1. Hartl FU, Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 2009; 16(6): 574–581.
2. Taipale M, Jarosz DF, Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol 2010; 11(7): 515–528.
3. Horwich AL, Apetri AC, Fenton WA. The GroEL/GroES cis cavity as a passive anti-aggregation device. FEBS Lett 2009; 583(16): 2654–2662.
4. Wegele H, Müller L, Buchner J. Hsp70 and Hsp90 – a relay team for protein folding. Rev Physiol Biochem Pharmacol 2004; 151: 1–44.
5. Nakamoto H, Vigh L. The small heat shock proteins and their clients. Cell Mol Life Sci 2007; 64(3): 294–306.
6. Laskey RA, Honda BM, Mills AD et al. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature 1978; 275(5679): 416–420.
7. Besche HC, Haas W, Gygi SP et al. Isolation of mammalian 26S proteasomes and p97/VCP complexes using the ubiquitin-like domain from HHR23B reveals novel proteasome-associated proteins. Biochemistry 2009; 48(11): 2538–2549.
8. Brugge JS, Erikson E, Erikson RL. The specific interaction of the Rous sarcoma virus transforming protein, pp60src, with two cellular proteins. Cell 1981; 25(2): 363–372.
9. Sreedhar AS, Kalmár E, Csermely P et al. Hsp90 isoforms: functions, expression and clinical importance. FEBS Lett 2004; 562(1–3): 11–15.
10. Tsutsumi S, Neckers L. Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis. Cancer Sci 2007; 98(10): 1536–1539.
11. Eustace BK, Sakurai T, Stewart JK et al. Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness. Nat Cell Biol 2004; 6(6): 507–514.
12. Dutta R, Inouye M. GHKL, an emergent ATPase/kinase superfamily. Trends Biochem Sci 2000; 25(1): 24–28.
13. Hainzl O, Lapina MC, Buchner J et al. The charged linker region is an important regulator of Hsp90 function. J Biol Chem 2009; 284(34): 22559–22567.
14. Hawle P, Siepmann M, Harst A et al. The middle domain of Hsp90 acts as a discriminator between different types of client proteins. Mol Cell Biol 2006; 26(22): 8385–5395.
15. Minami Y, Kimura Y, Kawasaki H et al. The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. Mol Cell Biol 1994; 14(2): 1459–1464.
16. Young JC, Obermann WM, Hartl FU. Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90. J Biol Chem 1998; 273(29): 18007–18010.
17. Prodromou C, Panaretou B, Chohan S et al. The ATPase cycle of Hsp90 drives a molecular ‚clamp‘ via transient dimerization of the N-terminal domains. EMBO J 2000; 19(16): 4383–4392.
18. Panaretou B, Siligardi G, Meyer P et al. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell 2002; 10(6): 1307–1318.
19. Richter K, Walter S, Buchner J. The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J Mol Biol 2004; 342(5): 1403–1413.
20. Lee P, Shabbir A, Cardozo C et al. Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase. Mol Biol Cell 2004; 15(4): 1785–1792.
21. Roe SM, Ali MM, Meyer P et al. The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell 2004; 116(1): 87–98.
22. Wandinger SK, Richter K, Buchner J. The Hsp90 chaperone machinery. J Biol Chem 2008; 283(27): 18473–18477.
23. Workman P. Altered states: selectively drugging the Hsp90 cancer chaperone. Trends Mol Med 2004; 10(2): 47–51.
24. Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000; 100(1): 57–70.
25. Kitano H. Cancer robustness: tumour tactics. Nature 2003; 426(6963): 125.
26. Kobayashi S, Boggon TJ, Dayaram T et al. EGFR mutation and resistance of non-small-cell lung cancer to gefitinib. N Engl J Med 2005; 352(8): 786–792.
27. Pashtan I, Tsutsumi S, Wang S et al. Targeting Hsp90 prevents escape of breast cancer cells from tyrosine kinase inhibition. Cell Cycle 2008; 7(18): 2936–2941.
28. Sangster TA, Lindquist S, Queitsch C. Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance. Bioessays 2004; 26(4): 348–362.
29. Gatenby RA, Maini PK. Mathematical oncology: cancer summed up. Nature 2003; 421(6921): 321.
30. Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005; 5(10): 761–772.
31. Whitesell L, Mimnaugh EG, De Costa B et al. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci U S A 1994; 91(18): 8324–8328.
32. Kamal A, Thao L, Sensintaffar J et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003; 425(6956): 407–410.
33. Whitesell L, Bagatell R, Falsey R. The stress response: implications for the clinical development of hsp90 inhibitors. Curr Cancer Drug Targets 2003; 3(5): 349–358.
34. Blagg BS, Kerr TD. Hsp90 inhibitors: small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation. Med Res Rev 2006; 26(3): 310–338.
35. DeBoer C, Meulman PA, Wnuk RJ et al. Geldanamycin, a new antibiotic. J Antibiot (Tokyo) 1970; 23(9): 442–447.
36. Supko JG, Hickman RL, Grever MR et al. Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent. Cancer Chemother Pharmacol 1995; 36(4): 305–315.
37. Porter JR, Ge J, Lee J et al. Ansamycin inhibitors of Hsp90: nature’s prototype for anti-chaperone therapy. Curr Top Med Chem 2009; 9(15): 1386–1418.
38. Roe SM, Prodromou C, O’Brien R et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 1999; 42(2): 260–266.
39. Soga S, Shiotsu Y, Akinaga S et al. Development of radicicol analogues. Curr Cancer Drug Targets 2003; 3(5): 359–369.
40. Chiosis G, Timaul MN, Lucas B et al. A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells. Chem Biol 2001; 8(3): 289–299.
41. Taldone T, Chiosis G. Purine-scaffold Hsp90 inhibitors. Curr Top Med Chem 2009; 9(15): 1436–1446.
42. Cheung KM, Matthews TP, James K et al. The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors. Bioorg Med Chem Lett 2005; 15(14): 3338–3343.
43. Marcu MG, Chadli A, Bouhouche I et al. 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(47): 37181–37186.
44. Holzbeierlein JM, Windsperger A, Vielhauer G. Hsp90: a drug target? Curr Oncol Rep 2010; 12(2): 95–101.
45. Smith JR, Clarke PA, de Billy E et al. Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors. Oncogene 2009; 28(2): 157–169.
46. Westerheide SD, Bosman JD, Mbadugha BN et al. Celastrols as inducers of the heat shock response and cytoprotection. J Biol Chem 2004; 279(53): 56053–56060.
47. Zhang T, Li Y, Yu Y et al. Characterization of celastrol to inhibit hsp90 and cdc37 interaction. J Biol Chem 2009; 284(51): 35381–35389.
48. Kim YS, Alarcon SV, Lee S et al. Update on Hsp90 inhibitors in clinical trial. Curr Top Med Chem 2009; 9(15): 1479–1492.
49. Burris HA 3rd, Berman D, Murthy B et al. Tanespimycin pharmacokinetics: a randomized dose-escalation crossover phase 1 study of two formulations. Cancer Chemother Pharmacol 2011; 67(5): 1045–1054.
50. Chandran T, Katragadda U, Teng Q et al. Design and evaluation of micellar nanocarriers for 17-allyamino-17-demethoxygeldanamycin (17-AAG). Int J Pharm 2010; 392(1–2): 170–177.
51. Xiong MP, Yáñez JA, Kwon GS et al. A cremophor-free formulation for tanespimycin (17-AAG) using PEO-b-PDLLA micelles: characterization and pharmacokinetics in rats. J Pharm Sci 2009; 98(4): 1577–1586.
52. Grem JL, Morrison G, Guo XD et al. Phase I and pharmacologic study of 17-(allylamino)-17-demethoxygeldanamycin in adult patients with solid tumors. J Clin Oncol 2005; 23(9): 1885–1893.
53. Banerji U, O’Donnell A, Scurr M et al. Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. J Clin Oncol 2005; 23(18): 4152–4161.
54. Solit DB, Osman I, Polsky D et al. Phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with metastatic melanoma. Clin Cancer Res 2008; 14(24): 8302–8307.
55. Ramalingam SS, Egorin MJ, Ramanathan RK et al. A phase I study of 17-allylamino-17-demethoxygeldanamycin combined with paclitaxel in patients with advanced solid malignancies. Clin Cancer Res 2008; 14(11): 3456–3461.
56. Tse AN, Klimstra DS, Gonen M et al. A phase 1 dose-escalation study of irinotecan in combination with 17-allylamino-17-demethoxygeldanamycin in patients with solid tumors. Clin Cancer Res 2008; 14(20): 6704–6711.
57. Hubbard J, Erlichman C, Toft DO et al. Phase I study of 17-allylamino-17 demethoxygeldanamycin, gemcitabine and/or cisplatin in patients with refractory solid tumors. Invest New Drugs 2011; 29(3): 473–480.
58. Richardson PG, Badros AZ, Jagannath S et al. Tanespimycin with bortezomib: activity in relapsed/refractory patients with multiple myeloma. Br J Haematol 2010; 150(4): 428–437.
59. Modi S, Stopeck AT, Gordon MS et al. Combination of trastuzumab and tanespimycin (17-AAG, KOS-953) is safe and active in trastuzumab-refractory HER-2 overexpressing breast cancer: a phase I dose-escalation study. J Clin Oncol 2007; 25(34): 5410–5417.
60. Tsuruo T, Naito M, Tomida A et al. Molecular targeting therapy of cancer: drug resistance, apoptosis and survival signal. Cancer Sci 2003; 94(1): 15–21.
61. Kelland LR, Sharp SY, Rogers PM et al. DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J Natl Cancer Inst 1999; 91(22): 1940–1949.
62. Gaspar N, Sharp SY, Pacey S et al. Acquired resistance to 17-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin) in glioblastoma cells. Cancer Res 2009; 69(5): 1966–1975.
63. Kim HR, Kang HS, Kim HD. Geldanamycin induces heat shock protein expression through activation of HSF1 in K562 erythroleukemic cells. IUBMB Life 1999; 48(4): 429–433.
64. McCollum AK, TenEyck CJ, Stensgard B et al. P-Glycoprotein-mediated resistance to Hsp90-directed therapy is eclipsed by the heat shock response. Cancer Res 2008; 68(18): 7419–7427.
65. Ramanathan RK, Egorin MJ, Erlichman C et al. Phase I pharmacokinetic and pharmacodynamic study of 17-dimethylaminoethylamino-17-demethoxygeldanamycin, an inhibitor of heat-shock protein 90, in patients with advanced solid tumors. J Clin Oncol 2010; 28(9): 1520–1526.
66. Kummar S, Gutierrez ME, Gardner ER et al. Phase I trial of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat shock protein inhibitor, administered twice weekly in patients with advanced malignancies. Eur J Cancer 2010; 46(2): 340–347.
67. Lancet JE, Gojo I, Burton M et al. Phase I study of the heat shock protein 90 inhibitor alvespimycin (KOS-1022, 17-DMAG) administered intravenously twice weekly to patients with acute myeloid leukemia. Leukemia 2010; 24(4): 699–705.
68. Sequist LV, Gettinger S, Senzer NN et al. Activity of IPI-504, a novel heat-shock protein 90 inhibitor, in patients with molecularly defined non-small-cell lung cancer. J Clin Oncol 2010; 28(33): 4953–4960.