus 로고
    • Heat shock protein-90, IL-6 and IL-10 in bladder cancer
    • Cardillo M.R., et al. Heat shock protein-90, IL-6 and IL-10 in bladder cancer. Anticancer Res. 20:2000;4579-4583
    • (2000) Anticancer Res. , vol.20 , pp. 4579-4583
    • Cardillo, M.R.1
  • 41
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J., et al. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell. 94:1998;471-480
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1
  • 42
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto R.I. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12:1998;3788-3796
    • (1998) Genes Dev. , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 43
    • 0033890818 scopus 로고    scopus 로고
    • Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents
    • Bagatell R., et al. Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents. Clin. Cancer Res. 6:2000;3312-3318
    • (2000) Clin. Cancer Res. , vol.6 , pp. 3312-3318
    • Bagatell, R.1
  • 44
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe S.M., et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. 42:1999;260-266
    • (1999) J. Med. Chem. , vol.42 , pp. 260-266
    • Roe, S.M.1
  • 45
    • 0036718795 scopus 로고    scopus 로고
    • ATPases as drug targets: Learning from their structure
    • Chene P. ATPases as drug targets: learning from their structure. Nat. Rev. Drug Discov. 1:2002;665-673
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 665-673
    • Chene, P.1
  • 46
    • 0036836964 scopus 로고    scopus 로고
    • Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase
    • Chiosis G., et al. Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase. Bioorg. Med. Chem. 10:2002;3555-3564
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3555-3564
    • Chiosis, G.1
  • 47
    • 0347360283 scopus 로고    scopus 로고
    • Adenine derived inhibitors of the molecular chaperone HSP90-SAR explained through multiple X-ray structures
    • Dymock B., et al. Adenine derived inhibitors of the molecular chaperone HSP90-SAR explained through multiple X-ray structures. Bioorg. Med. Chem. Lett. 14:2004;325-328
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 325-328
    • Dymock, B.1
  • 48
    • 0141509074 scopus 로고    scopus 로고
    • Cancer: The rules of attraction
    • Neckers L., Lee Y.S. Cancer: the rules of attraction. Nature. 425:2003;357-359
    • (2003) Nature , vol.425 , pp. 357-359
    • Neckers, L.1    Lee, Y.S.2
  • 49
    • 0344511727 scopus 로고    scopus 로고
    • Crystal Structure and Molecular Modeling of 17-DMAG in Complex with Human Hsp90
    • Jez J.M., et al. Crystal Structure and Molecular Modeling of 17-DMAG in Complex with Human Hsp90. Chem. Biol. 10:2003;361-368
    • (2003) Chem. Biol. , vol.10 , pp. 361-368
    • Jez, J.M.1
  • 50
    • 0033081968 scopus 로고    scopus 로고
    • Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)- domain co-chaperones
    • Prodromou C., et al. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)- domain co-chaperones. EMBO J. 18:1999;754-762
    • (1999) EMBO J. , vol.18 , pp. 754-762
    • Prodromou, C.1
  • 51
    • 0036303385 scopus 로고    scopus 로고
    • Stimulation of the weak ATPase activity of human hsp90 by a client protein
    • McLaughlin S.H., et al. Stimulation of the weak ATPase activity of human hsp90 by a client protein. J. Mol. Biol. 315:2002;787-798
    • (2002) J. Mol. Biol. , vol.315 , pp. 787-798
    • McLaughlin, S.H.1
  • 52
    • 0742269688 scopus 로고    scopus 로고
    • The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)
    • Roe S.M., et al. The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell. 116:2004;87-98
    • (2004) Cell , vol.116 , pp. 87-98
    • Roe, S.M.1
  • 53
    • 0036931438 scopus 로고    scopus 로고
    • Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1
    • Panaretou B., et al. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol. Cell. 10:2002;1307-1318
    • (2002) Mol. Cell , vol.10 , pp. 1307-1318
    • Panaretou, B.1
  • 54
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of hsp90: Implications for ATP hydrolysis and client protein and cochaperone interactions
    • Meyer P., et al. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol. Cell. 11:2003;647-658
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1
  • 55
    • 0035134468 scopus 로고    scopus 로고
    • Quantitative immunohistochemical evaluation of HER2/neu expression with HercepTest™ in breast carcinoma by image analysis
    • Hatanaka Y., et al. Quantitative immunohistochemical evaluation of HER2/neu expression with HercepTest™ in breast carcinoma by image analysis. Pathol. Int. 51:2001;33-36
    • (2001) Pathol. Int. , vol.51 , pp. 33-36
    • Hatanaka, Y.1
  • 56
    • 0037174940 scopus 로고    scopus 로고
    • Radicicol-sensitive peptide binding to the N-terminal portion of GRP94
    • Vogen S., et al. Radicicol-sensitive peptide binding to the N-terminal portion of GRP94. J. Biol. Chem. 277:2002;40742-40750
    • (2002) J. Biol. Chem. , vol.277 , pp. 40742-40750
    • Vogen, S.1
  • 57
    • 0031193541 scopus 로고    scopus 로고
    • Induction of heat shock proteins by tyrosine kinase inhibitors in rat cardiomyocytes and myogenic cells confers protection against simulated ischemia
    • Conde A.G., et al. Induction of heat shock proteins by tyrosine kinase inhibitors in rat cardiomyocytes and myogenic cells confers protection against simulated ischemia. J. Mol. Cell. Cardiol. 29:1997;1927-1938
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , pp. 1927-1938
    • Conde, A.G.1
  • 58
    • 0032900282 scopus 로고    scopus 로고
    • Geldanamycin provides posttreatment protection against glutamate- induced oxidative toxicity in a mouse hippocampal cell line
    • Xiao N., et al. Geldanamycin provides posttreatment protection against glutamate- induced oxidative toxicity in a mouse hippocampal cell line. J. Neurochem. 72:1999;95-101
    • (1999) J. Neurochem. , vol.72 , pp. 95-101
    • Xiao, N.1
  • 59
    • 0036319568 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock proteins in brain and protects against focal cerebral ischemia
    • Lu A., et al. Geldanamycin induces heat shock proteins in brain and protects against focal cerebral ischemia. J. Neurochem. 81:2002;355-364
    • (2002) J. Neurochem. , vol.81 , pp. 355-364
    • Lu, A.1
  • 60
    • 0030035038 scopus 로고    scopus 로고
    • Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase
    • Hu J., Seeger C. Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase. Proc. Natl. Acad. Sci. U. S. A. 93:1996;1060-1064
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1060-1064
    • Hu, J.1    Seeger, C.2
  • 61
    • 0035923585 scopus 로고    scopus 로고
    • Host cell factor requirement for hepatitis C virus enzyme maturation
    • Waxman L., et al. Host cell factor requirement for hepatitis C virus enzyme maturation. Proc. Natl. Acad. Sci. U. S. A. 98:2001;13931-13935
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 13931-13935
    • Waxman, L.1
  • 62
    • 1442349120 scopus 로고    scopus 로고
    • Geldanamycin, a ligand of heat shock protein 90, inhibits the replication of herpes simplex virus type 1 in vitro
    • Li Y.H., et al. Geldanamycin, a ligand of heat shock protein 90, inhibits the replication of herpes simplex virus type 1 in vitro. Antimicrob. Agents Chemother. 48:2004;867-872
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 867-872
    • Li, Y.H.1
  • 63
    • 0034614455 scopus 로고    scopus 로고
    • Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription
    • O'Keeffe B., et al. Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription. J. Biol. Chem. 275:2000;279-287
    • (2000) J. Biol. Chem. , vol.275 , pp. 279-287
    • O'Keeffe, B.1
  • 64
    • 0034654091 scopus 로고    scopus 로고
    • Effects of geldanamycin, a heat-shock protein 90-binding agent, on T cell function and T cell nonreceptor protein tyrosine kinases
    • Yorgin P.D., et al. Effects of geldanamycin, a heat-shock protein 90-binding agent, on T cell function and T cell nonreceptor protein tyrosine kinases. J. Immunol. 164:2000;2915-2923
    • (2000) J. Immunol. , vol.164 , pp. 2915-2923
    • Yorgin, P.D.1
  • 65
    • 0032959003 scopus 로고    scopus 로고
    • Immunosuppressive effects of the heat shock protein 90-binding antibiotic geldanamycin
    • Sugita T., et al. Immunosuppressive effects of the heat shock protein 90-binding antibiotic geldanamycin. Biochem. Mol. Biol. Int. 47:1999;587-595
    • (1999) Biochem. Mol. Biol. Int. , vol.47 , pp. 587-595
    • Sugita, T.1
  • 66
    • 0037023741 scopus 로고    scopus 로고
    • Requirement for a hsp90 chaperone-dependent MEK1/2-ERK pathway for B cell antigen receptor-induced cyclin D2 expression in mature B lymphocytes
    • Piatelli M.J., et al. Requirement for a hsp90 chaperone-dependent MEK1/2-ERK pathway for B cell antigen receptor-induced cyclin D2 expression in mature B lymphocytes. J. Biol. Chem. 277:2002;12144-12150
    • (2002) J. Biol. Chem. , vol.277 , pp. 12144-12150
    • Piatelli, M.J.1
  • 67
    • 0035182221 scopus 로고    scopus 로고
    • Stress management - Heat shock protein-70 and the regulation of apoptosis
    • Beere H.M., Green D.R. Stress management - heat shock protein-70 and the regulation of apoptosis. Trends Cell Biol. 11:2001;6-10
    • (2001) Trends Cell Biol. , vol.11 , pp. 6-10
    • Beere, H.M.1    Green, D.R.2
  • 68
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler A., et al. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum. Mol. Genet. 10:2001;1307-1315
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A.1
  • 69
    • 0036852712 scopus 로고    scopus 로고
    • Pharmacological prevention of Parkinson disease in Drosophila
    • Auluck P.K., Bonini N.M. Pharmacological prevention of Parkinson disease in Drosophila. Nat. Med. 8:2002;1185-1186
    • (2002) Nat. Med. , vol.8 , pp. 1185-1186
    • Auluck, P.K.1    Bonini, N.M.2
  • 70
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford S.L., Lindquist S. Hsp90 as a capacitor for morphological evolution. Nature. 396:1998;336-342
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2


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