참고문헌
- Pearl, L. H. and Prodromou, C. (2006) Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75: 271-294. https://doi.org/10.1146/annurev.biochem.75.103004.142738
- Gimnez Ortiz, A. and Montalar Salcedo, J. (2010) Heat shock proteins as targets in oncology. Clin. Transl. Oncol. 12: 166-173. https://doi.org/10.1007/s12094-010-0486-8
- Pearl, L. H., Prodromou, C. and Workman, P. (2008) The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem. J. 410: 439-453. https://doi.org/10.1042/BJ20071640
- Fukuyo, Y., Hunt, C. R. and Horikoshi, N. (2010) Geldanamycin and its anti-cancer activities. Cancer Lett. 290: 24-35. https://doi.org/10.1016/j.canlet.2009.07.010
- Uehara, Y., Hori, M., Takeuchi, T. and Umezawa, H. (1986) Phenotypic change from transformed to normal induced by benzoquinonoid ansamycins accompanies inactivation of p60src in rat kidney cells infected with rous sarcoma virus. Mol. Cell. Biol. 6: 2198-2206.
- Jez, J. M., Chen, C., Rastelli, G., Stroud, R. M. and Santi, D. V. (2003) Crystal structure and molecular modeling of 17- DMAG in complex with human Hsp90. Chem. Biol. 10: 361-368. https://doi.org/10.1016/S1074-5521(03)00075-9
- Solit, D. B. (2008) Phase II trial of 17-allylamino-17- demethoxygeldanamycin in patients with metastatic melanoma. Clin. Cancer Res. 40: 8302-8307.
- Amolins, M. W. and Blagg, B. S. J. (2009) Natural product inhibitors of Hsp90: Potential leads for drug discovery. Mini- Rev. Medi. Chem. 9: 140-152 https://doi.org/10.2174/138955709787316056
- Hartl, F. U. and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: From nascent chain to folded protein. Science 295: 1852-1858. https://doi.org/10.1126/science.1068408
- Buchner, J. (1999) Hsp90 & Co. a holding for folding. Trends Biochem. Sci. 24: 136-142. https://doi.org/10.1016/S0968-0004(99)01373-0
- Mayer, M. P. and Bukau, B. (2005) Hsp70 chaperones: Cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62: 670-684. https://doi.org/10.1007/s00018-004-4464-6
- Blagg, B. S. J. and Kerr, T. D. (2006) Hsp90 inhibitors: Small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation Med. Res. Rev. 26: 310-338. https://doi.org/10.1002/med.20052
- Schlesinger, M. J. (1994) How the cell copes with stress and the function of heat shock proteins. Pediatr. Res. 36: 1-6. https://doi.org/10.1203/00006450-199407001-00001
- 한지숙 (2007) 항암제 및 퇴행성 신경질환 치료제로써의 Hsp90 억제제 개발 동향, Biochemistry and Molecular Biology News 12월호. 1-6.
- Donnelly, A. and Blagg, B. S. (2008) Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket. Curr. Med. Chem. 15: 2702-2717. https://doi.org/10.2174/092986708786242895
- Karapanagiotou, E. M., Syrigos, K. and Saif, M. W. (2009) Heat shock protein inhibitors and vaccines as new agents in cancer treatment. Expert Opin. Investig. Drugs. 18: 161-174. https://doi.org/10.1517/13543780802715792
- Pratt, W. B., Galigniana, M. D., Harrell, J. M. and DeFranco, D. B. (2004) Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement. Cell Signal 16: 857-872. https://doi.org/10.1016/j.cellsig.2004.02.004
- Zhang, H. and Burrows, F. (2004) Targeting multiple signal transduction pathways through inhibition of Hsp90. J. Mol. Med. 82: 488-499.
- Adams, J. and Elliot, P. J. (2000) New agents in cancer clinical trials. Oncogene 19: 6687-6892. https://doi.org/10.1038/sj.onc.1204088
- Neckers, L. and Ivy, S. P. (2003) Heat shock protein 90. Curr. Opin. Oncol. 15: 419-424. https://doi.org/10.1097/00001622-200311000-00003
- Neckers, L. and Neckers, K. (2002) Heat-shock protein 90 inhibitors as novel cancer chemotherapeutic agents. Expert Opin. Emerg. Drugs. 7: 277-288. https://doi.org/10.1517/14728214.7.2.277
- Nimmanapalli, R., O'Bryan, E. and Bhalla, K. (2001) Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lowers Bcr-Abl levels and induces apoptosis and differentiation of Bcr-Abl-positive human leukemic blasts. Cancer Res. 61: 1799-1804.
- Xu, W. and Neckers, L. (2007) Targeting the molecular chaperone heat shock protein 90 provides a multifaceted effect on diverse cell signaling pathways of cancer cells. Clin. Cancer Res. 13: 1625-1629. https://doi.org/10.1158/1078-0432.CCR-06-2966
- Hanahan, D. and Weinberg, R. A. (2000) The hallmarks of cancer review. Cell 100: 57-70. https://doi.org/10.1016/S0092-8674(00)81683-9
- Workman, P., Burrows, F., Neckers, L. and Rosen, N. (2007) Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress. Ann. N. Y. Acad. Sci. 1113: 202-216. https://doi.org/10.1196/annals.1391.012
- Sreedhar, A. S., Kalmar, E., and Csermely, P. (2004) Hsp90 isoforms: functions, expression and clinical importance. FEBS Lett. 562: 11-15. https://doi.org/10.1016/S0014-5793(04)00229-7
- Becker, B. (2004) Induction of Hsp90 protein expression in malignant melanomas and melanoma metastases. Exp. Dermatol. 13: 27-32.
- Chiosis, G., Huezo, H., Rosen, N., Mimnaugh, E., Whitesell, L. and Neckers, L. (2003) 17AAG: Low target binding affinity and potent cell activity finding an explanation. Mol. Cancer Ther. 2: 123-129. https://doi.org/10.4161/cbt.2.2.235
- Schnur, R. C., Corman, M. L., Gallaschun, R. J., Cooper, B. A., Dee, M. F., Doty, J. L., Muzzi, M. L., DiOrio, C. I., Barbacci, E. G., Miller, P. E., Pollack, V. A., Savage, D. M., Sloan, D. E., Pustilnik, L. R., Moyer, J. D. and Moyer, M. P. (1995) erbB-2 oncogene inhibition by geldanamycin derivatives: Synthesis, mechanism of action, and structure-activity relationships. J. Med. Chem. 38: 3813-3820. https://doi.org/10.1021/jm00019a011
- Hossain, C. F., Okuyama, E. and Yamazaki, M. (1996) A new series of coumarin derivatives having monoamine oxidase inhibitory activity from Monascus anka. Chem. Pharm. Bull. 44: 1535-1539. https://doi.org/10.1248/cpb.44.1535
- Yasukawa, K., Takahashi, M., Natori, S., Kawai, K., Yamazaki, M., Takeuchi, M. and Takido, M. (1994) Azaphilones inhibit tumor promotion by 12-O-tetradecanoylphorbol-13-acetate in two-stage carcinogenesis in mice. Oncology 51: 108-112. https://doi.org/10.1159/000227320
- Akihisa, T., Tokuda, H., Ukiwa, M., Kivota, A., Yasukawa, K., Sakamoto, N., Kimura, Y., Suzuki, T., Takayasu, J. and Nishino, H. (2005) Anti-tumor-initiating effects of monascin, an azaphilonoid pigment from the extract of Monascus pilosus fermented rice (red-mold rice). J. Chem. Biodivers. 2: 1305-1309. https://doi.org/10.1002/cbdv.200590101
- Akihisa, T., Tokuda, H., Yasukawa, K., Ukiwa, M., Kivota, A., Sakamoto, N., Suzuki, T., Tanabe, N., Nishino, H. and Kavasu, J. (2005) Azaphilones, furanoisophthalides, and amino acids from the extracts of Monascus pilosus-fermented rice (red-mold rice) and their chemopreventive effects. J. Agric. Food Chem. 53: 562-565. https://doi.org/10.1021/jf040199p
- Su, N. W., Lin, Y. L., Lee, M. H. and Ho, C. H. (2005) Ankaflavin from Monascus-fermented red rice exhibits selective cytotoxic effect and induces cell death on Hep G2 cells. J. Agric. Food Chem. 53: 1949-1954. https://doi.org/10.1021/jf048310e
- Knecht, A. and Humpf, H. U. (2006) Cytotoxic and antimitotic effects of N-containing Monascus metabolites studied using immortalized human kidney epithelial cells. Mol. Nutr. Food Res. 50: 406-412. https://doi.org/10.1002/mnfr.200500238
- Omura, S., Tanaka, H., Ikead, H. and Masuma, R. (1993) Isochromophilones I and II, novel inhibitors against gp120-CD4 binding from Penicillium sp. J. Antibiot. 46: 1908-1911. https://doi.org/10.7164/antibiotics.46.1908
- Kono, K., Tanaka, M., Ono, Y., Hosoya, T., Ogita, T. and Kohama, T. (2001) S-15183a and b, new sphingosine kinase inhibitors, produced by a fungus. J. Antibiot. 54: 415-420. https://doi.org/10.7164/antibiotics.54.415
- Musso, L., Dallavalle, S. and Merlini, L. (2010) Natural and semisynthetic azaphilones as a new scaffold for Hsp90 inhibitors. Bioorg. Med. Chem. 18: 6031-6043. https://doi.org/10.1016/j.bmc.2010.06.068
- Patel, H. J., Modi, S., Chiosis, G. and Taldone, T. (2011) Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment. Expert Opin. Drug Discov. 6: 559-587. https://doi.org/10.1517/17460441.2011.563296
- Ammon, H. P. and Wahl, M. A. (1991) Pharmacology of Curcuma longa. Planta Med. 57: 1-7. https://doi.org/10.1055/s-2006-960004
- Kim, N. W., Piatyszek, M. A., Prowse, K. R., Harley, C. B., West, M. D., Ho, P. L. C., Coviello, G. M., Wright, W. E., Weinrich, S. L. and Shay, J. W. (1994) Specific association of human telomerase activity with immortal cells and cancer. Science 266: 2011-2015. https://doi.org/10.1126/science.7605428
- Bodnar, A. G., Ouellette, M., Frolkis, M., Holt, S. E., Chiu, C. P., Morin, G. B., Harley, C. B., Shay, J. W., Lichtsteiner S. and Wright, W. E. (1998) Extension of lifespan by introduction of telomerase into normal human cells. Science 279: 349-352. https://doi.org/10.1126/science.279.5349.349
- Hahn, W. C., Counter, C. M., Lundberg, A. S., Beijersbergen, R. L., Brooks, M. W. and Weinberg, R. A. (1999) Creation of human tumour cells with defined genetic elements. Nature 400: 464-468. https://doi.org/10.1038/22780
- Seimiya, H., Sawada, H., Muramatsu, Y., Shimizu, M., Ohko, K., Yamane, K. and Tsuruo, T. (2000) Involvement of 14-3- 3 proteins in nuclear localization of telomerase. EMBO J. 19: 2652-2661. https://doi.org/10.1093/emboj/19.11.2652
- Keppler, B. R., Grady, A. T. and Jarstfer. M. B. (2006) The biochemical role of the heat shock protein 90 chaperone complex in establishing human telomerase activity. J. Biol. Chem. 281: 19840-19848. https://doi.org/10.1074/jbc.M511067200
- Holt, S. E., Aisner, D. L., Baur, J., Tesmer, V. M., Dy, M., Ouellette, M., Trager, J. B., Morin, G. B. Toft, D. O., Shay, J. W., Wright, W. E. and White, M. A. (1999) Functional requirement of p23 and Hsp90 in telomerase complexes. Genes Dev. 13: 817-826. https://doi.org/10.1101/gad.13.7.817
- Forsythe, H. L., Jarvis, J. L., Turner, J. W., Elmore, L. W. and Holt, S. E. (2001) Stable association of hsp90 and p23, but not hsp70, with active human telomerase. J. Biol. Chem. 276: 15571-15574. https://doi.org/10.1074/jbc.C100055200
- Lee, J. H. and Chung, I. K. (2010) Curcumin inhibits nuclear localization of telomerase by dissociating the Hsp90 co-chaperone p23 from hTERT. Cancer Lett. 290: 76-86. https://doi.org/10.1016/j.canlet.2009.08.026
- Teiten, M. H., Reuter, S., Schmucker, S., Dicato, M. and Diederich, M. (2009) Induction of heat shock response by curcumin in human leukemia cells. Cancer Lett. 279: 145-154. https://doi.org/10.1016/j.canlet.2009.01.031
- Davenport, J., Manjarrez, J. R., Peterson, L., Krumm, B., Blagg, B. S. and Matts, R. L. (2011) Gambogic acid, a natural product inhibitor of Hsp90. J. Nat. Prod. 74: 1085-1092. https://doi.org/10.1021/np200029q
- Yang, Y., Yang, L., You, Q. D., Nie, F. F., Gu, H. Y., Zhao, L., Wang, X. T. and Guo, Q. L. (2007) Differential apoptotic induction of gambogic acid, a novel anticancer natural product, on hepatoma cells and normal hepatocytes. Cancer Lett. 256: 259-266. https://doi.org/10.1016/j.canlet.2007.06.014
- Zhao, L., Guo, Q. L., You, Q. D., Wu, Z. Q. and Gu, H. Y. (2004) Gambogic acid induces apoptosis and regulates expressions of Bax and Bcl-2 protein in human gastric carcinoma MGC-803 cells. Biol. Pharm. Bull. 27: 998-1003. https://doi.org/10.1248/bpb.27.998
- Pandey, M. K., Sung, B., Ahn, K. S., Kunnumakkara, A. B., Chaturvedi, M. M. and Aggarwal, B. B. (2007) Gambogic acid, a novel ligand for transferrin receptor, potentiates TNFinduced apoptosis through modulation of the nuclear factorkappaB signaling pathway. Blood 110: 3517-3525. https://doi.org/10.1182/blood-2007-03-079616
- Ortiz-Sanchez, E., Daniels, T. R., Helguera, G., Martinez- Maza, O., Bonavida, B. and Penichet, M. L. (2009) Enhanced cytotoxicity of an anti-transferrin receptor IgG3-avidin fusion protein in combination with gambogic acid against human malignant hematopoietic cells: Functional relevance of iron, the receptor, and reactive oxygen species. Leukemia 23: 59-70. https://doi.org/10.1038/leu.2008.270
- Galam, L., Hadden, M. K., Ma, Z., Ye, Q. Z., Yun, B. G., Blagg, B. S. and Matts, R. L. (2007) High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90- dependent refolding of firefly luciferase. Bioorg. Med. Chem. 15: 1939-1946. https://doi.org/10.1016/j.bmc.2007.01.004
- Ren, Y., Yuan, C., Chai, H. B., Ding, Y., Li, X. C., Ferreira, D. and Kinghorn, A. D. (2011) Absolute configuration of (-)- gambogic acid, an antitumor agent. J. Nat. Prod. 74: 460-463. https://doi.org/10.1021/np100422z
- Kim, J. E., Kim, A. R., Kim, M. J. and Park, S. N. (2011) Antibacterial, antioxidative and antiaging effects of Allium cepa peel extracts. Appl. Chem. Eng. 22: 178-184.
- Powers, M. V. and Workman, P. (2007) Inhibitors of the heat shock response: Biology and pharmacology. FEBS Lett. 581: 3758-3769. https://doi.org/10.1016/j.febslet.2007.05.040
- Nagai, N., Nakai, A. and Nagata, K. (1995) Quercetin suppresses heat shock response by down regulation of HSF1. Biochem. Biophys. Res. Commun. 208: 1099-1105. https://doi.org/10.1006/bbrc.1995.1447
- Aalinkeel, R., Bindukumar, B., Reynolds, J. L., Sykes, D. E., Mahajan, S. D., Chadha, K. C. and Schwartz, S. A. (2008) The dietary bioflavonoid, quercetin, selectively induces apoptosis of prostate cancer cells by down-regulating the expression of heat shock protein 90. The Prostate 68: 1773-1789. https://doi.org/10.1002/pros.20845
- Matter, W. F., Brown, R. F. and Vlahos, C. J. (1992) The inhibition of phosphatidylinositol 3-kinase by quercetin and analogs. Biochem. Biophys. Res. Commun. 186: 624-631. https://doi.org/10.1016/0006-291X(92)90792-J
- Levy, J., Teuerstein, I., Marbach, M., Radian, S. and Sharoni, Y. (1984) Tyrosine protein kinase activity in the DMBAinduced rat mammary tumor: Inhibition by quercetin. Biochem. Biophys. Res. Chem. 123: 1227-1233. https://doi.org/10.1016/S0006-291X(84)80264-8
- Cueto, M., Jensen, P. R. and Fenical, W. (2000) N-Meth ylsansalvamide, a cytotoxic cyclic depsipeptide from a marine fungus of the genus fusarium. Phytochem. 55: 223-226. https://doi.org/10.1016/S0031-9422(00)00280-6
- Hwang, Y., Rowley, D., Rhodes, D., Gertsch, J., Fenical, W. and Bushman, F. (1999) Mechanism of inhibition of a poxvirus topoisomerase by the marine natural product sansalvamide A. Mol. Pharmacol. 55: 1049-1053.
- Belofsky, G. N., Jensen, P. R. and Fenical, W. (1999) Sansalvamide: A new cytotoxic cyclic depsipeptide produced by a marine fungus of the genus fusarium. Tetrahedron Lett. 40: 2913-2916. https://doi.org/10.1016/S0040-4039(99)00393-7
- Styers, T. J., Kekec, A., Rodriguez, R. A., Brown, J. D., Cajica, J., Pan, P. S., Parry, E., Carroll, C. L., Medina, I., Corral, R., Lapera, S., Otrubova, K., Pan, C. M., Mcguire, K. L. and Mcalpine, S. R. (2006) Synthesis of sansalvamide A derivatives and their cytotoxicity in the MSS colon cancer cell line HT-29. Bioorg. Med. Chem. 14: 5625-5631. https://doi.org/10.1016/j.bmc.2006.04.031
- Rodriguez, R. A., Pan, P. S., Pan, C. M., Ravula, S., Lapera, S. A., Singh, E. K., Styers, T. J., Brown, J. D., Cajica, J., Parry, E., Otrubova, K. and Mcalpine, S. R. (2007) Synthesis of second-generation sansalvamide A derivatives: Novel templates as potential antitumor agents. J. Org. Chem. 72: 1980- 2002. https://doi.org/10.1021/jo061830j
- Pan, P. S., Vasko, R. C., Lapera, S. A., Johnson, V. A., Sellers, R. P., Lin, C. C., Pan, C. M., Davis, M. R., Ardi, V. C. and Mcalpine, S. R. (2009) A comprehensive study of sansalvamide A derivatives: The structure-activity relationships of 78 derivatives in two pancreatic cancer cell lines. Bioorg. Med. Chem. 17: 5806-5825. https://doi.org/10.1016/j.bmc.2009.07.017
- Vasko, R. C., Rodriguez, R. A., Cunningham, C. N., Ardi, V. C., Agard, D. A. and Mcalpine, S. R. (2010) Mechanistic studies of sansalvamide A-amide: An allosteric modulator of Hsp90. ACS Med. Chem. Lett. 1: 4-8. https://doi.org/10.1021/ml900003t
- Sellers, R. P., Alexander, L. D. and Johnson, V. A. (2010) Design and synthesis of Hsp90 inhibitors: exploring the SAR of sansalvamide A derivatives. Bioorg. Med. Chem. 18: 6822-6856. https://doi.org/10.1016/j.bmc.2010.07.042
- Hannay, J. A. and Yu, D. (2003) Silibinin: a thorny therapeutic for EGF-R expressing tumors? Cancer. Biol. Ther. 2: 532-533.
- Gazak, R., Walterova, D. and Kren, V. (2007) Silybin and silymarin-new and emerging applications in medicine. Curr. Med. Chem. 14: 315-338. https://doi.org/10.2174/092986707779941159
- Lu, P., Mamiya, T., Lu, L. L., Mouri, A., Niwa, M., Hiramatsu, M., Zou, L. B., Nagai, T., Ikejima, T. and Nabeshima, T. (2009) Silibinin attenuates amyloid beta(25-35) peptideinduced memory impairments: implication of inducible nitric-oxide synthase and tumor necrosis factor-alpha in mice. J. Pharmacol. Exp. Ther. 331: 319-326. https://doi.org/10.1124/jpet.109.155069
- Zhao, H., Brandt, G. E., Galam, L., Matts, R. L. and Blagg, B. S. (2011) Identification and initial SAR of silybin: An Hsp90 inhibitor. Bioorg. Med. Chem. Lett. 21: 2659-2664. https://doi.org/10.1016/j.bmcl.2010.12.088
- Kastan, M. B. and Bartek, J. (2004) Cell-cycle checkpoints and cancer. Nature 432: 316-323. https://doi.org/10.1038/nature03097
- Winters, M. (2006) Ancient medicine, modern use: Withania somnifera and its potential role in integrative oncology. Altern. Med. Rev. 11: 269-277.
- Matsuda, H., Murakami, T., Kishi, A. and Yoshikawa, M. (2001) Structures of withanosides I, II, III, IV, V, VI, and VII, new withanolide glycosides, from the roots of Indian Withania somnifera Dunal. and inhibitory activity for tachyphylaxis to clonidine in isolated guinea-pig ileum. Bioorg. Med. Chem. 9: 1499-1507. https://doi.org/10.1016/S0968-0896(01)00024-4
- Ray, A. and Gupta, M. (1994) Withasteroids, a growing group of naturally occurring steroidal lactones. Fortschr. Chem. Org. Naturst. 63: 1-106.
- Alhindawi, M. K., Alkhafaji, S. H. and Abdulnabi, M. H. (1992) Anti-granuloma activity of Iraqi Withania-somnifera. J. Ethnopharmacol. 37: 113-116. https://doi.org/10.1016/0378-8741(92)90069-4
- Mishra, L., Singh, B. and Dagenias, S. (2000) Scientific basis for the therapeutic use of Withania somnifera (ashwagandha): a review. Altern. Med. Rev. 5: 334-336.
- Owais, M., Sharad, K. S., Shehbaz, A. and Saleemuddin, M. (2005) Antibacterial efficacy of Withania somnifera (ashwagandha) an indigenous medicinal plant against experimental murine salmonellosis. Phytomedicine 12: 229-235. https://doi.org/10.1016/j.phymed.2003.07.012
- Bhattacharya, A., Ghosal, S. and Bhattacharya, S. K. (2001) Anti-oxidant effect of Withania somnifera glycowithanolides in chronic footshock stress-induced perturbations of oxidative free radical scavenging enzymes and lipid peroxidation in rat frontal cortex and striatum. J. Ethnopharmacol. 74: 1-6. https://doi.org/10.1016/S0378-8741(00)00309-3
- Yu, Y. K., Hamza, A., Zhang, T., Gu, M. C., Zou, P., Newman, B., Li, Y. Y., Gunatilaka, A. A. L., Zhan, C. G. and Sun, D. X. (2010) Withaferin A targets heat shock protein 90 in pancreatic cancer cells. Biochem. Pharmacol. 79: 542-551. https://doi.org/10.1016/j.bcp.2009.09.017
- Chiosis, G. (2006) Targeting chaperones in transformed systems - a focus on Hsp90 and cancer. Expert Opin. Ther. Targets 10: 37-50. https://doi.org/10.1517/14728222.10.1.37
- Neckers, L. (2003) Development of small molecule Hsp90 inhibitors: utilizing both forward and reverse chemical genomics for drug identification. Curr. Med. Chem. 10: 733-739. https://doi.org/10.2174/0929867033457818
- Grover, A., Shandilya, A., Agrawal, V., Pratik, P., Bhasme, D., Bisaria, V. S. and Sundar, D. (2011) Hsp90/Cdc37 Chaperone/ co-chaperone complex, a novel junction anticancer target elucidated by the mode of action of herbal drug withaferin A. BMC Bioinformatics 12: Suppl 1:S30. https://doi.org/10.1186/1471-2105-12-S1-S30
- Yu, Y., Hamza, A., Zhang, T., Gu, M., Zou, P., Newman, B., Li, Y., Gunatilaka, A. A., Zhan, C. G. and Sun, D. (2010) Withaferin A targets heat shock protein 90 in pancreatic cancer cells. Biochem. Pharmacol. 79: 542-551. https://doi.org/10.1016/j.bcp.2009.09.017