Geldanamycin as a potential anti-cancer agent: Its molecular target and biochemical activity

Investigational New Drugs

Volumn 17, Issue 4, 1999, Pages 361-373

  Neckers, Len ^a,b   Schulte, Theodor W ^a   Mimnaugh, Edward ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b NONE   (United States)

Author keywords

Benzoquinone ansamycin; Chaperone; Geldanamycin; Hsp90

Indexed keywords

ANTINEOPLASTIC ANTIBIOTIC; CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE KINASE;

CELL PROLIFERATION; CELL SURVIVAL; DRUG PROTEIN BINDING; DRUG TARGETING; PRIORITY JOURNAL; REVIEW;

ANIMALS; ANTIBIOTICS, ANTINEOPLASTIC; BENZOQUINONES; HSP90 HEAT-SHOCK PROTEINS; HUMANS; LACTAMS, MACROCYCLIC; QUINONES;

EID: 0033502429     PISSN: 01676997     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006382320697     Document Type: Review

References (116)

1. Ferrarini M, Heltai S, Zocchi MR, Rugarli C: Unusual expression and localization of heat-shock proteins in human tumor cells. Int J Cancer 51: 613-619, 1992
2. Mickey E, Brandon SE, Smale G, Lloyd D, Weber LA: Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein. Mol Cell Biol 9: 2615-2626, 1989
3. Perdew GH, Hord N, Hollenback CE, Welsh MJ: Localization and characterization of the 86- and 84-kDa heat shock proteins in Hepa lclc7 cells. Exp Cell Res 209: 350-356, 1993
4. Little E, Ramakrishnan M, Roy B, Gazit G, Lee AS: The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications. Crit Rev Eukaryot Gene Expr 4: 1-18, 1994
5. Wearsch PA, Nicchitta CV: Purification and partial molecular characterization of GRP94, an ER resident chaperone. Protein Expr Purif 7: 1114-1121, 1996
6. Chen CF, Chen Y, Dai K, Chen PL, Riley DJ, Lee WH: A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock. Mol Cell Biol 16: 4691-4699, 1996
7. Song HY, Dunbar JD, Zhang YX, Guo D, Donner DB: Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J Biol Chem 270: 3574-3581, 1995
8. Minami Y, Kawasaki H, Miyata Y, Suzuki K, Yahara I: Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90. J Biol Chem 266: 10099-10103, 1991
9. Minami Y, Kimura Y, Kawasaki H, Suzuki K, Yahara I: The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. Mol Cell Biol 14: 1459-1464, 1994
10. Akner G, Mossberg K, Sundqvist KG, Gustafsson JA, Wikstrom AC: Evidence for reversible, non-microlubule and non-microfilament-dependent nuclear translocation of hsp90 after heat shock in human fibroblasts. Eur J Cell Biol 58: 356-364, 1992
11. Gasc JM, Renoir JM, Faber LE, Delahaye F, Baulieu EE: Nuclear localization of two steroid receptor-associated proteins, hsp90 and p59. Exp Cell Res 186: 362-367, 1990
12. Neckers L, Mimnaugh E, Schulte T: The Hsp90 chaperone family. In: Latchman D (ed) Stress Proteins. Springer-Verlag, Heidelberg, 1998, pp 9-2
13. Smith DF, Whitesell L, Katsanis E: Molecular chaperones: Biology and prospects for pharmacological intervention. Pharmacological Reviews 50: 493-513, 1998
14. 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 79: 129-168, 1998
15. Toft DO: Recent advances in the study of Hsp90 structure and mechanism of action. TEM 9: 238-243, 1998
16. Bohen SP, Yamamoto KR: Isolation of Hsp90 mutants by screening for decreased steroid receptor function. Proc Natl Acad Sci USA 90: 11424-11428, 1993
17. Picard D, Khursheed B, Garabedian MJ, Fortin MG, Lindquist S, Yamamoto KR: Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature 348: 166-168, 1990
18. Xu Y, Lindquist S: Heat-shock protein hsp90 governs the activity of pp60v-src kinase. Proc Natl Acad Sci USA 90: 7074-7078, 1993
19. Whitesell L, Mimnaugh EG, De CB, Myers CE. Neckers LM: Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 91: 8324-8328, 1994
20. Johnson JL, Toft DO: Binding of p23 and hsp90 during assembly with the progesterone receptor. Mol Endocrinol 9: 670-678, 1995
21. Smith DF, Whitesell L, Nair SC, Chen S, Prapapanich V, Rimerman RA: Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol Cell Biol 15: 6804-6812, 1995
22. Sullivan W, Stensgard B, Caucutt G, Bartha B, McMahon N, Alnemri ES, Litwack G, Toft D: Nucleotides and two functional states of hsp90. J Biol Chem 272: 8007-8012, 1997
23. An WG, Schnur RC, Neckers L, Blagosklonny MV: Depletion of p185erbB2, Raf-1 and mutant P53 proteins by geldanamycin derivatives correlates well with antiproliferative activity. Cancer Chemother Pharmacol 40: 60-64, 1997
24. Sepp LL, Ma Z, Lebwohl DE, Vinitsky A, Rosen N: Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases. J Biol Chem 270: 16580-16587, 1995
25. Mimnaugh EG, Chavany C, Neckers L: Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J Biol Chem 271: 22796-227801, 1996
26. Whitesell L, Suthphin P, An W, Schulte T, Blagosklonny M, Neckers L: Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo. Oncogene 14: 2809-2816, 1997
27. Schnur R, Corman M, Gallaschun K, Cooper B, Dee M, Doty J, Muzzi M, Moyer J. DiOrio C, Barbacci E et al.: Inhibition of the oncogene product p185erbB-2 in vitro and in vivo by geldanamycin and dihydrogeldanamycin derivatives. J Med Chem 38: 3806-3812, 1995
28. Paine-Murrieta G, Cook P, Taylor C, Whitesell L: Novel anti-breast cancer activity of benzoquinone ansamycins (Abstract). Proc Am Assoc Cancer Res 39: 175, 1998
29. Grenert JP, Sullivan WP, Fadden P, Haystead T, Clark J, Mimnaugh E, Krutzsch H, Ochel HJ, Schulte TW, Sausville E, Neckers LM, Toft DO: The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J Biol Chem 272: 23843-23850, 1997
30. Prodromou C, Roe SM, Piper PW, Pearl LH: A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone [see comments]. Nat Struct Biol 4: 477-482, 1997
31. Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP: Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89: 239-250, 1997
32. Bergerat A, de MB, Gadelle D, Varoutas PC, Nicolas A, Forterre P: An atypical topoisomerase II from Archaea with implications for meiotic recombination [see comments]. Nature 386: 414-417, 1997
33. Csermely P, Kajtar J, Hollosi M, Jalsovszky G, Holly S, Kahn CR, Gergely PJ, Soti C, Mihaly K, Somogyi J: ATP induces a conformational change of the 90-kDa heat shock protein (hsp90). J Biol Chem 268: 1901-1907, 1993
34. Nadeau K, Das A, Walsh CT: Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases. J Biol Chem 268: 1479-1487, 1993
35. Csermely P, Miyata Y, Schnaider T, Yuhara I: Autophosphorylation of grp94 (endoplasmin). J Biol Chem 270: 6381-6388, 1995
36. Wearsch PA, Nicchilla CV: Interaction of endoplasmic reticulum chaperone C;KP94 with peptide substrates is adenine nucleotide-independent. J Biol Chem 272: 5152-5156, 1997
37. Jakob U, Scheibel T, Bose S, Reinstein J, Buchner J: Assessment of the ATP binding properties of Hsp90. J Biol Chem 271: 10035-10041, 1996
38. Scheibel T, Neuhofen S, Weikl T, Mayr C, Reinstein J, Vogel PD, Buchner J: ATP-binding properties of human Hsp90. J Biol Chem 272: 18608-18613, 1997
39. Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH: Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90: 65-75, 1997
40. Louvion JF, Warth R, Picard D: Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast. Proc Natl Acad Sci USA 93: 13937-13942, 1996
41. Johnson BD, Schumacher RJ, Ross ED, Toft DO: Hop modulates hsp70/hsp90 interactions in protein folding. J Biol Chem 273: 3679-3686, 1998
42. Panaretou B, Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH: ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo EMBO J 17: 4829-4836, 1998
43. Prodromou C, Siligardi CJ, O'Brien R, Woolfson DN, Regan L, Panaretou B, Ladbury JE, Piper PW, Pearl LH: Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPK)-domain co-chaperones. EMBO J 18: 754-762, 1999
44. Schulte TW, Akinaga S, Soga S, Sullivan W, Stensgard B, Toft D, Neckers LM: Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress and Chaperones 3: 100-108, 1998
45. Sharma SV, Agatsuma T, Nakano H: Targeting of the protein chaperone Hsp90 by the transformation suppressing agent, radicicol. Oncogene 16: 2639-2645, 1998
46. Roe SM, Prodromou C, O'Brien R, Ladbury JE, Piper PW, Pearl LH: Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 42: 260-266, 1999
47. Blagosklonny MV, Toretsky J, Bohen S, Neckers L: Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90. Proc Natl Acad Sci USA 93: 8379-8383, 1996
48. Sepehrnia B, Paz IB, Dasgupta G, Momand J: Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell. J Biol Chem 271: 15084-15090, 1996
49. Blagosklonny MV, Toretsky J, Neckers L: Geldanamycin selectively destabilizes and conformationally alters mutated p53. Oncogene 11: 933-939, 1995
50. Jove R, Hanafusa H: Cell transformation by the viral src oncogene. Annu Rev Cell Biol 3: 31-56, 1987
51. v-src, with two cellular proteins. Cell 25: 363-372, 1981
52. Opperman H, Levinson W, Bishop JM: A cellular protein that associates with the transforming protein of the Rous sarcoma virus is also a heat shock protein. Proc Natl Acad Sci USA 78: 1067-1071, 1981
53. Dai K, Kobayashi R, Beach D: Physical interaction of mammalian CDC37 with CDK4. J Biol Chem 271: 22030-22034, 1996
54. Stepanova L, Leng X, Parker SB, Harper JW: Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev 10: 1491-1502, 1996
55. v-src to the plasma membrane. Proc Natl Acad Sci USA 79: 7117-7121, 1982
56. Brugge JS, Yonemoto W, Darrow D: Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: analysis of the turnover and distribution of this complex. Mol Cell Biol 3: 9-19, 1983
57. src with cellular proteins pp50 and pp90. Curr Top Microbiol Immunol 123: 1-22, 1986
58. v-src mutants that induce different cell transformation parameters. J Virol 60: 849-857, 1986
59. Nathan DF, Lindquist S: Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol Cell Biol 15: 3917-3925, 1995
60. Dey B, Caplan AJ, Boschelli F: The Ydj1 molecular chaperone facilitates formation of active p60v-src in yeast. Mol Biol Cell 7: 91-100, 1996
61. Kimura Y, Yahara I, Lindquist S: Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways [see comments]. Science 268: 1362-1365, 1995
62. Chang HC, Nathan DF, Lindquist S: In vivo analysis of the Hsp90 cochaperone Stil (p60). Mol Cell Biol 17: 318-325, 1997
63. Duina AA, Chang HC, Marsh JA, Lindquist S, Gaber RF: A cyclophilin function in Hsp90-dependent signal transduction. Science 274: 1713-1715, 1996
64. Dey B, Lightbody JJ, Boschelli F: CDC37 is required for p60v-src activity in yeast. Mol Biol Cell 7: 1405-1417, 1996
65. Kimura Y, Rutherford SL, Miyata Y, Yahara I, Freeman BC, Yue L, Morimoto RI, Lindquist S: Cdc37 is a molecular chaperone with specific functions in signal transduction. Genes Dev 11: 1775-1785, 1997
66. Uehara Y, Hori M, Takeuchi T, Umezawa H: 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, 1986
67. Uehara Y, Murakami Y, Suzukake TK, Moriya Y, Sano H, Shibata K, Omura S: Effects of herbimycin derivatives on src oncogene function in relation to antitumor activity. J Antibiot (Tokyo) 41: 831-834, 1988
68. Hutchison KA, Stancato LF, Jove R, Pratt WB: The protein-protein complex between pp60v-src and hsp90 is stabilized by molybdate, vanadate, tungstate, and an endogenous cytosolic metal. J Biol Chem 267: 13952-13957, 1992
69. Hartson SD, Matts RL: Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function. Biochemistry 33: 8912-8920, 1994
70. Hartson SD, Barrett DJ, Burn P, Matts RL: Hsp90-mediated folding of the lymphoid cell kinase p561ck. Biochemistry 35: 13451-13459, 1996
71. Lipsich LA, Cutt J, Brugge JS: Association of the transforming proteins of Rous, Fujinami and Y73 avian sarcoma viruses with the same two cellular proteins. Mol Cell Biol 2: 875-880, 1982
72. Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF: A pahway 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 Chaperones 1: 237-250, 1996
73. Aligue R, Akhavan NH, Russell P: A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90. Embo J 13: 6099-6106, 1994
74. Miller P, DiOrio C, Moyer M, Schnur RC, Bruskin A, Cullen W, Moyer JD: Depletion of the erbB-2 gene product p185 by benzoquinoid ansamycins. Cancer Res 54: 2724-2730, 1994
75. Chavany C, Mimnaugh E, Miller P, Bitton R, Nguyen P, Trepel J, Whitesell L, Schnur R, Moyer J, Neckers L: p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2. J Biol Chem 271: 4974-4977, 1996
76. Sakagami M, Morrison P, Welch WJ: Benzoquinoid ansamycins (herbimycin A and geldanamycin) interfere with the maturation of growth factor receptor tyrosine kinases. Cell Stress Chap 4: 19-28, 1999
77. Marshall CJ: Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80: 179-185, 1995
78. Morrison DK, Cutler RE: The complexity of Raf-1 regulation. Curr Opin Cell Biol 9: 174-179, 1997
79. Stancato LF, Chow YH, Hutchison KA, Perdew GH, Jove R, Pratt WB: Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. J Biol Chem 268: 21711-21716, 1993
80. Wartmann M, Davis RJ: The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex. J Biol Chem 269: 6695-6701, 1994
81. Stancato LF, Hutchison KA, Chakraborti PK, Simons SJ, Pratt WB: Differential effects of the reversible thiol-reactive agents arsenite and methyl methanethiosulfonate on steroid binding by the glucocorticoid receptor. Biochemistry 32: 3729-3736, 1993
82. Stancato LF, Chow YH, Owens GJ, Yem AW, Deibel MJ, Jove R, Pratt WB: The native v-Raf.hsp90.p50 heterocomplex contains a novel immunophilin of the FK506 binding class. J Biol Chem 269: 22157-22161, 1994
83. Schulte TW, Blagosklonny MV, Ingui C, Neckers L: Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J Biol Chem 270: 24585-24588, 1995
84. Schulte TW, An WG, Neckers LM: Geldanamycin-induced destabilization of Raf-1 involves the proteasome. Biochem Biophys Res Commun 239: 655-659, 1997
85. Whitesell L, Cook P: Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol Endocrinol 10: 705-712, 1996
86. Schulte TW, Blagosklonny MV, Romanova L, Mushinski JF, Monia BP, Johnston JF, Nguyen P, Trepel J, Neckers LM: Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway. Mol Cell Biol 16: 5839-5845, 1996
87. Stancato LF, Silverstein AM, Owens GT, Chow YH, Jove R, Pratt WB: The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase. J Biol Chem 272: 4013-4020, 1997
88. van der Straten A, Rommel C, Dickson B, Hafen E: The heat shock protein 83 (Hsp83) is required for Raf-mediated signalling in Drosophila. Embo J 16: 1961-1969, 1997
89. Miyata Y, Yahara I: The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J Biol Chem 267: 7042-7047, 1992
90. Shi Y, Brown ED, Walsh CT: Expression of recombinant human casein kinase II and recombinant heat shock protein 90 in Escherichia coli and characterization of their interactions. Proc Natl Acad Sci USA 91: 2767-2771, 1994
91. Sherr CJ: Cycling on cue. Cell 75: 551-555, 1994
92. Weinberg RA: The retinoblasloma protein and cell cycle control. Cell 81: 323-330, 1995
93. Lamphere L, Fiore F, Xu X, Brizuela L, Keezer S, Sardet C, Draetta GF, Gyuris J: Interaction between Cdc37 and Cdk4 in human cells. Oncogene 14: 1999-2004, 1997
94. Akagi T, Ono H, Shimotohno K: Tyrosine kinase inhibitor herbimycin A reduces the stability of cyclin-dependent kinase Cdk6 protein in T-cells. Oncogene 13: 399-405, 1996
95. Taussig R, Gilman AG: Mammalian membrane-bound adenylyl cyclases. J Biol Chem 270: 1-4, 1995
96. Inanobe A, Takahashi K, Katada T: Association of the beta gamma subunits of trimeric GTP-binding proteins with 90-kDa heat shock protein, hsp90. J Biochem (Tokyo) 115: 486-492, 1994
97. Schmidt CJ, Neer EJ: In vitro synthesis of G protein βγ dimers. J Biol Chem 266: 4538-4544, 1991
98. Higgins JB, Casey PJ: In vitro processing of recombinant G protein γ subunits. Requiriments for assembly of an active βγ complex. J Biol Chem 269: 9067-9073, 1994
99. Mende U, Schmidt CJ, Yi F, Spring DJ, Neer EJ: The G protein γ subunit. Requirements for dimerization with β subunits. J Biol Chem 270: 15892-15898, 1995
100. Weiner T, Liu E, Craven R, Cance W: Expression of focal adhesion kinase gene and invasive cancer. Lancet 342: 1024-1025, 1993
101. Owens L, Xu L, Craven R, Dent G, Weiner T, Kornberg L, Liu E, Cance W: Overexpression of the focal adhesion kinase (p125FAK) in invasive human tumors. Cancer Res 55: 2752-2755, 1995
102. Ochel H-J, Schulte T, Nguyen P, Trepel J, Neckers L: The benzoquinone ansamycin geldanamycin stimulates proteo-lytic degradation of focal adhesion kinase. Mol Gen Met 66: 24-30, 1999
103. Supko JG, Hickman RL, Grever MR, Malspeis L: Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent. Cancer Chemother Pharmacol 36: 305-315, 1995
104. Jameel A, Law M, Coombes RC, Luqmani YA: Significance of heat shock protein 90 as prognostic indicator in breast cancer. Int J Oncol 2: 1075-1080, 1993
105. Yano M, Naito Z, Tanaka S, Asano G: Expression and roles of heat shock proteins in human breast cancer. Jpn J Cancer Res 87: 908-915, 1996
106. Yufu Y, Nishimura J, Nawata H: High constitutive expression of heat shock protein 90α in human acute leukemia cells. Leuk Res 16: 597-605, 1992
107. Lebeau J, Chalony C, Prosperi MT, Goubin G: Constitutive overexpression of 89 kDa heat shock protein gene in the HBL100 human mammary cell line converted to a tumorigenic phenotype by the EJ/T24 Harvey-ras oncogene. Oncogene 6: 1125-1132, 1991
108. Ferrarini M, Heltai S, Zocchi MR, Rugarli C: Unusual expression and localization of heat-shock proteins in human tumor cells. Int J Cancer 51: 613-619, 1992
109. Gabai VL, Mosina VA, Budagova KR, Kabakov AE: Spontaneous overexpression of heat shock protein in Ehrlich ascites carcinoma cells during in vivo growth. Biochem Mol Int 35: 95-102, 1995
110. Jameel A, Skilton RA, Campbell TA, Chander SK, Coombes RC, Luqmani YA: Clinical and biological significance of HSP89a in human breast cancer. Int J Cancer 50: 409-415, 1992
111. Redeuilh G, Moncharmon B, Secco C, Baulieu EE: Subunit composition of the molybdate-stabilized "8-9S" nontransformed estradiol receptor purified from calf uterus. J Biol Chem 262: 6969-6975, 1987
112. Veldscholte J, Berrevoets CA, Brinkmann AO, Grootegoed JA, Mulder E: Anti-androgens and the mutated androgen receptor of LNCaP cells: differential effects on binding affinity, heat-shock protein interaction, and transcription activation. Biochemistry 31: 2393-2399, 1992
113. Aumais J, Lee H, R L, JH W: Selective interaction of Hsp90 with an estrogen receptor ligand-binding domain containing a point mutation. J Biol Chem 272: 12229-12235, 1997
114. Nguyen D, Chen A, Mixon A, Schrump D: Sequence-dependent enhancement of taxol sensitivity in non-small cell lung cancer by erbB-2 tyrosine kinase inhibitor NSC330507 (Abstract). Proc Am Assoc Cane Res 40: 485, 1999
115. Schulte T, Neckers L: The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to Hsp90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 42: 273-279, 1998
116. Nair SC, Rimerman RA, Toran EJ, Chen S, Prapapanich V, Butts RN, Smith DF: Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor. Mol Cell Biol 17: 594-603, 1997