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Volumn 8, Issue 7, 2003, Pages 307-315

Potential for proteasome inhibition in the treatment of cancer

Author keywords

[No Author keywords available]

Indexed keywords

7 ETHYL 10 HYDROXYCAMPTOTHECIN; ALDEHYDE DERIVATIVE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORONIC ACID DERIVATIVE; BORTEZOMIB; CEP 1612; CYCLOPHOSPHAMIDE; DACLIZUMAB; DOXORUBICIN; ETOPOSIDE; FLUOROURACIL; IRINOTECAN; LACTACYSTIN; PACLITAXEL; PROTEASOME; PROTEASOME INHIBITOR; UNCLASSIFIED DRUG;

EID: 0037376230     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6446(03)02647-3     Document Type: Review
Times cited : (235)

References (72)
  • 1
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • Kisselev A.F., Goldberg A.L. Proteasome inhibitors: from research tools to drug candidates. Chem. Biol. 8:2001;739-758.
    • (2001) Chem. Biol. , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 2
    • 0029556491 scopus 로고
    • Catalytic mechanism of the 20S proteasome of Thermoplasma acidophilum revealed by X-ray crystallography
    • Stock D., et al. Catalytic mechanism of the 20S proteasome of Thermoplasma acidophilum revealed by X-ray crystallography. Cold Spring Harb. Symp. Quant. Biol. 60:1995;525-532.
    • (1995) Cold Spring Harb. Symp. Quant. Biol. , vol.60 , pp. 525-532
    • Stock, D.1
  • 3
    • 0030854371 scopus 로고    scopus 로고
    • Ubiquitin-dependent destruction of topoisomerase I is stimulated by the antitumor drug camptothecin
    • Desai S.D., et al. Ubiquitin-dependent destruction of topoisomerase I is stimulated by the antitumor drug camptothecin. J. Biol. Chem. 272:1997;24159-24164.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24159-24164
    • Desai, S.D.1
  • 4
    • 0034193276 scopus 로고    scopus 로고
    • Proteasome inhibition circumvents solid tumor resistance to topoisomerase II-directed drugs
    • Ogiso Y., et al. Proteasome inhibition circumvents solid tumor resistance to topoisomerase II-directed drugs. Cancer Res. 60:2000;2429-2434.
    • (2000) Cancer Res. , vol.60 , pp. 2429-2434
    • Ogiso, Y.1
  • 5
    • 0033817518 scopus 로고    scopus 로고
    • Lack of multicellular drug resistance observed in human ovarian and prostate carcinoma treated with the proteasome inhibitor PS-341
    • Frankel A., et al. Lack of multicellular drug resistance observed in human ovarian and prostate carcinoma treated with the proteasome inhibitor PS-341. Clin. Cancer Res. 6:2000;3719-3728.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 3719-3728
    • Frankel, A.1
  • 6
    • 0343091329 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system and increased sensitivity of B-CLL lymphocytes to apoptotic death activation
    • Masdehors P., et al. Ubiquitin-proteasome system and increased sensitivity of B-CLL lymphocytes to apoptotic death activation. Leuk. Lymphoma. 38:2000;499-504.
    • (2000) Leuk. Lymphoma , vol.38 , pp. 499-504
    • Masdehors, P.1
  • 7
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
    • Pagano M., et al. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science. 269:1995;682-685.
    • (1995) Science , vol.269 , pp. 682-685
    • Pagano, M.1
  • 8
    • 12944283204 scopus 로고    scopus 로고
    • Increased proteasome degradation of cyclin-dependent kinase inhibitor p27 is associated with a decreased overall survival in mantle cell lymphoma
    • Chiarle R., et al. Increased proteasome degradation of cyclin-dependent kinase inhibitor p27 is associated with a decreased overall survival in mantle cell lymphoma. Blood. 95:2000;619-626.
    • (2000) Blood , vol.95 , pp. 619-626
    • Chiarle, R.1
  • 9
    • 17744375952 scopus 로고    scopus 로고
    • Androgen-driven prostate epithelial cell proliferation and differentiation in vivo involve the regulation of p27
    • Waltregny D., et al. Androgen-driven prostate epithelial cell proliferation and differentiation in vivo involve the regulation of p27. Mol. Endocrinol. 15:2001;765-782.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 765-782
    • Waltregny, D.1
  • 10
    • 0035328584 scopus 로고    scopus 로고
    • Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS-341: Implications for systemic nuclear factor-kappaB inhibition
    • Cusack J.C. Jr, et al. Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS-341: implications for systemic nuclear factor-kappaB inhibition. Cancer Res. 61:2001;3535-3540.
    • (2001) Cancer Res. , vol.61 , pp. 3535-3540
    • Cusack J.C. Jr1
  • 11
    • 0032429122 scopus 로고    scopus 로고
    • Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts
    • An B., et al. Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts. Cell Death Differ. 5:1998;1062-1075.
    • (1998) Cell Death Differ. , vol.5 , pp. 1062-1075
    • An, B.1
  • 12
    • 0033068154 scopus 로고    scopus 로고
    • The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro
    • Winston J.T., et al. The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro. Genes Dev. 13:1999;270-283.
    • (1999) Genes Dev. , vol.13 , pp. 270-283
    • Winston, J.T.1
  • 13
    • 0033083158 scopus 로고    scopus 로고
    • Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP
    • Spencer E., et al. Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP. Genes Dev. 13:1999;284-294.
    • (1999) Genes Dev. , vol.13 , pp. 284-294
    • Spencer, E.1
  • 14
    • 0028970734 scopus 로고
    • Stimulation-dependent I kappa B alpha phosphorylation marks the NF-kappa B inhibitor for degradation via the ubiquitin-proteasome pathway
    • Alkalay I., et al. Stimulation-dependent I kappa B alpha phosphorylation marks the NF-kappa B inhibitor for degradation via the ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. U. S. A. 92:1995;10599-10603.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 10599-10603
    • Alkalay, I.1
  • 15
    • 0030041147 scopus 로고    scopus 로고
    • Multiple myeloma cell adhesion-induced interleukin-6 expression in bone marrow stromal cells involves activation of NF-kappa B
    • Chauhan D., et al. Multiple myeloma cell adhesion-induced interleukin-6 expression in bone marrow stromal cells involves activation of NF-kappa B. Blood. 87:1996;1104-1112.
    • (1996) Blood , vol.87 , pp. 1104-1112
    • Chauhan, D.1
  • 16
    • 0036624741 scopus 로고    scopus 로고
    • Biologic sequelae of nuclear factor-kappaB blockade in multiple myeloma: Therapeutic applications
    • Mitsiades N., et al. Biologic sequelae of nuclear factor-kappaB blockade in multiple myeloma: therapeutic applications. Blood. 99:2002;4079-4086.
    • (2002) Blood , vol.99 , pp. 4079-4086
    • Mitsiades, N.1
  • 17
    • 0032588317 scopus 로고    scopus 로고
    • NF-kappaB induces expression of the Bcl-2 homologue A1/Bfl-1 to preferentially suppress chemotherapy-induced apoptosis
    • Wang C.Y., et al. NF-kappaB induces expression of the Bcl-2 homologue A1/Bfl-1 to preferentially suppress chemotherapy-induced apoptosis. Mol. Cell. Biol. 19:1999;5923-5929.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5923-5929
    • Wang, C.Y.1
  • 18
    • 0033621956 scopus 로고    scopus 로고
    • The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L)
    • Chen C., et al. The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L). Mol. Cell. Biol. 20:2000;2687-2695.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2687-2695
    • Chen, C.1
  • 19
    • 0033177897 scopus 로고    scopus 로고
    • NF-kappaB and chemoresistance: Potentiation of cancer drugs via inhibition of NF-kappaB
    • Cusack J.C., et al. NF-kappaB and chemoresistance: potentiation of cancer drugs via inhibition of NF-kappaB. Drug Resist. Updates. 2:1999;271-273.
    • (1999) Drug Resist. Updates , vol.2 , pp. 271-273
    • Cusack, J.C.1
  • 20
    • 0033565217 scopus 로고    scopus 로고
    • Expression of a dominant-negative mutant inhibitor-kappaBalpha of nuclear factor-kappaB in human head and neck squamous cell carcinoma inhibits survival, proinflammatory cytokine expression, and tumor growth in vivo
    • Duffey D.C., et al. Expression of a dominant-negative mutant inhibitor-kappaBalpha of nuclear factor-kappaB in human head and neck squamous cell carcinoma inhibits survival, proinflammatory cytokine expression, and tumor growth in vivo. Cancer Res. 59:1999;3468-3474.
    • (1999) Cancer Res. , vol.59 , pp. 3468-3474
    • Duffey, D.C.1
  • 21
    • 0035207110 scopus 로고    scopus 로고
    • The role of nuclear factor-kappaB in the biology and treatment of multiple myeloma
    • Berenson J.R., et al. The role of nuclear factor-kappaB in the biology and treatment of multiple myeloma. Semin. Oncol. 28:2001;626-633.
    • (2001) Semin. Oncol. , vol.28 , pp. 626-633
    • Berenson, J.R.1
  • 22
    • 0032905030 scopus 로고    scopus 로고
    • Control of inducible chemoresistance: Enhanced anti-tumor therapy through increased apoptosis by inhibition of NF-kappaB
    • Wang C.Y., et al. Control of inducible chemoresistance: enhanced anti-tumor therapy through increased apoptosis by inhibition of NF-kappaB. Nat. Med. 5:1999;412-417.
    • (1999) Nat. Med. , vol.5 , pp. 412-417
    • Wang, C.Y.1
  • 23
    • 0032539702 scopus 로고    scopus 로고
    • Potent and selective inhibitors of the proteasome: Dipeptidyl boronic acids
    • Adams J., et al. Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids. Bioorg. Med. Chem. Lett. 8:1998;333-338.
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 333-338
    • Adams, J.1
  • 24
    • 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., et al. Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res. 58:1998;4342-4348.
    • (1998) Cancer Res. , vol.58 , pp. 4342-4348
    • Orlowski, R.Z.1
  • 25
    • 0034237661 scopus 로고    scopus 로고
    • Apoptosis and radiosensitization of hodgkin cells by proteasome inhibition
    • Pajonk F., et al. Apoptosis and radiosensitization of hodgkin cells by proteasome inhibition. Int. J. Radiat. Oncol. Biol. Phys. 47:2000;1025-1032.
    • (2000) Int. J. Radiat. Oncol. Biol. Phys. , vol.47 , pp. 1025-1032
    • Pajonk, F.1
  • 26
    • 0035864344 scopus 로고    scopus 로고
    • Inhibition of NF-kappaB sensitizes human pancreatic carcinoma cells to apoptosis induced by etoposide (VP16) or doxorubicin
    • Arlt A., et al. Inhibition of NF-kappaB sensitizes human pancreatic carcinoma cells to apoptosis induced by etoposide (VP16) or doxorubicin. Oncogene. 20:2001;859-868.
    • (2001) Oncogene , vol.20 , pp. 859-868
    • Arlt, A.1
  • 27
    • 0035422206 scopus 로고    scopus 로고
    • Ubiquitin/26S proteasome-mediated degradation of topoisomerase I as a resistance mechanism to camptothecin in tumor cells
    • Desai S.D., et al. Ubiquitin/26S proteasome-mediated degradation of topoisomerase I as a resistance mechanism to camptothecin in tumor cells. Cancer Res. 61:2001;5926-5932.
    • (2001) Cancer Res. , vol.61 , pp. 5926-5932
    • Desai, S.D.1
  • 28
    • 0033802887 scopus 로고    scopus 로고
    • Synergistic cytotoxic interactions between sodium butyrate, MG132 and camptothecin in human retinoblastoma Y79 cells
    • Lauricella M., et al. Synergistic cytotoxic interactions between sodium butyrate, MG132 and camptothecin in human retinoblastoma Y79 cells. Tumour Biol. 21:2000;337-348.
    • (2000) Tumour Biol. , vol.21 , pp. 337-348
    • Lauricella, M.1
  • 29
    • 0033865860 scopus 로고    scopus 로고
    • Synergistic antitumor effects of a selective proteasome inhibitor and TNF in mice
    • Golab J., et al. Synergistic antitumor effects of a selective proteasome inhibitor and TNF in mice. Anticancer Res. 20:2000;1717-1721.
    • (2000) Anticancer Res. , vol.20 , pp. 1717-1721
    • Golab, J.1
  • 30
    • 0035866355 scopus 로고    scopus 로고
    • CEP1612, a dipeptidyl proteasome inhibitor, induces p21WAF1 and p27KIP1 expression and apoptosis and inhibits the growth of the human lung adenocarcinoma A-549 in nude mice
    • Sun J., et al. CEP1612, a dipeptidyl proteasome inhibitor, induces p21WAF1 and p27KIP1 expression and apoptosis and inhibits the growth of the human lung adenocarcinoma A-549 in nude mice. Cancer Res. 61:2001;1280-1284.
    • (2001) Cancer Res. , vol.61 , pp. 1280-1284
    • Sun, J.1
  • 31
    • 0031906567 scopus 로고    scopus 로고
    • The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-alpha-initiated apoptosis
    • Delic J., et al. The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-alpha-initiated apoptosis. Br. J. Cancer. 77:1998;1103-1107.
    • (1998) Br. J. Cancer , vol.77 , pp. 1103-1107
    • Delic, J.1
  • 32
    • 0035215010 scopus 로고    scopus 로고
    • Postischemic (6-Hour) treatment with recombinant human tissue plasminogen activator and proteasome inhibitor PS-519 reduces infarction in a rat model of embolic focal cerebral ischemia
    • Zhang L., et al. Postischemic (6-Hour) treatment with recombinant human tissue plasminogen activator and proteasome inhibitor PS-519 reduces infarction in a rat model of embolic focal cerebral ischemia. Stroke. 32:2001;2926-2931.
    • (2001) Stroke , vol.32 , pp. 2926-2931
    • Zhang, L.1
  • 33
    • 0033918122 scopus 로고    scopus 로고
    • Proteasome inhibitor PS519 reduces infarction and attenuates leukocyte infiltration in a rat model of focal cerebral ischemia
    • Phillips J.B., et al. Proteasome inhibitor PS519 reduces infarction and attenuates leukocyte infiltration in a rat model of focal cerebral ischemia. Stroke. 31:2000;1686-1693.
    • (2000) Stroke , vol.31 , pp. 1686-1693
    • Phillips, J.B.1
  • 34
    • 0036379624 scopus 로고    scopus 로고
    • Early clinical experience with the novel proteasome inhibitor PS-519
    • Shah I.M., et al. Early clinical experience with the novel proteasome inhibitor PS-519. Br. J. Clin. Pharmacol. 54:2002;269-276.
    • (2002) Br. J. Clin. Pharmacol. , vol.54 , pp. 269-276
    • Shah, I.M.1
  • 35
    • 0033152760 scopus 로고    scopus 로고
    • Proteasome inhibitors: A novel class of potent and effective antitumor agents
    • Adams J., et al. Proteasome inhibitors: a novel class of potent and effective antitumor agents. Cancer Res. 59:1999;2615-2622.
    • (1999) Cancer Res. , vol.59 , pp. 2615-2622
    • Adams, J.1
  • 36
    • 0032885416 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 in cancer therapy
    • Teicher B.A., et al. The proteasome inhibitor PS-341 in cancer therapy. Clin. Cancer Res. 5:1999;2638-2645.
    • (1999) Clin. Cancer Res. , vol.5 , pp. 2638-2645
    • Teicher, B.A.1
  • 37
    • 0034902354 scopus 로고    scopus 로고
    • Novel proteasome inhibitor PS-341 inhibits activation of nuclear factor-kappaB, cell survival, tumor growth, and angiogenesis in squamous cell carcinoma
    • Sunwoo J.B., et al. Novel proteasome inhibitor PS-341 inhibits activation of nuclear factor-kappaB, cell survival, tumor growth, and angiogenesis in squamous cell carcinoma. Clin. Cancer Res. 7:2001;1419-1428.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1419-1428
    • Sunwoo, J.B.1
  • 38
    • 0034788065 scopus 로고    scopus 로고
    • Molecular pathways that modify tumor radiation response
    • Pervan M., et al. Molecular pathways that modify tumor radiation response. Am. J. Clin. Oncol. 24:2001;481-485.
    • (2001) Am. J. Clin. Oncol. , vol.24 , pp. 481-485
    • Pervan, M.1
  • 39
    • 0035341494 scopus 로고    scopus 로고
    • Enhancement of radiosensitivity by proteasome inhibition: Implications for a role of NF-kB
    • Russo S.M., et al. Enhancement of radiosensitivity by proteasome inhibition: Implications for a role of NF-kB. Int. J. Radiat. Oncol. Biol. Phys. 50:2001;183-193.
    • (2001) Int. J. Radiat. Oncol. Biol. Phys. , vol.50 , pp. 183-193
    • Russo, S.M.1
  • 40
    • 0000640680 scopus 로고    scopus 로고
    • PS-341 enhances chemotherapeutic effect in human xenograft models
    • Abstract
    • Pink, M. et al. (2002) PS-341 enhances chemotherapeutic effect in human xenograft models, Proc. Am. Assoc. Cancer Res. 43, 158 (Abstract).
    • (2002) Proc. Am. Assoc. Cancer Res. , vol.43 , pp. 158
    • Pink, M.1
  • 41
    • 0012383819 scopus 로고    scopus 로고
    • Docetaxel followed by PS-341 results in phosphorylation and stabilization of p27 and increases response in non-small cell lung carcinoma (NSCLC)
    • Gumerlock P.H., et al. Docetaxel followed by PS-341 results in phosphorylation and stabilization of p27 and increases response in non-small cell lung carcinoma (NSCLC). Clin. Cancer Res. 7:2001;157.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 157
    • Gumerlock, P.H.1
  • 42
    • 0035300479 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells
    • Hideshima T., et al. The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res. 61:2001;3071-3076.
    • (2001) Cancer Res. , vol.61 , pp. 3071-3076
    • Hideshima, T.1
  • 43
    • 79960971274 scopus 로고    scopus 로고
    • Generation of PS-341-adapted human multiple myeloma cells as experimental tools for analysis of proteasome function in cancer
    • Abstract
    • Steiner, P. et al. (2001) Generation of PS-341-adapted human multiple myeloma cells as experimental tools for analysis of proteasome function in cancer. Blood 98, 310a (Abstract).
    • (2001) Blood , vol.98
    • Steiner, P.1
  • 44
    • 0036735298 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 inhibits human myeloma cell growth in vivo and prolongs survival in a murine model
    • LeBlanc R., et al. Proteasome inhibitor PS-341 inhibits human myeloma cell growth in vivo and prolongs survival in a murine model. Cancer Res. 62:2002;4996-5000.
    • (2002) Cancer Res. , vol.62 , pp. 4996-5000
    • LeBlanc, R.1
  • 45
    • 0036023407 scopus 로고    scopus 로고
    • A Phase I trial of the novel proteasome inhibitor PS341 in advanced solid tumor malignancies
    • Aghajanian C., et al. A Phase I trial of the novel proteasome inhibitor PS341 in advanced solid tumor malignancies. Clin. Cancer Res. 8:2002;2505-2511.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 2505-2511
    • Aghajanian, C.1
  • 46
    • 0000481441 scopus 로고    scopus 로고
    • Phase I study of the proteasome inhibitor bortezomib (PS-341, Velcade™) in combination with pegylated liposomal doxorubicin (Doxil®) in patients with refractory hematologic malignancies
    • Orlowski R.Z., et al. Phase I study of the proteasome inhibitor bortezomib (PS-341, Velcade™) in combination with pegylated liposomal doxorubicin (Doxil®) in patients with refractory hematologic malignancies. Blood. 100:2002;105a.
    • (2002) Blood , vol.100
    • Orlowski, R.Z.1
  • 47
    • 0001100607 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic Phase I study of PS-341 and gemcitabine in patients with advanced solid tumors
    • Ryan, D.P. et al. (2002) Pharmacokinetic and pharmacodynamic Phase I study of PS-341 and gemcitabine in patients with advanced solid tumors. Proc. Am. Soc. Clin. Oncol.38th Annual Meeting 21, 95a.
    • (2002) Proc. Am. Soc. Clin. Oncol. 38th Annual Meeting , vol.21
    • Ryan, D.P.1
  • 48
    • 0001100610 scopus 로고    scopus 로고
    • Phase I dose-escalation study of the proteasome inhibitor, PS-341, plus irinotecan in patients with advanced solid tumors
    • Clark, J.W. et al. (2002) Phase I dose-escalation study of the proteasome inhibitor, PS-341, plus irinotecan in patients with advanced solid tumors. Proc. Am. Soc. Clin. Oncol. 38th Annual Meeting 21, 93a.
    • (2002) Proc. Am. Soc. Clin. Oncol. 38th Annual Meeting , vol.21
    • Clark, J.W.1
  • 49
    • 0003305854 scopus 로고    scopus 로고
    • Dose-dependent inhibition of 20S proteasome results in serum IL-6 and PSA decline in patients (pts) with androgen-independent prostate cancer (AI PCa) treated with the proteasome inhibitor PS-341
    • Logothetis, C.J. et al. (2001) Dose-dependent inhibition of 20S proteasome results in serum IL-6 and PSA decline in patients (pts) with androgen-independent prostate cancer (AI PCa) treated with the proteasome inhibitor PS-341. Proc. Am. Soc. Clin. Oncol. 37th Annual Meeting 20, 186a.
    • (2001) Proc. Am. Soc. Clin. Oncol. 37th Annual Meeting , vol.20
    • Logothetis, C.J.1
  • 50
    • 0001343234 scopus 로고    scopus 로고
    • Phase I study of PS-341, a novel proteasome inhibitor, in patients with advanced malignancies
    • Papandreou, C.N. et al. (2000) Phase I study of PS-341, a novel proteasome inhibitor, in patients with advanced malignancies. Proc. Am. Soc. Clin. Oncol. 36th Annual Meeting 19, 190a.
    • (2000) Proc. Am. Soc. Clin. Oncol. 36th Annual Meeting , vol.19
    • Papandreou, C.N.1
  • 51
    • 0003208559 scopus 로고    scopus 로고
    • PS-341: Phase I study of a novel proteasome inhibitor with pharmacodynamic endpoints
    • Hamilton, A.L. et al. (2001) PS-341: Phase I study of a novel proteasome inhibitor with pharmacodynamic endpoints. Proc. Am. Soc. Clin. Oncol. 37th Annual Meeting 20, 85a.
    • (2001) Proc. Am. Soc. Clin. Oncol. 37th Annual Meeting , vol.20
    • Hamilton, A.L.1
  • 52
    • 0003230750 scopus 로고    scopus 로고
    • Phase II study of the proteasome inhibitor PS-341 in multiple myeloma patients (pts) with relapsed/refractory disease: results from cohort 1 analysis
    • Richardson, P.G. et al. (2002) Phase II study of the proteasome inhibitor PS-341 in multiple myeloma patients (pts) with relapsed/refractory disease: results from cohort 1 analysis. Proc. Am. Soc. Clin. Oncol. 38th Annual Meeting 21, 11a.
    • (2002) Proc. Am. Soc. Clin. Oncol. 38th Annual Meeting , vol.21
    • Richardson, P.G.1
  • 53
    • 0003320840 scopus 로고    scopus 로고
    • PS-341 is active in multiple myeloma: Preliminary report of a Phase I trial of the proteasome inhibitor PS-341 in patients with hematologic malignancies
    • Stinchcombe T.E., et al. PS-341 is active in multiple myeloma: Preliminary report of a Phase I trial of the proteasome inhibitor PS-341 in patients with hematologic malignancies. Blood. 96:2000;516a.
    • (2000) Blood , vol.96
    • Stinchcombe, T.E.1
  • 54
    • 0000481440 scopus 로고    scopus 로고
    • A Phase II multicenter study of the proteasome inhibitor bortezomib (Velcade™ formerly PS-341) in multiple myeloma patients (pts) with relapsed/refractory disease
    • Richardson P., et al. A Phase II multicenter study of the proteasome inhibitor bortezomib (Velcade™ formerly PS-341) in multiple myeloma patients (pts) with relapsed/refractory disease. Blood. 100:2002;104a.
    • (2002) Blood , vol.100
    • Richardson, P.1
  • 55
    • 0035798622 scopus 로고    scopus 로고
    • 26 S proteasome-mediated degradation of topoisomerase II cleavable complexes
    • Mao Y., et al. 26 S proteasome-mediated degradation of topoisomerase II cleavable complexes. J. Biol. Chem. 276:2001;40652-40658.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40652-40658
    • Mao, Y.1
  • 56
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • Yang Y., et al. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science. 288:2000;874-877.
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1
  • 57
    • 0034635952 scopus 로고    scopus 로고
    • Bax degradation by the ubiquitin/proteasome-dependent pathway: Involvement in tumor survival and progression
    • Li B., Dou Q.P. Bax degradation by the ubiquitin/proteasome-dependent pathway: involvement in tumor survival and progression. Proc. Natl. Acad. Sci. U. S. A. 97:2000;3850-3855.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3850-3855
    • Li, B.1    Dou, Q.P.2
  • 58
    • 0033533499 scopus 로고    scopus 로고
    • Phosphorylation and proteasome-dependent degradation of Bcl-2 in mitotic-arrested cells after microtubule damage
    • Chadebech P., et al. Phosphorylation and proteasome-dependent degradation of Bcl-2 in mitotic-arrested cells after microtubule damage. Biochem. Biophys. Res. Commun. 262:1999;823-827.
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 823-827
    • Chadebech, P.1
  • 59
    • 0033833068 scopus 로고    scopus 로고
    • Pyk2 and FAK differentially regulate progression of the cell cycle
    • Zhao J., et al. Pyk2 and FAK differentially regulate progression of the cell cycle. J. Cell Sci. 113:2000;3063-3072.
    • (2000) J. Cell Sci. , vol.113 , pp. 3063-3072
    • Zhao, J.1
  • 60
    • 0034597619 scopus 로고    scopus 로고
    • Cut8, essential for anaphase, controls localization of 26S proteasome, facilitating destruction of cyclin and Cut2
    • Tatebe H., Yanagida M. Cut8, essential for anaphase, controls localization of 26S proteasome, facilitating destruction of cyclin and Cut2. Curr. Biol. 10:2000;1329-1338.
    • (2000) Curr. Biol. , vol.10 , pp. 1329-1338
    • Tatebe, H.1    Yanagida, M.2
  • 61
    • 0029957947 scopus 로고    scopus 로고
    • Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation
    • Clurman B.E., et al. Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation. Genes Dev. 10:1996;1979-1990.
    • (1996) Genes Dev. , vol.10 , pp. 1979-1990
    • Clurman, B.E.1
  • 62
    • 0032511893 scopus 로고    scopus 로고
    • Interaction with cyclin-dependent kinases and PCNA modulates proteasome-dependent degradation of p21
    • Cayrol C., Ducommun B. Interaction with cyclin-dependent kinases and PCNA modulates proteasome-dependent degradation of p21. Oncogene. 17:1998;2437-2444.
    • (1998) Oncogene , vol.17 , pp. 2437-2444
    • Cayrol, C.1    Ducommun, B.2
  • 63
    • 0030810984 scopus 로고    scopus 로고
    • The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin
    • Segnitz B., Gehring U. The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin. J. Biol. Chem. 272:1997;18694-18701.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18694-18701
    • Segnitz, B.1    Gehring, U.2
  • 64
    • 0033551374 scopus 로고    scopus 로고
    • MYC oncogenes and human neoplastic disease
    • Nesbit C.E., et al. MYC oncogenes and human neoplastic disease. Oncogene. 18:1999;3004-3016.
    • (1999) Oncogene , vol.18 , pp. 3004-3016
    • Nesbit, C.E.1
  • 65
    • 0032787671 scopus 로고    scopus 로고
    • Degradation of Id proteins by the ubiquitin-proteasome pathway
    • Bounpheng M.A., et al. Degradation of Id proteins by the ubiquitin-proteasome pathway. FASEB J. 13:1999;2257-2264.
    • (1999) FASEB J. , vol.13 , pp. 2257-2264
    • Bounpheng, M.A.1
  • 66
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF- kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella V.J., et al. The ubiquitin-proteasome pathway is required for processing the NF- kappa B1 precursor protein and the activation of NF-kappa B. Cell. 78:1994;773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1
  • 67
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53(1)
    • Maki C.G., et al. In vivo ubiquitination and proteasome-mediated degradation of p53(1). Cancer Res. 56:1996;2649-2654.
    • (1996) Cancer Res. , vol.56 , pp. 2649-2654
    • Maki, C.G.1
  • 68
    • 0029834371 scopus 로고    scopus 로고
    • E7 protein of human papilloma virus-16 induces degradation of retinoblastoma protein through the ubiquitin-proteasome pathway
    • Boyer S.N., et al. E7 protein of human papilloma virus-16 induces degradation of retinoblastoma protein through the ubiquitin-proteasome pathway. Cancer Res. 56:1996;4620-4624.
    • (1996) Cancer Res. , vol.56 , pp. 4620-4624
    • Boyer, S.N.1
  • 69
    • 0034875305 scopus 로고    scopus 로고
    • Chemosensitization of pancreatic cancer by inhibition of the 26S proteasome
    • Bold R.J., et al. Chemosensitization of pancreatic cancer by inhibition of the 26S proteasome. J. Surg. Res. 100:2001;11-17.
    • (2001) J. Surg. Res. , vol.100 , pp. 11-17
    • Bold, R.J.1
  • 70
    • 0003346451 scopus 로고    scopus 로고
    • Antitumor activity of the proteasome inhibitor PS-341 in mantle cell lymphoma B cells
    • Abstract
    • Pham L., et al. Antitumor activity of the proteasome inhibitor PS-341 in mantle cell lymphoma B cells. Blood. 98:2001;465a. Abstract.
    • (2001) Blood , vol.98
    • Pham, L.1
  • 71
    • 0034981649 scopus 로고    scopus 로고
    • 26S proteasome inhibition induces apoptosis and limits growth of human pancreatic cancer
    • Shah S.A., et al. 26S proteasome inhibition induces apoptosis and limits growth of human pancreatic cancer. J. Cell. Biochem. 82:2001;110-122.
    • (2001) J. Cell. Biochem. , vol.82 , pp. 110-122
    • Shah, S.A.1
  • 72
    • 0036172154 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341, a potential therapeutic agent for adult T- cell leukemia
    • Tan C., Waldmann T.A. Proteasome inhibitor PS-341, a potential therapeutic agent for adult T- cell leukemia. Cancer Res. 62:2002;1083-1086.
    • (2002) Cancer Res. , vol.62 , pp. 1083-1086
    • Tan, C.1    Waldmann, T.A.2


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