메뉴 건너뛰기




Volumn 3, Issue 5, 2003, Pages 349-358

The stress response: Implications for the clinical development of Hsp90 inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; ACETYLSALICYLIC ACID; CHAPERONE; DNA; GELDANAMYCIN; HEAT SHOCK FACTOR 1; HEAT SHOCK FACTOR 2; HEAT SHOCK FACTOR 4; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; IBUPROFEN; INDOMETACIN; PROTEIN INHIBITOR; QUERCETIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0141819958     PISSN: 15680096     EISSN: None     Source Type: Journal    
DOI: 10.2174/1568009033481787     Document Type: Review
Times cited : (183)

References (100)
  • 1
    • 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. Pharmacol. Rev. 1998, 50, 493-513.
    • (1998) Pharmacol. Rev. , vol.50 , pp. 493-513
    • Smith, D.F.1    Whitesell, L.2    Katsanis, E.3
  • 2
    • 0016840757 scopus 로고
    • Induced thermal resistance in hela cells
    • Gerner, E. W.; Schneider, M. J. Induced Thermal Resistance in Hela Cells. Nature 1975, 256, 500-502.
    • (1975) Nature , vol.256 , pp. 500-502
    • Gerner, E.W.1    Schneider, M.J.2
  • 3
    • 0032850421 scopus 로고    scopus 로고
    • A method for the quantitative an alysis of human heat shock gene expression using a multiplex RT-PCR assay
    • Wang, S. M.; Khandekar, J. D.; Kaul, K. L.; Winchester, D. J.; Morimoto, R. I. A Method for the Quantitative an alysis of Human Heat Shock Gene Expression Using a Multiplex RT-PCR Assay. Cell Stress Chap. 1999, 4, 153-161.
    • (1999) Cell Stress Chap. , vol.4 , pp. 153-161
    • Wang, S.M.1    Khandekar, J.D.2    Kaul, K.L.3    Winchester, D.J.4    Morimoto, R.I.5
  • 4
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. Folding of Newly Translated Proteins in Vivo: the Role of Molecular Chaperones. Annu. Rev. Biochem. 2001, 70, 603-647.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 5
    • 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. 1998, 79, 129-168.
    • (1998) Pharmacol. Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaskka, Z.4    Nardai, G.5
  • 6
    • 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 Biotech. 1998, 16, 833-838.
    • (1998) Nature Biotech. , vol.16 , pp. 833-838
    • Morimoto, R.I.1    Santoro, M.G.2
  • 7
    • 0035989680 scopus 로고    scopus 로고
    • Hsp90 as a new therapeutic target for cancer therapy: The story unfolds
    • Maloney, A.; Workman, P. Hsp90 as a New Therapeutic Target for Cancer Therapy: the Story Unfolds. Expert Opin. Biol. Ther. 2002, 2, 3-24.
    • (2002) Expert Opin. Biol. Ther. , vol.2 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 8
    • 0035176758 scopus 로고    scopus 로고
    • The Hsp90 chaperone as a promising drug target
    • Piper, P. W. The Hsp90 Chaperone as a Promising Drug Target. Curr. Opin. Invest. Drugs 2001, 2, 1606-1610.
    • (2001) Curr. Opin. Invest. Drugs , vol.2 , pp. 1606-1610
    • Piper, P.W.1
  • 9
    • 0032862606 scopus 로고    scopus 로고
    • New aspects in the vertebrate heat shock factor system: Hsf3 and Hsf4
    • Nakai, A. New Aspects in the Vertebrate Heat Shock Factor System: Hsf3 and Hsf4. Cell Stress Chap. 1999, 4, 86-93.
    • (1999) Cell Stress Chap. , vol.4 , pp. 86-93
    • Nakai, A.1
  • 10
    • 0027406535 scopus 로고
    • Characterization of a novel chicken heat shock transcription factor, HSF3, suggests a new regulatory pathway
    • Nakai, A.; Morimoto, R. I. Characterization of a Novel Chicken Heat Shock Transcription Factor, HSF3, Suggests a New Regulatory Pathway. Mol. Cell Biol. 1993, 13, 1983-1997.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 1983-1997
    • Nakai, A.1    Morimoto, R.I.2
  • 11
    • 0025755922 scopus 로고
    • Heat shock factor and the heat shock response
    • Sorger, P. K. Heat Shock Factor and the Heat Shock Response. Cell 1991, 65, 363-366.
    • (1991) Cell , vol.65 , pp. 363-366
    • Sorger, P.K.1
  • 12
    • 0028896839 scopus 로고
    • Heat-inducible DNA binding of purified heat shock transcription factor 1
    • Goodson, M. L.; Sarge, K. D. Heat-Inducible DNA Binding of Purified Heat Shock Transcription Factor 1. J. Biol. Chem. 1995, 270, 2447-2450.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2447-2450
    • Goodson, M.L.1    Sarge, K.D.2
  • 13
    • 0032780311 scopus 로고    scopus 로고
    • Heat shock factor function and regulation in response to cellular stress, growth and differentiation signals
    • Morano, K. A.; Thiele, D. J. Heat Shock Factor Function and Regulation in Response to Cellular Stress, Growth and Differentiation Signals. Gene. Exp. 1999, 7, 271-282.
    • (1999) Gene. Exp. , vol.7 , pp. 271-282
    • Morano, K.A.1    Thiele, D.J.2
  • 15
    • 0026746491 scopus 로고
    • Activation of heat shock factor 2 during hemin-induced differentiation of human erythroleukemnia cells
    • Sistonen, L.; Sarge, K. D.; Phillips, B.; Morimoto, R. I. Activation of Heat Shock Factor 2 During Hemin-Induced Differentiation of Human Erythroleukemnia Cells. Mol. Cell Biol. 1992, 12, 4104-4111.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 4104-4111
    • Sistonen, L.1    Sarge, K.D.2    Phillips, B.3    Morimoto, R.I.4
  • 16
    • 0030966628 scopus 로고    scopus 로고
    • Overexpression of HSF2-Beta inhibits hemin-induced heat shock gene expression and erythroid differentiation in K562 cells
    • Leppa, S.; Pirkkala, L.; Saarento, H.; Sarge, K. D.; Sistonen, L. Overexpression of HSF2-Beta Inhibits Hemin-Induced Heat Shock Gene Expression and Erythroid Differentiation in K562 Cells. J. Biol. Chem. 1997, 272, 15293-15298.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15293-15298
    • Leppa, S.1    Pirkkala, L.2    Saarento, H.3    Sarge, K.D.4    Sistonen, L.5
  • 17
    • 0034674061 scopus 로고    scopus 로고
    • JNK targeting phosphorylation of heat shock factor-1 suppress its transcriptional activity
    • Dai, R.; Frejtag, W.; He, B.; Zhang, Y.; Mivechi, N. F. JNK Targeting and Phosphorylation of Heat Shock Factor-1 Suppress Its Transcriptional Activity. J. Biol. Chem. 2000, 275, 18210-18218.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18210-18218
    • Dai, R.1    Frejtag, W.2    He, B.3    Zhang, Y.4    Mivechi, N.F.5
  • 18
    • 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. Devel. 1998, 12, 3788-3796.
    • (1998) Genes. Devel. , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 19
    • 17744372861 scopus 로고    scopus 로고
    • Roles of the heat shock transcription factors in regulation of the heat shock response and beyond
    • Pirkkala, L.; Nykanen, P.; Sistonen, L. Roles of the Heat Shock Transcription Factors in Regulation of the Heat Shock Response and Beyond. FASEB J. 2001, 15, 1118-1131.
    • (2001) FASEB J. , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykanen, P.2    Sistonen, L.3
  • 20
    • 0032571397 scopus 로고    scopus 로고
    • Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis
    • Mcmillan, D. R.; Xiao, X.; Shao, L.; Graves, K.; Benjamin, I. J. Targeted Disruption of Heat Shock Transcription Factor 1 Abolishes Thermotolerance and Protection against Heat-Inducible Apoptosis. J. Biol. Chem. 1998, 273, 7523-7528.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7523-7528
    • Mcmillan, D.R.1    Xiao, X.2    Shao, L.3    Graves, K.4    Benjamin, I.J.5
  • 21
    • 0033229880 scopus 로고    scopus 로고
    • HSF1 Is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice
    • Xiao, X.; Zuo, X.; Davis, A. A.; Mcmillan, D. R.; Curry, B. B.; Richardson, J. A.; Benjamin, I. J. HSF1 Is Required for Extra-Embryonic Development, Postnatal Growth and Protection During Inflammatory Responses in Mice. EMBO J. 1999, 18, 5943-5952.
    • (1999) EMBO J. , vol.18 , pp. 5943-5952
    • Xiao, X.1    Zuo, X.2    Davis, A.A.3    Mcmillan, D.R.4    Curry, B.B.5    Richardson, J.A.6    Benjamin, I.J.7
  • 22
    • 0030988941 scopus 로고    scopus 로고
    • Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation
    • Kline, M. P.Morimoto, R. I. Repression of the Heat Shock Factor 1 Transcriptional Activation Domain Is Modulated by Constitutive Phosphorylation. Mol. Cell Biol. 1997, 17, 2107-2115.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2107-2115
    • Kline, M.P.1    Morimoto, R.I.2
  • 23
    • 0032541032 scopus 로고    scopus 로고
    • Transcriptional activity of heat shock factor 1 at 37 degrees C is repressed through phosphorylation on two distinct serine residues by glycogen synthase kinase 3 and protein kinases calpha and czeta
    • Chu, B.; Zhong, R.; Soncin, F.; Stevenson, M. A.; Calderwood, S. K. Transcriptional Activity of Heat Shock Factor 1 At 37 Degrees C Is Repressed Through Phosphorylation on Two Distinct Serine Residues by Glycogen Synthase Kinase 3 and Protein Kinases Calpha and Czeta. J. Biol. Chem. 1998, 273, 18640-18646.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18640-18646
    • Chu, B.1    Zhong, R.2    Soncin, F.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 24
    • 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.; Guo, Y.; Guettouche, T.; Smith, D. F.; Voellmy, R. Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) That Forms a Stress-Sensitive Complex with HSF1. Cell 1998, 94, 471-480.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 25
    • 0031866191 scopus 로고    scopus 로고
    • HSP90 interacts with and regulates the activity of heat shock factor 1 in xenopus oocytes
    • Ali, A.; Bharadwaj, S.; O'Carroll, R.; Ovsenek, N. HSP90 Interacts with and Regulates the Activity of Heat Shock Factor 1 in Xenopus Oocytes. Mol. Cell Biol. 1998, 18, 4949-4960.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 4949-4960
    • Ali, A.1    Bharadwaj, S.2    O'Carroll, R.3    Ovsenek, N.4
  • 26
    • 0033499798 scopus 로고    scopus 로고
    • Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 in vivo
    • Bharadwaj, S.; Ali, A.; Ovsenek, N. Multiple Components of the HSP90 Chaperone Complex Function in Regulation of Heat Shock Factor 1 in Vivo. Mol. Cell Biol. 1999, 19, 8033-8041.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 8033-8041
    • Bharadwaj, S.1    Ali, A.2    Ovsenek, N.3
  • 27
    • 0030324952 scopus 로고    scopus 로고
    • A pathway of multi-chaperone interactions common to diverse regulatory proteins estrogen receptor, fes tyrosine kinase, heat shock transcription factor HSF1, and the aryl hydrocarbon receptor
    • Nair, S. C.; Toran, E. J.; Rimerman, R. A.; Hjermstad, S.; Smithgall, T. E.; Smith, D. F. A Pathway of Multi-Chaperone Interactions Common to Diverse Regulatory Proteins: Estrogen Receptor, Fes Tyrosine Kinase, Heat Shock Transcription Factor HSF1, and the Aryl Hydrocarbon Receptor. Cell Stress Chap. 1996, 1, 237-250.
    • (1996) Cell Stress Chap. , vol.1 , pp. 237-250
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hjermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 28
    • 0027475243 scopus 로고
    • Hsp90 chaperonins possess atpase activity and bind heat shock transcription factors and peptidyl prolyl isomerases
    • Nadeau, K.; Das, A.; Walsh, C. T. Hsp90 Chaperonins Possess Atpase Activity and Bind Heat Shock Transcription Factors and Peptidyl Prolyl Isomerases. J. Biol. Chem. 1993, 268, 1479-1487.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1479-1487
    • Nadeau, K.1    Das, A.2    Walsh, C.T.3
  • 29
    • 0030043401 scopus 로고    scopus 로고
    • Activation of heat shock factor 1 DNA biniding precedes stress-induced serine phosphorylation
    • Cotto, J. J.; Kline, M.; Morimoto, R. I. Activation of Heat Shock Factor 1 DNA Biniding Precedes Stress-Induced Serine Phosphorylation. J. Biol. Chem. 1996, 271, 3355-3358.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3355-3358
    • Cotto, J.J.1    Kline, M.2    Morimoto, R.I.3
  • 30
    • 0031055277 scopus 로고    scopus 로고
    • Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active factor trimers
    • Xia, W.; Voellmy, R. Hyperphosphorylation of Heat Shock Transcription Factor 1 Is Correlated with Transcriptional Competence and Slow Dissociation of Active Factor Trimers. J. Biol. Chem. 1997, 272, 4094-4102.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4094-4102
    • Xia, W.1    Voellmy, R.2
  • 32
    • 0032612322 scopus 로고    scopus 로고
    • Stress-induced activation of the heat-shock response: Cell and molecular biology of heat-shock factors
    • Cotto, J. J.; Morimoto, R. I. Stress-Induced Activation of the Heat-Shock Response: Cell and Molecular Biology of Heat-Shock Factors. Biochem. Soc. Symp. 1999, 64, 105-118.
    • (1999) Biochem. Soc. Symp. , vol.64 , pp. 105-118
    • Cotto, J.J.1    Morimoto, R.I.2
  • 33
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-Specific transcriptional repressors
    • Shi, Y.; Mosser, D. D.; Morimoto, R. I. Molecular Chaperones as HSF1-Specific Transcriptional Repressors. Genes. Devel. 1998, 12, 654-666.
    • (1998) Genes. Devel. , vol.12 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 34
    • 0035824621 scopus 로고    scopus 로고
    • Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex
    • Guo, Y.; Guettouche, T.; Fenna, M.; Boellmann, F.; Pratt, W. B.; to ft, D. O.; Smith, D. F.; Voellmy, R. Evidence for a Mechanism of Repression of Heat Shock Factor 1 Transcriptional Activity by a Multichaperone Complex. J. Biol. Chem. 2001, 276, 45791-45799.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45791-45799
    • Guo, Y.1    Guettouche, T.2    Fenna, M.3    Boellmann, F.4    Pratt, W.B.5    Toft, D.O.6    Smith, D.F.7    Voellmy, R.8
  • 35
    • 0028847062 scopus 로고
    • Short circuiting stress protein expression via a tyrosine kinase inhibitor, herbimycin A
    • Hegde, R.; Zuo, J.; Voellmy, R.; Welch, W. Short Circuiting Stress Protein Expression Via a Tyrosine Kinase Inhibitor, Herbimycin A. J. Cell Physiol. 1995, 165, 186.
    • (1995) J. Cell Physiol. , vol.165 , pp. 186
    • Hegde, R.1    Zuo, J.2    Voellmy, R.3    Welch, W.4
  • 36
    • 0025744556 scopus 로고
    • Induction of Hsp72/73 by herbimycin A, an inhibitor of transformation by tyrosine kinase oncogenes
    • Murakami, Y.; Uehara, Y.; Yamamoto, C.; Fukazawa, H.; Mizuno, S. Induction of Hsp72/73 by Herbimycin A, an Inhibitor of Transformation by Tyrosine Kinase Oncogenes. Exp. Cell Res. 1991, 195, 338-344.
    • (1991) Exp. Cell Res. , vol.195 , pp. 338-344
    • Murakami, Y.1    Uehara, Y.2    Yamamoto, C.3    Fukazawa, H.4    Mizuno, S.5
  • 37
    • 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.; Paine-Murrieta, G.; Taylor, C.; Pulcini, E.; Akinaga, S.; Benjamin, I.; Whitesell, L. Induction of a Heat Shock Factor 1-Dependent Stress Response Alters the Cytotoxic Activity of Hsp90 Binding Agents. Clin. Cancer Res. 2000, 6, 3312-3318.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 3312-3318
    • Bagatell, R.1    Paine-Murrieta, G.2    Taylor, C.3    Pulcini, E.4    Akinaga, S.5    Benjamin, I.6    Whitesell, L.7
  • 38
    • 0031006855 scopus 로고    scopus 로고
    • Xenopus heat shock factor 1 is a nuclear protein before heat stress
    • Mercier, P. A.; Foksa, J.; Ovsenek, N.; Westwood, J. T. Xenopus Heat Shock Factor 1 Is a Nuclear Protein Before Heat Stress. J. Biol. Chem. 1997, 272, 14147-14151.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14147-14151
    • Mercier, P.A.1    Foksa, J.2    Ovsenek, N.3    Westwood, J.T.4
  • 39
    • 0033536006 scopus 로고    scopus 로고
    • Rapid and reversible relocalization of heat shock factor 1 within seconds to nuclear stress granules
    • Jolly, C.; Usson, Y.; Morimoto, R. I. Rapid and Reversible Relocalization of Heat Shock Factor 1 Within Seconds to Nuclear Stress Granules. Proc. Natl. Acad. Sci. USA 1999, 96, 6769-6774.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6769-6774
    • Jolly, C.1    Usson, Y.2    Morimoto, R.I.3
  • 40
    • 0030878952 scopus 로고    scopus 로고
    • Geldanamycin-stmulated destabilization of mutated p53 is mediated by the proteasome in vivo
    • Whitesell, L.; Sutphin, P.; An, W. G.; Schulte, T.; Blagosklonny, M. V.; Neckers, L. Geldanamycin-Stmulated Destabilization of Mutated p53 is Mediated by the Proteasome in vivo. Oncogene 1997, 14, 2809-2816.
    • (1997) Oncogene , vol.14 , pp. 2809-2816
    • Whitesell, L.1    Sutphin, P.2    An, W.G.3    Schulte, T.4    Blagosklonny, M.V.5    Neckers, L.6
  • 42
    • 0035490924 scopus 로고    scopus 로고
    • Proteasome inhibitors differentially affect heat shock protein response in cancer cells
    • Ashok, B. T.; Kim, E.; Mittelman, A.; Tiwari, R. K. Proteasome Inhibitors Differentially Affect Heat Shock Protein Response in Cancer Cells. Int. J. MoL Med. 2001, 8, 385-390.
    • (2001) Int. J. MoL Med. , vol.8 , pp. 385-390
    • Ashok, B.T.1    Kim, E.2    Mittelman, A.3    Tiwari, R.K.4
  • 44
    • 4243592951 scopus 로고    scopus 로고
    • Biologic rationale for the combination of an Hsp90 an tagonist with a proteasome inhibitor
    • Mimnaugh, E. G.; Neckers, L. Biologic Rationale for the Combination of an Hsp90 an tagonist with a Proteasome Inhibitor. Clin. Cancer Res. 2001, 7 (Supplement), 3779s.
    • (2001) Clin. Cancer Res. , vol.7 , Issue.SUPPL.
    • Mimnaugh, E.G.1    Neckers, L.2
  • 46
    • 0037067712 scopus 로고    scopus 로고
    • Geldanamycin leads to superoxide formation by enzymatic and non-enzymatic redox cycling. Implications for studies of Hsp90 and endothelial cell nitric-oxide synthase
    • Dikalov, S.; Landmesser, U.; Harrison, D. G. Geldanamycin Leads to Superoxide Formation by Enzymatic and Non-Enzymatic Redox Cycling. Implications for Studies of Hsp90 and Endothelial Cell Nitric-Oxide Synthase. J. Biol. Chem. 2002, 277, 25480-25485.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25480-25485
    • Dikalov, S.1    Landmesser, U.2    Harrison, D.G.3
  • 47
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • Schulte, T. W.; Akinaga, S.; Soga, S.; Sullivan, W.; Stensgard, B.; Toft, D.; Neckers, L. M. Antibiotic Radicicol Binds to the N-Terminal Domain of Hsp90 and Shares Important Biologic Activities with Geldanamycin. Cell Stress Chap. 1998, 3, 100-108.
    • (1998) Cell Stress Chap. , vol.3 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3    Sullivan, W.4    Stensgard, B.5    Toft, D.6    Neckers, L.M.7
  • 48
    • 0031891726 scopus 로고    scopus 로고
    • Geldanamycin, an Hsp90/GRP94-binding drug, induces increased transcription of endoplasmic reticulum (ER) chaperones via the ER stress pathway
    • Lawson, B.; Brewer, J. W.; Hendershot, L. M. Geldanamycin, an Hsp90/GRP94-Binding Drug, Induces Increased Transcription of Endoplasmic Reticulum (ER) Chaperones Via the ER Stress Pathway. J. Cell Physiol. 1998, 174, 170-178.
    • (1998) J. Cell Physiol. , vol.174 , pp. 170-178
    • Lawson, B.1    Brewer, J.W.2    Hendershot, L.M.3
  • 49
    • 0035966320 scopus 로고    scopus 로고
    • The unfolding tale of the unfolded protein response
    • Ma, Y.; Hendershot, L. M. The Unfolding Tale of the Unfolded Protein Response. Cell 2001, 107, 827-830.
    • (2001) Cell , vol.107 , pp. 827-830
    • Ma, Y.1    Hendershot, L.M.2
  • 50
    • 0027251913 scopus 로고
    • Correlation of the survival of ovarian cancer patients with mrna expression of the 60kda heat shock protein Hsp60
    • Kimura, E.; Erns, R. E.; Alcaraz, J. E.; Arboleda, J.; Slamon, D. J.; Howell, S. B. Correlation of the Survival of Ovarian Cancer Patients with Mrna Expression of the 60kda Heat Shock Protein Hsp60. J. Clin. Oncol. 1993, 11, 891-898.
    • (1993) J. Clin. Oncol. , vol.11 , pp. 891-898
    • Kimura, E.1    Erns, R.E.2    Alcaraz, J.E.3    Arboleda, J.4    Slamon, D.J.5    Howell, S.B.6
  • 51
    • 0027503365 scopus 로고
    • Heat shock protein Hsp70 in patients with axillary lymph node-negative breast cancer: Prognostic implications
    • Ciocca, D. R.; Clark, G. M.; Tandon, A. K.; Fuqua, S. A. W.; Welch, W. J.; Mcguire, W. L. Heat Shock Protein Hsp70 in Patients with Axillary Lymph Node- Negative Breast Cancer: Prognostic Implications. J. Natl. Cancer Inst. 1993, 85, 570-574.
    • (1993) J. Natl. Cancer Inst. , vol.85 , pp. 570-574
    • Ciocca, D.R.1    Clark, G.M.2    Tandon, A.K.3    Fuqua, S.A.W.4    Welch, W.J.5    Mcguire, W.L.6
  • 52
    • 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 1998, 34, 942-943.
    • (1998) Eur. J. Cancer , vol.34 , pp. 942-943
    • Conroy, S.E.1    Sasieni, P.D.2    Fentiman, I.3    Latchman, D.S.4
  • 53
    • 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. 1995, 1, 1217-1222.
    • (1995) Clin. Cancer Res. , vol.1 , pp. 1217-1222
    • Ralhan, R.1    Kaur, J.2
  • 54
    • 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 1995, 63, 774-779.
    • (1995) Int. J Cancer , vol.63 , pp. 774-779
    • Kaur, J.1    Ralhan, R.2
  • 55
    • 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. 1997, 33, 873-877.
    • (1997) Euro. J. Cancer , vol.33 , pp. 873-877
    • Santarosa, M.1    Favaro, D.2    Quaia, M.3    Galligioni, E.4
  • 56
    • 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. an alysis of Heat Shock Protein Expression in Myeloid Leukaemia Cells by Flow Cytometry. Br. J. Haematol. 1995, 90, 163-168.
    • (1995) Br. J. Haematol. , vol.90 , pp. 163-168
    • Chant, I.D.1    Rose, P.E.2    Morris, A.G.3
  • 57
    • 0026664393 scopus 로고
    • High constitutive expression of heat shock protein 90a in human acute leukemia cells
    • Yufu, Y.; Nishimura, J.; Nawata, H. High Constitutive Expression of Heat Shock Protein 90a in Human Acute Leukemia Cells. Leuk. Res. 1992, 16, 597-605.
    • (1992) Leuk. Res. , vol.16 , pp. 597-605
    • Yufu, Y.1    Nishimura, J.2    Nawata, H.3
  • 59
    • 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. 1996, 87, 908-915.
    • (1996) Jpn. J. Cancer Res. , vol.87 , pp. 908-915
    • Yano, M.1    Naito, Z.2    Tanaka, S.3    Asano, G.4
  • 61
    • 0033988478 scopus 로고    scopus 로고
    • Antibodies to heat shock protein 90 in osteosarcoma patients correlate with response to neoadjuvant chemotherapy
    • Trieb, K.; Gerth, R.; Holzer, G.; Grohs, J. G.; Berger, P.; Kotz, R. an tibodies to Heat Shock Protein 90 in Osteosarcoma Patients Correlate with Response to Neoadjuvant Chemotherapy. Br. J. Cancer 2000, 82, 85-87.
    • (2000) Br. J. Cancer , vol.82 , pp. 85-87
    • Trieb, K.1    Gerth, R.2    Holzer, G.3    Grohs, J.G.4    Berger, P.5    Kotz, R.6
  • 62
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death: Survival proteins in cancer
    • Jaattela, M. Escaping Cell Death: Survival Proteins in Cancer. Exp. Cell Res. 1999, 248, 30-43.
    • (1999) Exp. Cell Res. , vol.248 , pp. 30-43
    • Jaattela, M.1
  • 63
    • 0030999750 scopus 로고    scopus 로고
    • Apoptosis and the dilemma of cancer chemotherapy
    • Hannun, Y. Apoptosis and the Dilemma of Cancer Chemotherapy. Blood 1997, 89, 1845-1853.
    • (1997) Blood , vol.89 , pp. 1845-1853
    • Hannun, Y.1
  • 64
    • 0030016274 scopus 로고    scopus 로고
    • Drug resistance against gemcitabine and topotecan mediated by constitutive Hsp70 overexpression in vitro: Implication of quercetin as sensitizer in chemotherapy
    • Sliutz, G.; Karlseder, J.; Tempfer, C.; Orel, L.; Holzer, G.; Simon, M. M. Drug Resistance against Gemcitabine and Topotecan Mediated by Constitutive Hsp70 Overexpression in Vitro: Implication of Quercetin as Sensitizer in Chemotherapy. Br. J. Cancer 1996, 74, 172-177.
    • (1996) Br. J. Cancer , vol.74 , pp. 172-177
    • Sliutz, G.1    Karlseder, J.2    Tempfer, C.3    Orel, L.4    Holzer, G.5    Simon, M.M.6
  • 68
    • 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.; Rohde, M.; Brand, K.; Bastholm, L.; Elling, F.; Jaattela, M. 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 2000, 97, 7871-7876.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7871-7876
    • Nylandsted, J.1    Rohde, M.2    Brand, K.3    Bastholm, L.4    Elling, F.5    Jaattela, M.6
  • 69
    • 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 1997, 94, 12949-12956.
    • (1997) Proc. Natl. Acad Sci. USA , vol.94 , pp. 12949-12956
    • Nathan, D.E.1    Vos, M.H.2    Lindquist, S.3
  • 70
    • 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. 1998, 217, 420-431.
    • (1998) Proc. Soc. Exp. Biol. Med. , vol.217 , pp. 420-431
    • Pratt, W.B.1
  • 71
    • 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 2002, 110, 281-284.
    • (2002) Cell , vol.110 , pp. 281-284
    • Morimoto, R.I.1
  • 72
    • 0027484097 scopus 로고
    • Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes
    • Smith, D. F. Dynamics of Heat Shock Protein 90-Progesterone Receptor Binding and the Disactivation Loop Model for Steroid Receptor Complexes. Mol. Endo. 1993, 7, 1418-1429.
    • (1993) Mol. Endo. , vol.7 , pp. 1418-1429
    • Smith, D.F.1
  • 73
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone an samycins: 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 an samycins: Essential Role for Stress Proteins in Oncogenic Transformation. Proc. Natl. Acad. Sci. USA 1994, 91, 8324-8328.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 74
    • 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. 1998, 18, 1517-1524.
    • (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
  • 75
    • 0029737509 scopus 로고    scopus 로고
    • Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90
    • Blagosklonny, M. V.; to retsky, J.; Bohen, S.; Neckers, L. Mutant Conformation of p53 Translated in Vitro or in Vivo Requires Functional HSP90. Proc. Natl. Acad. Sci. USA 1996, 93, 8379-8383.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 76
    • 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. 1996, 271, 15084-15090.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15084-15090
    • Sepehrnia, B.1    Paz, I.B.2    Dasgupta, G.3    Momand, J.4
  • 77
    • 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 1998, 396, 336-342.
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 78
    • 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 2002, 417, 618-624.
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3
  • 79
    • 0017748765 scopus 로고
    • Geldanamycin inhibition of 3-methylcholanthrene-induced rat embryo cell transformation
    • Price, P. J.; Suk, W. A.; Skeen, P. C.; Spahn, G. J.; Chirigos, M. A. Geldanamycin Inhibition of 3-Methylcholanthrene-Induced Rat Embryo Cell Transformation. Proc. Soc. Exp. Biol. Med. 1977, 155, 461-463.
    • (1977) Proc. Soc. Exp. Biol. Med. , vol.155 , pp. 461-463
    • Price, P.J.1    Suk, W.A.2    Skeen, P.C.3    Spahn, G.J.4    Chirigos, M.A.5
  • 80
    • 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.; Hostein, I.; Bancrji, U.; Stefano, F. D.; Maloney, A.; Walton, M.; Judson, I.; Workman, P. 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 2000, 19, 4125-4133.
    • (2000) Oncogene , vol.19 , pp. 4125-4133
    • Clarke, P.A.1    Hostein, I.2    Bancrji, U.3    Stefano, F.D.4    Maloney, A.5    Walton, M.6    Judson, I.7    Workman, P.8
  • 81
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou, B.; Prodromou, C.; Roe, S. M.; O'Brien, R.; Ladbury, J. E.; Piper, P. W.; Pearl, L. H. ATP Binding and Hydrolysis Are Essential to the Function of the Hsp90 Molecular Chaperone in Vivo. EMBO J. 1998, 17, 4829-4836.
    • (1998) EMBO J. , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 83
    • 0025024265 scopus 로고
    • Discordant expression of heat shock protein mrnas in tissues of heat-stressed rats
    • Blake, M. J.; Gershon, D.; Fargnoli, J.; Holbrook, N. J. Discordant Expression of Heat Shock Protein Mrnas in Tissues of Heat-Stressed Rats. J. Biol. Chem. 1990, 265, 15275-15279.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15275-15279
    • Blake, M.J.1    Gershon, D.2    Fargnoli, J.3    Holbrook, N.J.4
  • 84
    • 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. 2002, 81, 355-364.
    • (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
  • 85
    • 0030048735 scopus 로고    scopus 로고
    • Regulatory differences in the stress response of hippocampal neurons and glial cells after heat shock
    • Marcuccilli, C. J.; Mathur, S. K.; Morimoto, R. I.; Miller, R. J. Regulatory Differences in the Stress Response of Hippocampal Neurons and Glial Cells After Heat Shock. J. Neurosci. 1996, 16, 478-485.
    • (1996) J. Neurosci. , vol.16 , pp. 478-485
    • Marcuccilli, C.J.1    Mathur, S.K.2    Morimoto, R.I.3    Miller, R.J.4
  • 86
    • 0028016330 scopus 로고
    • Deficient induction of human Hsp70 heat shock gene transcription in Y79 retinoblastoma cells despite activation of heat shock factor 1
    • Mathur, S. K.; Sistonen, L.; Brown, I. R.; Murphy, S. P.; Sarge, K. D.; Morimoto, R. I. Deficient Induction of Human Hsp70 Heat Shock Gene Transcription in Y79 Retinoblastoma Cells Despite Activation of Heat Shock Factor 1. Proc. Natl. Acad. Sci. USA 1994, 91, 8695-8699.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8695-8699
    • Mathur, S.K.1    Sistonen, L.2    Brown, I.R.3    Murphy, S.P.4    Sarge, K.D.5    Morimoto, R.I.6
  • 87
    • 0030791142 scopus 로고    scopus 로고
    • Potentiation of heat stress-induced Hsp70 expression in vivo by aspirin
    • Fawcett, T. W.; Xu, Q.; Holbrook, N. J. Potentiation of Heat Stress-Induced Hsp70 Expression in Vivo by Aspirin. Cell Stress Chap. 1997, 2, 104-109.
    • (1997) Cell Stress Chap. , vol.2 , pp. 104-109
    • Fawcett, T.W.1    Xu, Q.2    Holbrook, N.J.3
  • 88
    • 0029161913 scopus 로고
    • Pharmacological modulation of heat shock factor I by an tiinflammatory drugs results in protection against stress-induced cellular damage
    • Lee, B. S.; Chen, J.; an gelidis, C.; Jurivich, D. A.; Morimoto, R. I. Pharmacological Modulation of Heat Shock Factor I by an tiinflammatory Drugs Results in Protection against Stress-Induced Cellular Damage. Proc. Natl. Acad. Sci. USA 1995, 92, 7207-7211.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7207-7211
    • Lee, B.S.1    Chen, J.2    Angelidis, C.3    Jurivich, D.A.4    Morimoto, R.I.5
  • 89
    • 0031590444 scopus 로고    scopus 로고
    • Quercetin inhibits heat shock protein induction but not heat shock factor DNA-binding in human breast carcinoma cells
    • Hansen, R. K.; Oesterreich, S.; Lemieux, P.; Sarge, K. D.; Fuqua, S. A. Quercetin Inhibits Heat Shock Protein Induction But Not Heat Shock Factor DNA-Binding in Human Breast Carcinoma Cells. Biochem. Biophys. Res. Comm. 1997, 239, 851-856.
    • (1997) Biochem. Biophys. Res. Comm. , vol.239 , pp. 851-856
    • Hansen, R.K.1    Oesterreich, S.2    Lemieux, P.3    Sarge, K.D.4    Fuqua, S.A.5
  • 90
    • 0029664396 scopus 로고    scopus 로고
    • Modulation of prostaglandin al-induced thermotolerance by quercetin in human leukemic cells: Role of heat shock protein 70
    • Elia, G.; Amici, C.; Rossi, A.; Santoro, M. G. Modulation of Prostaglandin Al-Induced Thermotolerance by Quercetin in Human Leukemic Cells: Role of Heat Shock Protein 70. Cancer Res. 1996, 56, 210-217.
    • (1996) Cancer Res. , vol.56 , pp. 210-217
    • Elia, G.1    Amici, C.2    Rossi, A.3    Santoro, M.G.4
  • 91
    • 0029999052 scopus 로고    scopus 로고
    • Phase I clinical trial of the flavonoid quercetin: Pharmacokinetics and evidence for in vivo tyrosine kinase inhibition
    • Ferry, D. R.; Smith, A.; Malkhandi, J.; Fyfe, D. W.; Detakats, P. G.; and erson, D.; Baker, J.; Kerr, D. J. Phase I Clinical Trial of the Flavonoid Quercetin: Pharmacokinetics and Evidence for in Vivo Tyrosine Kinase Inhibition. Clin. Cancer Res. 1996, 2, 659-668.
    • (1996) Clin. Cancer Res. , vol.2 , pp. 659-668
    • Ferry, D.R.1    Smith, A.2    Malkhandi, J.3    Fyfe, D.W.4    Detakats, P.G.5    Anderson, D.6    Baker, J.7    Kerr, D.J.8
  • 93
    • 0029794271 scopus 로고    scopus 로고
    • Overexpression of heat shock protein 72 in transgenic mice decreases infarct size in vivo
    • Hutter, J. J.; Mestril, R.; Tam, E. K.; Sievers, R. E.; Dillmann, W. H.; Wolfe, C. L. Overexpression of Heat Shock Protein 72 in Transgenic Mice Decreases Infarct Size in Vivo. Circulation. 1996, 94, 1408-1411.
    • (1996) Circulation , vol.94 , pp. 1408-1411
    • Hutter, J.J.1    Mestril, R.2    Tam, E.K.3    Sievers, R.E.4    Dillmann, W.H.5    Wolfe, C.L.6
  • 94
    • 0032519663 scopus 로고    scopus 로고
    • Protection against myocardial dysfunction after a brief ischemic period in transgenic mice expressing inducible heat shock protein 70
    • Trost, S. U.; Omens, J. H.; Karlon, W. J.; Meyer, M.; Mestril, R.; Covell, J. W.; Dillmann, W. H. Protection against Myocardial Dysfunction after a Brief Ischemic Period in Transgenic Mice Expressing Inducible Heat Shock Protein 70. J. Clin. Invest. 1998, 101, 855-862.
    • (1998) J. Clin. Invest. , vol.101 , pp. 855-862
    • Trost, S.U.1    Omens, J.H.2    Karlon, W.J.3    Meyer, M.4    Mestril, R.5    Covell, J.W.6    Dillmann, W.H.7
  • 95
    • 0030765644 scopus 로고    scopus 로고
    • Transgenic mice expressing the human inducible Hsp70 have hippocampal neurons resistant to ischemic injury
    • Plumier, J. C.; Krueger, A. M.; Currie, R. W.; Kontoyiannis, D.; Kollias, G.; Pagoulatos, G. N. Transgenic Mice Expressing the Human Inducible Hsp70 Have Hippocampal Neurons Resistant to Ischemic Injury. Cell Stress Chap. 1997, 2, 162-167.
    • (1997) Cell Stress Chap. , vol.2 , pp. 162-167
    • Plumier, J.C.1    Krueger, A.M.2    Currie, R.W.3    Kontoyiannis, D.4    Kollias, G.5    Pagoulatos, G.N.6
  • 97
    • 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.; Lau, S. S.; Dillmann, W. H.; Mestril, R. Induction of Heat Shock Proteins by Tyrosine Kinase Inhibitors in Rat Cardiomyocytes and Myogenic Cells Confers Protection against Simulated Ischemia. J. Mol. Cell Cardiol. 1997, 29, 1927-1938.
    • (1997) J. Mol. Cell Cardiol. , vol.29 , pp. 1927-1938
    • Conde, A.G.1    Lau, S.S.2    Dillmann, W.H.3    Mestril, R.4
  • 100
    • 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.; Lurz, R.; Lueder, G.; Priller, J.; Hayer-Hartl, M. K.; Hartl, F. U.; Lehrach, H.; Wanker, E. E. Geldanamycin Activates a Heat Shock Response and Inhibits Huntingtin Aggregation in a Cell Culture Model of Huntington's Disease. Hum. Mol. Genet. 2001, 10, 1307-1315.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3    Priller, J.4    Hayer-Hartl, M.K.5    Hartl, F.U.6    Lehrach, H.7    Wanker, E.E.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.