메뉴 건너뛰기




Volumn 71, Issue 2, 2008, Pages 117-124

Tubulin-perturbing naphthoquinone spiroketals

Author keywords

Hsp70; Microtubules; p21WAF1; Thioredoxin reductase

Indexed keywords

5' HYDROXY 4'H SPIRO[1,3 DIOXOLANE 2,1' NAPHTHALEN] 4' ONE; 5' METHOXY 4'H SPIRO[1,3 DIOXANE 2,1' NAPHTHALEN] 4' ONE; [8 (FURAN 3 YLMETHOXY) 1 OXO 1,4 DIHYDRONAPHTHALENE 4 SPIRO 2' NAPHTHO[1',8' DE][1',3] [DIOXIN]; BETA TUBULIN; COLCHICINE; NAPHTHOQUINONE; PACLITAXEL; SR 7; TH 169; TH 223; TUBULIN; UNCLASSIFIED DRUG;

EID: 38549166138     PISSN: 17470277     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2007.00616.x     Document Type: Article
Times cited : (11)

References (36)
  • 3
    • 0034684526 scopus 로고    scopus 로고
    • Novel synthetic approaches to the palmarumycin skeleton
    • Coutts I.G.C., Allcock R.W., Scheeren H.W. (2000) Novel synthetic approaches to the palmarumycin skeleton. Tetrahedron Lett 41 : 9105 9107.
    • (2000) Tetrahedron Lett , vol.41 , pp. 9105-9107
    • Coutts, I.G.C.1    Allcock, R.W.2    Scheeren, H.W.3
  • 4
    • 0033582778 scopus 로고    scopus 로고
    • Total synthesis of the spiroketal naphthoquinone (+)-diepoxin
    • Wipf P., Jung J-K. (1999) Total synthesis of the spiroketal naphthoquinone (+)-diepoxin. J Org Chem 64 : 1092 1093.
    • (1999) J Org Chem , vol.64 , pp. 1092-1093
    • Wipf, P.1    Jung, J.-K.2
  • 5
    • 0035819338 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of deoxypreussomerin a and palmarumycin CP1 and related naphthoquinone spiroketals
    • Wipf P., Jung J-K., Rodriguez S., Lazo J.S. (2001) Synthesis and biological evaluation of deoxypreussomerin A and palmarumycin CP1 and related naphthoquinone spiroketals. Tetrahedron 57 : 283 296.
    • (2001) Tetrahedron , vol.57 , pp. 283-296
    • Wipf, P.1    Jung, J.-K.2    Rodriguez, S.3    Lazo, J.S.4
  • 6
    • 0029836750 scopus 로고    scopus 로고
    • Total synthesis of the antimitotic marine natural product (+)-curacin a
    • Wipf P., Xu W. (1996) Total synthesis of the antimitotic marine natural product (+)-curacin A. J Org Chem 61 : 6556 6562.
    • (1996) J Org Chem , vol.61 , pp. 6556-6562
    • Wipf, P.1    Xu, W.2
  • 7
    • 0021163546 scopus 로고
    • Separation of active tubulin and microtubule associated proteins by ultracentrifugation and isolation of a component causing the formation of microtubule bundles
    • Hamel E., Lin C.M. (1984) Separation of active tubulin and microtubule associated proteins by ultracentrifugation and isolation of a component causing the formation of microtubule bundles. Biochemistry 23 : 4173 4184.
    • (1984) Biochemistry , vol.23 , pp. 4173-4184
    • Hamel, E.1    Lin, C.M.2
  • 8
    • 0037171849 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of structurally highly modified analogues of the antimitotic natural product curacin a
    • Wipf P., Reeves J.T., Balachandran R., Day B.W. (2002) Synthesis and biological evaluation of structurally highly modified analogues of the antimitotic natural product curacin A. J Med Chem 45 : 1901 1917.
    • (2002) J Med Chem , vol.45 , pp. 1901-1917
    • Wipf, P.1    Reeves, J.T.2    Balachandran, R.3    Day, B.W.4
  • 9
    • 0038460882 scopus 로고    scopus 로고
    • Simplified discodermolide analogues: Synthesis and biological evaluation of 4-epi-7-dehydroxy-14,16-didemethyl-(+)-discodermolides as microtubule-stabilizing agents
    • Choy N., Shin Y., Nguyen P.Q., Curran D.P., Balachandran R., Madiraju C., Day B.W. (2003) Simplified discodermolide analogues: synthesis and biological evaluation of 4-epi-7-dehydroxy-14,16-didemethyl-(+)-discodermolides as microtubule-stabilizing agents. J Med Chem 46 : 2846 2864.
    • (2003) J Med Chem , vol.46 , pp. 2846-2864
    • Choy, N.1    Shin, Y.2    Nguyen, P.Q.3    Curran, D.P.4    Balachandran, R.5    Madiraju, C.6    Day, B.W.7
  • 10
    • 0031913357 scopus 로고    scopus 로고
    • Structure-activity analysis of the interaction of curacin A, the potent colchicine site antimitotic agent with tubulin and effects of analogs on the growth of MCF-7 breast cancer cells
    • Verdier-Pinard P., Lai J.Y., Yoo H.D., Yu J., Marquez B., Nagle D.G., Nambu M., White J.D., Falck J.R., Gerwick W.H., Day B.W., Hamel E. (1998) Structure-activity analysis of the interaction of curacin A, the potent colchicine site antimitotic agent with tubulin and effects of analogs on the growth of MCF-7 breast cancer cells. Mol Pharmacol 53 : 62 76.
    • (1998) Mol Pharmacol , vol.53 , pp. 62-76
    • Verdier-Pinard, P.1    Lai, J.Y.2    Yoo, H.D.3    Yu, J.4    Marquez, B.5    Nagle, D.G.6    Nambu, M.7    White, J.D.8    Falck, J.R.9    Gerwick, W.H.10    Day, B.W.11    Hamel, E.12
  • 12
    • 0028331925 scopus 로고
    • 2-Methoxyestradiol, an endogenous mammalian metabolite, inhibits tubulin polymerization by interacting at the colchicine site
    • D'Amato R.J., Lin C.M., Flynn E., Folkman J., Hamel E. (1994) 2-Methoxyestradiol, an endogenous mammalian metabolite, inhibits tubulin polymerization by interacting at the colchicine site. Proc Natl Acad Sci USA 91 : 3964 3968.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3964-3968
    • D'Amato, R.J.1    Lin, C.M.2    Flynn, E.3    Folkman, J.4    Hamel, E.5
  • 13
    • 33744958179 scopus 로고    scopus 로고
    • Thioredoxin reductase 1 deficiency reverses tumor phenotype and tumorigenecity of lung carcinoma cells
    • Yoo M-H., Xu X-M., Carlson B.A., Gladyshev V.N., Hatfield D.L. (2006) Thioredoxin reductase 1 deficiency reverses tumor phenotype and tumorigenecity of lung carcinoma cells. J Biol Chem 281 : 13005 13008.
    • (2006) J Biol Chem , vol.281 , pp. 13005-13008
    • Yoo, M.-H.1    Xu, X.-M.2    Carlson, B.A.3    Gladyshev, V.N.4    Hatfield, D.L.5
  • 14
    • 0033674365 scopus 로고    scopus 로고
    • Z-1,1-Dichloro-2,3-diphenylcyclopropanes block human prostate carcinoma cell proliferation, inhibit prostate specific antigen expression and initiate apoptosis
    • Balachandran R., Grant S.G., Welsh M.J., Day B.W. (2000) Z-1,1-Dichloro-2,3-diphenylcyclopropanes block human prostate carcinoma cell proliferation, inhibit prostate specific antigen expression and initiate apoptosis. Prostate 45 : 277 288.
    • (2000) Prostate , vol.45 , pp. 277-288
    • Balachandran, R.1    Grant, S.G.2    Welsh, M.J.3    Day, B.W.4
  • 16
    • 0028360795 scopus 로고
    • Interaction of ethacrynic acid with bovine brain tubulin
    • Luduena R.F., Roach M.C., Epstein D.L. (1994) Interaction of ethacrynic acid with bovine brain tubulin. Biochem Pharmacol 47 : 1677 1681.
    • (1994) Biochem Pharmacol , vol.47 , pp. 1677-1681
    • Luduena, R.F.1    Roach, M.C.2    Epstein, D.L.3
  • 17
    • 0022271604 scopus 로고
    • Diethylstilbestrol: The binding and effects of diethylstilbestrol upon the polymerisation and depolymerisation of purified microtubule protein in vitro
    • Sharp D.C., Perry J.M. (1985) Diethylstilbestrol: the binding and effects of diethylstilbestrol upon the polymerisation and depolymerisation of purified microtubule protein in vitro. Carcinogenesis 6 : 865 871.
    • (1985) Carcinogenesis , vol.6 , pp. 865-871
    • Sharp, D.C.1    Perry, J.M.2
  • 18
    • 0030473213 scopus 로고    scopus 로고
    • The mechanism of benzene-induced leukemia: A hypothesis and speculations on the causes of leukemia
    • Smith M.T. (1996) The mechanism of benzene-induced leukemia: a hypothesis and speculations on the causes of leukemia. Environ Health Perspect 104 (Suppl. 6 1219 1225.
    • (1996) Environ Health Perspect , vol.104 , Issue.6 , pp. 1219-1225
    • Smith, M.T.1
  • 19
    • 1642430703 scopus 로고    scopus 로고
    • Microtubule targeted anticancer agents and apoptosis
    • Bhalla K.N. (2003) Microtubule targeted anticancer agents and apoptosis. Oncogene 22 : 9075 9086.
    • (2003) Oncogene , vol.22 , pp. 9075-9086
    • Bhalla, K.N.1
  • 20
    • 0347917093 scopus 로고    scopus 로고
    • Cell cycle targeted therapies
    • Swanton C. (2004) Cell cycle targeted therapies. Lancet Oncol 5 : 27 36.
    • (2004) Lancet Oncol , vol.5 , pp. 27-36
    • Swanton, C.1
  • 22
    • 24644441050 scopus 로고    scopus 로고
    • The thioredoxin reductase/thioredoxin system: Novel redox targets for cancer therapy
    • Biaglow J.E., Miller R.A. (2005) The thioredoxin reductase/thioredoxin system: novel redox targets for cancer therapy. Cancer Biol Ther 4 : 6 13.
    • (2005) Cancer Biol Ther , vol.4 , pp. 6-13
    • Biaglow, J.E.1    Miller, R.A.2
  • 23
    • 33751181030 scopus 로고    scopus 로고
    • On the potential of thioredoxin reductase inhibitors for cancer therapy
    • Urig S., Becker K. (2006) On the potential of thioredoxin reductase inhibitors for cancer therapy. Semin Cancer Biol 16 : 452 465.
    • (2006) Semin Cancer Biol , vol.16 , pp. 452-465
    • Urig, S.1    Becker, K.2
  • 24
    • 0344875019 scopus 로고    scopus 로고
    • Thioredoxin: A key regulator of cardiovascular homeostasis
    • Yamawaki H., Haendeler J., Berk B.C. (2003) Thioredoxin: a key regulator of cardiovascular homeostasis. Circ Res 93 : 1029 1033.
    • (2003) Circ Res , vol.93 , pp. 1029-1033
    • Yamawaki, H.1    Haendeler, J.2    Berk, B.C.3
  • 25
    • 19444381651 scopus 로고    scopus 로고
    • Direct association of hematopoietin with thioredoxin constitutes a redox signal transduction in activation of AP-1/NF-kappaB
    • Li Y., Liu W., Xing G., Tian C., Zhu Y., He F. (2005) Direct association of hematopoietin with thioredoxin constitutes a redox signal transduction in activation of AP-1/NF-kappaB. Cell Signal 17 : 985 996.
    • (2005) Cell Signal , vol.17 , pp. 985-996
    • Li, Y.1    Liu, W.2    Xing, G.3    Tian, C.4    Zhu, Y.5    He, F.6
  • 26
    • 33751178410 scopus 로고    scopus 로고
    • The thioredoxin system in cancer
    • Arner E.S.J., Holmgren A. (2006) The thioredoxin system in cancer. Semin Cancer Biol 16 : 420 426.
    • (2006) Semin Cancer Biol , vol.16 , pp. 420-426
    • Arner, E.S.J.1    Holmgren, A.2
  • 28
    • 0034608892 scopus 로고    scopus 로고
    • Selective depletion of heat shock protein 70 (Hsp70) activates a tumor specific death program that is independent of caspases and bypasses Bcl-2
    • Nylandsted J., Rohde M., Brand K., Bastholm L., Elling F., Jaattela M. (2000) Selective depletion of heat shock protein 70 (Hsp70) activates a tumor specific death program that is independent of caspases and bypasses Bcl-2. Proc Natl Acad Sci USA 97 : 7871 7876.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7871-7876
    • Nylandsted, J.1    Rohde, M.2    Brand, K.3    Bastholm, L.4    Elling, F.5    Jaattela, M.6
  • 30
    • 0032481131 scopus 로고    scopus 로고
    • Prostate carcinoma cell death resulting from inhibition of proteosome activity is independent of functional Bcl-2 and p53
    • Herrmann J.L., Briones F. Jr., Brisbay S., Logothetis C.J., McDonnell T.J. (1998) Prostate carcinoma cell death resulting from inhibition of proteosome activity is independent of functional Bcl-2 and p53. Oncogene 17 : 2889 2899.
    • (1998) Oncogene , vol.17 , pp. 2889-2899
    • Herrmann, J.L.1    Briones Jr., F.2    Brisbay, S.3    Logothetis, C.J.4    McDonnell, T.J.5
  • 31
    • 33746330168 scopus 로고    scopus 로고
    • Hsp70 molecular chaperones: Emerging roles in human disease and identification of small molecule modulators
    • Brodsky J.L., Chiosis G. (2006) Hsp70 molecular chaperones: emerging roles in human disease and identification of small molecule modulators. Curr Top Med Chem 6 : 1215 1225.
    • (2006) Curr Top Med Chem , vol.6 , pp. 1215-1225
    • Brodsky, J.L.1    Chiosis, G.2
  • 32
    • 15244351845 scopus 로고    scopus 로고
    • Granzyme a induces caspase-independent mitochondrial damage, a required first step for apoptosis
    • Martinvalet D., Zhu P., Lieberman J. (2005) Granzyme A induces caspase-independent mitochondrial damage, a required first step for apoptosis. Immunity 22 : 355 370.
    • (2005) Immunity , vol.22 , pp. 355-370
    • Martinvalet, D.1    Zhu, P.2    Lieberman, J.3
  • 33
    • 20444371005 scopus 로고    scopus 로고
    • Control of cell fate by Hsp70: More than an evanescent meeting
    • Morishima N. (2005) Control of cell fate by Hsp70: more than an evanescent meeting. J Biochem 137 : 449 453.
    • (2005) J Biochem , vol.137 , pp. 449-453
    • Morishima, N.1
  • 34
    • 14644435819 scopus 로고    scopus 로고
    • Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
    • Rohde M., Daugaard M., Jensen M.H., Helin K., Nylandsted J., Jäättelä M. (2005) Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev 19 : 570 582.
    • (2005) Genes Dev , vol.19 , pp. 570-582
    • Rohde, M.1    Daugaard, M.2    Jensen, M.H.3    Helin, K.4    Nylandsted, J.5    Jäättelä, M.6
  • 35
    • 3543019075 scopus 로고    scopus 로고
    • Expression of a dominant negative heat shock factor-1 construct inhibits aneuploidy in prostate carcinoma cells
    • Wang Y., Theriault J.R., He H., Gong J., Calderwood S.K. (2004) Expression of a dominant negative heat shock factor-1 construct inhibits aneuploidy in prostate carcinoma cells. J Biol Chem 279 : 32651 32659.
    • (2004) J Biol Chem , vol.279 , pp. 32651-32659
    • Wang, Y.1    Theriault, J.R.2    He, H.3    Gong, J.4    Calderwood, S.K.5
  • 36
    • 13844269240 scopus 로고    scopus 로고
    • P21 stability: Linking chaperones to a cell cycle checkpoint
    • Liu G., Lozano G. (2005) p21 stability: linking chaperones to a cell cycle checkpoint. Cancer Cell 7 : 113 114.
    • (2005) Cancer Cell , vol.7 , pp. 113-114
    • Liu, G.1    Lozano, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.