메뉴 건너뛰기




Volumn 4 S, Issue 1, 2012, Pages 375-391

New applications of old metal-binding drugs in the treatment of human cancer

Author keywords

Chymotrypsin like activity; Clioquinol; Copper; Disulfiram; Dithiocarbamates; Proteasome inhibitor; Review; Ubiquitin proteasome pathway; Zinc

Indexed keywords

8 QUINOLINOL DERIVATIVE; ANTINEOPLASTIC METAL COMPLEX; BORTEZOMIB; CARBOPLATIN; CISPLATIN; CLIOQUINOL; COPPER; COPPER DERIVATIVE; CYANOCOBALAMIN; DIETHYLDITHIOCARBAMIC ACID; DISULFIRAM; DITHIOCARBAMIC ACID DERIVATIVE; GLUCONATE COPPER; GOLD DERIVATIVE; INDAZOLIUM TETRACHLOROBIS(INDAZOLE)RUTHENATE; NAMI A; OXALIPLATIN; PROTEASOME; PYRROLIDINEDITHIOCARBAMIC ACID; RUTHENIUM DERIVATIVE; UBIQUITIN; UNCLASSIFIED DRUG; ZINC; ZINC DERIVATIVE; ANTINEOPLASTIC AGENT; CHELATING AGENT; COORDINATION COMPOUND;

EID: 84869482208     PISSN: 19450516     EISSN: 19450524     Source Type: Journal    
DOI: 10.2741/274     Document Type: Article
Times cited : (40)

References (139)
  • 1
    • 24644486532 scopus 로고    scopus 로고
    • Current status of platinum-based antitumor drugs
    • E. Wong and C. M. Giandomenico: Current status of platinum-based antitumor drugs. Chem Rev, 99(9), 2451-66 (1999)
    • (1999) Chem Rev , vol.99 , Issue.9 , pp. 2451-2466
    • Wong, E.1    Giandomenico, C.M.2
  • 2
    • 0036080202 scopus 로고    scopus 로고
    • Recent progress in the development of anticancer agents
    • S. Eckhardt: Recent progress in the development of anticancer agents. Curr Med Chem Anticancer Agents, 2(3), 419-39 (2002)
    • (2002) Curr Med Chem Anticancer Agents , vol.2 , Issue.3 , pp. 419-439
    • Eckhardt, S.1
  • 3
    • 0027218815 scopus 로고
    • Metal compounds in therapy and diagnosis
    • M. J. Abrams and B. A. Murrer: Metal compounds in therapy and diagnosis. Science, 261(5122), 725-30 (1993)
    • (1993) Science , vol.261 , Issue.5122 , pp. 725-730
    • Abrams, M.J.1    Murrer, B.A.2
  • 4
    • 0141811013 scopus 로고    scopus 로고
    • Recent developments in the field of tumorinhibiting metal complexes
    • M. Galanski, V. B. Arion, M. A. Jakupec and B. K. Keppler: Recent developments in the field of tumorinhibiting metal complexes. Curr Pharm Des, 9(25), 2078- 89 (2003)
    • (2003) Curr Pharm des , vol.9 , Issue.25 , pp. 2078-2089
    • Galanski, M.1    Arion, V.B.2    Jakupec, M.A.3    Keppler, B.K.4
  • 5
    • 23244459221 scopus 로고    scopus 로고
    • Update of the preclinical situation of anticancer platinum complexes: Novel design strategies and innovative analytical approaches
    • M. Galanski, M. A. Jakupec and B. K. Keppler: Update of the preclinical situation of anticancer platinum complexes: novel design strategies and innovative analytical approaches. Curr Med Chem, 12(18), 2075-94 (2005)
    • (2005) Curr Med Chem , vol.12 , Issue.18 , pp. 2075-2094
    • Galanski, M.1    Jakupec, M.A.2    Keppler, B.K.3
  • 6
    • 67349260256 scopus 로고    scopus 로고
    • Organometallic compounds in oncology: Implications of novel organotins as antitumor agents
    • A. Alama, B. Tasso, F. Novelli and F. Sparatore: Organometallic compounds in oncology: implications of novel organotins as antitumor agents. Drug Discov Today, 14(9-10), 500-8 (2009)
    • (2009) Drug Discov Today , vol.14 , Issue.9-10 , pp. 500-508
    • Alama, A.1    Tasso, B.2    Novelli, F.3    Sparatore, F.4
  • 7
    • 0022337278 scopus 로고
    • Preclinical studies identifying carboplatin as a viable cisplatin alternative
    • K. R. Harrap: Preclinical studies identifying carboplatin as a viable cisplatin alternative. Cancer Treat Rev, 12 Suppl A, 21-33 (1985)
    • (1985) Cancer Treat Rev , vol.12 , Issue.SUPPL. A , pp. 21-33
    • Harrap, K.R.1
  • 9
    • 0031962945 scopus 로고    scopus 로고
    • Cytotoxic effects of gold(III) complexes on established human tumor cell lines sensitive and resistant to cisplatin
    • P. Calamai, S. Carotti, A. Guerri, T. Mazzei, L. Messori, E. Mini, P. Orioli and G. P. Speroni: Cytotoxic effects of gold(III) complexes on established human tumor cell lines sensitive and resistant to cisplatin. Anticancer Drug Des, 13(1), 67-80 (1998)
    • (1998) Anticancer Drug des , vol.13 , Issue.1 , pp. 67-80
    • Calamai, P.1    Carotti, S.2    Guerri, A.3    Mazzei, T.4    Messori, L.5    Mini, E.6    Orioli, P.7    Speroni, G.P.8
  • 10
    • 0021248450 scopus 로고
    • Antineoplastic activity and toxicity of an organometallic complex of ruthenium(II) in comparison with cis-PDD in mice bearing solid malignant neoplasms
    • G. Sava, S. Zorzet, T. Giraldi, G. Mestroni and G. Zassinovich: Antineoplastic activity and toxicity of an organometallic complex of ruthenium(II) in comparison with cis-PDD in mice bearing solid malignant neoplasms. Eur J Cancer Clin Oncol, 20(6), 841-7 (1984)
    • (1984) Eur J Cancer Clin Oncol , vol.20 , Issue.6 , pp. 841-847
    • Sava, G.1    Zorzet, S.2    Giraldi, T.3    Mestroni, G.4    Zassinovich, G.5
  • 11
    • 33645277617 scopus 로고    scopus 로고
    • Redox behavior of tumor-inhibiting ruthenium(III) complexes and effects of physiological reductants on their binding to GMP
    • P. Schluga, C. G. Hartinger, A. Egger, E. Reisner, M. Galanski, M. A. Jakupec and B. K. Keppler: Redox behavior of tumor-inhibiting ruthenium(III) complexes and effects of physiological reductants on their binding to GMP. Dalton Trans(14), 1796-802 (2006)
    • (2006) Dalton Trans , vol.14 , pp. 1796-1802
    • Schluga, P.1    Hartinger, C.G.2    Egger, A.3    Reisner, E.4    Galanski, M.5    Jakupec, M.A.6    Keppler, B.K.7
  • 12
    • 59049102354 scopus 로고    scopus 로고
    • Modulation of the metastatic progression of breast cancer with an organometallic ruthenium compound
    • A. Bergamo, A. Masi, P. J. Dyson and G. Sava: Modulation of the metastatic progression of breast cancer with an organometallic ruthenium compound. Int J Oncol, 33(6), 1281-9 (2008)
    • (2008) Int J Oncol , vol.33 , Issue.6 , pp. 1281-1289
    • Bergamo, A.1    Masi, A.2    Dyson, P.J.3    Sava, G.4
  • 15
    • 0026612437 scopus 로고
    • Na[trans-RuCl4(DMSO)Im], a metal complex of ruthenium with antimetastatic properties
    • G. Sava, S. Pacor, G. Mestroni and E. Alessio: Na[trans-RuCl4(DMSO)Im], a metal complex of ruthenium with antimetastatic properties. Clin Exp Metastasis, 10(4), 273-80 (1992)
    • (1992) Clin Exp Metastasis , vol.10 , Issue.4 , pp. 273-280
    • Sava, G.1    Pacor, S.2    Mestroni, G.3    Alessio, E.4
  • 16
    • 0028872614 scopus 로고
    • Effects of ruthenium complexes on experimental tumors: Irrelevance of cytotoxicity for metastasis inhibition
    • G. Sava, S. Pacor, A. Bergamo, M. Cocchietto, G. Mestroni and E. Alessio: Effects of ruthenium complexes on experimental tumors: irrelevance of cytotoxicity for metastasis inhibition. Chem Biol Interact, 95(1-2), 109-26 (1995)
    • (1995) Chem Biol Interact , vol.95 , Issue.1-2 , pp. 109-126
    • Sava, G.1    Pacor, S.2    Bergamo, A.3    Cocchietto, M.4    Mestroni, G.5    Alessio, E.6
  • 20
    • 0034771648 scopus 로고    scopus 로고
    • Analysis of serum copper and zinc concentrations in cancer patients
    • M. Zowczak, M. Iskra, L. Torlinski and S. Cofta: Analysis of serum copper and zinc concentrations in cancer patients. Biol Trace Elem Res, 82(1-3), 1-8 (2001)
    • (2001) Biol Trace Elem Res , vol.82 , Issue.1-3 , pp. 1-8
    • Zowczak, M.1    Iskra, M.2    Torlinski, L.3    Cofta, S.4
  • 21
    • 0021358988 scopus 로고
    • Serum ceruloplasmin and copper levels in patients with primary brain tumors
    • L. Turecky, P. Kalina, E. Uhlikova, S. Namerova and J. Krizko: Serum ceruloplasmin and copper levels in patients with primary brain tumors. Klin Wochenschr, 62(4), 187-9 (1984)
    • (1984) Klin Wochenschr , vol.62 , Issue.4 , pp. 187-189
    • Turecky, L.1    Kalina, P.2    Uhlikova, E.3    Namerova, S.4    Krizko, J.5
  • 22
    • 0036800770 scopus 로고    scopus 로고
    • Serum and tissue trace elements in patients with breast cancer in Taiwan
    • H. W. Kuo, S. F. Chen, C. C. Wu, D. R. Chen and J. H. Lee: Serum and tissue trace elements in patients with breast cancer in Taiwan. Biol Trace Elem Res, 89(1), 1-11 (2002)
    • (2002) Biol Trace Elem Res , vol.89 , Issue.1 , pp. 1-11
    • Kuo, H.W.1    Chen, S.F.2    Wu, C.C.3    Chen, D.R.4    Lee, J.H.5
  • 23
    • 0021720704 scopus 로고
    • Comparison between concentrations of trace elements in normal and neoplastic human breast tissue
    • S. L. Rizk and H. H. Sky-Peck: Comparison between concentrations of trace elements in normal and neoplastic human breast tissue. Cancer Res, 44(11), 5390-4 (1984)
    • (1984) Cancer Res , vol.44 , Issue.11 , pp. 5390-5394
    • Rizk, S.L.1    Sky-Peck, H.H.2
  • 24
    • 0037222751 scopus 로고    scopus 로고
    • Copper and ceruloplasmin status in serum of prostate and colon cancer patients
    • S. B. Nayak, V. R. Bhat, D. Upadhyay and S. L. Udupa: Copper and ceruloplasmin status in serum of prostate and colon cancer patients. Indian J Physiol Pharmacol, 47(1), 108-10 (2003)
    • (2003) Indian J Physiol Pharmacol , vol.47 , Issue.1 , pp. 108-110
    • Nayak, S.B.1    Bhat, V.R.2    Upadhyay, D.3    Udupa, S.L.4
  • 26
    • 0018817726 scopus 로고
    • The zinc and copper content of blood leucocytes and plasma from patients with benign and malignant prostates
    • F. K. Habib, T. C. Dembinski and S. R. Stitch: The zinc and copper content of blood leucocytes and plasma from patients with benign and malignant prostates. Clin Chim Acta, 104(3), 329-35 (1980)
    • (1980) Clin Chim Acta , vol.104 , Issue.3 , pp. 329-335
    • Habib, F.K.1    Dembinski, T.C.2    Stitch, S.R.3
  • 27
    • 0019202882 scopus 로고
    • Endothelial cell phagokinesis in response to specific metal ions
    • B. R. McAuslan and W. Reilly: Endothelial cell phagokinesis in response to specific metal ions. Exp Cell Res, 130(1), 147-57 (1980)
    • (1980) Exp Cell Res , vol.130 , Issue.1 , pp. 147-157
    • McAuslan, B.R.1    Reilly, W.2
  • 28
    • 0022689931 scopus 로고
    • Considerations on the mechanism of the angiogenic response
    • P. M. Gullino: Considerations on the mechanism of the angiogenic response. Anticancer Res, 6(2), 153-8 (1986)
    • (1986) Anticancer Res , vol.6 , Issue.2 , pp. 153-158
    • Gullino, P.M.1
  • 29
    • 0032104855 scopus 로고    scopus 로고
    • Copper stimulates proliferation of human endothelial cells under culture
    • G. F. Hu: Copper stimulates proliferation of human endothelial cells under culture. J Cell Biochem, 69(3), 326- 35 (1998)
    • (1998) J Cell Biochem , vol.69 , Issue.3 , pp. 326-335
    • Hu, G.F.1
  • 30
    • 34248136112 scopus 로고    scopus 로고
    • Vascular endothelial growth factor and vascular endothelial growth factor receptor inhibitors as anti-angiogenic agents in cancer therapy
    • A. Veeravagu, A. R. Hsu, W. Cai, L. C. Hou, V. C. Tse and X. Chen: Vascular endothelial growth factor and vascular endothelial growth factor receptor inhibitors as anti-angiogenic agents in cancer therapy. Recent Pat Anticancer Drug Discov, 2(1), 59-71 (2007)
    • (2007) Recent Pat Anticancer Drug Discov , vol.2 , Issue.1 , pp. 59-71
    • Veeravagu, A.1    Hsu, A.R.2    Cai, W.3    Hou, L.C.4    Tse, V.C.5    Chen, X.6
  • 33
    • 4644362728 scopus 로고    scopus 로고
    • Role of copper in tumour angiogenesis - Clinical implications
    • A. Nasulewicz, A. Mazur and A. Opolski: Role of copper in tumour angiogenesis-clinical implications. J Trace Elem Med Biol, 18(1), 1-8 (2004)
    • (2004) J Trace Elem Med Biol , vol.18 , Issue.1 , pp. 1-8
    • Nasulewicz, A.1    Mazur, A.2    Opolski, A.3
  • 34
    • 0037058676 scopus 로고    scopus 로고
    • The copper chelator trientine has an antiangiogenic effect against hepatocellular carcinoma, possibly through inhibition of interleukin-8 production
    • M. Moriguchi, T. Nakajima, H. Kimura, T. Watanabe, H. Takashima, Y. Mitsumoto, T. Katagishi, T. Okanoue and K. Kagawa: The copper chelator trientine has an antiangiogenic effect against hepatocellular carcinoma, possibly through inhibition of interleukin-8 production. Int J Cancer, 102(5), 445-52 (2002)
    • (2002) Int J Cancer , vol.102 , Issue.5 , pp. 445-452
    • Moriguchi, M.1    Nakajima, T.2    Kimura, H.3    Watanabe, T.4    Takashima, H.5    Mitsumoto, Y.6    Katagishi, T.7    Okanoue, T.8    Kagawa, K.9
  • 35
    • 0032756159 scopus 로고    scopus 로고
    • Angiogenesis and cancer control: From concept to therapeutic trial
    • S. Brem: Angiogenesis and Cancer Control: From Concept to Therapeutic Trial. Cancer Control, 6(5), 436- 458 (1999)
    • (1999) Cancer Control , vol.6 , Issue.5 , pp. 436-458
    • Brem, S.1
  • 36
    • 0034937998 scopus 로고    scopus 로고
    • Copper control as an antiangiogenic anticancer therapy: Lessons from treating Wilson's disease
    • G. J. Brewer: Copper control as an antiangiogenic anticancer therapy: lessons from treating Wilson's disease. Exp Biol Med (Maywood), 226(7), 665-73 (2001)
    • (2001) Exp Biol Med (Maywood) , vol.226 , Issue.7 , pp. 665-673
    • Brewer, G.J.1
  • 37
    • 33747499821 scopus 로고    scopus 로고
    • The role of copper in tumour angiogenesis
    • S. A. Lowndes and A. L. Harris: The role of copper in tumour angiogenesis. J Mammary Gland Biol Neoplasia, 10(4), 299-310 (2005)
    • (2005) J Mammary Gland Biol Neoplasia , vol.10 , Issue.4 , pp. 299-310
    • Lowndes, S.A.1    Harris, A.L.2
  • 39
    • 85013312416 scopus 로고
    • Tumor angiogenesis: Therapeutic implications
    • J. Folkman: Tumor angiogenesis: therapeutic implications. N Engl J Med, 285(21), 1182-6 (1971)
    • (1971) N Engl J Med , vol.285 , Issue.21 , pp. 1182-1186
    • Folkman, J.1
  • 40
    • 0015311426 scopus 로고
    • Anti-angiogenesis: New concept for therapy of solid tumors
    • J. Folkman: Anti-angiogenesis: new concept for therapy of solid tumors. Ann Surg, 175(3), 409-16 (1972)
    • (1972) Ann Surg , vol.175 , Issue.3 , pp. 409-416
    • Folkman, J.1
  • 43
    • 33645991187 scopus 로고    scopus 로고
    • Zinc at pharmacologic concentrations affects cytokine expression and induces apoptosis of human peripheral blood mononuclear cells
    • K. L. Chang, T. C. Hung, B. S. Hsieh, Y. H. Chen, T. F. Chen and H. L. Cheng: Zinc at pharmacologic concentrations affects cytokine expression and induces apoptosis of human peripheral blood mononuclear cells. Nutrition, 22(5), 465-74 (2006)
    • (2006) Nutrition , vol.22 , Issue.5 , pp. 465-474
    • Chang, K.L.1    Hung, T.C.2    Hsieh, B.S.3    Chen, Y.H.4    Chen, T.F.5    Cheng, H.L.6
  • 44
    • 65349136466 scopus 로고    scopus 로고
    • The important role of the apoptotic effects of zinc in the development of cancers
    • R. B. Franklin and L. C. Costello: The important role of the apoptotic effects of zinc in the development of cancers. J Cell Biochem, 106(5), 750-7 (2009)
    • (2009) J Cell Biochem , vol.106 , Issue.5 , pp. 750-757
    • Franklin, R.B.1    Costello, L.C.2
  • 45
    • 0028819948 scopus 로고
    • Dosedependent opposite effect of zinc on apoptosis in mouse thymocytes
    • M. Provinciali, G. Di Stefano and N. Fabris: Dosedependent opposite effect of zinc on apoptosis in mouse thymocytes. Int J Immunopharmacol, 17(9), 735-44 (1995)
    • (1995) Int J Immunopharmacol , vol.17 , Issue.9 , pp. 735-744
    • Provinciali, M.1    Di Stefano, G.2    Fabris, N.3
  • 46
    • 49749124150 scopus 로고    scopus 로고
    • Intracellular zinc homeostasis and zinc signaling
    • M. Murakami and T. Hirano: Intracellular zinc homeostasis and zinc signaling. Cancer Sci, 99(8), 1515-22 (2008)
    • (2008) Cancer Sci , vol.99 , Issue.8 , pp. 1515-1522
    • Murakami, M.1    Hirano, T.2
  • 47
    • 0035060404 scopus 로고    scopus 로고
    • Effects of selenium and zinc supplementation on nutritional status in patients with cancer of digestive tract
    • A. Federico, P. Iodice, P. Federico, A. Del Rio, M. C. Mellone and G. Catalano: Effects of selenium and zinc supplementation on nutritional status in patients with cancer of digestive tract. Eur J Clin Nutr, 55(4), 293-7 (2001)
    • (2001) Eur J Clin Nutr , vol.55 , Issue.4 , pp. 293-297
    • Federico, A.1    Iodice, P.2    Federico, P.3    Del Rio, A.4    Mellone, M.C.5    Catalano, G.6
  • 50
    • 34250665634 scopus 로고    scopus 로고
    • Zinc as an anti-tumor agent in prostate cancer and in other cancers
    • R. B. Franklin and L. C. Costello: Zinc as an anti-tumor agent in prostate cancer and in other cancers. Arch Biochem Biophys, 463(2), 211-7 (2007)
    • (2007) Arch Biochem Biophys , vol.463 , Issue.2 , pp. 211-217
    • Franklin, R.B.1    Costello, L.C.2
  • 51
    • 24344501287 scopus 로고    scopus 로고
    • Copper, zinc, and Cu/Zn ratio in carcinoma of the gallbladder
    • S. K. Gupta, S. P. Singh and V. K. Shukla: Copper, zinc, and Cu/Zn ratio in carcinoma of the gallbladder. J Surg Oncol, 91(3), 204-8 (2005)
    • (2005) J Surg Oncol , vol.91 , Issue.3 , pp. 204-208
    • Gupta, S.K.1    Singh, S.P.2    Shukla, V.K.3
  • 52
    • 0020589944 scopus 로고
    • Copper and zinc levels in normal and malignant tissues
    • E. J. Margalioth, J. G. Schenker and M. Chevion: Copper and zinc levels in normal and malignant tissues. Cancer, 52(5), 868-72 (1983)
    • (1983) Cancer , vol.52 , Issue.5 , pp. 868-872
    • Margalioth, E.J.1    Schenker, J.G.2    Chevion, M.3
  • 53
    • 0016137826 scopus 로고
    • Trace elements in noraml and malignant human breast tissue
    • A. E. Schwartz, G. W. Leddicotte, R. W. Fink and E. W. Friedman: Trace elements in noraml and malignant human breast tissue. Surgery, 76(2), 325-9 (1974)
    • (1974) Surgery , vol.76 , Issue.2 , pp. 325-329
    • Schwartz, A.E.1    Leddicotte, G.W.2    Fink, R.W.3    Friedman, E.W.4
  • 54
    • 0029911793 scopus 로고    scopus 로고
    • The yeast ZRT1 gene encodes the zinc transporter protein of a high-affinity uptake system induced by zinc limitation
    • H. Zhao and D. Eide: The yeast ZRT1 gene encodes the zinc transporter protein of a high-affinity uptake system induced by zinc limitation. Proc Natl Acad Sci U S A, 93(6), 2454-8 (1996)
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.6 , pp. 2454-2458
    • Zhao, H.1    Eide, D.2
  • 56
    • 33745512125 scopus 로고    scopus 로고
    • The clinical relevance of the metabolism of prostate cancer; Zinc and tumor suppression: Connecting the dots
    • L. C. Costello and R. B. Franklin: The clinical relevance of the metabolism of prostate cancer; zinc and tumor suppression: connecting the dots. Mol Cancer, 5, 17 (2006)
    • (2006) Mol Cancer , vol.5 , pp. 17
    • Costello, L.C.1    Franklin, R.B.2
  • 59
    • 33749024777 scopus 로고    scopus 로고
    • Reassessing epithelial to mesenchymal transition as a prerequisite for carcinoma invasion and metastasis
    • J. J. Christiansen and A. K. Rajasekaran: Reassessing epithelial to mesenchymal transition as a prerequisite for carcinoma invasion and metastasis. Cancer Res, 66(17), 8319-26 (2006)
    • (2006) Cancer Res , vol.66 , Issue.17 , pp. 8319-8326
    • Christiansen, J.J.1    Rajasekaran, A.K.2
  • 60
    • 0018187738 scopus 로고
    • A heatstable polypeptide component of an ATP-dependent proteolytic system from reticulocytes
    • A. Ciehanover, Y. Hod and A. Hershko: A heatstable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochem Biophys Res Commun, 81(4), 1100-5 (1978)
    • (1978) Biochem Biophys Res Commun , vol.81 , Issue.4 , pp. 1100-1105
    • Ciehanover, A.1    Hod, Y.2    Hershko, A.3
  • 61
    • 0019000271 scopus 로고
    • Proposed role of ATP in protein breakdown: Conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis
    • A. Hershko, A. Ciechanover, H. Heller, A. L. Haas and I. A. Rose: Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc Natl Acad Sci U S A, 77(4), 1783-6 (1980)
    • (1980) Proc Natl Acad Sci U S A , vol.77 , Issue.4 , pp. 1783-1786
    • Hershko, A.1    Ciechanover, A.2    Heller, H.3    Haas, A.L.4    Rose, I.A.5
  • 62
    • 33745674468 scopus 로고    scopus 로고
    • Drug discovery in the ubiquitin-proteasome system
    • G. Nalepa, M. Rolfe and J. W. Harper: Drug discovery in the ubiquitin-proteasome system. Nat Rev Drug Discov, 5(7), 596-613 (2006)
    • (2006) Nat Rev Drug Discov , vol.5 , Issue.7 , pp. 596-613
    • Nalepa, G.1    Rolfe, M.2    Harper, J.W.3
  • 63
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • A. Ciechanover: The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J, 17(24), 7151-60 (1998)
    • (1998) EMBO J , vol.17 , Issue.24 , pp. 7151-7160
    • Ciechanover, A.1
  • 64
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: A suitable antineoplastic target
    • J. Adams: The proteasome: a suitable antineoplastic target. Nat Rev Cancer, 4(5), 349-60 (2004)
    • (2004) Nat Rev Cancer , vol.4 , Issue.5 , pp. 349-360
    • Adams, J.1
  • 66
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • W. Baumeister, J. Walz, F. Zuhl and E. Seemuller: The proteasome: paradigm of a self-compartmentalizing protease. Cell, 92(3), 367-80 (1998)
    • (1998) Cell , vol.92 , Issue.3 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 68
    • 0033613196 scopus 로고    scopus 로고
    • The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study
    • M. Groll, W. Heinemeyer, S. Jager, T. Ullrich, M. Bochtler, D. H. Wolf and R. Huber: The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proc Natl Acad Sci U S A, 96(20), 10976-83 (1999)
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.20 , pp. 10976-10983
    • Groll, M.1    Heinemeyer, W.2    Jager, S.3    Ullrich, T.4    Bochtler, M.5    Wolf, D.H.6    Huber, R.7
  • 69
    • 0033529596 scopus 로고    scopus 로고
    • The proteasome, a novel protease regulated by multiple mechanisms
    • G. N. DeMartino and C. A. Slaughter: The proteasome, a novel protease regulated by multiple mechanisms. J Biol Chem, 274(32), 22123-6 (1999)
    • (1999) J Biol Chem , vol.274 , Issue.32 , pp. 22123-22126
    • Demartino, G.N.1    Slaughter, C.A.2
  • 70
    • 0036777957 scopus 로고    scopus 로고
    • The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides
    • A. L. Goldberg, P. Cascio, T. Saric and K. L. Rock: The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides. Mol Immunol, 39(3-4), 147-64 (2002)
    • (2002) Mol Immunol , vol.39 , Issue.3-4 , pp. 147-164
    • Goldberg, A.L.1    Cascio, P.2    Saric, T.3    Rock, K.L.4
  • 71
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • O. Coux, K. Tanaka and A. L. Goldberg: Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem, 65, 801-47 (1996)
    • (1996) Annu Rev Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 72
    • 33645669213 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system
    • D. Nandi, P. Tahiliani, A. Kumar and D. Chandu: The ubiquitin-proteasome system. J Biosci, 31(1), 137-55 (2006)
    • (2006) J Biosci , vol.31 , Issue.1 , pp. 137-155
    • Nandi, D.1    Tahiliani, P.2    Kumar, A.3    Chandu, D.4
  • 73
    • 0037852202 scopus 로고    scopus 로고
    • The proteasome: Structure, function, and role in the cell
    • J. Adams: The proteasome: structure, function, and role in the cell. Cancer Treat Rev, 29 Suppl 1, 3-9 (2003)
    • (2003) Cancer Treat Rev , vol.29 , Issue.SUPPL. 1 , pp. 3-9
    • Adams, J.1
  • 74
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • A. Ciechanover, A. Orian and A. L. Schwartz: Ubiquitin-mediated proteolysis: biological regulation via destruction. Bioessays, 22(5), 442-51 (2000)
    • (2000) Bioessays , vol.22 , Issue.5 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 75
    • 33644859083 scopus 로고    scopus 로고
    • The ubiquitin proteolytic system: From a vague idea, through basic mechanisms, and onto human diseases and drug targeting
    • A. Ciechanover: The ubiquitin proteolytic system: from a vague idea, through basic mechanisms, and onto human diseases and drug targeting. Neurology, 66(2 Suppl 1), S7- 19 (2006)
    • (2006) Neurology , vol.66 , Issue.2 SUPPL. 1
    • Ciechanover, A.1
  • 76
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • J. Adams: The development of proteasome inhibitors as anticancer drugs. Cancer Cell, 5(5), 417-21 (2004)
    • (2004) Cancer Cell , vol.5 , Issue.5 , pp. 417-421
    • Adams, J.1
  • 77
    • 35448971525 scopus 로고    scopus 로고
    • The putative roles of the ubiquitin/proteasome pathway in resistance to anticancer therapy
    • L. Smith, M. J. Lind, P. J. Drew and L. Cawkwell: The putative roles of the ubiquitin/proteasome pathway in resistance to anticancer therapy. Eur J Cancer, 43(16), 2330-8 (2007)
    • (2007) Eur J Cancer , vol.43 , Issue.16 , pp. 2330-2338
    • Smith, L.1    Lind, M.J.2    Drew, P.J.3    Cawkwell, L.4
  • 78
    • 0033178142 scopus 로고    scopus 로고
    • Proteasome inhibitors as potential novel anticancer agents
    • Q. P. Dou and B. Li: Proteasome inhibitors as potential novel anticancer agents. Drug Resist Updat, 2(4), 215-223 (1999)
    • (1999) Drug Resist Updat , vol.2 , Issue.4 , pp. 215-223
    • Dou, Q.P.1    Li, B.2
  • 79
    • 0034635952 scopus 로고    scopus 로고
    • Bax degradation by the ubiquitin/proteasome-dependent pathway: Involvement in tumor survival and progression
    • B. Li and Q. P. Dou: Bax degradation by the ubiquitin/proteasome- dependent pathway: involvement in tumor survival and progression. Proc Natl Acad Sci U S A, 97(8), 3850-5 (2000)
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.8 , pp. 3850-3855
    • Li, B.1    Dou, Q.P.2
  • 80
    • 0031048236 scopus 로고    scopus 로고
    • Increased proteasome-dependent degradation of the cyclindependent kinase inhibitor p27 in aggressive colorectal carcinomas
    • M. Loda, B. Cukor, S. W. Tam, P. Lavin, M. Fiorentino, G. F. Draetta, J. M. Jessup and M. Pagano: Increased proteasome-dependent degradation of the cyclindependent kinase inhibitor p27 in aggressive colorectal carcinomas. Nat Med, 3(2), 231-4 (1997)
    • (1997) Nat Med , vol.3 , Issue.2 , pp. 231-234
    • Loda, M.1    Cukor, B.2    Tam, S.W.3    Lavin, P.4    Fiorentino, M.5    Draetta, G.F.6    Jessup, J.M.7    Pagano, M.8
  • 82
    • 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
    • B. An, R. H. Goldfarb, R. Siman and Q. P. Dou: 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(12), 1062-75 (1998)
    • (1998) Cell Death Differ , vol.5 , Issue.12 , pp. 1062-1075
    • An, B.1    Goldfarb, R.H.2    Siman, R.3    Dou, Q.P.4
  • 83
    • 0030962262 scopus 로고    scopus 로고
    • P53-dependent induction of apoptosis by proteasome inhibitors
    • U. G. Lopes, P. Erhardt, R. Yao and G. M. Cooper: p53-dependent induction of apoptosis by proteasome inhibitors. J Biol Chem, 272(20), 12893-6 (1997)
    • (1997) J Biol Chem , vol.272 , Issue.20 , pp. 12893-12896
    • Lopes, U.G.1    Erhardt, P.2    Yao, R.3    Cooper, G.M.4
  • 84
    • 41549133200 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy: Lessons from the first decade
    • R. Z. Orlowski and D. J. Kuhn: Proteasome inhibitors in cancer therapy: lessons from the first decade. Clin Cancer Res, 14(6), 1649-57 (2008)
    • (2008) Clin Cancer Res , vol.14 , Issue.6 , pp. 1649-1657
    • Orlowski, R.Z.1    Kuhn, D.J.2
  • 85
    • 0035300479 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells
    • T. Hideshima, P. Richardson, D. Chauhan, V. J. Palombella, P. J. Elliott, J. Adams and K. C. Anderson: The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res, 61(7), 3071-6 (2001)
    • (2001) Cancer Res , vol.61 , Issue.7 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3    Palombella, V.J.4    Elliott, P.J.5    Adams, J.6    Anderson, K.C.7
  • 87
    • 0033817518 scopus 로고    scopus 로고
    • Lack of multicellular drug resistance observed in human ovarian and prostate carcinoma treated with the proteasome inhibitor PS-341
    • A. Frankel, S. Man, P. Elliott, J. Adams and R. S. Kerbel: Lack of multicellular drug resistance observed in human ovarian and prostate carcinoma treated with the proteasome inhibitor PS-341. Clin Cancer Res, 6(9), 3719- 28 (2000)
    • (2000) Clin Cancer Res , vol.6 , Issue.9 , pp. 3719-3728
    • Frankel, A.1    Man, S.2    Elliott, P.3    Adams, J.4    Kerbel, R.S.5
  • 88
    • 0345447210 scopus 로고    scopus 로고
    • Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy
    • R. C. Kane, P. F. Bross, A. T. Farrell and R. Pazdur: Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy. Oncologist, 8(6), 508-13 (2003)
    • (2003) Oncologist , vol.8 , Issue.6 , pp. 508-513
    • Kane, R.C.1    Bross, P.F.2    Farrell, A.T.3    Pazdur, R.4
  • 90
    • 33745728140 scopus 로고    scopus 로고
    • Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132
    • L. J. Crawford, B. Walker, H. Ovaa, D. Chauhan, K. C. Anderson, T. C. Morris and A. E. Irvine: Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132. Cancer Res, 66(12), 6379-86 (2006)
    • (2006) Cancer Res , vol.66 , Issue.12 , pp. 6379-6386
    • Crawford, L.J.1    Walker, B.2    Ovaa, H.3    Chauhan, D.4    Anderson, K.C.5    Morris, T.C.6    Irvine, A.E.7
  • 91
    • 0036020941 scopus 로고    scopus 로고
    • NF-kappaB as a therapeutic target in cancer
    • R. Z. Orlowski and A. S. Baldwin, Jr.: NF-kappaB as a therapeutic target in cancer. Trends Mol Med, 8(8), 385-9 (2002)
    • (2002) Trends Mol Med , vol.8 , Issue.8 , pp. 385-389
    • Orlowski, R.Z.1    Baldwin Jr., A.S.2
  • 92
    • 0642349188 scopus 로고    scopus 로고
    • Differential effects of the proteasome inhibitor bortezomib on apoptosis and angiogenesis in human prostate tumor xenografts
    • S. Williams, C. Pettaway, R. Song, C. Papandreou, C. Logothetis and D. J. McConkey: Differential effects of the proteasome inhibitor bortezomib on apoptosis and angiogenesis in human prostate tumor xenografts. Mol Cancer Ther, 2(9), 835-43 (2003)
    • (2003) Mol Cancer Ther , vol.2 , Issue.9 , pp. 835-843
    • Williams, S.1    Pettaway, C.2    Song, R.3    Papandreou, C.4    Logothetis, C.5    McConkey, D.J.6
  • 99
    • 66949155833 scopus 로고    scopus 로고
    • Green tea polyphenols block the anticancer effects of bortezomib and other boronic acid-based proteasome inhibitors
    • E. B. Golden, P. Y. Lam, A. Kardosh, K. J. Gaffney, E. Cadenas, S. G. Louie, N. A. Petasis, T. C. Chen and A. H. Schonthal: Green tea polyphenols block the anticancer effects of bortezomib and other boronic acid-based proteasome inhibitors. Blood, 113(23), 5927-37 (2009)
    • (2009) Blood , vol.113 , Issue.23 , pp. 5927-5937
    • Golden, E.B.1    Lam, P.Y.2    Kardosh, A.3    Gaffney, K.J.4    Cadenas, E.5    Louie, S.G.6    Petasis, N.A.7    Chen, T.C.8    Schonthal, A.H.9
  • 102
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells
    • R. Schreck, B. Meier, D. N. Mannel, W. Droge and P. A. Baeuerle: Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells. J Exp Med, 175(5), 1181-94 (1992)
    • (1992) J Exp Med , vol.175 , Issue.5 , pp. 1181-1194
    • Schreck, R.1    Meier, B.2    Mannel, D.N.3    Droge, W.4    Baeuerle, P.A.5
  • 103
    • 50249190929 scopus 로고
    • Rheumatoid arthritis and its treatment with gold salts - Results of six years' experience
    • J. Forestier: Rheumatoid arthritis and its treatment with gold salts - results of six years' experience. J Lab Clin Med, 20, 827-840 (1935)
    • (1935) J Lab Clin Med , vol.20 , pp. 827-840
    • Forestier, J.1
  • 104
    • 38149122340 scopus 로고    scopus 로고
    • Gold derivatives for cancer treatment
    • E. R. Tiekink: Gold derivatives for cancer treatment. Bioinorg Chem Applns, 53, 1-9 (2003)
    • (2003) Bioinorg Chem Applns , vol.53 , pp. 1-9
    • Tiekink, E.R.1
  • 105
  • 106
    • 35748937356 scopus 로고    scopus 로고
    • Gold complexes as prospective metal-based anticancer drugs
    • V. Milacic, D. Fregona and Q. P. Dou: Gold complexes as prospective metal-based anticancer drugs. Histol Histopathol, 23(1), 101-8 (2008)
    • (2008) Histol Histopathol , vol.23 , Issue.1 , pp. 101-108
    • Milacic, V.1    Fregona, D.2    Dou, Q.P.3
  • 107
    • 0000566702 scopus 로고
    • The chemistry of gold drugs
    • P. J. Sadler and R. E. Sue: The chemistry of gold drugs. Met Based Drugs, 1(2-3), 107-44 (1994)
    • (1994) Met Based Drugs , vol.1 , Issue.2-3 , pp. 107-144
    • Sadler, P.J.1    Sue, R.E.2
  • 108
    • 0032734670 scopus 로고    scopus 로고
    • A Screening Strategy for Metal Antitumor Agents as Exemplified by Gold(III) Complexes
    • S. P. Fricker: A Screening Strategy for Metal Antitumor Agents as Exemplified by Gold(III) Complexes. Met Based Drugs, 6(4-5), 291-300 (1999)
    • (1999) Met Based Drugs , vol.6 , Issue.4-5 , pp. 291-300
    • Fricker, S.P.1
  • 109
    • 15944361817 scopus 로고    scopus 로고
    • Gold dithiocarbamate derivatives as potential antineoplastic agents: Design, spectroscopic properties, and in vitro antitumor activity
    • L. Ronconi, L. Giovagnini, C. Marzano, F. Bettio, R. Graziani, G. Pilloni and D. Fregona: Gold dithiocarbamate derivatives as potential antineoplastic agents: design, spectroscopic properties, and in vitro antitumor activity. Inorg Chem, 44(6), 1867-81 (2005)
    • (2005) Inorg Chem , vol.44 , Issue.6 , pp. 1867-1881
    • Ronconi, L.1    Giovagnini, L.2    Marzano, C.3    Bettio, F.4    Graziani, R.5    Pilloni, G.6    Fregona, D.7
  • 110
    • 33644855554 scopus 로고    scopus 로고
    • Gold(III) dithiocarbamate derivatives for the treatment of cancer: Solution chemistry, DNA binding, and hemolytic properties
    • L. Ronconi, C. Marzano, P. Zanello, M. Corsini, G. Miolo, C. Macca, A. Trevisan and D. Fregona: Gold(III) dithiocarbamate derivatives for the treatment of cancer: solution chemistry, DNA binding, and hemolytic properties. J Med Chem, 49(5), 1648-57 (2006)
    • (2006) J Med Chem , vol.49 , Issue.5 , pp. 1648-1657
    • Ronconi, L.1    Marzano, C.2    Zanello, P.3    Corsini, M.4    Miolo, G.5    Macca, C.6    Trevisan, A.7    Fregona, D.8
  • 111
    • 2442532684 scopus 로고    scopus 로고
    • Gold(III) compounds as new family of anticancer drugs
    • L. Messori, G. Marcon and P. Orioli: Gold(III) compounds as new family of anticancer drugs. Bioinorg Chem Appl, 177-87 (2003)
    • (2003) Bioinorg Chem Appl , pp. 177-187
    • Messori, L.1    Marcon, G.2    Orioli, P.3
  • 112
    • 0022542073 scopus 로고
    • Effect of diethyldithiocarbamate on cisdiamminedichloroplatinum( II)-induced cytotoxicity, DNA cross-linking, and gamma-glutamyl transpeptidase inhibition
    • D. L. Bodenner, P. C. Dedon, P. C. Keng and R. F. Borch: Effect of diethyldithiocarbamate on cisdiamminedichloroplatinum( II)-induced cytotoxicity, DNA cross-linking, and gamma-glutamyl transpeptidase inhibition. Cancer Res, 46(6), 2745-50 (1986)
    • (1986) Cancer Res , vol.46 , Issue.6 , pp. 2745-2750
    • Bodenner, D.L.1    Dedon, P.C.2    Keng, P.C.3    Borch, R.F.4
  • 113
    • 0029585833 scopus 로고
    • Solution structure of a cisplatin-induced DNA interstrand cross-link
    • H. Huang, L. Zhu, B. R. Reid, G. P. Drobny and P. B. Hopkins: Solution structure of a cisplatin-induced DNA interstrand cross-link. Science, 270(5243), 1842-5 (1995)
    • (1995) Science , vol.270 , Issue.5243 , pp. 1842-1845
    • Huang, H.1    Zhu, L.2    Reid, B.R.3    Drobny, G.P.4    Hopkins, P.B.5
  • 114
    • 33751275548 scopus 로고    scopus 로고
    • A novel anticancer gold(III) dithiocarbamate compound inhibits the activity of a purified 20S proteasome and 26S proteasome in human breast cancer cell cultures and xenografts
    • V. Milacic, D. Chen, L. Ronconi, K. R. Landis- Piwowar, D. Fregona and Q. P. Dou: A novel anticancer gold(III) dithiocarbamate compound inhibits the activity of a purified 20S proteasome and 26S proteasome in human breast cancer cell cultures and xenografts. Cancer Res, 66(21), 10478-86 (2006)
    • (2006) Cancer Res , vol.66 , Issue.21 , pp. 10478-10486
    • Milacic, V.1    Chen, D.2    Ronconi, L.3    Landis- Piwowar, K.R.4    Fregona, D.5    Dou, Q.P.6
  • 115
    • 73849121224 scopus 로고    scopus 로고
    • Inhibition of tumor proteasome activity by gold-dithiocarbamato complexes via both redox-dependent and -independent processes
    • X. Zhang, M. Frezza, V. Milacic, L. Ronconi, Y. Fan, C. Bi, D. Fregona and Q. P. Dou: Inhibition of tumor proteasome activity by gold-dithiocarbamato complexes via both redox-dependent and -independent processes. J Cell Biochem, 109(1), 162-72 (2010)
    • (2010) J Cell Biochem , vol.109 , Issue.1 , pp. 162-172
    • Zhang, X.1    Frezza, M.2    Milacic, V.3    Ronconi, L.4    Fan, Y.5    Bi, C.6    Fregona, D.7    Dou, Q.P.8
  • 116
    • 0026439016 scopus 로고
    • A review of the pharmacokinetics and pharmacodynamics of disulfiram and its metabolites
    • B. Johansson: A review of the pharmacokinetics and pharmacodynamics of disulfiram and its metabolites. Acta Psychiatr Scand Suppl, 369, 15-26 (1992)
    • (1992) Acta Psychiatr Scand Suppl , vol.369 , pp. 15-26
    • Johansson, B.1
  • 117
    • 0020033519 scopus 로고
    • Human aldehyde dehydrogenase: Mechanism of inhibition of disulfiram
    • R. C. Vallari and R. Pietruszko: Human aldehyde dehydrogenase: mechanism of inhibition of disulfiram. Science, 216(4546), 637-9 (1982)
    • (1982) Science , vol.216 , Issue.4546 , pp. 637-639
    • Vallari, R.C.1    Pietruszko, R.2
  • 118
    • 0024426368 scopus 로고
    • Prospects for a rational pharmacotherapy of alcoholism
    • R. E. Meyer: Prospects for a rational pharmacotherapy of alcoholism. J Clin Psychiatry, 50(11), 403-12 (1989)
    • (1989) J Clin Psychiatry , vol.50 , Issue.11 , pp. 403-412
    • Meyer, R.E.1
  • 119
    • 11144224746 scopus 로고    scopus 로고
    • Disulfiram facilitates intracellular Cu uptake and induces apoptosis in human melanoma cells
    • D. Cen, D. Brayton, B. Shahandeh, F. L. Meyskens, Jr. and P. J. Farmer: Disulfiram facilitates intracellular Cu uptake and induces apoptosis in human melanoma cells. J Med Chem, 47(27), 6914-20 (2004)
    • (2004) J Med Chem , vol.47 , Issue.27 , pp. 6914-6920
    • Cen, D.1    Brayton, D.2    Shahandeh, B.3    Meyskens Jr., F.L.4    Farmer, P.J.5
  • 120
    • 33751285781 scopus 로고    scopus 로고
    • Disulfiram, a clinically used anti-alcoholism drug and copper-binding agent, induces apoptotic cell death in breast cancer cultures and xenografts via inhibition of the proteasome activity
    • D. Chen, Q. C. Cui, H. Yang and Q. P. Dou: Disulfiram, a clinically used anti-alcoholism drug and copper-binding agent, induces apoptotic cell death in breast cancer cultures and xenografts via inhibition of the proteasome activity. Cancer Res, 66(21), 10425-33 (2006)
    • (2006) Cancer Res , vol.66 , Issue.21 , pp. 10425-10433
    • Chen, D.1    Cui, Q.C.2    Yang, H.3    Dou, Q.P.4
  • 122
    • 0036132060 scopus 로고    scopus 로고
    • Cu/Zn superoxide dismutase plays a role in angiogenesis
    • M. Marikovsky, N. Nevo, E. Vadai and C. Harris- Cerruti: Cu/Zn superoxide dismutase plays a role in angiogenesis. Int J Cancer, 97(1), 34-41 (2002)
    • (2002) Int J Cancer , vol.97 , Issue.1 , pp. 34-41
    • Marikovsky, M.1    Nevo, N.2    Vadai, E.3    Harris- Cerruti, C.4
  • 124
    • 0024440536 scopus 로고
    • A randomized, controlled dose response study of intravenous sodium diethyldithiocarbamate in patients with advanced human immunodeficiency virus infection
    • C. S. Kaplan, E. A. Petersen, D. Yocum and E. M. Hersh: A randomized, controlled dose response study of intravenous sodium diethyldithiocarbamate in patients with advanced human immunodeficiency virus infection. Life Sci, 45(22), iii-ix (1989)
    • (1989) Life Sci , vol.45 , Issue.22
    • Kaplan, C.S.1    Petersen, E.A.2    Yocum, D.3    Hersh, E.M.4
  • 125
    • 54549114503 scopus 로고    scopus 로고
    • Ni(II), Cu(II), and Zn(II) diethyldithiocarbamate complexes show various activities against the proteasome in breast cancer cells
    • B. Cvek, V. Milacic, J. Taraba and Q. P. Dou: Ni(II), Cu(II), and Zn(II) diethyldithiocarbamate complexes show various activities against the proteasome in breast cancer cells. J Med Chem, 51(20), 6256-8 (2008)
    • (2008) J Med Chem , vol.51 , Issue.20 , pp. 6256-6258
    • Cvek, B.1    Milacic, V.2    Taraba, J.3    Dou, Q.P.4
  • 126
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • R. Verma, L. Aravind, R. Oania, W. H. McDonald, J. R. Yates, 3rd, E. V. Koonin and R. J. Deshaies: Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science, 298(5593), 611-5 (2002)
    • (2002) Science , vol.298 , Issue.5593 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates, J.R.5    Koonin, E.V.6    Deshaies, R.J.7
  • 128
    • 48649110541 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate-zinc(II) and - Copper(II) complexes induce apoptosis in tumor cells by inhibiting the proteasomal activity
    • V. Milacic, D. Chen, L. Giovagnini, A. Diez, D. Fregona and Q. P. Dou: Pyrrolidine dithiocarbamate-zinc(II) and - copper(II) complexes induce apoptosis in tumor cells by inhibiting the proteasomal activity. Toxicol Appl Pharmacol, 231(1), 24-33 (2008)
    • (2008) Toxicol Appl Pharmacol , vol.231 , Issue.1 , pp. 24-33
    • Milacic, V.1    Chen, D.2    Giovagnini, L.3    Diez, A.4    Fregona, D.5    Dou, Q.P.6
  • 132
    • 10344249883 scopus 로고    scopus 로고
    • Metalprotein attenuating compounds and Alzheimer's disease
    • C. W. Ritchie, A. I. Bush and C. L. Masters: Metalprotein attenuating compounds and Alzheimer's disease. Expert Opin Investig Drugs, 13(12), 1585-92 (2004)
    • (2004) Expert Opin Investig Drugs , vol.13 , Issue.12 , pp. 1585-1592
    • Ritchie, C.W.1    Bush, A.I.2    Masters, C.L.3
  • 133
    • 23844482456 scopus 로고    scopus 로고
    • Clioquinol down-regulates mutant huntingtin expression in vitro and mitigates pathology in a Huntington's disease mouse model
    • T. Nguyen, A. Hamby and S. M. Massa: Clioquinol down-regulates mutant huntingtin expression in vitro and mitigates pathology in a Huntington's disease mouse model. Proc Natl Acad Sci U S A, 102(33), 11840-5 (2005)
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.33 , pp. 11840-11845
    • Nguyen, T.1    Hamby, A.2    Massa, S.M.3
  • 134
    • 45849091277 scopus 로고
    • Prophylaxis and therapy of amebiasis and shigellosis with iodochlorhydroxyquin
    • L. M. Gholz and W. L. Arons: Prophylaxis and Therapy of Amebiasis and Shigellosis with Iodochlorhydroxyquin. Am J Trop Med Hyg, 13, 396-401 (1964)
    • (1964) Am J Trop Med Hyg , vol.13 , pp. 396-401
    • Gholz, L.M.1    Arons, W.L.2
  • 135
    • 2942750367 scopus 로고    scopus 로고
    • Clioquinol, a drug for Alzheimer's disease specifically interfering with brain metal metabolism: Structural characterization of its zinc(II) and copper(II) complexes
    • M. Di Vaira, C. Bazzicalupi, P. Orioli, L. Messori, B. Bruni and P. Zatta: Clioquinol, a drug for Alzheimer's disease specifically interfering with brain metal metabolism: structural characterization of its zinc(II) and copper(II) complexes. Inorg Chem, 43(13), 3795-7 (2004)
    • (2004) Inorg Chem , vol.43 , Issue.13 , pp. 3795-3797
    • Di Vaira, M.1    Bazzicalupi, C.2    Orioli, P.3    Messori, L.4    Bruni, B.5    Zatta, P.6
  • 136
    • 33847746963 scopus 로고    scopus 로고
    • Clioquinol, a therapeutic agent for Alzheimer's disease, has proteasomeinhibitory, androgen receptor-suppressing, apoptosis-inducing, and antitumor activities in human prostate cancer cells and xenografts
    • D. Chen, Q. C. Cui, H. Yang, R. A. Barrea, F. H. Sarkar, S. Sheng, B. Yan, G. P. Reddy and Q. P. Dou: Clioquinol, a therapeutic agent for Alzheimer's disease, has proteasomeinhibitory, androgen receptor-suppressing, apoptosis-inducing, and antitumor activities in human prostate cancer cells and xenografts. Cancer Res, 67(4), 1636-44 (2007)
    • (2007) Cancer Res , vol.67 , Issue.4 , pp. 1636-1644
    • Chen, D.1    Cui, Q.C.2    Yang, H.3    Barrea, R.A.4    Sarkar, F.H.5    Sheng, S.6    Yan, B.7    Reddy, G.P.8    Dou, Q.P.9
  • 137
    • 1542270307 scopus 로고    scopus 로고
    • Organic copper complexes as a new class of proteasome inhibitors and apoptosis inducers in human cancer cells
    • K. G. Daniel, P. Gupta, R. H. Harbach, W. C. Guida and Q. P. Dou: Organic copper complexes as a new class of proteasome inhibitors and apoptosis inducers in human cancer cells. Biochem Pharmacol, 67(6), 1139-51 (2004)
    • (2004) Biochem Pharmacol , vol.67 , Issue.6 , pp. 1139-1151
    • Daniel, K.G.1    Gupta, P.2    Harbach, R.H.3    Guida, W.C.4    Dou, Q.P.5
  • 138
    • 73949101373 scopus 로고    scopus 로고
    • Novel 8-hydroxylquinoline analogs induce copperdependent proteasome inhibition and cell death in human breast cancer cells
    • V. Milacic, P. Jiao, B. Zhang, B. Yan and Q. P. Dou: Novel 8-hydroxylquinoline analogs induce copperdependent proteasome inhibition and cell death in human breast cancer cells. Int J Oncol, 35(6), 1481-91 (2009)
    • (2009) Int J Oncol , vol.35 , Issue.6 , pp. 1481-1491
    • Milacic, V.1    Jiao, P.2    Zhang, B.3    Yan, B.4    Dou, Q.P.5
  • 139
    • 77949267166 scopus 로고    scopus 로고
    • Tumor cellular proteasome inhibition and growth suppression by 8-hydroxyquinoline and clioquinol requires their capabilities to bind copper and transport copper into cells
    • S. Zhai, L. Yang, Q. C. Cui, Y. Sun, Q. P. Dou and B. Yan: Tumor cellular proteasome inhibition and growth suppression by 8-hydroxyquinoline and clioquinol requires their capabilities to bind copper and transport copper into cells. J Biol Inorg Chem, 15(2), 259-69 (2010)
    • (2010) J Biol Inorg Chem , vol.15 , Issue.2 , pp. 259-269
    • Zhai, S.1    Yang, L.2    Cui, Q.C.3    Sun, Y.4    Dou, Q.P.5    Yan, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.