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Volumn 59, Issue 12, 1999, Pages 2798-2801

Eponemycin exerts its antitumor effect through the inhibition of proteasome function

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; DIHYDROEPONEMYCIN; EPONEMYCIN; PROTEASOME; UNCLASSIFIED DRUG;

EID: 0033564512     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (146)

References (23)
  • 1
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt, W., and Wolf, D. H. Proteasomes: destruction as a programme. Trends Biochem. Sci., 21: 96-102, 1996.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 2
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class 1-restricted antigen processing
    • Pamer, E., and Cresswell, P. Mechanisms of MHC class 1-restricted antigen processing. Annu. Rev. Immunol., 16: 323-358, 1998.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 3
    • 0029591482 scopus 로고
    • The genetics of proteasomes and antigen processing
    • Monaco, J. J., and Nandi, D. The genetics of proteasomes and antigen processing. Annu. Rev. Genet., 29: 729-754, 1995.
    • (1995) Annu. Rev. Genet. , vol.29 , pp. 729-754
    • Monaco, J.J.1    Nandi, D.2
  • 4
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella, V. J., Rando, O. J., Goldberg, A. L., and Maniatis, T. The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell, 78: 773-785, 1994.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 5
    • 0029807944 scopus 로고    scopus 로고
    • How proteolysis drives the cell cycle
    • Washington DC
    • King, R. W., Deshaies, R. J., Peters, J. M., and Kirschner, M. W. How proteolysis drives the cell cycle. Science (Washington DC), 274: 1652-1659, 1996.
    • (1996) Science , vol.274 , pp. 1652-1659
    • King, R.W.1    Deshaies, R.J.2    Peters, J.M.3    Kirschner, M.W.4
  • 6
    • 0031021991 scopus 로고    scopus 로고
    • The ubiquitin-mediated proteolytic pathway as a therapeutic area
    • Rolfe, M., Chiu, M. I., and Pagano, M. The ubiquitin-mediated proteolytic pathway as a therapeutic area. J. Mol. Med., 75: 5-17, 1997.
    • (1997) J. Mol. Med. , vol.75 , pp. 5-17
    • Rolfe, M.1    Chiu, M.I.2    Pagano, M.3
  • 7
    • 0031973765 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in cancer
    • Spataro, V., Norbury, C., and Harris, A. L. The ubiquitin-proteasome pathway in cancer. Br. J. Cancer, 77: 448-455, 1998.
    • (1998) Br. J. Cancer , vol.77 , pp. 448-455
    • Spataro, V.1    Norbury, C.2    Harris, A.L.3
  • 8
    • 0031660899 scopus 로고    scopus 로고
    • Eponemycin analogs: Synthesis and use as probes of angiogenesis
    • Sin, N., Meng, L., Auth, H., and Crews, C. M. Eponemycin analogs: synthesis and use as probes of angiogenesis. Bioorg. Med. Chem., 6: 1209-1217, 1998.
    • (1998) Bioorg. Med. Chem. , vol.6 , pp. 1209-1217
    • Sin, N.1    Meng, L.2    Auth, H.3    Crews, C.M.4
  • 9
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Washington DC
    • Fenteany, G., Standaert, R. F., Lane, W. S., Choi, S., Corey, E. J., and Schreiber, S. L. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science (Washington DC), 268: 726-731, 1995.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 10
    • 0025015309 scopus 로고
    • Eponemycin, a new antibiotic active against B16 melanoma. I. Production, isolation, structure and biological activity
    • Tokyo
    • Sugawara, K., Hatori, M., Nishiyama, Y., Tomita, K., Kamei, H., Konishi, M., and Oki, T. Eponemycin, a new antibiotic active against B16 melanoma. I. Production, isolation, structure and biological activity. J. Antibiot. (Tokyo), 43: 8-18, 1990.
    • (1990) J. Antibiot. , vol.43 , pp. 8-18
    • Sugawara, K.1    Hatori, M.2    Nishiyama, Y.3    Tomita, K.4    Kamei, H.5    Konishi, M.6    Oki, T.7
  • 12
    • 0026595367 scopus 로고
    • Alternative exon usage and processing of the major hislocompatibility complex-encoded proteasome subunits
    • Früh, K., Yang, Y., Arnold, D., Chambers, J., Wu, L., Waters, J. B., Spies, T., and Peterson, P. A. Alternative exon usage and processing of the major hislocompatibility complex-encoded proteasome subunits. J. Biol. Chem., 267: 22131-22140, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22131-22140
    • Früh, K.1    Yang, Y.2    Arnold, D.3    Chambers, J.4    Wu, L.5    Waters, J.B.6    Spies, T.7    Peterson, P.A.8
  • 13
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee, D. H., and Goldberg, A. L. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol., 8: 397-403, 1998.
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 14
    • 0032502719 scopus 로고    scopus 로고
    • Lactacystin, proteasome function, and cell fate
    • Fenteany, G., and Schreiber, S. L. Lactacystin, proteasome function, and cell fate. J. Biol. Chem., 273: 8545-8548, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8545-8548
    • Fenteany, G.1    Schreiber, S.L.2
  • 15
    • 0029937677 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of the proteasome by lactacystin: A central role for clasto-lactacystin β-lactone
    • Dick, L. R., Cruikshank, A. A., Grenier, L., Melandri, F. D., Nunes, S. L., and Stein, R. L. Mechanistic studies on the inactivation of the proteasome by lactacystin: a central role for clasto-lactacystin β-lactone. J. Biol. Chem., 271: 7273-7276, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7273-7276
    • Dick, L.R.1    Cruikshank, A.A.2    Grenier, L.3    Melandri, F.D.4    Nunes, S.L.5    Stein, R.L.6
  • 16
    • 0027214605 scopus 로고
    • Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • Lond.
    • Gaczynska, M., Rock, K. L., and Goldberg, A. L. Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature (Lond.), 365: 264-267, 1993.
    • (1993) Nature , vol.365 , pp. 264-267
    • Gaczynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 17
    • 0030012069 scopus 로고    scopus 로고
    • Design and synthesis of novel protease inhibitors. Tripeptide α′,β′-epoxyketones as nanomolar inactivators of the proteasome
    • Spaltenstein, A., Leban, J. J., Huang, J. J., Reinhardt, K. R., Viveros, O. H., Sigafoos, J., and Crouch, R. Design and synthesis of novel protease inhibitors. Tripeptide α′,β′-epoxyketones as nanomolar inactivators of the proteasome. Tetrahedron Lett., 37: 1343-1346, 1996.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 1343-1346
    • Spaltenstein, A.1    Leban, J.J.2    Huang, J.J.3    Reinhardt, K.R.4    Viveros, O.H.5    Sigafoos, J.6    Crouch, R.7
  • 18
    • 0030294381 scopus 로고    scopus 로고
    • Specific inhibition of the chymotrypsin-like activity of the proteasome induces a bipolar morphology in neuroblastoma cells
    • Fenteany, G., and Schreiber, S. L. Specific inhibition of the chymotrypsin-like activity of the proteasome induces a bipolar morphology in neuroblastoma cells. Chem. Biol., 3: 905-912, 1996.
    • (1996) Chem. Biol. , vol.3 , pp. 905-912
    • Fenteany, G.1    Schreiber, S.L.2
  • 20
    • 0030869925 scopus 로고    scopus 로고
    • Apoptosis of Ewing's sarcoma cells is accompanied by accumulation of ubiquitinated proteins
    • Soldatenkov, V. A., and Dritschilo, A. Apoptosis of Ewing's sarcoma cells is accompanied by accumulation of ubiquitinated proteins. Cancer Res., 57: 3881-3885, 1997.
    • (1997) Cancer Res. , vol.57 , pp. 3881-3885
    • Soldatenkov, V.A.1    Dritschilo, A.2
  • 22
    • 0031906567 scopus 로고    scopus 로고
    • The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-α-initiated apoptosis
    • Delic, J., Masdehors, P., Omura, S., Cosset, J. M., Dumont, J., Binet, J. L., and Magdelenat, H. The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-α-initiated apoptosis. Br. J. Cancer, 77: 1103-1107, 1998.
    • (1998) Br. J. Cancer , vol.77 , pp. 1103-1107
    • Delic, J.1    Masdehors, P.2    Omura, S.3    Cosset, J.M.4    Dumont, J.5    Binet, J.L.6    Magdelenat, H.7
  • 23
    • 0032189685 scopus 로고    scopus 로고
    • Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor
    • Orlowski, R. Z., Eswara, J. R., Lafond-Walker, A., Grever, M. R., Orlowski, M., and Dang, C. V. Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res., 58: 4342-4348, 1998.
    • (1998) Cancer Res. , vol.58 , pp. 4342-4348
    • Orlowski, R.Z.1    Eswara, J.R.2    Lafond-Walker, A.3    Grever, M.R.4    Orlowski, M.5    Dang, C.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.