메뉴 건너뛰기




Volumn 2, Issue 2, 2003, Pages 131-138

Auditing the pharmacological accounts for Hsp90 molecular chaperone inhibitors: Unfolding the relationship between pharmacokinetics and pharmacodynamics

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; 17-(ALLYLAMINO)-17-DEMETHOXYGELDANAMYCIN; BENZOQUINONE DERIVATIVE; DRUG DERIVATIVE; ENZYME INHIBITOR; HEAT SHOCK PROTEIN 90; MACROCYCLIC LACTAM; PROTEIN SERINE THREONINE KINASE; RIFABUTIN;

EID: 0043269344     PISSN: 15357163     EISSN: 15388514     Source Type: Journal    
DOI: None     Document Type: Note
Times cited : (115)

References (44)
  • 1
    • 0036840774 scopus 로고    scopus 로고
    • Challenges of PK/PD measurements in modern drug development
    • DOI 10.1016/S0959-8049(02)00395-7, PII S0959804902003957
    • Workman, P. Challenges of PK/PD measurements in modern drug development. Eur. J. Cancer, 38: 2189-2193, 2002. (Pubitemid 35223253)
    • (2002) European Journal of Cancer , vol.38 , Issue.16 , pp. 2189-2193
    • Workman, P.1
  • 3
    • 0042855994 scopus 로고    scopus 로고
    • 17AAG: Low-target binding affinity and potent cell activity-finding an explanation
    • Chiosis, G., Huezo, H., Rosen, N., Mimnaugh, E., Whitesell, L., and Neckers, L. 17AAG: low-target binding affinity and potent cell activity-finding an explanation. Mol. Cancer Ther., 2: 123-129, 2003.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 123-129
    • Chiosis, G.1    Huezo, H.2    Rosen, N.3    Mimnaugh, E.4    Whitesell, L.5    Neckers, L.6
  • 4
    • 0027753718 scopus 로고
    • Pharmacokinetics and Cancer Chemotherapy
    • Cold Spring Harbor, New York: Cold Spring Harbor Press
    • Workman, P., and Graham, M. A. (eds.), Pharmacokinetics and Cancer Chemotherapy. Cancer Surveys, Vol. 17. Cold Spring Harbor, New York: Cold Spring Harbor Press, 1993.
    • (1993) Cancer Surveys , vol.17
    • Workman, P.1    Graham, M.A.2
  • 5
    • 0037237884 scopus 로고    scopus 로고
    • How much gets there and what does it do? The need for better pharmacokinetic and pharmacodynamic endpoints in contemporary drug discovery and development
    • (Ed Cook, GRJ), Current Pharmaceutical Design, in press
    • Workman P. How much gets there and what does it do? The need for better pharmacokinetic and pharmacodynamic endpoints in contemporary drug discovery and development. In: Radiolabelled Compounds for Drug Discovery and Development (Ed Cook, GRJ), Current Pharmaceutical Design, in press, 2003.
    • (2003) Radiolabelled Compounds for Drug Discovery and Development
    • Workman, P.1
  • 6
    • 0036219609 scopus 로고    scopus 로고
    • Hsp90 inhibitors as novel cancer chemotherapeutic agents
    • DOI 10.1016/S1471-4914(02)02316-X, PII S147149140202316X
    • Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol. Med., 8 (Suppl.): S55-S61, 2002. (Pubitemid 34297080)
    • (2002) Trends in Molecular Medicine , vol.8 , Issue.4 SUPPL.
    • Neckers, L.1
  • 7
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • DOI 10.1517/14712598.2.1.3
    • Maloney, A., and Workman, P. HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin. Biol. Ther, 2: 3-24, 2002. (Pubitemid 34462457)
    • (2002) Expert Opinion on Biological Therapy , vol.2 , Issue.1 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 8
    • 0037025173 scopus 로고    scopus 로고
    • Addiction to oncogenes
    • Wash. DC
    • Weinstein, I. B. Addiction to oncogenes. Science (Wash. DC), 297: 63-64, 2002.
    • (2002) Science , vol.297 , pp. 63-64
    • Weinstein, I.B.1
  • 9
    • 0035902115 scopus 로고    scopus 로고
    • Proliferation, cell cycle and apoptosis in cancer
    • DOI 10.1038/35077213
    • Evan, G. I., and Vousden, K. H. Proliferation, cell cycle and apoptosis in cancer research. Nature (Lond.), 411: 342-348, 2001. (Pubitemid 32467043)
    • (2001) Nature , vol.411 , Issue.6835 , pp. 342-348
    • Evan, G.I.1    Vousden, K.H.2
  • 10
    • 0033951278 scopus 로고    scopus 로고
    • Structure and in vivo function of Hsp90
    • DOI 10.1016/S0959-440X(99)00047-0
    • Prodromou, C., and Pearl, L. H. Structure and in vivo function of Hsp90. Curr. Opin. Struct. Biol., 10: 46-51, 2000. (Pubitemid 30099326)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.1 , pp. 46-51
    • Pearl, L.H.1    Prodromou, C.2
  • 11
    • 0029056501 scopus 로고
    • Preclinical pharmacologic evaluation of geldanamycin as an antitumour agent
    • Supko, J. G., Hickman, R. L., Grever, M. R., and Malspeis, L. Preclinical pharmacologic evaluation of geldanamycin as an antitumour agent. Cancer Chemother. Pharmacol., 36: 305-310, 1995.
    • (1995) Cancer Chemother. Pharmacol. , vol.36 , pp. 305-310
    • Supko, J.G.1    Hickman, R.L.2    Grever, M.R.3    Malspeis, L.4
  • 12
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • DOI 10.1007/s002800050817
    • Schulte, T. W., and Neckers, L. M. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamcyin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother. Pharmacol., 42: 273-279, 1998. (Pubitemid 28393843)
    • (1998) Cancer Chemotherapy and Pharmacology , vol.42 , Issue.4 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 13
    • 0035300564 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function by ansamycins causes the morphological and functional differentiation of breast cancer cells
    • Munster, P. N., Srethapakdi, M., Moasser, M. M., and Rosen, N. Inhibition of heat shock protein 90 function by ansamycins causes the morphological and functional differentiation of breast cancer cells. Cancer Res., 61: 2945-2952, 2001. (Pubitemid 32691939)
    • (2001) Cancer Research , vol.61 , Issue.7 , pp. 2945-2952
    • Munster, P.N.1    Srethapakdi, M.2    Moasser, M.M.3    Rosen, N.4
  • 14
    • 0035872442 scopus 로고    scopus 로고
    • Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis
    • Hostein, I., Robertson, D., Di Stefano, F., Workman, P., and Clarke, P. A. Inhibition of signal transduction by 17-allylamino-17-demethoxy-geldanamycin results in cytostasis and apoptosis. Cancer Res., 61: 4003-4009, 2001. (Pubitemid 32720963)
    • (2001) Cancer Research , vol.61 , Issue.10 , pp. 4003-4009
    • Hostein, I.1    Robertson, D.2    DiStefano, F.3    Workman, P.4    Clarke, P.A.5
  • 15
    • 0033579175 scopus 로고    scopus 로고
    • DT-diaphorase expression and tumor cell sensitivity to 17- allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90
    • Bethesda
    • Kelland, L. R., Sharp, S. Y., Rogers, P. M., Myers, T. G., and Workman, P. DT-diaphorase expression and tumor cell sensitivity to 17- allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J. Natl. Cancer Inst. (Bethesda), 91: 1940-1949, 1999.
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 17
    • 0037075232 scopus 로고    scopus 로고
    • Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2
    • DOI 10.1038/sj/onc/1205184
    • Basso, A. D., Solit, D. B., Munster, P. N., and Rosen, N. Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene, 21: 1159-1166, 2002. (Pubitemid 34185232)
    • (2002) Oncogene , vol.21 , Issue.8 , pp. 1159-1166
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 18
    • 0042166816 scopus 로고    scopus 로고
    • 17-DMAG (NSC 707545), a water-soluble geldanamycin analog, has superior in vitro and in vivo antitumour activity compared to the hsp90 inhibitor 17-AAG
    • Smith, V., Sausville, E. A., Camalier, R. F., Fiebig, H. H., and Burger, A. M. 17-DMAG (NSC 707545), a water-soluble geldanamycin analog, has superior in vitro and in vivo antitumour activity compared to the hsp90 inhibitor 17-AAG. Eur. J. Cancer, 38 (Suppl. 7): S60, 2002.
    • (2002) Eur. J. Cancer , vol.38 , Issue.SUPPL. 7
    • Smith, V.1    Sausville, E.A.2    Camalier, R.F.3    Fiebig, H.H.4    Burger, A.M.5
  • 19
    • 0012977234 scopus 로고    scopus 로고
    • Clinical pharmacokinetics of 17-(allylamino)-17-demethoxygeldanamycin and the active metabolite 17-(allylamino)-17-demethoxygeldanamycin given as a one-hour infusion daily for 5 days
    • Agnew, E. B., Wilson, R. H., Morrison, G., Neckers, L. M., Takimoto, C., H., and Grem, J. L. Clinical pharmacokinetics of 17-(allylamino)-17- demethoxygeldanamycin and the active metabolite 17-(allylamino)-17- demethoxygeldanamycin given as a one-hour infusion daily for 5 days. Proc. Am. Assoc. Cancer Res., 43: 1349, 2002.
    • (2002) Proc. Am. Assoc. Cancer Res. , vol.43 , pp. 1349
    • Agnew, E.B.1    Wilson, R.H.2    Morrison, G.3    Neckers, L.M.4    Takimoto, C.H.5    Grem, J.L.6
  • 22
    • 0001148460 scopus 로고    scopus 로고
    • Phase I trial of the heat shock protein 90 (HSP90) inhibitor 17-(allylamino)-17- demethoxygeldanamycin (17AAG). Pharmacokinetic (PK) profile and pharmacodynamic (PD) endpoints
    • Banerji, U., O'Donnell, A., Scurr, M., Benson, C., Hanwell, J., Clark, S., Raynaud, F., Turner, A., Walton, M., Workman, P., and Judson, I. Phase I trial of the heat shock protein 90 (HSP90) inhibitor 17-(allylamino)-17- demethoxygeldanamycin (17AAG). Pharmacokinetic (PK) profile and pharmacodynamic (PD) endpoints. Proc. Am. Soc. Clin. Oncol., 20: 82a, 2001.
    • (2001) Proc. Am. Soc. Clin. Oncol. , vol.20
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3    Benson, C.4    Hanwell, J.5    Clark, S.6    Raynaud, F.7    Turner, A.8    Walton, M.9    Workman, P.10    Judson, I.11
  • 25
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • DOI 10.1093/emboj/17.16.4829
    • Panaretou, B., Prodromou, C., Roe, S. M., O'Brien, R., Ladbury, J. E., Piper, P. W., and Pearl, L. H. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J., 17: 4829-4836, 1998. (Pubitemid 28377183)
    • (1998) EMBO Journal , vol.17 , Issue.16 , 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
  • 26
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • DOI 10.1021/jm980403y
    • Roe, S. M., Prodromou, C., O'Brien. R., Ladbury, J. E., Piper, P. W., and Pearl, L. H. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumour antibiotics radicicol and geldanamycin. J. Med. Chem., 42: 260-266, 1999. (Pubitemid 29069861)
    • (1999) Journal of Medicinal Chemistry , vol.42 , Issue.2 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 27
    • 0035832106 scopus 로고    scopus 로고
    • LY294002-geldanamycin heterodimers as selective inhibitors of the PI3K and PI3K-related family
    • DOI 10.1016/S0960-894X(01)00099-3, PII S0960894X01000993
    • Chiosis, G., Rosen, N., and Sepp-Lorenzino, L. LY294002-geldanamycin heterodimers as selective inhibitors of the PI3K and PI3K-related family. Bioorg. Med. Chem. Lett., 11: 909-913, 2001. (Pubitemid 32226213)
    • (2001) Bioorganic and Medicinal Chemistry Letters , vol.11 , Issue.7 , pp. 909-913
    • Chiosis, G.1    Rosen, N.2    Sepp-Lorenzino, L.3
  • 28
    • 0006886916 scopus 로고    scopus 로고
    • PC3 human prostate xenograft retention of, and oncoprotein modulation by, 17-(allylamino)-17-demethoxygeldanamycin (17AAG) in vivo
    • Egorin, M. J., Sentz, D. L., Zuhowski, E. G., Dobson, J. M., Schulte, T. W., Neckers, L. M., and Eiseman, J. L. PC3 human prostate xenograft retention of, and oncoprotein modulation by, 17-(allylamino)-17-demethoxygeldanamycin (17AAG) in vivo. Proc. Am. Assoc. Cancer Res., 40: 3409, 1999.
    • (1999) Proc. Am. Assoc. Cancer Res. , vol.40 , pp. 3409
    • Egorin, M.J.1    Sentz, D.L.2    Zuhowski, E.G.3    Dobson, J.M.4    Schulte, T.W.5    Neckers, L.M.6    Eiseman, J.L.7
  • 29
    • 0032101569 scopus 로고    scopus 로고
    • Metabolism of 17-(allylamino)-17-demethoxygeldanamycin (NSC 330507) by murine and human hepatic preparations
    • Egorin, M. J., Rosen, D. M., Wolff, J. H., Callery, P. S., Musser, S. M., and Eiseman, J. L. Metabolism of 17-(allylamino)-17-demethoxygeldanamycin (NSC 330507) by murine and human hepatic preparations. Cancer Res., 58: 2385-2396, 1998. (Pubitemid 28252699)
    • (1998) Cancer Research , vol.58 , Issue.11 , pp. 2385-2396
    • Egorin, M.J.1    Rosen, D.M.2    Wolff, J.H.3    Callery, P.S.4    Musser, S.M.5    Eiseman, J.L.6
  • 30
    • 0036339108 scopus 로고    scopus 로고
    • ErbB2 overexpression in an ovarian cancer cell line confers sensitivity to the HSP90 inhibitor geldanamycin
    • Smith, V., Hobbs, S., Court, W., Eccles, S., Workman, P., and Kelland, L. R. ErbB2 overexpression in an ovarian cancer cell line confers sensitivity to the HSP90 inhibitor geldanamycin. Anticancer Res., 22: 1993- 2000, 2002.
    • (2002) Anticancer Res. , vol.22 , pp. 1993-2000
    • Smith, V.1    Hobbs, S.2    Court, W.3    Eccles, S.4    Workman, P.5    Kelland, L.R.6
  • 31
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto, R. I. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev., 12: 3788-3796, 1998. (Pubitemid 29024840)
    • (1998) Genes and Development , vol.12 , Issue.24 , pp. 3788-3796
    • Morimoto, R.I.1
  • 32
    • 0034710542 scopus 로고    scopus 로고
    • Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone
    • Clarke, P. A., Hostein, I., Banerji, U., DiStefano, F., Maloney, A., Walton, M., and Workman, P. Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17- demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone. Oncogene, 19: 4125-4133, 2000.
    • (2000) Oncogene , vol.19 , pp. 4125-4133
    • Clarke, P.A.1    Hostein, I.2    Banerji, U.3    DiStefano, F.4    Maloney, A.5    Walton, M.6    Workman, P.7
  • 33
    • 0000593108 scopus 로고    scopus 로고
    • Validation of pharmacodynamic endpoints for the Hsp90 molecular chaperone inhibitor 17-allylamino 17-demethoxygeldanamycin (17AAG) in a human tumor xenograft model
    • Banerji, U., Walton, M., Raynaud, F., Kelland, L., Judson, I., and Workman, P. Validation of pharmacodynamic endpoints for the Hsp90 molecular chaperone inhibitor 17-allylamino 17-demethoxygeldanamycin (17AAG) in a human tumor xenograft model. Proc. Am. Assoc. Cancer Res., 42: 4473, 2001.
    • (2001) Proc. Am. Assoc. Cancer Res. , vol.42 , pp. 4473
    • Banerji, U.1    Walton, M.2    Raynaud, F.3    Kelland, L.4    Judson, I.5    Workman, P.6
  • 35
    • 0029665779 scopus 로고    scopus 로고
    • Mammalian p50(Cdc37) is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Stepanova, L., Leng, X., Parker, S. B., and Harper, J. W. Mammalian p50cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes CDK4. Genes Dev., 10: 1491-1502, 1996. (Pubitemid 26260706)
    • (1996) Genes and Development , vol.10 , Issue.12 , pp. 1491-1502
    • Stepanova, L.1    Leng, X.2    Parker, S.B.3    Wade, H.J.4
  • 36
    • 0036359767 scopus 로고    scopus 로고
    • Scaling down imaging: Molecular mapping of cancer in mice
    • Weissleder, R. Scaling down imaging: molecular mapping of cancer in mice. Nat. Cancer Rev., 2: 1-8, 2002.
    • (2002) Nat. Cancer Rev. , vol.2 , pp. 1-8
    • Weissleder, R.1
  • 38
    • 0037163668 scopus 로고    scopus 로고
    • Use of radiolabelled choline as a pharmacodynamic marker for the signal transduction inhibitor geldanamycin
    • DOI 10.1038/sj.bjc.6600558
    • Lui, D., Hutchinson, O. C., Osman, S., Price, P., Workman, P., and Aboagye, E. O. Use of radiolabelled choline as a pharmacodynamic marker for the signal transduction inhibitor geldanamycin. Br. J. Cancer, 87: 783-789, 2002. (Pubitemid 35178757)
    • (2002) British Journal of Cancer , vol.87 , Issue.7 , pp. 783-789
    • Liu, D.1    Hutchinson, O.C.2    Osman, S.3    Price, P.4    Workman, P.5    Aboagye, E.O.6
  • 39
    • 0034890377 scopus 로고    scopus 로고
    • Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB-and schedule-dependent manner
    • Munster, P. N., Basso, A., Solit, D., Norton, L., and Rosen, L. Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB- and schedule-dependent manner. Clin. Cancer Res., 7: 2228-2236, 2001. (Pubitemid 32751619)
    • (2001) Clinical Cancer Research , vol.7 , Issue.8 , pp. 2228-2236
    • Munster, P.N.1    Basso, A.2    Solit, D.3    Norton, L.4    Rosen, N.5
  • 40
    • 0035071607 scopus 로고    scopus 로고
    • 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
    • DOI 10.1016/S1074-5521(01)00015-1, PII S1074552101000151
    • Chiosis, G., Timaul, M. N., Lucas, B., Munster, M. N., Zheng, F. F., Sepp-Lorenzino, L., and Rosen, N. 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., 8: 289-299, 2001. (Pubitemid 32296118)
    • (2001) Chemistry and Biology , vol.8 , Issue.3 , pp. 289-299
    • Chiosis, G.1    Timaul, M.N.2    Lucas, B.3    Munster, P.N.4    Zheng, F.F.5    Sepp-Lorenzino, L.6    Rosen, N.7
  • 41
    • 0036836964 scopus 로고    scopus 로고
    • Development of a purine-based novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase
    • Chiosis, G., Huezo, H., Lucas, B., and Rosen, N. Development of a purine-based novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase. Bioorg. Med. Chem., 10: 3555-3564, 2002.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3555-3564
    • Chiosis, G.1    Huezo, H.2    Lucas, B.3    Rosen, N.4
  • 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
    • DOI 10.1074/jbc.M003701200
    • Marcu, M. G., Chadli, A., Bouhouche, I., Catelli, M., and Neckers, L. 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., 275: 37181-37186, 2000. (Pubitemid 32002137)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.47 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.