메뉴 건너뛰기




Volumn 5, Issue 10, 2005, Pages 761-772

HSP90 and the chaperoning of cancer

Author keywords

[No Author keywords available]

Indexed keywords

17 DEMETHOXY 17 ALLYLAMINOGELDANAMYCIN; ANSAMYCIN DERIVATIVE; BENZOQUINONE; BETA ZEARALENOL; BORTEZOMIB; CELL CYCLE PROTEIN 37; CHAPERONE; CISPLATIN; COUMAMYCIN; COUMARIN DERIVATIVE; CYTARABINE; CYTOSTATIC AGENT; CYTOTOXIC AGENT; DEPSIPEPTIDE; GELDANAMYCIN; GEMCITABINE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 90; HISTONE DEACETYLASE INHIBITOR; IMMUNOPHILIN; MACROLIDE; NOVOBIOCIN; PROTEIN P23; PROTEIN P50; PURINE DERIVATIVE; PYRAZOLE DERIVATIVE; RADICICOL; TAXANE DERIVATIVE; TRASTUZUMAB; UNCLASSIFIED DRUG; VORINOSTAT;

EID: 25844519550     PISSN: 1474175X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrc1716     Document Type: Review
Times cited : (2107)

References (148)
  • 2
    • 1642471825 scopus 로고    scopus 로고
    • Heat-shock proteins as regulators of apoptosis
    • Takayama, S., Reed, J. C. & Homma, S. Heat-shock proteins as regulators of apoptosis. Oncogene 22, 9041-9047 (2003).
    • (2003) Oncogene , vol.22 , pp. 9041-9047
    • Takayama, S.1    Reed, J.C.2    Homma, S.3
  • 4
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection
    • Morimoto, R. I. & Santoro, M. G. Stress-inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection. Nature Biotechnol. 16, 833-838 (1998).
    • (1998) Nature Biotechnol. , vol.16 , pp. 833-838
    • Morimoto, R.I.1    Santoro, M.G.2
  • 5
    • 0031018610 scopus 로고    scopus 로고
    • Heat shock response - Pathophysiological implications
    • Leppa, S. & Sistonen, L. Heat shock response - pathophysiological implications. Ann. Med. 29, 73-78 (1997).
    • (1997) Ann. Med. , vol.29 , pp. 73-78
    • Leppa, S.1    Sistonen, L.2
  • 6
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly, C. & Morimoto, R. I. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J. Natl. Cancer Inst. 92, 1564-1572 (2000).
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 7
    • 0032416104 scopus 로고    scopus 로고
    • Molecular chaperones: Biology and prospects for pharmacological intervention
    • Smith, D. F., Whitesell, L. & Katsanis, E. Molecular chaperones: biology and prospects for pharmacological intervention. Pharm. Rev. 50, 493-513 (1998).
    • (1998) Pharm. Rev. , vol.50 , pp. 493-513
    • Smith, D.F.1    Whitesell, L.2    Katsanis, E.3
  • 8
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 & Co. - A holding for folding
    • Buchner, J. Hsp90 & Co. - a holding for folding. Trends Biochem. Sci. 24, 136-141 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 136-141
    • Buchner, J.1
  • 9
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review
    • Csermely, P., Schnaider, T., Soti, C., Prohaskka, Z. & Nardai, G. The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 79, 129-168 (1998).
    • (1998) Pharmacol. Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaskka, Z.4    Nardai, G.5
  • 10
    • 0025175208 scopus 로고
    • Reduced levels of hsp90 compromise steroid receptor action in vivo
    • Picard, D. et al. Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature 348, 166-168 (1990).
    • (1990) Nature , vol.348 , pp. 166-168
    • Picard, D.1
  • 11
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman, B. C. & Yamamoto, K. R. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296, 2232-2235 (2002). Surprising evidence that chaperones not only have a role in regulating the activation of signal transduction pathways, but can also modulate cellular activities by assisting in the termination of transcriptional responses.
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 12
    • 0038466354 scopus 로고    scopus 로고
    • Tumor-derived, chaperone-rich cell lysate activates dendritic cells and elicits potent antitumor immunity
    • Zeng, Y., Feng, H., Graner, M. W. & Katsanis, E. Tumor-derived, chaperone-rich cell lysate activates dendritic cells and elicits potent antitumor immunity. Blood 101, 4485-4491 (2003).
    • (2003) Blood , vol.101 , pp. 4485-4491
    • Zeng, Y.1    Feng, H.2    Graner, M.W.3    Katsanis, E.4
  • 13
    • 19944425916 scopus 로고    scopus 로고
    • Heat shock proteins and their use as anticancer vaccines
    • Parmiani, G. et al. Heat shock proteins and their use as anticancer vaccines. Clin. Cancer Res. 10, 8142-8146 (2004).
    • (2004) Clin. Cancer Res. , vol.10 , pp. 8142-8146
    • Parmiani, G.1
  • 14
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent
    • Smith, D. F. et al. Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol. Cell. Biol. 15, 6804-6812 (1995). Describes the cyclical chaperone interactions that were shown in rabbit reticulocyte lysate to regulate the high affinity binding of hormone by steroid receptors and how this cycling is disrupted by geldanamycin.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6804-6812
    • Smith, D.F.1
  • 15
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • Nathan, D. E., Vos, M. H. & Lindquist, S. In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc. Natl Acad. Sci. USA 94, 12949-12956 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12949-12956
    • Nathan, D.E.1    Vos, M.H.2    Lindquist, S.3
  • 16
    • 0031895351 scopus 로고    scopus 로고
    • The hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
    • Pratt, W. B. The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc. Soc. Exp. Biol. Med. 217, 420-431 (1998).
    • (1998) Proc. Soc. Exp. Biol. Med. , vol.217 , pp. 420-431
    • Pratt, W.B.1
  • 17
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: An integrative map of physical and genetic interactions mediated by the hsp90 chaperone
    • Zhao, R. et al. Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120, 715-727 (2005).
    • (2005) Cell , vol.120 , pp. 715-727
    • Zhao, R.1
  • 18
    • 0037047429 scopus 로고    scopus 로고
    • Dynamic remodeling of transcription complexes by molecular chaperones
    • Morimoto, R. I. Dynamic remodeling of transcription complexes by molecular chaperones. Cell 110, 281-284 (2002).
    • (2002) Cell , vol.110 , pp. 281-284
    • Morimoto, R.I.1
  • 19
    • 0037228526 scopus 로고    scopus 로고
    • Evidence for an epigenetic mechanism by which Hsp90 acts as a capacitor for morphological evolution
    • Sollars, V. et al. Evidence for an epigenetic mechanism by which Hsp90 acts as a capacitor for morphological evolution. Nature Genet. 33, 70-74 (2003).
    • (2003) Nature Genet. , vol.33 , pp. 70-74
    • Sollars, V.1
  • 20
  • 21
    • 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, 336-342 (1998). Groundbreaking report that the chaperone function of HSP90 can buffer genetic variation in D. melanogaster, allowing it to accumulate silently until it is released in the face of environmental stress to be acted on by natural selection.
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 22
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor of phenotypic variation
    • Queitsch, C., Sangster, T. A. & Lindquist, S. Hsp90 as a capacitor of phenotypic variation. Nature 417, 618-624 (2002).
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3
  • 23
    • 0742287679 scopus 로고    scopus 로고
    • Waddington's widget: Hsp90 and the inheritance of acquired characters
    • Ruden, D. M., Garfinkel, M. D., Sollars, V. E. & Lu, X. Waddington's widget: Hsp90 and the inheritance of acquired characters. Semin. Cell Dev. Biol. 14, 301-310 (2003).
    • (2003) Semin. Cell Dev. Biol. , vol.14 , pp. 301-310
    • Ruden, D.M.1    Garfinkel, M.D.2    Sollars, V.E.3    Lu, X.4
  • 24
    • 1842782331 scopus 로고    scopus 로고
    • Under cover: Causes, effects and implications of Hsp90-mediated genetic capacitance
    • Sangster, T. A., Lindquist, S. & Queitsch, C. Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance. Bioessays 26, 348-362 (2004).
    • (2004) Bioessays , vol.26 , pp. 348-362
    • Sangster, T.A.1    Lindquist, S.2    Queitsch, C.3
  • 25
    • 0037379626 scopus 로고    scopus 로고
    • Between genotype and phenotype: Protein chaperones and evolvability
    • Rutherford, S. L. Between genotype and phenotype: protein chaperones and evolvability. Nature Rev. Genet. 4, 263-274 (2003).
    • (2003) Nature Rev. Genet. , vol.4 , pp. 263-274
    • Rutherford, S.L.1
  • 26
    • 4143095430 scopus 로고    scopus 로고
    • Altered Hsp90 function in cancer: A unique therapeutic opportunity
    • Bagatell, R. & Whitesell, L. Altered Hsp90 function in cancer: a unique therapeutic opportunity. Mol. Cancer Ther. 3, 1021-1030 (2004).
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 1021-1030
    • Bagatell, R.1    Whitesell, L.2
  • 27
    • 0141988694 scopus 로고    scopus 로고
    • An evolutionary model of carcinogenesis
    • Gatenby R. A. & Vincent, T. L. An evolutionary model of carcinogenesis. Cancer Res. 63, 6212-6220 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 6212-6220
    • Gatenby, R.A.1    Vincent, T.L.2
  • 28
    • 0027251913 scopus 로고
    • Correlation of the survival of ovarian cancer patients with mRNA expression of the 60kDa heat shock protein Hsp60
    • Kimura, E. et al. Correlation of the survival of ovarian cancer patients with mRNA expression of the 60kDa heat shock protein Hsp60. J. Clin. Oncol. 11, 891-898 (1993).
    • (1993) J. Clin. Oncol. , vol.11 , pp. 891-898
    • Kimura, E.1
  • 29
    • 0027503365 scopus 로고
    • Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: Prognostic implications
    • Ciocca, D. R. et al. Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: prognostic implications. J. Natl Cancer Inst. 85, 570-574 (1993).
    • (1993) J. Natl. Cancer Inst. , vol.85 , pp. 570-574
    • Ciocca, D.R.1
  • 30
    • 0032058966 scopus 로고    scopus 로고
    • Autoantibodies to the 90kDa heat shock protein and poor survival in breast cancer patients
    • Conroy, S. E., Sasieni, P. D., Fentiman, I. & Latchman, D. S. Autoantibodies to the 90kDa heat shock protein and poor survival in breast cancer patients. Eur. J. Cancer 34, 942-943 (1998).
    • (1998) Eur. J. Cancer , vol.34 , pp. 942-943
    • Conroy, S.E.1    Sasieni, P.D.2    Fentiman, I.3    Latchman, D.S.4
  • 31
    • 0028970484 scopus 로고
    • Differential expression of Mr 70, 000 heat shock protein in normal, premalignant, and malignant human uterine cervix
    • Ralhan, R. & Kaur, J. Differential expression of Mr 70, 000 heat shock protein in normal, premalignant, and malignant human uterine cervix. Clin. Cancer Res. 1, 1217-1222 (1995).
    • (1995) Clin. Cancer Res. , vol.1 , pp. 1217-1222
    • Ralhan, R.1    Kaur, J.2
  • 32
    • 0029642276 scopus 로고
    • Differential expression of 70-kDa heat shock-protein in human oral tumorigenesis
    • Kaur, J. & Ralhan, R. Differential expression of 70-kDa heat shock-protein in human oral tumorigenesis. Int. J. Cancer 63, 774-779 (1995).
    • (1995) Int. J. Cancer , vol.63 , pp. 774-779
    • Kaur, J.1    Ralhan, R.2
  • 33
    • 0030750217 scopus 로고    scopus 로고
    • Expression of heat shock protein 72 in renal cell carcinoma: Possible role and prognostic implications in cancer patients
    • Santarosa, M., Favaro, D., Quaia, M. & Galligioni, E. Expression of heat shock protein 72 in renal cell carcinoma: possible role and prognostic implications in cancer patients. Euro. J. Cancer. 33, 873-877 (1997).
    • (1997) Euro. J. Cancer. , vol.33 , pp. 873-877
    • Santarosa, M.1    Favaro, D.2    Quaia, M.3    Galligioni, E.4
  • 34
    • 0029011834 scopus 로고
    • Analysis of heat shock protein expression in myeloid leukaemia cells by flow cytometry
    • Chant, I. D., Rose, P. E. & Morris, A. G. Analysis of heat shock protein expression in myeloid leukaemia cells by flow cytometry. Br. J. Haematol. 90, 163-168 (1995).
    • (1995) Br. J. Haematol. , vol.90 , pp. 163-168
    • Chant, I.D.1    Rose, P.E.2    Morris, A.G.3
  • 35
    • 0026664393 scopus 로고
    • High constitutive expression of heat shock protein 90α in human acute leukemia cells
    • Yufu, Y., Nishimura, J. & Nawata, H. High constitutive expression of heat shock protein 90α in human acute leukemia cells. Leuk. Res. 16, 597-605 (1992).
    • (1992) Leuk. Res. , vol.16 , pp. 597-605
    • Yufu, Y.1    Nishimura, J.2    Nawata, H.3
  • 36
    • 0026544498 scopus 로고
    • Clinical and biological significance of Hsp90a in human breast cancer
    • Jameel, A. et al. Clinical and biological significance of Hsp90a in human breast cancer. Int. J. Cancer 50, 409-415 (1992).
    • (1992) Int. J. Cancer , vol.50 , pp. 409-415
    • Jameel, A.1
  • 37
    • 0029849363 scopus 로고    scopus 로고
    • Expression and roles of heat shock proteins in human breast cancer
    • Yano, M., Naito, Z., Tanaka, S. & Asano, G. Expression and roles of heat shock proteins in human breast cancer. Jpn. J. Cancer Res. 87, 908-915 (1996).
    • (1996) Jpn. J. Cancer Res. , vol.87 , pp. 908-915
    • Yano, M.1    Naito, Z.2    Tanaka, S.3    Asano, G.4
  • 38
    • 0031733457 scopus 로고    scopus 로고
    • Prognostic significance of heat shock proteins HSP70 and HSP90 in endometrial carcinomas
    • Nanbu, K. et al. Prognostic significance of heat shock proteins HSP70 and HSP90 in endometrial carcinomas. Cancer Detection & Prevention. 22, 549-555 (1998).
    • (1998) Cancer Detection & Prevention , vol.22 , pp. 549-555
    • Nanbu, K.1
  • 39
    • 0033988478 scopus 로고    scopus 로고
    • Antibodies to heat shock protein 90 in osteosarcoma patients correlate with response to neoadjuvant chemotherapy
    • Trieb, K. et al. Antibodies to heat shock protein 90 in osteosarcoma patients correlate with response to neoadjuvant chemotherapy. Br. J. Cancer 82, 85-87 (2000).
    • (2000) Br. J. Cancer , vol.82 , pp. 85-87
    • Trieb, K.1
  • 40
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • Mosser, D. D. & Morimoto, R. I. Molecular chaperones and the stress of oncogenesis. Oncogene 23, 2907-2918 (2004).
    • (2004) Oncogene , vol.23 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 41
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death: Survival proteins in cancer
    • Jaattela, M. Escaping cell death: survival proteins in cancer. Exp. Cell Res. 248, 30-43 (1999).
    • (1999) Exp. Cell Res. , vol.248 , pp. 30-43
    • Jaattela, M.1
  • 42
    • 0030999750 scopus 로고    scopus 로고
    • Apoptosis and the dilemma of cancer chemotherapy
    • Hannun, Y. Apoptosis and the dilemma of cancer chemotherapy. Blood 89, 1845-1853 (1997).
    • (1997) Blood , vol.89 , pp. 1845-1853
    • Hannun, Y.1
  • 43
    • 0030016274 scopus 로고    scopus 로고
    • Drug resistance against gemcitabine and topotecan mediated by constitutive hsp70 overexpression in vitro: Implication of quercetin as sensitiser in chemotherapy
    • Sliutz, G. et al. Drug resistance against gemcitabine and topotecan mediated by constitutive hsp70 overexpression in vitro: implication of quercetin as sensitiser in chemotherapy. Br. J. Cancer 74, 172-177 (1996).
    • (1996) Br. J. Cancer , vol.74 , pp. 172-177
    • Sliutz, G.1
  • 44
    • 0033830374 scopus 로고    scopus 로고
    • The chaperone function of hsp70 is required for protection against stress-induced apoptosis
    • Mosser, D. D. et al. The chaperone function of hsp70 is required for protection against stress-induced apoptosis. Mol. Cell. Biol. 20, 7146-7159 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7146-7159
    • Mosser, D.D.1
  • 45
    • 10944266160 scopus 로고    scopus 로고
    • Hsp72 inhibits apoptosis upstream of the mitochondria and not through interactions with Apaf-1
    • Steel, R. et al. et al. Hsp72 inhibits apoptosis upstream of the mitochondria and not through interactions with Apaf-1. J. Biol. Chem. 279, 51490-51499 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 51490-51499
    • Steel, R.1
  • 46
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • Mosser, D. D., Caron, A. W., Bourget, L., Denis-Larose, C. & Massie, B. Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol. Cell. Biol. 17, 5317-5327 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5317-5327
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 47
    • 0034608892 scopus 로고    scopus 로고
    • Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2
    • Nylandsted, J. et al. Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2. Proc. Natl Acad. Sci. USA 97, 7871-7876 (2000). Demonstrates differential requirements for HSP70 in the growth and survival of breast cancer cells compared with normal cells.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7871-7876
    • Nylandsted, J.1
  • 48
    • 14644435819 scopus 로고    scopus 로고
    • Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
    • Rohde, M. et al. Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev. 19, 570-582 (2005).
    • (2005) Genes Dev. , Issue.19 , pp. 570-582
    • Rohde, M.1
  • 49
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • Basso, A. D. et al. Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J. Biol. Chem. 277, 39858-39866 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 39858-39866
    • Basso, A.D.1
  • 50
    • 0037458627 scopus 로고    scopus 로고
    • Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis
    • Vanden Berghe, T., Kalai, M., van Loo, G., Declercq, W. & Vandenabeele, P. Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis. J. Biol. Chem. 278, 5622-5629 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 5622-5629
    • Vanden Berghe, T.1    Kalai, M.2    Van Loo, G.3    Declercq, W.4    Vandenabeele, P.5
  • 51
    • 0036187476 scopus 로고    scopus 로고
    • TNF-induced recruitment and activation of the IκK complex require Cdc37 and Hsp90
    • Chen, G., Cao, P. & Goeddel, D. V. TNF-induced recruitment and activation of the IκK complex require Cdc37 and Hsp90. Mol. Cell 9, 401-410 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 401-410
    • Chen, G.1    Cao, P.2    Goeddel, D.V.3
  • 52
    • 0033524442 scopus 로고    scopus 로고
    • Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90
    • Xu, Y., Singer, M. A. & Lindquist, S. Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90. Proc. Natl Acad. Sci. USA 96, 109-114 (1999).
    • (1999) Proc. Natl. Sci. USA , vol.96 , pp. 109-114
    • Xu, Y.1    Singer, M.A.2    Lindquist, S.3
  • 53
    • 0019485241 scopus 로고
    • A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein
    • Oppermann, H., Levinson, W. & Bishop, J. M. A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein. Proc. Natl Acad. Sci. USA 78, 1067-1071 (1981).
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 1067-1071
    • Oppermann, H.1    Levinson, W.2    Bishop, J.M.3
  • 54
    • 0020661643 scopus 로고
    • Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: Analysis of the turnover and distribution of this complex
    • Brugge, J., Yonemoto, W. & Darrow, D. Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: analysis of the turnover and distribution of this complex. Mol. Cell. Biol. 3, 9-19 (1983).
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 9-19
    • Brugge, J.1    Yonemoto, W.2    Darrow, D.3
  • 55
    • 0027291238 scopus 로고
    • Heat-shock protein hsp90 governs the activity of pp60vsrc kinase
    • Xu, Y. & Lindquist, S. Heat-shock protein hsp90 governs the activity of pp60vsrc kinase. Proc. Natl Acad. Sci. USA 90, 7074-7078 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7074-7078
    • Xu, Y.1    Lindquist, S.2
  • 56
    • 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, E. G., De Costa, B., Myers, C. E. & Neckers, L. M. 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 91, 8324-8328 (1994). Identification of geldanamycin as the first small-molecule inhibitor of HSP90 chaperone function.
    • (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
  • 57
    • 10344243547 scopus 로고    scopus 로고
    • Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures
    • Muller, L., Schaupp, A., Walerych, D., Wegele, H. & Buchner, J. Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures. J. Biol. Chem. 279, 48846-48854 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 48846-48854
    • Muller, L.1    Schaupp, A.2    Walerych, D.3    Wegele, H.4    Buchner, J.5
  • 58
    • 10344239940 scopus 로고    scopus 로고
    • Hsp90 chaperones wild-type p53 tumor suppressor protein
    • Walerych, D. et al. Hsp90 chaperones wild-type p53 tumor suppressor protein. J. Biol. Chem. 279, 48836-48845 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 48836-48845
    • Walerych, D.1
  • 59
    • 0031909866 scopus 로고    scopus 로고
    • The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent
    • Whitesell, L., Sutphin, P. D., Pulcini, E. J., Martinez, J. D. & Cook, P. H. The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent. Mol. Cell. Biol. 18, 1517-1524 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1517-1524
    • Whitesell, L.1    Sutphin, P.D.2    Pulcini, E.J.3    Martinez, J.D.4    Cook, P.H.5
  • 60
    • 0029737509 scopus 로고    scopus 로고
    • Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90
    • Blagosklonny, M. V., Toretsky, J., Bohen, S. & Neckers, L. Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90. Proc. Natl Acad. Sci. USA 93, 8379-8383 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 61
    • 15844363948 scopus 로고    scopus 로고
    • Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell
    • Sepehrnia, B., Paz, I. B., Dasgupta, G. & Momand, J. Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell. J. Biol. Chem. 271, 15084-15090 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 15084-15090
    • Sepehrnia, B.1    Paz, I.B.2    Dasgupta, G.3    Momand, J.4
  • 62
    • 1642268986 scopus 로고    scopus 로고
    • Hsp90 isoforms: Functions, expression and clinical importance
    • Sreedhar, A. S., Kalmar, E., Csermely, P. & Shen, Y. F. Hsp90 isoforms: functions, expression and clinical importance. FEBS Lett. 562, 11-15 (2004).
    • (2004) FEBS Lett. , vol.562 , pp. 11-15
    • Sreedhar, A.S.1    Kalmar, E.2    Csermely, P.3    Shen, Y.F.4
  • 63
    • 2942716692 scopus 로고    scopus 로고
    • Functional proteomic screens reveal an essential extracellular role for hsp90 α in cancer cell invasiveness
    • Eustace, B. K. et al. Functional proteomic screens reveal an essential extracellular role for hsp90 α in cancer cell invasiveness. Nature Cell Biol. 6, 507-514 (2004).
    • (2004) Nature Cell Biol. , vol.6 , pp. 507-514
    • Eustace, B.K.1
  • 64
    • 0037040975 scopus 로고    scopus 로고
    • The role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation
    • Grammatikakis, N. et al. The role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation. J. Biol. Chem. 277, 8312-8320 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 8312-8320
    • Grammatikakis, N.1
  • 65
    • 0035718899 scopus 로고    scopus 로고
    • Structure, function, and mechanism of the Hsp90 molecular chaperone
    • Pearl, L. H. & Prodromou, C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv. Protein Chem. 59, 157-186 (2001).
    • (2001) Adv. Protein Chem. , vol.59 , pp. 157-186
    • Pearl, L.H.1    Prodromou, C.2
  • 66
    • 0141596939 scopus 로고    scopus 로고
    • Structure and functional relationships of Hsp90
    • Prodromou, C. & Pearl, L. H. Structure and functional relationships of Hsp90. Curr. Cancer Drug Targets 3, 301-323 (2003).
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 301-323
    • Prodromou, C.1    Pearl, L.H.2
  • 67
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an hsp90-geldanamycin complex: Targeting of a protein chaperone by an anti-tumor agent
    • Stebbins, C. E. et al. Crystal structure of an hsp90-geldanamycin complex: targeting of a protein chaperone by an anti-tumor agent. Cell 89, 239-250 (1997).
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1
  • 68
    • 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, 65-75 (1997). Identification and characterization of the binding pocket for geldanamycin on HSP90 as an atypical ATPase site.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1
  • 69
    • 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, 647-658 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1
  • 70
    • 17044403753 scopus 로고    scopus 로고
    • Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding
    • Huai, Q. et al. Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding. Structure (Camb) 13, 579-590 (2005).
    • (2005) Structure (Camb) , vol.13 , pp. 579-590
    • Huai, Q.1
  • 71
    • 2942533020 scopus 로고    scopus 로고
    • The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site
    • Harris, S. F., Shiau, A. K. & Agard, D. A. The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure (Camb) 12, 1087-1097 (2004).
    • (2004) Structure (Camb) , vol.12 , pp. 1087-1097
    • Harris, S.F.1    Shiau, A.K.2    Agard, D.A.3
  • 72
    • 0033985080 scopus 로고    scopus 로고
    • GHKL, an emergent ATPase/kinase superfamily
    • Dutta, R. & Inouye, M. GHKL, an emergent ATPase/kinase superfamily. Trends Biochem. Sci. 25, 24-28 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 24-28
    • Dutta, R.1    Inouye, M.2
  • 73
    • 7944225978 scopus 로고    scopus 로고
    • Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform
    • McLaughlin, S. H., Ventouras, L. A., Lobbezoo, B. & Jackson, S. E. Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform. J. Mol. Biol. 344, 813-826 (2004). Biophysical evidence for an alternative to the 'molecular clamp' model of HSP90 chaperoning action.
    • (2004) J. Mol. Biol. , vol.344 , pp. 813-826
    • McLaughlin, S.H.1    Ventouras, L.A.2    Lobbezoo, B.3    Jackson, S.E.4
  • 74
    • 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, 87-98 (2004).
    • (2004) Cell , vol.116 , pp. 87-98
    • Roe, S.M.1
  • 75
    • 12344291243 scopus 로고    scopus 로고
    • Hsp90 and Cdc37 - A chaperone cancer conspiracy
    • Pearl, L. H. Hsp90 and Cdc37 - a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 15, 55-61 (2005).
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 55-61
    • Pearl, L.H.1
  • 76
    • 0036510547 scopus 로고    scopus 로고
    • A nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90
    • Soti, C., Racz, A. & Csermely, P. A nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. J. Biol. Chem. 277, 7066-7075 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 7066-7075
    • Soti, C.1    Racz, A.2    Csermely, P.3
  • 77
    • 10744221887 scopus 로고    scopus 로고
    • Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery
    • Meyer, P. et al. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. Embo J. 3, 511-519 (2004).
    • (2004) Embo J. , vol.3 , pp. 511-519
    • Meyer, P.1
  • 78
    • 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, 1307-1318 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 1307-1318
    • Panaretou, B.1
  • 79
    • 18544386399 scopus 로고    scopus 로고
    • Binding of ATP to heat shock protein 90: Evidence for an ATP-binding site in the C-terminal domain
    • Garnier, C. et al. Binding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domain. J. Biol. Chem. 277, 12208-12214 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 12208-12214
    • Garnier, C.1
  • 80
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler, C. et al. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199-210 (2000). Structural elucidation of how multichaperone complexes can be formed by adapter proteins.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1
  • 81
    • 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, 754-762 (1999).
    • (1999) Embo J. , vol.18 , pp. 754-762
    • Prodromou, C.1
  • 82
    • 3242893125 scopus 로고    scopus 로고
    • Quantum chemical calculations and mutational analysis suggest heat shock protein 90 catalyzes trans-cis isomerization of geldanamycin
    • Lee, Y. S., Marcu, M. G. & Neckers, L. Quantum chemical calculations and mutational analysis suggest heat shock protein 90 catalyzes trans-cis isomerization of geldanamycin. Chem. Biol. 11, 991-998 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 991-998
    • Lee, Y.S.1    Marcu, M.G.2    Neckers, L.3
  • 83
    • 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, 260-266 (1999).
    • (1999) J. Med. Chem. , vol.42 , pp. 260-266
    • Roe, S.M.1
  • 84
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu, W. et al. Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc. Natl Acad. Sci. USA 99, 12847-12852 (2002). Identification of a mechanism by which chaperone interactions regulate the cellular level of a receptor-linked tyrosine kinase.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12847-12852
    • Xu, W.1
  • 85
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: Interactions with a steroid receptor and a protein kinase
    • Nathan, D. F. & Lindquist, S. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15, 3917-3925 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 86
    • 0034015979 scopus 로고    scopus 로고
    • A transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in Caenorhabditis elegans
    • Birnby, D. A. et al. A transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in Caenorhabditis elegans. Genetics 155, 85-104 (2000).
    • (2000) Genetics , vol.155 , pp. 85-104
    • Birnby, D.A.1
  • 87
    • 0032980876 scopus 로고    scopus 로고
    • Genetic analysis of viable Hsp90 alleles reveals a critical role in Drosophila spermatogenesis
    • Yue, L. et al. Genetic analysis of viable Hsp90 alleles reveals a critical role in Drosophila spermatogenesis. Genetics 151, 1065-1079 (1999).
    • (1999) Genetics , vol.151 , pp. 1065-1079
    • Yue, L.1
  • 88
    • 0036735298 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 inhibits human myeloma cell growth in vivo and prolongs survival in a murine model
    • LeBlanc, R. et al. Proteasome inhibitor PS-341 inhibits human myeloma cell growth in vivo and prolongs survival in a murine model. Cancer Res. 62, 4996-5000 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 4996-5000
    • Leblanc, R.1
  • 89
    • 16644376293 scopus 로고    scopus 로고
    • Development of a fluorescence polarization assay for the molecular chaperone Hsp90
    • Kim, J. et al. Development of a fluorescence polarization assay for the molecular chaperone Hsp90. J. Biomol. Screen. 9, 375-381 (2004).
    • (2004) J. Biomol. Screen. , vol.9 , pp. 375-381
    • Kim, J.1
  • 90
    • 2642521990 scopus 로고    scopus 로고
    • Therapeutic and diagnostic implications of Hsp90 activation
    • Kamal, A., Boehm, M. F. & Burrows, F. J. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol. Med. 10, 283-290 (2004).
    • (2004) Trends Mol. Med. , vol.10 , pp. 283-290
    • Kamal, A.1    Boehm, M.F.2    Burrows, F.J.3
  • 91
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal, A. et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 425, 407-410 (2003). First evidence that HSP90 in tumour cells is found in multimolecular complexes with higher affinity for 17AAG than the largely uncomplexed HSP90 found in normal cells. This paper provides a biochemical explanation for why a useful therapeutic index might exist for HSP90 inhibitors.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1
  • 92
    • 1142273472 scopus 로고    scopus 로고
    • Altered states: Selectively drugging the Hsp90 cancer chaperone
    • Workman, P. Altered states: selectively drugging the Hsp90 cancer chaperone. Trends Mol. Med. 10, 47-51 (2004).
    • (2004) Trends Mol. Med. , vol.10 , pp. 47-51
    • Workman, P.1
  • 93
    • 3042656869 scopus 로고    scopus 로고
    • Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions
    • Yun, B. G., Huang, W., Leach, N., Hartson, S. D. & Matts, R. L. Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions. Biochemistry 43, 8217-8229 (2004).
    • (2004) Biochemistry , vol.43 , pp. 8217-8229
    • Yun, B.G.1    Huang, W.2    Leach, N.3    Hartson, S.D.4    Matts, R.L.5
  • 94
    • 0034594644 scopus 로고    scopus 로고
    • Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins
    • Marcu, M. G., Schulte, T. W. & Neckers, L. Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J. Natl Cancer Inst. 92, 242-248 (2000).
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 242-248
    • Marcu, M.G.1    Schulte, T.W.2    Neckers, L.3
  • 95
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the C-terminus of the chaperone
    • Marcu, M. G., Chadli, A., Bouhouche, I., Catelli, M. & Neckers, L. M. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the C-terminus of the chaperone. J. Biol. Chem. 275, 37181-37186 (2000). Biochemical evidence for a second, cryptic ATP-binding site in HSP90 that binds the antibiotic novobiocin, albeit with very low affinity.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 96
    • 0033231024 scopus 로고    scopus 로고
    • A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90
    • Itoh, H. et al. A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90. Biochem. J. 343, 697-703 (1999).
    • (1999) Biochem. J. , vol.343 , pp. 697-703
    • Itoh, H.1
  • 97
    • 10744220096 scopus 로고    scopus 로고
    • The heat shock protein 90-targeting drug cisplatin selectively inhibits steroid receptor activation
    • Rosenhagen, M. C. et al. The heat shock protein 90-targeting drug cisplatin selectively inhibits steroid receptor activation. Mol. Endocrinol. 17, 1991-2001 (2003).
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1991-2001
    • Rosenhagen, M.C.1
  • 98
    • 0029664590 scopus 로고    scopus 로고
    • Cell-cycle arrest and p53 accumulation induced by geldanamycin in human ovarian tumour cells
    • McIlwrath, A. J., Brunton, V. G. & Brown, R. Cell-cycle arrest and p53 accumulation induced by geldanamycin in human ovarian tumour cells. Cancer Chemother. Pharmacol. 37, 423-428 (1996).
    • (1996) Cancer Chemother. Pharmacol. , vol.37 , pp. 423-428
    • McIlwrath, A.J.1    Brunton, V.G.2    Brown, R.3
  • 99
    • 7544243762 scopus 로고    scopus 로고
    • Geldanamycin induces mitotic catastrophe and subsequent apoptosis in human glioma cells
    • Nomura, M. et al. Geldanamycin induces mitotic catastrophe and subsequent apoptosis in human glioma cells. J. Cell. Physiol. 201, 374-384 (2004).
    • (2004) J. Cell. Physiol. , vol.201 , pp. 374-384
    • Nomura, M.1
  • 100
    • 0034660856 scopus 로고    scopus 로고
    • Inhibition of Hsp90 function by ansamycins causes retinoblastoma gene product-dependent G1 arrest
    • Srethapakdi, M., Liu, F., Tavorath, R. & Rosen, N. Inhibition of Hsp90 function by ansamycins causes retinoblastoma gene product-dependent G1 arrest. Cancer Res. 60, 3940-3946 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 3940-3946
    • Srethapakdi, M.1    Liu, F.2    Tavorath, R.3    Rosen, N.4
  • 101
    • 0035872442 scopus 로고    scopus 로고
    • Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis
    • Hostein, I., Robertson, D., DiStefano, F., Workman, P. & Clarke, P. A. Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17- demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res. 61, 4003-4009 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 4003-4009
    • Hostein, I.1    Robertson, D.2    DiStefano, F.3    Workman, P.4    Clarke, P.A.5
  • 102
    • 10344225631 scopus 로고    scopus 로고
    • Hsp90 inhibitors deplete key anti-apoptotic proteins in pediatric solid tumor cells and demonstrate synergistic anticancer activity with cisplatin
    • Bagatell, R., Beliakoff, J., David, C. L., Marron, M. T. & Whitesell, L. Hsp90 inhibitors deplete key anti-apoptotic proteins in pediatric solid tumor cells and demonstrate synergistic anticancer activity with cisplatin. Int. J. Cancer 113, 179-188 (2005).
    • (2005) Int. J. Cancer , vol.113 , pp. 179-188
    • Bagatell, R.1    Beliakoff, J.2    David, C.L.3    Marron, M.T.4    Whitesell, L.5
  • 104
    • 0034886833 scopus 로고    scopus 로고
    • Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: Sequence and tumor biology matters
    • See: E. A. Sausville, Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: sequence and tumor biology matters, Clin. Cancer Res. 7, 2155-2158 (2001).
    • (2001) Clin. Cancer Res. , vol.7 , pp. 2155-2158
    • Sausville, E.A.1
  • 105
    • 0034890377 scopus 로고    scopus 로고
    • Clin. Cancer Res. 7, 2228-2236 (2001). Evidence for the ability of HSP90 inhibitors to increase the anticancer activity of cytotoxic chemotherapeutic agents.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 2228-2236
  • 106
    • 0037075232 scopus 로고    scopus 로고
    • Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2
    • Basso, A. D., Solit, D. B., Munster, P. N. & Rosen, N. Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene 21, 1159-1166 (2002).
    • (2002) Oncogene , vol.21 , pp. 1159-1166
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 107
    • 0141819961 scopus 로고    scopus 로고
    • Genes and proteins governing the cellular sensitivity to HSP90 inhibitors: A mechanistic perspective
    • Maloney, A., Clarke, P. A. & Workman, P. Genes and proteins governing the cellular sensitivity to HSP90 inhibitors: a mechanistic perspective. Curr. Cancer Drug Targets 3, 331-341 (2003).
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 331-341
    • Maloney, A.1    Clarke, P.A.2    Workman, P.3
  • 108
    • 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., Ellwood-Yen, K., Chiosis, G., Rosen, N. & Sawyers, C. L. 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, 3041-3044 (2002). Clinical BCR-ABL mutations that render the kinase resistant to the active site inhibitor imatinib (Glivec) remain HSP90-dependent and, as a result, quite sensitive to geldanamycin-stimulated degradation. Such a lack of cross-resistance provides the rationale for current clinical studies of 17AAG in imatinib-resistant patients.
    • (2002) Blood , vol.100 , pp. 3041-3044
    • Gorre, M.E.1    Ellwood-Yen, K.2    Chiosis, G.3    Rosen, N.4    Sawyers, C.L.5
  • 109
    • 2342625412 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal degradation of nucleophosmin-anaplastic lymphoma kinase induced by 17-allylamino-demethoxygeldanamycin: Role of the co-chaperone carboxyl heat shock protein 70-interacting protein
    • Bonvini, P., Dalla Rosa, H., Vignes, N. & Rosolen, A. Ubiquitination and proteasomal degradation of nucleophosmin-anaplastic lymphoma kinase induced by 17-allylamino-demethoxygeldanamycin: role of the co-chaperone carboxyl heat shock protein 70-interacting protein. Cancer Res. 64, 3256-3264 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 3256-3264
    • Bonvini, P.1    Dalla Rosa, H.2    Vignes, N.3    Rosolen, A.4
  • 110
    • 0142188139 scopus 로고    scopus 로고
    • Hormone-refractory breast cancer remains sensitive to the antitumor activity of heat shock protein 90 inhibitors
    • Beliakoff, J. et al. Hormone-refractory breast cancer remains sensitive to the antitumor activity of heat shock protein 90 inhibitors. Clin. Cancer Res. 9, 4961-4971 (2003).
    • (2003) Clin. Cancer Res. , vol.9 , pp. 4961-4971
    • Beliakoff, J.1
  • 111
    • 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, 986-993 (2002).
    • (2002) Clin. Cancer Res. , vol.8 , pp. 986-993
    • Solit, D.B.1
  • 112
    • 0036606332 scopus 로고    scopus 로고
    • Degradation of HER2 by ansamycins induces growth arrest and apoptosis in cells with HER2 overexpression via a HER3, phosphatidylinositol 3′-kinase-AKT-dependent pathway
    • Munster, P. N., Marchion, D. C., Basso, A. D. & Rosen, N. Degradation of HER2 by ansamycins induces growth arrest and apoptosis in cells with HER2 overexpression via a HER3, phosphatidylinositol 3′-kinase-AKT-dependent pathway. Cancer Res. 62, 3132-3137 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 3132-3137
    • Munster, P.N.1    Marchion, D.C.2    Basso, A.D.3    Rosen, N.4
  • 113
    • 0038404927 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function down-regulates akt kinase and sensitizes tumors to taxol
    • Solit, D. B., Basso, A. D., Olshen, A. B., Scher, H. I. & Rosen, N. Inhibition of heat shock protein 90 function down-regulates akt kinase and sensitizes tumors to taxol. Cancer Res. 63, 2139-2144 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 2139-2144
    • Solit, D.B.1    Basso, A.D.2    Olshen, A.B.3    Scher, H.I.4    Rosen, N.5
  • 114
    • 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, 3312-3318 (2000).
    • (2000) Clin. Cancer Res. , vol.6 , pp. 3312-3318
    • Bagatell, R.1
  • 115
    • 0034710542 scopus 로고    scopus 로고
    • Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone
    • Clarke, P. A. et al. Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17- demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone. Oncogene. 19, 4125-4133 (2000).
    • (2000) Oncogene , vol.19 , pp. 4125-4133
    • Clarke, P.A.1
  • 116
    • 1942485334 scopus 로고    scopus 로고
    • 17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models
    • Burger, A. M., Fiebig, H. H., Stinson, S. F. & Sausville, E. A. 17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models. Anticancer Drugs 15, 377-387 (2004).
    • (2004) Anticancer Drugs , vol.15 , pp. 377-387
    • Burger, A.M.1    Fiebig, H.H.2    Stinson, S.F.3    Sausville, E.A.4
  • 117
    • 0036319568 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock proteins in brain and protects against focal cerebral ischemia
    • Lu, A., Ran, R., Parmentier-Batteur, S., Nee, A. & Sharp, F. R. Geldanamycin induces heat shock proteins in brain and protects against focal cerebral ischemia. J. Neurochem. 81, 355-364 (2002).
    • (2002) J. Neurochem. , vol.81 , pp. 355-364
    • Lu, A.1    Ran, R.2    Parmentier-Batteur, S.3    Nee, A.4    Sharp, F.R.5
  • 118
    • 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, 1307-1315 (2001).
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A.1
  • 119
    • 13244267202 scopus 로고    scopus 로고
    • Mechanisms of suppression of α-synuclein neurotoxicity by geldanamycin in Drosophila
    • Auluck, P. K., Meulener, M. C. & Bonini, N. M. Mechanisms of suppression of α-synuclein neurotoxicity by geldanamycin in Drosophila. J. Biol. Chem. 280, 2873-2878 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 2873-2878
    • Auluck, P.K.1    Meulener, M.C.2    Bonini, N.M.3
  • 120
    • 0034743361 scopus 로고    scopus 로고
    • Plasma pharmacokinetics and tissue distribution of 17-(allylamino)-17- demethoxygeldanamycin (NSC 330507) in CD2F1 mice1
    • Egorin, M. J. et al. Plasma pharmacokinetics and tissue distribution of 17-(allylamino)-17-demethoxygeldanamycin (NSC 330507) in CD2F1 mice1. Cancer Chemother. Pharmacol. 47, 291-302 (2001).
    • (2001) Cancer Chemother. Pharmacol. , vol.47 , pp. 291-302
    • Egorin, M.J.1
  • 121
    • 0033579175 scopus 로고    scopus 로고
    • DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90
    • Kelland, L. R., Sharp, S. Y., Rogers, P. M., Myers, T. G. & Workman, P. DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J. Natl Cancer Inst. 91, 1940-1949 (1999).
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 122
    • 20044384168 scopus 로고    scopus 로고
    • Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer
    • Goetz, M. P. et al. Phase I trial of 17-allylamino-17- demethoxygeldanamycin in patients with advanced cancer. J. Clin. Oncol. 23, 1078-1087 (2005).
    • (2005) J. Clin. Oncol. , vol.23 , pp. 1078-1087
    • Goetz, M.P.1
  • 123
  • 124
    • 20144375312 scopus 로고    scopus 로고
    • Phase I and pharmacologic study of 17-(allylamino)-17- demethoxygeldanamycin in adult patients with solid tumors
    • Grem, J. L. et al. Phase I and pharmacologic study of 17-(allylamino)-17-demethoxygeldanamycin in adult patients with solid tumors. J. Clin. Oncol. 23, 1885-1893 (2005).
    • (2005) J. Clin. Oncol. , vol.23 , pp. 1885-1893
    • Grem, J.L.1
  • 125
    • 23044441106 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies
    • Banerji, U. et al. Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. J. Clin. Oncol. 23, 4152-4161 (2005). Report of a phase I trial of 17AAG demonstrating the modulation of HSP90 function by systemically tolerable drug exposures and the stabilization of disease in two melanoma patients.
    • (2005) J. Clin. Oncol. , vol.23 , pp. 4152-4161
    • Banerji, U.1
  • 126
    • 0346995281 scopus 로고    scopus 로고
    • Combination treatment with 17-N-allylamino-17-demethoxy geldanamycin and acute irradiation produces supra-additive growth suppression in human prostate carcinoma spheroids
    • Enmon, R. et al. Combination treatment with 17-N-allylamino-17-demethoxy geldanamycin and acute irradiation produces supra-additive growth suppression in human prostate carcinoma spheroids. Cancer Res. 63, 8393-8399 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 8393-8399
    • Enmon, R.1
  • 127
    • 9144261127 scopus 로고    scopus 로고
    • Geldanamycin and 17-allylamino-17-demethoxygeldanamycin potentiate the in vitro and in vivo radiation response of cervical tumor cells via the heat shock protein 90-mediated intracellular signaling and cytotoxicity
    • Bisht, K. S. et al. Geldanamycin and 17-allylamino-17- demethoxygeldanamycin potentiate the in vitro and in vivo radiation response of cervical tumor cells via the heat shock protein 90-mediated intracellular signaling and cytotoxicity. Cancer Res. 63, 8984-8995 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 8984-8995
    • Bisht, K.S.1
  • 128
    • 4143105237 scopus 로고    scopus 로고
    • Geldanamycin enhances cisplatin cytotoxicity through loss of Akt activation in A549 cells
    • McCollum, A., Toft, D. O. & Erlichman, C. Geldanamycin enhances cisplatin cytotoxicity through loss of Akt activation in A549 cells. Clin. Cancer Res. 9 (Suppl.), 6178 (2003).
    • (2003) Clin. Cancer Res. , vol.9 , Issue.SUPPL. , pp. 6178
    • McCollum, A.1    Toft, D.O.2    Erlichman, C.3
  • 129
    • 0038069088 scopus 로고    scopus 로고
    • Geldanamycin and its 17-allylamino-17-demethoxy analogue antagonize the action of cisplatin in human colon adenocarcinoma cells: Differential caspase activation as a basis for interaction
    • Vasilevskaya, I. A., Rakitina, T. V. & O'Dwyer, P. J. Geldanamycin and its 17-allylamino-17-demethoxy analogue antagonize the action of cisplatin in human colon adenocarcinoma cells: differential caspase activation as a basis for interaction. Cancer Res. 63, 3241-3246 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 3241-3246
    • Vasilevskaya, I.A.1    Rakitina, T.V.2    O'Dwyer, P.J.3
  • 130
    • 4444311881 scopus 로고    scopus 로고
    • Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity
    • Mimnaugh, E. G. et al. Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity. Mol. Cancer Ther. 3, 551-566 (2004).
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 551-566
    • Mimnaugh, E.G.1
  • 132
    • 0345734267 scopus 로고    scopus 로고
    • Coadministration of the heat shock protein 90 antagonist 17-allylamino-17-demethoxygeldanamycin with suberoylanilide hydroxamic acid or sodium butyrate synergistically induces apoptosis in human leukemia cells
    • Rahmani, M. et al. Coadministration of the heat shock protein 90 antagonist 17-allylamino-17-demethoxygeldanamycin with suberoylanilide hydroxamic acid or sodium butyrate synergistically induces apoptosis in human leukemia cells. Cancer Res. 63, 8420-8427 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 8420-8427
    • Rahmani, M.1
  • 133
    • 0037012344 scopus 로고    scopus 로고
    • Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228
    • Yu, X. et al. Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228. J. Natl Cancer Inst. 94, 504-513 (2002).
    • (2002) J. Natl. Cancer Inst. , vol.94 , pp. 504-513
    • Yu, X.1
  • 134
    • 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, 325-328 (2004).
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 325-328
    • Dymock, B.1
  • 135
    • 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., Lucas, B., Shtil, A., Huezo, H. & Rosen, N. 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, 3555-3564 (2002).
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3555-3564
    • Chiosis, G.1    Lucas, B.2    Shtil, A.3    Huezo, H.4    Rosen, N.5
  • 136
    • 1642503079 scopus 로고    scopus 로고
    • High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity
    • Rowlands, M. G. et al. High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal. Biochem. 327, 176-183 (2004).
    • (2004) Anal. Biochem. , vol.327 , pp. 176-183
    • Rowlands, M.G.1
  • 137
    • 27644509738 scopus 로고    scopus 로고
    • The anticancer activity of the fungal metabolite terrecyclic acid A is associated with modulation of multiple cellular stress response pathways
    • in the press
    • Turbyville, T. J., Wijeratne, E. M. K., Whitesell, L. & Gunatilaka, A. A. L. The anticancer activity of the fungal metabolite terrecyclic acid A is associated with modulation of multiple cellular stress response pathways. Mol. Cancer Ther. (in the press).
    • Mol. Cancer Ther.
    • Turbyville, T.J.1    Wijeratne, E.M.K.2    Whitesell, L.3    Gunatilaka, A.A.L.4
  • 138
    • 4143089911 scopus 로고    scopus 로고
    • Discovery of novel small molecule Hsp90 complex inhibitors using a forward chemical genetics approach
    • Barbosa, J. A. et al. Discovery of novel small molecule Hsp90 complex inhibitors using a forward chemical genetics approach. Clin. Cancer Res. 9 (Suppl.), 6176 (2003).
    • (2003) Clin. Cancer Res. , vol.9 , Issue.SUPPL. , pp. 6176
    • Barbosa, J.A.1
  • 139
    • 0034608532 scopus 로고    scopus 로고
    • Synthesis and evaluation of geldanamycin-testosterone hybrids
    • Kuduk, S. D. et al. Synthesis and evaluation of geldanamycin-testosterone hybrids. Bioorg. Med. Chem. Lett. 10, 1303-1306 (2000).
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 1303-1306
    • Kuduk, S.D.1
  • 140
    • 0034655207 scopus 로고    scopus 로고
    • Identification of a geldanamycin dimer that induces the selective degradation of HER-family tyrosine kinases
    • Zheng, F. F. et al. Identification of a geldanamycin dimer that induces the selective degradation of HER-family tyrosine kinases. Cancer Res. 60, 2090-2094 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 2090-2094
    • Zheng, F.F.1
  • 141
    • 10644292744 scopus 로고    scopus 로고
    • Engineered biosynthesis of geldanamycin analogs for Hsp90 inhibition
    • Patel, K. et al. Engineered biosynthesis of geldanamycin analogs for Hsp90 inhibition. Chem. Biol. 11, 1625-1633 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 1625-1633
    • Patel, K.1
  • 142
    • 0033564430 scopus 로고    scopus 로고
    • KF25706, a novel oxime derivative of radicicol, exhibits in vivo antitumor activity via selective depletion of Hsp90 binding signaling molecules
    • Soga, S. et al. KF25706, a novel oxime derivative of radicicol, exhibits in vivo antitumor activity via selective depletion of Hsp90 binding signaling molecules. Cancer Res. 59, 2931-2938 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 2931-2938
    • Soga, S.1
  • 143
    • 11244337455 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of 17-demethoxy 17-[[(2-dimethylamino)ethyl]amino]geldanamycin (17DMAG, NSC 707545) in C. B-17 SCID mice bearing MDA-MB-231 human breast cancer xenografts
    • Eiseman, J. L. et al. Pharmacokinetics and pharmacodynamics of 17-demethoxy 17-[[(2-dimethylamino)ethyl]amino]geldanamycin (17DMAG, NSC 707545) in C. B-17 SCID mice bearing MDA-MB-231 human breast cancer xenografts. Cancer Chemother. Pharmacol. 55, 21-32 (2005).
    • (2005) Cancer Chemother. Pharmacol. , vol.55 , pp. 21-32
    • Eiseman, J.L.1
  • 144
    • 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. W. et 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, 5839-5845 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5839-5845
    • Schulte, T.W.1
  • 145
    • 0029665779 scopus 로고    scopus 로고
    • Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Stepanova, L., Leng, X., Parker, S. B. & Harper, J. W. Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Devel. 10, 1491-1502 (1996).
    • (1996) Genes Devel. , vol.10 , pp. 1491-1502
    • Stepanova, L.1    Leng, X.2    Parker, S.B.3    Harper, J.W.4
  • 146
    • 0033118355 scopus 로고    scopus 로고
    • Functional requirement of p23 and Hsp90 in telomerase complexes
    • Holt, S. E. et al. Functional requirement of p23 and Hsp90 in telomerase complexes. Genes Devel. 13, 817-824 (1999).
    • (1999) Genes Devel. , vol.13 , pp. 817-824
    • Holt, S.E.1
  • 147
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 α-degradative pathway
    • Isaacs, J. S. et al. Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 α-degradative pathway. J. Biol. Chem. 277, 29936-29944 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.