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Volumn 9, Issue 15, 2009, Pages 1447-1461

Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases

Author keywords

Cancer; Celastrol; Gamendazole; Gedunin; Heat shock response; Hsp90; Novobiocin

Indexed keywords

17 DEMETHOXY 17 (2 DIMETHYLAMINOETHYLAMINO)GELDANAMYCIN; 4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; 7 DESACETYLCARBAMATEGEDUNIN; 7 OXOGEDUNIN; ANTINEOPLASTIC AGENT; AUY 922; CELASTROL; CELL CYCLE PROTEIN 37; CHAPERONE; CNF 2024; GAMENDAZOLE; GEDUNIN; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HISTONE DEACETYLASE INHIBITOR; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; NOVOBIOCIN; RADICICOL; ROMIDEPSIN; SNX 5422; TANESPIMYCIN; TRICHOSTATIN A; UNCLASSIFIED DRUG; VORINOSTAT;

EID: 74249108175     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802609789895683     Document Type: Review
Times cited : (48)

References (168)
  • 1
    • 58149159907 scopus 로고    scopus 로고
    • Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: Therapeutic approaches
    • Paul, S. Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: therapeutic approaches. Bioessays 2008, 30, 1172-1184.
    • (2008) Bioessays , vol.30 , pp. 1172-1184
    • Paul, S.1
  • 2
    • 67349104211 scopus 로고    scopus 로고
    • Molecular mechanisms underlying polyalanine diseases
    • Messaed, C.; Rouleau, G. A. Molecular mechanisms underlying polyalanine diseases. Neurobiol. Dis. 2009, 34, 397-405.
    • (2009) Neurobiol. Dis , vol.34 , pp. 397-405
    • Messaed, C.1    Rouleau, G.A.2
  • 3
    • 49849084827 scopus 로고    scopus 로고
    • Redox control of endothelial function and dysfunction: Molecular mechanisms and therapeutic opportunities
    • Thomas, S. R.; Witting, P. K.; Drummond, G. R. Redox control of endothelial function and dysfunction: molecular mechanisms and therapeutic opportunities. Antioxid. Redox. Signal. 2008, 10, 1713-1753.
    • (2008) Antioxid. Redox. Signal , vol.10 , pp. 1713-1753
    • Thomas, S.R.1    Witting, P.K.2    Drummond, G.R.3
  • 5
    • 68549125412 scopus 로고    scopus 로고
    • Chronic myelogenous leukemia, BCR-ABL1+
    • Vardiman, J. W. Chronic myelogenous leukemia, BCR-ABL1+. Am. J. Clin. Pathol. 2009, 132, 250-260.
    • (2009) Am. J. Clin. Pathol , vol.132 , pp. 250-260
    • Vardiman, J.W.1
  • 6
    • 62549144871 scopus 로고    scopus 로고
    • CFTR and defective endocytosis: New insights in the renal phenotype of cystic fibrosis
    • Jouret, F.; Devuyst, O. CFTR and defective endocytosis: new insights in the renal phenotype of cystic fibrosis. Pflugers Arch. 2009, 457, 1227-1236.
    • (2009) Pflugers Arch , vol.457 , pp. 1227-1236
    • Jouret, F.1    Devuyst, O.2
  • 7
    • 67049172152 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress response and aging
    • Naidoo, N. The endoplasmic reticulum stress response and aging. Rev. Neurosci. 2009, 20, 23-37.
    • (2009) Rev. Neurosci , vol.20 , pp. 23-37
    • Naidoo, N.1
  • 9
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • Lehman, N. L. The ubiquitin proteasome system in neuropathology. Acta Neuropathol. 2009, 118, 329-347.
    • (2009) Acta Neuropathol , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 12
    • 46049094024 scopus 로고    scopus 로고
    • Heat shock proteins as novel therapeutic targets in cancer
    • Soo, E. T. L.; Yip, G. W. C.; Lwin, Z. M.; Kumar, S. D.; Bay, B.-H. Heat shock proteins as novel therapeutic targets in cancer. In Vivo 2008, 22, 311-316.
    • (2008) In Vivo , vol.22 , pp. 311-316
    • Soo, E.T.L.1    Yip, G.W.C.2    Lwin, Z.M.3    Kumar, S.D.4    Bay, B.-H.5
  • 13
    • 33846651282 scopus 로고    scopus 로고
    • Molecular chaperones and protein kinase quality control
    • Caplan, A. J.; Mandal, A. K.; Theodoraki, M. A. Molecular chaperones and protein kinase quality control. Trends Cell. Biol. 2007, 17, 87-92.
    • (2007) Trends Cell. Biol , vol.17 , pp. 87-92
    • Caplan, A.J.1    Mandal, A.K.2    Theodoraki, M.A.3
  • 14
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • Pearl, L. H.; Prodromou, C.; Workman, P. The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem. J. 2008, 410, 439-453.
    • (2008) Biochem. J , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 15
    • 61949212454 scopus 로고    scopus 로고
    • Visualizing the twists and turns of a molecular chaperone
    • Neckers, L.; Tsutsumi, S.; Mollapour, M. Visualizing the twists and turns of a molecular chaperone. Nat. Struct. Mol. Biol. 2009, 16, 235-236.
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 235-236
    • Neckers, L.1    Tsutsumi, S.2    Mollapour, M.3
  • 17
    • 0141819958 scopus 로고    scopus 로고
    • The stress response: Implications for the clinical development of Hsp90 inhibitors
    • Whitesell, L.; Bagatell, R.; Falsey, R. The stress response: implications for the clinical development of Hsp90 inhibitors. Curr. Cancer Drug Targets 2003, 3, 349-358.
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 349-358
    • Whitesell, L.1    Bagatell, R.2    Falsey, R.3
  • 18
    • 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.; Prohaszka, 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    Prohaszka, Z.4    Nardai, G.5
  • 19
    • 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 2003, 3, 331-341.
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 331-341
    • Maloney, A.1    Clarke, P.A.2    Workman, P.3
  • 20
    • 37649024109 scopus 로고    scopus 로고
    • Development and application of Hsp90 inhibitors
    • Solit, D. B.; Chiosis, G. Development and application of Hsp90 inhibitors. Drug Discov. Today 2008, 13, 38-43.
    • (2008) Drug Discov. Today , vol.13 , pp. 38-43
    • Solit, D.B.1    Chiosis, G.2
  • 21
    • 36849056135 scopus 로고    scopus 로고
    • Drug-mediated targeted disruption of multiple protein activities through functional inhibition of the Hsp90 chaperone complex
    • Stravopodis, D. J.; Margaritis, L. H.; Voutsinas, G. E. Drug-mediated targeted disruption of multiple protein activities through functional inhibition of the Hsp90 chaperone complex. Curr. Med. Chem. 2007, 14, 3122-3138.
    • (2007) Curr. Med. Chem , vol.14 , pp. 3122-3138
    • Stravopodis, D.J.1    Margaritis, L.H.2    Voutsinas, G.E.3
  • 22
    • 34249820803 scopus 로고    scopus 로고
    • Hsp90: A novel target for the disruption of multiple signaling cascades
    • Bishop, S. C.; Burlison, J. A.; Blagg, B. S. J. Hsp90: a novel target for the disruption of multiple signaling cascades. Curr. Cancer Drug Targets 2007, 7, 369-388.
    • (2007) Curr. Cancer Drug Targets , vol.7 , pp. 369-388
    • Bishop, S.C.1    Burlison, J.A.2    Blagg, B.S.J.3
  • 23
    • 33846157482 scopus 로고    scopus 로고
    • Hsp90 as a target for drug development
    • Chaudhury, S.; Welch, T. R.; Blagg, B. S. J. Hsp90 as a target for drug development. ChemMedChem 2006, 1, 1331-1340.
    • (2006) ChemMedChem , vol.1 , pp. 1331-1340
    • Chaudhury, S.1    Welch, T.R.2    Blagg, B.S.J.3
  • 24
    • 33646114761 scopus 로고    scopus 로고
    • Hsp90 inhibitors: Small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation
    • Blagg, B. S. J.; Kerr, T. D. Hsp90 inhibitors: small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation. Med. Res. Rev. 2006, 26, 310-338.
    • (2006) Med. Res. Rev , vol.26 , pp. 310-338
    • Blagg, B.S.J.1    Kerr, T.D.2
  • 25
    • 33746417580 scopus 로고    scopus 로고
    • Hsp90: A novel target for cancer therapy
    • Solit, D. B.; Rosen, N. Hsp90: a novel target for cancer therapy. Curr. Top. Med. Chem. 2006, 6, 1205-1214.
    • (2006) Curr. Top. Med. Chem , vol.6 , pp. 1205-1214
    • Solit, D.B.1    Rosen, N.2
  • 26
    • 61649098007 scopus 로고    scopus 로고
    • Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket
    • Donnelly, A.; Blagg, B. S. J. Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket. Curr. Med. Chem. 2008, 15, 2702-2717.
    • (2008) Curr. Med. Chem , vol.15 , pp. 2702-2717
    • Donnelly, A.1    Blagg, B.S.J.2
  • 27
    • 65449155145 scopus 로고    scopus 로고
    • Natural product inhibitors of Hsp90: Potential leads for drug discovery
    • Amolins, M. W.; Blagg, B. S. J. Natural product inhibitors of Hsp90: potential leads for drug discovery. Mini Rev. Med. Chem 2009, 9, 140-152.
    • (2009) Mini Rev. Med. Chem , vol.9 , pp. 140-152
    • Amolins, M.W.1    Blagg, B.S.J.2
  • 28
    • 44349149846 scopus 로고    scopus 로고
    • Gamendazole, an orally active indazole carboxylic acid male contraceptive agent, targets Hsp90AB1 (Hsp90BETA) and EEF1A1 (eEf1A), and stimulates Il1a transcription in rat sertoli cells
    • Tash, J. S.; Chakrasali, R.; Jakkaraj, S. R.; Hughes, J.; Smith, S. K.; Hornbaker, K.; Heckert, L. L.; Ozturk, S. B.; Hadden, M. K.; Kinzy, T. G.; Blagg, B. S. J.; Georg, G. I. Gamendazole, an orally active indazole carboxylic acid male contraceptive agent, targets Hsp90AB1 (Hsp90BETA) and EEF1A1 (eEf1A), and stimulates Il1a transcription in rat sertoli cells. Biol. Reprod. 2008, 78, 1139-1152.
    • (2008) Biol. Reprod , vol.78 , pp. 1139-1152
    • Tash, J.S.1    Chakrasali, R.2    Jakkaraj, S.R.3    Hughes, J.4    Smith, S.K.5    Hornbaker, K.6    Heckert, L.L.7    Ozturk, S.B.8    Hadden, M.K.9    Kinzy, T.G.10    Blagg, B.S.J.11    Georg, G.I.12
  • 29
    • 33746381708 scopus 로고    scopus 로고
    • Geldanamycin, radicicol, and chimeric inhibitors of the Hsp90 N-terminal ATP binding site
    • Hadden, M. K.; Lubbers, D. J.; Blagg, B. S. J. Geldanamycin, radicicol, and chimeric inhibitors of the Hsp90 N-terminal ATP binding site. Curr. Top. Med. Chem. 2006, 6, 1173-1182.
    • (2006) Curr. Top. Med. Chem , vol.6 , pp. 1173-1182
    • Hadden, M.K.1    Lubbers, D.J.2    Blagg, B.S.J.3
  • 30
    • 0141596941 scopus 로고    scopus 로고
    • Overview: Translating Hsp90 biology into Hsp90 drugs
    • Workman, P. Overview: translating Hsp90 biology into Hsp90 drugs. Curr. Cancer Drug Targets 2003, 3, 297-300.
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 297-300
    • Workman, P.1
  • 31
    • 33645839336 scopus 로고    scopus 로고
    • Chiosis, G.; Rodina, A.; Moulick, K. Emerging Hsp90 inhibitors: from discovery to clinic. Anticancer Agents Med. Chem. 2006, 6, 1-8.
    • Chiosis, G.; Rodina, A.; Moulick, K. Emerging Hsp90 inhibitors: from discovery to clinic. Anticancer Agents Med. Chem. 2006, 6, 1-8.
  • 33
    • 65349183594 scopus 로고    scopus 로고
    • Discovery of 5-substituted 2-amino-4-chloro-8-((4-methoxy-3,5-dimethylpyridin-2-yl)methyl)-7, 8-dihydropteridin-6(5H)-ones as potent and selective Hsp90- inhibitors
    • Li, X.; Shocron, E.; Song, A.; Patel, N.; Sun, C. L. Discovery of 5-substituted 2-amino-4-chloro-8-((4-methoxy-3,5-dimethylpyridin-2-yl)methyl)-7, 8-dihydropteridin-6(5H)-ones as potent and selective Hsp90- inhibitors. Bioorg. Med. Chem. Lett. 2009, 19, 2860-2864.
    • (2009) Bioorg. Med. Chem. Lett , vol.19 , pp. 2860-2864
    • Li, X.1    Shocron, E.2    Song, A.3    Patel, N.4    Sun, C.L.5
  • 34
    • 67649586399 scopus 로고    scopus 로고
    • Hadden, M. K.; Blagg, B. S. J. Synthesis and evaluation of radamide analogues, a chimera of radicicol and geldanamycin. J. Org. Chem. 2009, 74, 4697-4704.
    • Hadden, M. K.; Blagg, B. S. J. Synthesis and evaluation of radamide analogues, a chimera of radicicol and geldanamycin. J. Org. Chem. 2009, 74, 4697-4704.
  • 35
    • 66149188136 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of conformationally constrained cisamide Hsp90 inhibitors
    • Duerfeldt, A. S.; Brandt, G. E. L.; Blagg, B. S. J. Design, synthesis, and biological evaluation of conformationally constrained cisamide Hsp90 inhibitors. Org. Lett. 2009, 11, 2353-2360.
    • (2009) Org. Lett , vol.11 , pp. 2353-2360
    • Duerfeldt, A.S.1    Brandt, G.E.L.2    Blagg, B.S.J.3
  • 36
    • 33644979098 scopus 로고    scopus 로고
    • Radanamycin, a macrocyclic chimera of radicicol and geldanamycin
    • Wang, M.; Shen, G.; Blagg, B. S. J. Radanamycin, a macrocyclic chimera of radicicol and geldanamycin. Bioorg. Med. Chem. Lett. 2006, 16, 2459-2462.
    • (2006) Bioorg. Med. Chem. Lett , vol.16 , pp. 2459-2462
    • Wang, M.1    Shen, G.2    Blagg, B.S.J.3
  • 37
    • 20444465254 scopus 로고    scopus 로고
    • Radester, a novel inhibitor of the Hsp90 protein folding machinery
    • Shen, G.; Blagg, B. S. J. Radester, a novel inhibitor of the Hsp90 protein folding machinery. Org. Lett. 2005, 7, 2157-2160.
    • (2005) Org. Lett , vol.7 , pp. 2157-2160
    • Shen, G.1    Blagg, B.S.J.2
  • 38
    • 10044237881 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of a radicicol and geldanamycin chimera, radamide
    • Clevenger, R. C.; Blagg, B. S. J. Design, synthesis, and evaluation of a radicicol and geldanamycin chimera, radamide. Org. Lett. 2004, 6, 4459-4462.
    • (2004) Org. Lett , vol.6 , pp. 4459-4462
    • Clevenger, R.C.1    Blagg, B.S.J.2
  • 39
    • 7044269372 scopus 로고    scopus 로고
    • Syntheses of photolabile novobiocin analogues
    • Shen, G.; Yu, X. M.; Blagg, B. S. Syntheses of photolabile novobiocin analogues. Bioorg. Med. Chem. Lett. 2004, 14, 5903-5906.
    • (2004) Bioorg. Med. Chem. Lett , vol.14 , pp. 5903-5906
    • Shen, G.1    Yu, X.M.2    Blagg, B.S.3
  • 41
    • 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. 2000, 92, 242-248.
    • (2000) J. Natl. Cancer Inst , vol.92 , pp. 242-248
    • Marcu, M.G.1    Schulte, T.W.2    Neckers, L.3
  • 42
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl 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 carboxyl terminus of the chaperone. J. Biol. Chem. 2000, 275, 37181-37186.
    • (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
  • 43
    • 38349153572 scopus 로고    scopus 로고
    • A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells
    • Zhang, T.; Hamza, A.; Cao, X.; Wang, B.; Yu, S.; Zhan, C.-G.; Sun, D. A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells. Mol. Cancer Ther. 2008, 7, 162-170.
    • (2008) Mol. Cancer Ther , vol.7 , pp. 162-170
    • Zhang, T.1    Hamza, A.2    Cao, X.3    Wang, B.4    Yu, S.5    Zhan, C.-G.6    Sun, D.7
  • 44
    • 58149144382 scopus 로고    scopus 로고
    • Yi, F.; Regan, L. A novel class of small molecule inhibitors of Hsp90. ACS Chem. Biol. 2008, 3, 645-654.
    • Yi, F.; Regan, L. A novel class of small molecule inhibitors of Hsp90. ACS Chem. Biol. 2008, 3, 645-654.
  • 45
    • 63849342150 scopus 로고    scopus 로고
    • An Alphascreen-based high-throughput screen to identify inhibitors of Hsp90-cochaperone interaction
    • Yi, F.; Zhu, P.; Southall, N.; Inglese, J.; Austin, C. P.; Zheng, W.; Regan, L. An Alphascreen-based high-throughput screen to identify inhibitors of Hsp90-cochaperone interaction. J. Biomol. Screen. 2009, 14, 273-281.
    • (2009) J. Biomol. Screen , vol.14 , pp. 273-281
    • Yi, F.1    Zhu, P.2    Southall, N.3    Inglese, J.4    Austin, C.P.5    Zheng, W.6    Regan, L.7
  • 46
    • 42449136263 scopus 로고    scopus 로고
    • Cortajarena, A. L.; Yi, F.; Regan, L. Designed TPR modules as novel anticancer agents. ACS Chem. Biol. 2008, 3, 161-166.
    • Cortajarena, A. L.; Yi, F.; Regan, L. Designed TPR modules as novel anticancer agents. ACS Chem. Biol. 2008, 3, 161-166.
  • 47
    • 70350548428 scopus 로고    scopus 로고
    • 17 AAG for Hsp90 inhibition in cancer--from bench to bedside
    • Usmani, S. Z.; Bona, R.; Li, Z. 17 AAG for Hsp90 inhibition in cancer--from bench to bedside. Curr. Mol. Med. 2009, 9, 654-664.
    • (2009) Curr. Mol. Med , vol.9 , pp. 654-664
    • Usmani, S.Z.1    Bona, R.2    Li, Z.3
  • 48
    • 67650667501 scopus 로고    scopus 로고
    • Molecular Targets for Tumor Radiosensitization
    • Tofilon, P. J.; Camphausen, K. Molecular Targets for Tumor Radiosensitization. Chem. Rev. 2009, 109, 2974-2988.
    • (2009) Chem. Rev , vol.109 , pp. 2974-2988
    • Tofilon, P.J.1    Camphausen, K.2
  • 49
    • 58849160500 scopus 로고    scopus 로고
    • Heat shock protein 90 as a drug target: Some like it hot
    • Banerji, U. Heat shock protein 90 as a drug target: some like it hot. Clin. Cancer Res. 2009, 15, 9-14.
    • (2009) Clin. Cancer Res , vol.15 , pp. 9-14
    • Banerji, U.1
  • 51
    • 33746379315 scopus 로고    scopus 로고
    • Using natural product inhibitors to validate Hsp90 as a molecular target in cancer
    • Neckers, L. Using natural product inhibitors to validate Hsp90 as a molecular target in cancer. Curr. Top. Med. Chem. 2006, 6, 1163-1171.
    • (2006) Curr. Top. Med. Chem , vol.6 , pp. 1163-1171
    • Neckers, L.1
  • 52
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response: Biology and pharmacology
    • Powers, M. V.; Workman, P. Inhibitors of the heat shock response: biology and pharmacology. FEBS Lett. 2007, 581, 3758-3769.
    • (2007) FEBS Lett , vol.581 , pp. 3758-3769
    • Powers, M.V.1    Workman, P.2
  • 54
    • 0026702767 scopus 로고
    • The role of Hsp90 in fungal infection
    • Matthews, R.; Burnie, J. The role of Hsp90 in fungal infection. Immunol. Today 1992, 13, 345-348.
    • (1992) Immunol. Today , vol.13 , pp. 345-348
    • Matthews, R.1    Burnie, J.2
  • 56
    • 73449115305 scopus 로고    scopus 로고
    • Hsp90 and co-chaperones twist the functions of diverse client proteins
    • In Press
    • Zuehlke, A.; Johnson, J. L. Hsp90 and co-chaperones twist the functions of diverse client proteins. Biopolymers 2009, In Press.
    • (2009) Biopolymers
    • Zuehlke, A.1    Johnson, J.L.2
  • 58
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl, L. H.; Prodromou, C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 2006, 75, 271-294.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 59
    • 0033985080 scopus 로고    scopus 로고
    • GHKL, an emergent ATPase/kinase superfamily
    • Dutta, R.; Inouye, M. GHKL, an emergent ATPase/kinase superfamily. Trends Biochem. Sci. 2000, 25, 24-28.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 24-28
    • Dutta, R.1    Inouye, M.2
  • 60
    • 53149118242 scopus 로고    scopus 로고
    • The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts
    • Pratt, W. B.; Morishima, Y.; Osawa, Y. The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts. J. Biol. Chem. 2008, 283, 22885-22889.
    • (2008) J. Biol. Chem , vol.283 , pp. 22885-22889
    • Pratt, W.B.1    Morishima, Y.2    Osawa, Y.3
  • 61
    • 84934440933 scopus 로고    scopus 로고
    • Voellmy, R.; Boellmann, F. Chaperone Regulation of the Heat Shock Protein Response. In Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks, Csermely, P.; Vigh, L., Eds. Landes Bioscience and Springer Science+Business Media: New York, 2007; 594, pp 89-99.
    • Voellmy, R.; Boellmann, F. Chaperone Regulation of the Heat Shock Protein Response. In Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks, Csermely, P.; Vigh, L., Eds. Landes Bioscience and Springer Science+Business Media: New York, 2007; Vol. 594, pp 89-99.
  • 62
    • 33846861747 scopus 로고    scopus 로고
    • Targeting of multiple signalling pathways by heat shock protein 90 molecular chaperone inhibitors
    • Powers, M. V.; Workman, P. Targeting of multiple signalling pathways by heat shock protein 90 molecular chaperone inhibitors. Endocr. Relat. Cancer 2006, 13, 125-135.
    • (2006) Endocr. Relat. Cancer , vol.13 , pp. 125-135
    • Powers, M.V.1    Workman, P.2
  • 63
    • 0027475243 scopus 로고
    • Hsp90 chaperonins posses ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases
    • Nadeau, K.; Das, A.; Walsh, C. T. Hsp90 chaperonins posses 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
  • 65
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou, B.; Prodromou, C.; Roe, 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
  • 68
    • 44349097402 scopus 로고    scopus 로고
    • Structural studies on the co-chaperone Hop and its complexes with Hsp90
    • Onuoha, S. C.; Coulstock, E. T.; Grossmann, J. G.; Jackson, S. E. Structural studies on the co-chaperone Hop and its complexes with Hsp90. J. Mol. Biol. 2008, 379, 732-744.
    • (2008) J. Mol. Biol , vol.379 , pp. 732-744
    • Onuoha, S.C.1    Coulstock, E.T.2    Grossmann, J.G.3    Jackson, S.E.4
  • 69
    • 3042656869 scopus 로고    scopus 로고
    • Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interations
    • 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 interations. Biochemistry 2004, 43, 8217-8229.
    • (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
  • 70
    • 0033596852 scopus 로고    scopus 로고
    • Molybdate inhibitos Hsp90. induces structural changes in its C-terminal domain, and alters its interactions with substrates
    • Hartson, S. D.; Thulasiraman, V.; Huang, W.; Whitesell, L.; Matts, R. L. Molybdate inhibitos Hsp90. induces structural changes in its C-terminal domain, and alters its interactions with substrates. Biochemistry 1999, 38, 3837-3849.
    • (1999) Biochemistry , vol.38 , pp. 3837-3849
    • Hartson, S.D.1    Thulasiraman, V.2    Huang, W.3    Whitesell, L.4    Matts, R.L.5
  • 71
    • 0033596852 scopus 로고    scopus 로고
    • Molybdate inhibits Hsp90, induces structural changes in its C-terminal domain, and alters its interactions with substrates
    • Hartson, S. D.; Thulasiraman, V.; Huang, W.; Whitesell, L.; Matts, R. L. Molybdate inhibits Hsp90, induces structural changes in its C-terminal domain, and alters its interactions with substrates. Biochemistry 1999, 38, 3837-3849.
    • (1999) Biochemistry , vol.38 , pp. 3837-3849
    • Hartson, S.D.1    Thulasiraman, V.2    Huang, W.3    Whitesell, L.4    Matts, R.L.5
  • 73
    • 0038730655 scopus 로고    scopus 로고
    • Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: A distinct nucleotide specificity of the C-terminal ATP-binding site
    • Soti, C.; Vermes, A.; Haystead, T. A. J.; Csermely, P. Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding site. Eur. J. Biochem. 2003, 270, 2421-2428.
    • (2003) Eur. J. Biochem , vol.270 , pp. 2421-2428
    • Soti, C.1    Vermes, A.2    Haystead, T.A.J.3    Csermely, P.4
  • 74
    • 40149091263 scopus 로고    scopus 로고
    • Analysis of Hsp90 cochaperone interactions reveals a novel mechanism for TPR protein recognition
    • Chadli, A.; Bruinsma, E. S.; Stensgard, B.; Toft, D. Analysis of Hsp90 cochaperone interactions reveals a novel mechanism for TPR protein recognition. Biochemistry 2008, 47, 2850-2857.
    • (2008) Biochemistry , vol.47 , pp. 2850-2857
    • Chadli, A.1    Bruinsma, E.S.2    Stensgard, B.3    Toft, D.4
  • 75
    • 7044240678 scopus 로고    scopus 로고
    • Odunuga, O. O.; Longshaw, V. M.; Blatch, G. L. Hop: more than and Hsp70/Hsp90 adaptor protein. Bioessays 2004, 26, 1058-1068.
    • Odunuga, O. O.; Longshaw, V. M.; Blatch, G. L. Hop: more than and Hsp70/Hsp90 adaptor protein. Bioessays 2004, 26, 1058-1068.
  • 76
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery
    • Chen, S.; Smith, D. F. Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery. J. Biol. Chem. 1998, 273, 35194-35200.
    • (1998) J. Biol. Chem , vol.273 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 77
    • 4644318581 scopus 로고    scopus 로고
    • Davies, T. H.; Sanchez, E. R. FKBP52. Int. J. Biochem. Cell Biol. 2005, 37, 42-47.
    • Davies, T. H.; Sanchez, E. R. FKBP52. Int. J. Biochem. Cell Biol. 2005, 37, 42-47.
  • 79
    • 69249130057 scopus 로고    scopus 로고
    • The charged linker region is an important regulator of hsp90 function
    • Hainzl, O.; Lapina, M. C.; Buchner, J.; Richter, K. The charged linker region is an important regulator of hsp90 function. J. Biol. Chem. 2009, 284, 22559-22567.
    • (2009) J. Biol. Chem , vol.284 , pp. 22559-22567
    • Hainzl, O.1    Lapina, M.C.2    Buchner, J.3    Richter, K.4
  • 80
    • 33750983940 scopus 로고    scopus 로고
    • The middle domain of Hsp90 acts as a discriminator between different types of client proteins
    • Hawle, P.; Siepmann, M.; Harst, A.; Siderius, M.; Reusch, H. P.; Obermann, W. M. The middle domain of Hsp90 acts as a discriminator between different types of client proteins. Mol. Cell Biol. 2006, 26, 8385-8395.
    • (2006) Mol. Cell Biol , vol.26 , pp. 8385-8395
    • Hawle, P.1    Siepmann, M.2    Harst, A.3    Siderius, M.4    Reusch, H.P.5    Obermann, W.M.6
  • 81
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle sigment of Hsp90: Implications for ATP hydrolysis and client protein and cochaperone interactions
    • Meyer, P.; Prodromou, C.; Hu, B.; Vaughan, C.; Roe, S. M.; Panaretou, B.; Piper, P. W.; Pearl, L. H. Structural and functional analysis of the middle sigment of Hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol. Cell. 2003, 11, 647-658.
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6    Piper, P.W.7    Pearl, L.H.8
  • 83
    • 0037593900 scopus 로고    scopus 로고
    • Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone
    • Lotz, G. P.; Lin, H.; Harst, A.; Obermann, W. M. J. Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J. Biol. Chem. 2003, 278, 17228-17235.
    • (2003) J. Biol. Chem , vol.278 , pp. 17228-17235
    • Lotz, G.P.1    Lin, H.2    Harst, A.3    Obermann, W.M.J.4
  • 84
    • 33749538453 scopus 로고    scopus 로고
    • Convergent evolution of clamp-like binding sites in diverse chaperones
    • Stirling, P. C.; Bakhoum, S. F.; Feigl, A. B.; Leroux, M. R. Convergent evolution of clamp-like binding sites in diverse chaperones. Nat. Struct. Mol. Biol. 2006, 13, 865-870.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 865-870
    • Stirling, P.C.1    Bakhoum, S.F.2    Feigl, A.B.3    Leroux, M.R.4
  • 86
    • 0742269688 scopus 로고    scopus 로고
    • The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50cdc37
    • Roe, S. M.; Ali, M. M.; Meyer, P.; Vaughan, C. K.; Panaretou, B.; Piper, P. W. The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50cdc37. Cell 2004, 11, 87-98.
    • (2004) Cell , vol.11 , pp. 87-98
    • Roe, S.M.1    Ali, M.M.2    Meyer, P.3    Vaughan, C.K.4    Panaretou, B.5    Piper, P.W.6
  • 87
    • 51049093018 scopus 로고    scopus 로고
    • Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90
    • Cunningham, C. N.; Krukenberg, K. A.; Agard, D. A. Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90. J. Biol. Chem. 2008, 283, 21170-21178.
    • (2008) J. Biol. Chem , vol.283 , pp. 21170-21178
    • Cunningham, C.N.1    Krukenberg, K.A.2    Agard, D.A.3
  • 88
    • 0034720777 scopus 로고    scopus 로고
    • p50cdc37 is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules
    • Hartson, S. D.; Irwin, A. D.; Shao, J.; Scroggins, B. T.; Volk, L.; Huang, W.; Matts, R. L. p50cdc37 is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules. Biochemistry 2000, 39, 7631-7644.
    • (2000) Biochemistry , vol.39 , pp. 7631-7644
    • Hartson, S.D.1    Irwin, A.D.2    Shao, J.3    Scroggins, B.T.4    Volk, L.5    Huang, W.6    Matts, R.L.7
  • 89
    • 62949238913 scopus 로고    scopus 로고
    • New developments in Hsp90 inhibitors as anti-cancer therapeutics: Mechanisms, clinical prespective and more potential
    • Li, Y.; Zhang, T.; Schwartz, S. J.; Sun, D. New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical prespective and more potential. Drug Resist. Updat. 2009, 12, 17-27.
    • (2009) Drug Resist. Updat , vol.12 , pp. 17-27
    • Li, Y.1    Zhang, T.2    Schwartz, S.J.3    Sun, D.4
  • 90
    • 51449093764 scopus 로고    scopus 로고
    • Targeting Hsp90: Small-molecule inhibitors and their clinical development
    • Taldone, T.; Gozman, A.; Maharaj, R.; Chiosis, G. Targeting Hsp90: small-molecule inhibitors and their clinical development. Curr. Opin. Pharmcol. 2008, 8, 370-374.
    • (2008) Curr. Opin. Pharmcol , vol.8 , pp. 370-374
    • Taldone, T.1    Gozman, A.2    Maharaj, R.3    Chiosis, G.4
  • 91
    • 67650741952 scopus 로고    scopus 로고
    • Huang, K. H.; Veal, J. M.; Fadden, R. P.; Rice, J. W.; Eaves, J.; Strachan, J. P.; Barabasz, A. F.; Foley, B. E.; Barta, T. E.; Ma, W.; Silinski, M. A.; Hu, M.; Partridge, J. M.; Scott, A.; DuBois, L. G.; Freed, T.; Steed, P. M.; Ommen, A. J.; Smith, E. D.; Hughes, P. F.; Woodward, A. R.; Hanson, G. J.; McCall, W. S.; Markworth, C. J.; Hinkley, L.; Jenks, M.; Geng, L.; Lewis, M.; Otto, J.; Pronk, B.; Verleysen, K.; Hall, S. E. Discovery of novel 2-aminobenzamide inhibitors of heat shock protein 90 as potent, selective and orally active antitumor agents. J. Med. Chem. 2009, 52, 4288-4305.
    • Huang, K. H.; Veal, J. M.; Fadden, R. P.; Rice, J. W.; Eaves, J.; Strachan, J. P.; Barabasz, A. F.; Foley, B. E.; Barta, T. E.; Ma, W.; Silinski, M. A.; Hu, M.; Partridge, J. M.; Scott, A.; DuBois, L. G.; Freed, T.; Steed, P. M.; Ommen, A. J.; Smith, E. D.; Hughes, P. F.; Woodward, A. R.; Hanson, G. J.; McCall, W. S.; Markworth, C. J.; Hinkley, L.; Jenks, M.; Geng, L.; Lewis, M.; Otto, J.; Pronk, B.; Verleysen, K.; Hall, S. E. Discovery of novel 2-aminobenzamide inhibitors of heat shock protein 90 as potent, selective and orally active antitumor agents. J. Med. Chem. 2009, 52, 4288-4305.
  • 92
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D.; Weinberg, R. A. The hallmarks of cancer. Cell 2000, 100, 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 93
    • 64949083563 scopus 로고    scopus 로고
    • Inhibition of cancer invasion and metastasis by targeting the molecular chaperone heat-shock protein 90
    • Koga, F.; Kihara, K.; Neckers, L. Inhibition of cancer invasion and metastasis by targeting the molecular chaperone heat-shock protein 90. Anticancer Res. 2009, 29, 797-807.
    • (2009) Anticancer Res , vol.29 , pp. 797-807
    • Koga, F.1    Kihara, K.2    Neckers, L.3
  • 94
    • 33745174538 scopus 로고    scopus 로고
    • Heat shock protein-90 inhibitors: A chronicle from geldanamycin to today's agents
    • Chiosis, G.; Lopes, E. C.; Solit, D. Heat shock protein-90 inhibitors: a chronicle from geldanamycin to today's agents. Curr. Opin Investig. Drugs 2006, 7, 534-541.
    • (2006) Curr. Opin Investig. Drugs , vol.7 , pp. 534-541
    • Chiosis, G.1    Lopes, E.C.2    Solit, D.3
  • 95
    • 33845913216 scopus 로고    scopus 로고
    • Intracellular and extracellular functions of heat shock proteins: Repercussions in cancer therapy
    • Schmitt, E.; Gehrmann, M.; Brunet, M.; Multhoff, G.; Garrido, C. Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy. J. Leukoc. Bio. 2007, 81, 15-27.
    • (2007) J. Leukoc. Bio , vol.81 , pp. 15-27
    • Schmitt, E.1    Gehrmann, M.2    Brunet, M.3    Multhoff, G.4    Garrido, C.5
  • 96
    • 11844304102 scopus 로고    scopus 로고
    • In vivo stress preconditioning
    • Pespeni, M.; Hodnett, M.; Pittet, J. F. In vivo stress preconditioning. Methods 2005, 35, 158-164.
    • (2005) Methods , vol.35 , pp. 158-164
    • Pespeni, M.1    Hodnett, M.2    Pittet, J.F.3
  • 97
    • 43249125196 scopus 로고    scopus 로고
    • New insights into the mechanism of heat shock response activation
    • Shamovsky, I.; Nudler, E. New insights into the mechanism of heat shock response activation. Cell Mol. Life Sci. 2008, 65, 855-861.
    • (2008) Cell Mol. Life Sci , vol.65 , pp. 855-861
    • Shamovsky, I.1    Nudler, E.2
  • 98
    • 18244384703 scopus 로고    scopus 로고
    • Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress
    • Guettouche, T.; Boellmann, F.; Lane, W. S.; Voellmy, R. Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress. BMC Biochem. 2005, 6, 4.
    • (2005) BMC Biochem , vol.6 , pp. 4
    • Guettouche, T.1    Boellmann, F.2    Lane, W.S.3    Voellmy, R.4
  • 100
    • 60049098351 scopus 로고    scopus 로고
    • Neuroprotective activity and evaluation of Hsp90 inhibitors in an immortalized neuronal cell line
    • Lu, Y.; Ansar, S.; Michaelis, M. L.; Blagg, B. S. J. Neuroprotective activity and evaluation of Hsp90 inhibitors in an immortalized neuronal cell line. Bioorg. Med. Chem. 2009, 17, 1709-1715.
    • (2009) Bioorg. Med. Chem , vol.17 , pp. 1709-1715
    • Lu, Y.1    Ansar, S.2    Michaelis, M.L.3    Blagg, B.S.J.4
  • 102
    • 74249109889 scopus 로고    scopus 로고
    • To fold or not to fold: Modulation and consequences of Hsp90 inhibition
    • Peterson, L. B.; Blagg, B. S. J. To fold or not to fold: modulation and consequences of Hsp90 inhibition. Future Medicinal Chemistry 2009, 1, 267-283.
    • (2009) Future Medicinal Chemistry , vol.1 , pp. 267-283
    • Peterson, L.B.1    Blagg, B.S.J.2
  • 104
    • 0031647680 scopus 로고    scopus 로고
    • The regulation of heat shock proteins and their role in systemic lupus erythematosus
    • Stephanou, A.; Latchman, D. S.; Isenberg, D. A. The regulation of heat shock proteins and their role in systemic lupus erythematosus. Semin. Arthritis Rheum. 1998, 28, 155-162.
    • (1998) Semin. Arthritis Rheum , vol.28 , pp. 155-162
    • Stephanou, A.1    Latchman, D.S.2    Isenberg, D.A.3
  • 105
    • 55049085236 scopus 로고    scopus 로고
    • Endothelial nitric oxide (NO) and its pathophysiologic regulation
    • Chatterjee, A.; Black, S. M.; Catravas, J. D. Endothelial nitric oxide (NO) and its pathophysiologic regulation. Vascul. Pharmacol. 2008, 49, 134-140.
    • (2008) Vascul. Pharmacol , vol.49 , pp. 134-140
    • Chatterjee, A.1    Black, S.M.2    Catravas, J.D.3
  • 106
    • 10844230206 scopus 로고    scopus 로고
    • Stress-induced inhibtion of the NF-kB signaling pathway results from the insolubilization of the IkB kinase complex following its dissociation from heat shock protein 90
    • Pittet, J.-F.; Lee, H.; Pespeni, M.; O'Mahony, A.; Roux, J.; Welch, W. J. Stress-induced inhibtion of the NF-kB signaling pathway results from the insolubilization of the IkB kinase complex following its dissociation from heat shock protein 90. J. immunol. 2005, 174, 384-394.
    • (2005) J. immunol , vol.174 , pp. 384-394
    • Pittet, J.-F.1    Lee, H.2    Pespeni, M.3    O'Mahony, A.4    Roux, J.5    Welch, W.J.6
  • 107
    • 38449087767 scopus 로고    scopus 로고
    • Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase
    • Arthur, J. C.; Lich, J. D.; Aziz, R. K.; Kotb, M.; Ting, J. P. Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase. J. Immunol. 2007, 179, 6291-6296.
    • (2007) J. Immunol , vol.179 , pp. 6291-6296
    • Arthur, J.C.1    Lich, J.D.2    Aziz, R.K.3    Kotb, M.4    Ting, J.P.5
  • 108
    • 40649123232 scopus 로고    scopus 로고
    • Innate immunity meets with cellular stress at the IKK complex: Regulation of the IKK complex by Hsp70 and Hsp90
    • Salminen, A.; Paimela, T.; Suuronen, T.; Kaarniranta, K. Innate immunity meets with cellular stress at the IKK complex: regulation of the IKK complex by Hsp70 and Hsp90. Immunol. Lett. 2008, 117, 9-15.
    • (2008) Immunol. Lett , vol.117 , pp. 9-15
    • Salminen, A.1    Paimela, T.2    Suuronen, T.3    Kaarniranta, K.4
  • 109
    • 33845306864 scopus 로고    scopus 로고
    • Novobiocin: Redesigning a DNA gyrase inhibitor for selective inhibition of Hsp90
    • Burlison, J. A.; Neckers, L.; Smith, A. B.; Maxwell, A.; Blagg, B. S. J. Novobiocin: redesigning a DNA gyrase inhibitor for selective inhibition of Hsp90. J. Am. Chem. Soc. 2006, 128, 15529-15536.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 15529-15536
    • Burlison, J.A.1    Neckers, L.2    Smith, A.B.3    Maxwell, A.4    Blagg, B.S.J.5
  • 110
    • 16344364163 scopus 로고    scopus 로고
    • Epigallocatechin gallate inhibits aryl hydrocarbon receptor gene transcription through an indirect mechanism involving binding to a 90 KDa heat shock protein
    • Palermo, C. M.; Westlake, C. A.; Gasiewicz, T. A. Epigallocatechin gallate inhibits aryl hydrocarbon receptor gene transcription through an indirect mechanism involving binding to a 90 KDa heat shock protein. Biochemistry 2005, 44, 5041-5052.
    • (2005) Biochemistry , vol.44 , pp. 5041-5052
    • Palermo, C.M.1    Westlake, C.A.2    Gasiewicz, T.A.3
  • 111
    • 0033231024 scopus 로고    scopus 로고
    • A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone Hsp90
    • Itoh, H.; Ogura, M.; Komatsuda, A.; Wakui, H.; Miura, A. B.; Tashima, Y. A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone Hsp90. Biochem. J. 1999, 343, 697-703.
    • (1999) Biochem. J , vol.343 , pp. 697-703
    • Itoh, H.1    Ogura, M.2    Komatsuda, A.3    Wakui, H.4    Miura, A.B.5    Tashima, Y.6
  • 112
    • 0036510547 scopus 로고    scopus 로고
    • A nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90
    • Soti, C.; Raez, A.; Csermely, P. A nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. J. Biol. Chem. 2002, 277, 7066-7075.
    • (2002) J. Biol. Chem , vol.277 , pp. 7066-7075
    • Soti, C.1    Raez, A.2    Csermely, P.3
  • 114
    • 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. 2003, 63, 2139-2144.
    • (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
  • 115
    • 66449133399 scopus 로고
    • Novobiocin; a limited bacteriologic and clinical study of its use in forty-five patients
    • Nichols, R. L.; Finland, M. Novobiocin; a limited bacteriologic and clinical study of its use in forty-five patients. Antibiotic Med. Clin. Ther. 1956, 2, 241-257.
    • (1956) Antibiotic Med. Clin. Ther , vol.2 , pp. 241-257
    • Nichols, R.L.1    Finland, M.2
  • 116
    • 33646371009 scopus 로고    scopus 로고
    • Modulation of chaperone function and cochaperone interaction by novobiocin in C-terminal domain of Hsp90
    • Allan, R. K.; Mok, D.; Ward, B. K.; Ratajczak, T. Modulation of chaperone function and cochaperone interaction by novobiocin in C-terminal domain of Hsp90. J. Biol. Chem. 2006, 281, 7161-7171.
    • (2006) J. Biol. Chem , vol.281 , pp. 7161-7171
    • Allan, R.K.1    Mok, D.2    Ward, B.K.3    Ratajczak, T.4
  • 117
    • 37849037720 scopus 로고    scopus 로고
    • New novobiocin analogues as antiproliferative agents in breast cancer cells and potential inhibitors of heat shock protein 90
    • Bras, G. L.; Radanyi, C.; Peyrat, J. F.; Brion, J. D.; Alami, M.; Marsaud, V.; Stella, B.; Renoir, J. M. New novobiocin analogues as antiproliferative agents in breast cancer cells and potential inhibitors of heat shock protein 90. J. Med. Chem. 2007, 50, 6189-6200.
    • (2007) J. Med. Chem , vol.50 , pp. 6189-6200
    • Bras, G.L.1    Radanyi, C.2    Peyrat, J.F.3    Brion, J.D.4    Alami, M.5    Marsaud, V.6    Stella, B.7    Renoir, J.M.8
  • 118
    • 41849084518 scopus 로고    scopus 로고
    • Development of novobiocin analogues that manifest anti-proliferative activity against several cancer cell lines
    • Burlison, J. A.; Avila, C.; Vielhauer, G.; Lubbers, D. J.; Holzbeierlein, J.; Blagg, B. S. J. Development of novobiocin analogues that manifest anti-proliferative activity against several cancer cell lines. J. Org. Chem. 2008, 73, 2130-2137.
    • (2008) J. Org. Chem , vol.73 , pp. 2130-2137
    • Burlison, J.A.1    Avila, C.2    Vielhauer, G.3    Lubbers, D.J.4    Holzbeierlein, J.5    Blagg, B.S.J.6
  • 119
    • 41349108858 scopus 로고    scopus 로고
    • Synthesis and biological activity of simplified denoviose-coumarins related to novobiocin as potent inhibitors of heat-shock protein 90 (Hsp90)
    • Radanyi, C.; Bras, G. L.; Messaoudi, S.; Bouclier, C.; Peyrat, J. F.; Brion, J. D.; marsaud, V.; Renoir, J. M.; Alami, M. Synthesis and biological activity of simplified denoviose-coumarins related to novobiocin as potent inhibitors of heat-shock protein 90 (Hsp90). Bioorg. Med. Chem. Lett. 2008, 18, 2495-2498.
    • (2008) Bioorg. Med. Chem. Lett , vol.18 , pp. 2495-2498
    • Radanyi, C.1    Bras, G.L.2    Messaoudi, S.3    Bouclier, C.4    Peyrat, J.F.5    Brion, J.D.6    marsaud, V.7    Renoir, J.M.8    Alami, M.9
  • 121
    • 56449125983 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of coumarin ring derivatives of the novobiocin scaffold that exhibit antiproliferative activity
    • Donnelly, A. C.; Mays, J. R.; Burlison, J. A.; Nelson, J. T.; Vielhauer, g.; Holzbeierlein, J.; Blagg, B. S. J. The design, synthesis, and evaluation of coumarin ring derivatives of the novobiocin scaffold that exhibit antiproliferative activity. J. Org. Chem. 2008, 73, 8901-8920.
    • (2008) J. Org. Chem , vol.73 , pp. 8901-8920
    • Donnelly, A.C.1    Mays, J.R.2    Burlison, J.A.3    Nelson, J.T.4    Vielhauer, G.5    Holzbeierlein, J.6    Blagg, B.S.J.7
  • 122
    • 38149116851 scopus 로고    scopus 로고
    • Multiple kinases and system robustness: A link between Cdc37 and genome integrity
    • Caplan, A. J.; Ayan, A. M.; Wilis, I. M. Multiple kinases and system robustness: a link between Cdc37 and genome integrity. Cell Cycle 2007, 6, 3145-3147.
    • (2007) Cell Cycle , vol.6 , pp. 3145-3147
    • Caplan, A.J.1    Ayan, A.M.2    Wilis, I.M.3
  • 125
    • 74249091431 scopus 로고    scopus 로고
    • Regulation of the kinome: When to hold 'em and when to fold 'em
    • pe22
    • Karnitz, L. M.; Felts, S. J. Regulation of the kinome: when to hold 'em and when to fold 'em. STKE 2007, pe22, 1-3.
    • (2007) STKE , pp. 1-3
    • Karnitz, L.M.1    Felts, S.J.2
  • 126
    • 12344291243 scopus 로고    scopus 로고
    • Pearl, L. H. Hsp90 and Cdc37 - a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 2005, 15, 55-61.
    • Pearl, L. H. Hsp90 and Cdc37 - a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 2005, 15, 55-61.
  • 128
    • 59449107850 scopus 로고    scopus 로고
    • Targeting Cdc37: An alternative, kinase-directed strategy for disruption of oncogenic chaperoning
    • Smith, J. R.; Workman, P. Targeting Cdc37: an alternative, kinase-directed strategy for disruption of oncogenic chaperoning. Cell Cycle 2009, 8, 362-372.
    • (2009) Cell Cycle , vol.8 , pp. 362-372
    • Smith, J.R.1    Workman, P.2
  • 129
    • 37549060720 scopus 로고    scopus 로고
    • Targeting Cdc37 inhibits multiple signaling pathways and induces growth arrest in prostate cancer cells
    • Gray, P. J. J.; Stevenson, M. A.; Calderwood, S. K. Targeting Cdc37 inhibits multiple signaling pathways and induces growth arrest in prostate cancer cells. Cancer Res. 2007, 67, 11942-11950.
    • (2007) Cancer Res , vol.67 , pp. 11942-11950
    • Gray, P.J.J.1    Stevenson, M.A.2    Calderwood, S.K.3
  • 130
    • 58249112898 scopus 로고    scopus 로고
    • Silencing the cochaperone Cdc37 destabilizes kinase clients and sensitizes cancer cells to Hsp90 inhibitors
    • Smith, J. R.; Clarke, P. A.; Billy, E. D.; Workman, P. Silencing the cochaperone Cdc37 destabilizes kinase clients and sensitizes cancer cells to Hsp90 inhibitors. Oncogene 2008, 28, 157-169.
    • (2008) Oncogene , vol.28 , pp. 157-169
    • Smith, J.R.1    Clarke, P.A.2    Billy, E.D.3    Workman, P.4
  • 131
    • 19544390715 scopus 로고    scopus 로고
    • Herbal medications commonly used in the practice of rheumatology: Mechanisms of action, efficacy, and side effects
    • Setty, A. R.; Sigal, L. H. Herbal medications commonly used in the practice of rheumatology: mechanisms of action, efficacy, and side effects. Semin. Arthritis Rheum. 2005, 34, 773-784.
    • (2005) Semin. Arthritis Rheum , vol.34 , pp. 773-784
    • Setty, A.R.1    Sigal, L.H.2
  • 132
    • 70349921403 scopus 로고    scopus 로고
    • Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol
    • Sreeramulu, S.; Gande, S. L.; Gobel, M.; Schwalbe, H. Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol. Angew. Chem. Int. Ed. 2009, 48, 5853-5855.
    • (2009) Angew. Chem. Int. Ed , vol.48 , pp. 5853-5855
    • Sreeramulu, S.1    Gande, S.L.2    Gobel, M.3    Schwalbe, H.4
  • 133
    • 41649104650 scopus 로고    scopus 로고
    • Activation of heat shock and antioxidant responses by the natural product celastrol: Transcriptional signatures of a thiol-targeted molecule
    • Trott, A.; West, J. D.; Klaic, L.; Westerheide, S. D.; Silverman, R. B.; Morimoto, R. I.; Morano, K. A. Activation of heat shock and antioxidant responses by the natural product celastrol: transcriptional signatures of a thiol-targeted molecule. Mol. Biol. Cell 2008, 19, 1104-1112.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1104-1112
    • Trott, A.1    West, J.D.2    Klaic, L.3    Westerheide, S.D.4    Silverman, R.B.5    Morimoto, R.I.6    Morano, K.A.7
  • 135
    • 33749335282 scopus 로고    scopus 로고
    • Lamb, J.; Crawford, E. D.; Peck, D.; Modell, J. W.; Blat, i. C.; Wrobel, M. J.; Lerner, J.; Brunet, J.-P.; Subramanian, A.; Ross, K. N.; Reich, M.; hieronymus, h.; Wei, G.; Armstrong, S. A.; Haggarty, S. J.; Clemons, P. A.; Wei, R.; Carr, S. A.; Lander, E. S.; Golub, T. R. The connectivity map: using gene-expression signatures to connect small molecules, genes, and disease. Science 2006, 313, 1929-1935.
    • Lamb, J.; Crawford, E. D.; Peck, D.; Modell, J. W.; Blat, i. C.; Wrobel, M. J.; Lerner, J.; Brunet, J.-P.; Subramanian, A.; Ross, K. N.; Reich, M.; hieronymus, h.; Wei, G.; Armstrong, S. A.; Haggarty, S. J.; Clemons, P. A.; Wei, R.; Carr, S. A.; Lander, E. S.; Golub, T. R. The connectivity map: using gene-expression signatures to connect small molecules, genes, and disease. Science 2006, 313, 1929-1935.
  • 138
    • 3242694307 scopus 로고    scopus 로고
    • Neem - an omnipotent plant: A retrospection
    • Brahmachari, G. Neem - an omnipotent plant: a retrospection. Chembiochem 2004, 5, 408-421.
    • (2004) Chembiochem , vol.5 , pp. 408-421
    • Brahmachari, G.1
  • 139
    • 33646406554 scopus 로고    scopus 로고
    • Yang, H.; Chen, D.; Cui, Z. C.; Yuan, X.; Dou, W. P. Celastrol, a triterpene extracted from the chinese thunder of god vine, is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice. Cancer Res. 2006, 66, 4758-4765.
    • Yang, H.; Chen, D.; Cui, Z. C.; Yuan, X.; Dou, W. P. Celastrol, a triterpene extracted from the chinese "thunder of god vine," is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice. Cancer Res. 2006, 66, 4758-4765.
  • 140
    • 54549105458 scopus 로고    scopus 로고
    • Gedunin, a novel Hsp90 inhibitor: Semisynthesis of derivatives and preliminary structure-activity relationships
    • Brandt, G. E. L.; Schmidt, M. D.; Prisinzano, T. E.; Blagg, B. S. J. Gedunin, a novel Hsp90 inhibitor: semisynthesis of derivatives and preliminary structure-activity relationships. J. Med. Chem. 2008, 51, 6495-6502.
    • (2008) J. Med. Chem , vol.51 , pp. 6495-6502
    • Brandt, G.E.L.1    Schmidt, M.D.2    Prisinzano, T.E.3    Blagg, B.S.J.4
  • 141
    • 0035153897 scopus 로고    scopus 로고
    • Digging in the herb garden: Responding to a patient's query about thunder of god vine
    • Balick, M. J.; Lee, R. Digging in the herb garden: responding to a patient's query about thunder of god vine. Altern. Ther. Health Med. 2001, 7, 100-103.
    • (2001) Altern. Ther. Health Med , vol.7 , pp. 100-103
    • Balick, M.J.1    Lee, R.2
  • 142
    • 27644525018 scopus 로고    scopus 로고
    • Ultrastructural changes in leydig cells and cauda epididymal spematozoa induced by azadirachta indica leaves in albino rats
    • Aladakatti, R. H.; Ahamed, R. N. Ultrastructural changes in leydig cells and cauda epididymal spematozoa induced by azadirachta indica leaves in albino rats. Phytother. Res. 2005, 19, 756-766.
    • (2005) Phytother. Res , vol.19 , pp. 756-766
    • Aladakatti, R.H.1    Ahamed, R.N.2
  • 143
    • 21144437911 scopus 로고    scopus 로고
    • Plescla, J.; Salz, W.; Xia, F.; Pennati, m.; Zaffaroni, N.; Daidone, M. G.; Meli, M.; Dohi, T.; Fortugno, P.; Nefedova, Y.; Gabrilovich, D. I.; Colombo, G.; Altieri, D. C. Rational design of Shepheridin, a novel anticancer agent. Cancer Cell 2005, 7, 457-468.
    • Plescla, J.; Salz, W.; Xia, F.; Pennati, m.; Zaffaroni, N.; Daidone, M. G.; Meli, M.; Dohi, T.; Fortugno, P.; Nefedova, Y.; Gabrilovich, D. I.; Colombo, G.; Altieri, D. C. Rational design of Shepheridin, a novel anticancer agent. Cancer Cell 2005, 7, 457-468.
  • 145
    • 67349237892 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor induced modulation of anti-estrogen therapy
    • Thomas, S.; Munster, P. N. Histone deacetylase inhibitor induced modulation of anti-estrogen therapy. Cancer Lett. 2009, 280, 184-191.
    • (2009) Cancer Lett , vol.280 , pp. 184-191
    • Thomas, S.1    Munster, P.N.2
  • 147
    • 52649133274 scopus 로고    scopus 로고
    • HDAC6 inhibition enhances 17-AAG - mediated abrogation of hsp90 chaperone function in human leukemia cells
    • Rao, R.; Fiskus, W.; Yang, Y.; Lee, P.; Joshi, R.; Fernandez, P.; Mandawat, A.; Atadja, P.; Bradner, J. E.; Bhalla, K. HDAC6 inhibition enhances 17-AAG - mediated abrogation of hsp90 chaperone function in human leukemia cells. Blood 2008, 112, 1886-1893.
    • (2008) Blood , vol.112 , pp. 1886-1893
    • Rao, R.1    Fiskus, W.2    Yang, Y.3    Lee, P.4    Joshi, R.5    Fernandez, P.6    Mandawat, A.7    Atadja, P.8    Bradner, J.E.9    Bhalla, K.10
  • 148
    • 65549166880 scopus 로고    scopus 로고
    • HDAC6 modulates Hsp90 chaperone activity and regulates activation of aryl hydrocarbon receptor signaling
    • Kekatpure, V. D.; Dannenberg, A. J.; Subbaramaiah, K. HDAC6 modulates Hsp90 chaperone activity and regulates activation of aryl hydrocarbon receptor signaling. J. Biol. Chem. 2009, 284, 7436-7445.
    • (2009) J. Biol. Chem , vol.284 , pp. 7436-7445
    • Kekatpure, V.D.1    Dannenberg, A.J.2    Subbaramaiah, K.3
  • 149
    • 34548075217 scopus 로고    scopus 로고
    • Hydroxamic acid analogue histone deacetylase inhibitors attenuate estrogen receptor-a levels and transcriptional activity: A result of hyperacetylation and inhibition of chaperone function of heat shock protein 90
    • Fiskus, W.; Ren, Y.; Mohapatra, A.; Bali, P.; Mandawat, A.; Rao, R.; Herger, B.; Yang, Y.; Atadja, P.; Wu, J.; Bhalla, K. Hydroxamic acid analogue histone deacetylase inhibitors attenuate estrogen receptor-a levels and transcriptional activity: a result of hyperacetylation and inhibition of chaperone function of heat shock protein 90. Clin. Cancer Res. 2007, 13, 4882-4890.
    • (2007) Clin. Cancer Res , vol.13 , pp. 4882-4890
    • Fiskus, W.1    Ren, Y.2    Mohapatra, A.3    Bali, P.4    Mandawat, A.5    Rao, R.6    Herger, B.7    Yang, Y.8    Atadja, P.9    Wu, J.10    Bhalla, K.11
  • 151
    • 65749094681 scopus 로고    scopus 로고
    • Synergism of heat shock protein 90 and histone deacetylase inhibitors in synovial sarcoma
    • in press
    • Nguyen, A.; Su, L.; Campbell, B.; Poulin, N. M.; Nielsen, T. O. Synergism of heat shock protein 90 and histone deacetylase inhibitors in synovial sarcoma. Sarcoma 2009, 2009, in press.
    • (2009) Sarcoma , pp. 2009
    • Nguyen, A.1    Su, L.2    Campbell, B.3    Poulin, N.M.4    Nielsen, T.O.5
  • 152
    • 57149123666 scopus 로고    scopus 로고
    • Molecular chaperones in pathogen virulence: Emergin new targets for therapy
    • Neckers, L.; Tatu, U. Molecular chaperones in pathogen virulence: emergin new targets for therapy. Cell Host Microbe 2008, 4, 519-527.
    • (2008) Cell Host Microbe , vol.4 , pp. 519-527
    • Neckers, L.1    Tatu, U.2
  • 153
    • 47049090269 scopus 로고    scopus 로고
    • Stress, drugs, and evolution: The role of cellular signaling in fungal drug resistance
    • Cowen, L. E.; Steinback, W. J. Stress, drugs, and evolution: the role of cellular signaling in fungal drug resistance. Eukaryot. Cell 2008, 7, 747-764.
    • (2008) Eukaryot. Cell , vol.7 , pp. 747-764
    • Cowen, L.E.1    Steinback, W.J.2
  • 156
    • 0842281502 scopus 로고    scopus 로고
    • Recombinant antibodies: A natural partner in combinatorial antifungal therapy
    • Matthews, R. C.; Burnie, J. P. Recombinant antibodies: a natural partner in combinatorial antifungal therapy. Vaccine 2004, 22, 865-871.
    • (2004) Vaccine , vol.22 , pp. 865-871
    • Matthews, R.C.1    Burnie, J.P.2
  • 157
    • 0034117339 scopus 로고    scopus 로고
    • Characterization of heat-inducible expression and cloning of HtpG (Hsp90 homologue) of Porphyromonas gingivalis
    • Lopatin, D. E.; Combs, A.; Sweier, D. G.; Fenno, J. C.; Dhamija, S. Characterization of heat-inducible expression and cloning of HtpG (Hsp90 homologue) of Porphyromonas gingivalis. Infect. Immun. 2000, 68, 1980-1987.
    • (2000) Infect. Immun , vol.68 , pp. 1980-1987
    • Lopatin, D.E.1    Combs, A.2    Sweier, D.G.3    Fenno, J.C.4    Dhamija, S.5
  • 158
    • 34247513586 scopus 로고    scopus 로고
    • Chaperoning a cellular upheaval in malaria: Heat shock proteins in Plasmodium falciparum
    • Acharya, P.; Kumar, R.; Tatu, U. Chaperoning a cellular upheaval in malaria: heat shock proteins in Plasmodium falciparum. Mol. Biochem. Parasitol. 2007, 153, 85-94.
    • (2007) Mol. Biochem. Parasitol , vol.153 , pp. 85-94
    • Acharya, P.1    Kumar, R.2    Tatu, U.3
  • 159
    • 34848844683 scopus 로고    scopus 로고
    • Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum
    • Pavithra, S. R.; Kumar, R.; Tatu, U. Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum. PLoS Comput. Biol. 2007, 3, 1701-1715.
    • (2007) PLoS Comput. Biol , vol.3 , pp. 1701-1715
    • Pavithra, S.R.1    Kumar, R.2    Tatu, U.3
  • 160
    • 0034982311 scopus 로고    scopus 로고
    • Microbial molecular chaperones
    • Lund, P. A. Microbial molecular chaperones. Adv. Microb. Physiol. 2001, 44, 93-140.
    • (2001) Adv. Microb. Physiol , vol.44 , pp. 93-140
    • Lund, P.A.1
  • 161
    • 0037890192 scopus 로고    scopus 로고
    • The heat shock response of Escherichia coli
    • Arsene, F. The heat shock response of Escherichia coli. Int. J. Food Microbiol. 2000, 55, 3-9.
    • (2000) Int. J. Food Microbiol , vol.55 , pp. 3-9
    • Arsene, F.1
  • 162
    • 16244364801 scopus 로고    scopus 로고
    • Valle, J. R.-d.; Chavez-Salinas, S.; Medina, F.; Angel, R. M. d. Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells. J. Virol. 2005, 79, 4557-4567.
    • Valle, J. R.-d.; Chavez-Salinas, S.; Medina, F.; Angel, R. M. d. Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells. J. Virol. 2005, 79, 4557-4567.
  • 163
    • 65449118855 scopus 로고    scopus 로고
    • Heat-shock protein 90 is essential for stabilization of the hepatitis C virus nonstructural protein NS3
    • Ujino, S.; Yamaguchi, S.; Shimotohno, K.; Takaku, H. Heat-shock protein 90 is essential for stabilization of the hepatitis C virus nonstructural protein NS3. J. Biol. Chem. 2009, 284, 6841-6846.
    • (2009) J. Biol. Chem , vol.284 , pp. 6841-6846
    • Ujino, S.1    Yamaguchi, S.2    Shimotohno, K.3    Takaku, H.4
  • 166
    • 33745091537 scopus 로고    scopus 로고
    • Therapy through chaperones: Sense or antisense? Cystic fibrosis as a model disease
    • Amaral, M. D. Therapy through chaperones: Sense or antisense? Cystic fibrosis as a model disease. J. Inherit. Metab. Dis. 2006, 29, 477-487.
    • (2006) J. Inherit. Metab. Dis , vol.29 , pp. 477-487
    • Amaral, M.D.1
  • 167
    • 0034532302 scopus 로고    scopus 로고
    • Post-translational disruption of the DF508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes DF508 CFTR in the rabbit reticulocyte lysate
    • Fuller, W.; Cuthbert, A. W. Post-translational disruption of the DF508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes DF508 CFTR in the rabbit reticulocyte lysate. J. Biol. Chem. 2000, 275, 37462-37468.
    • (2000) J. Biol. Chem , vol.275 , pp. 37462-37468
    • Fuller, W.1    Cuthbert, A.W.2
  • 168


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