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Volumn 51, Issue 9, 2008, Pages 2600-2605

Chemical genetics: Exploring the role of the proteasome in cell biology using natural products and other small molecule proteasome inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

BORTEZOMIB; CELASTROL; EPIGALLOCATECHIN GALLATE; EPOXOMICIN; FLAVONOID; GENISTEIN; LACTACYSTIN; MYRICETIN; NATURAL PRODUCT; PRISTIMEROL; PROTEASOME INHIBITOR; QUERCETIN; SALINOSPORAMIDE A; TERPENOID; TRITERPENOID; WITHAFERIN A;

EID: 42949152860     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm070421s     Document Type: Review
Times cited : (20)

References (67)
  • 3
    • 0031710509 scopus 로고    scopus 로고
    • Chemical genetics resulting from a passion for synthetic organic chemistry
    • Schreiber, S. L. Chemical genetics resulting from a passion for synthetic organic chemistry. Bioorg. Med. Chem. 1998, 6, 1127-1152.
    • (1998) Bioorg. Med. Chem , vol.6 , pp. 1127-1152
    • Schreiber, S.L.1
  • 4
    • 0036181371 scopus 로고    scopus 로고
    • Development of the proteasome inhibitor PS-341
    • Adams, J. Development of the proteasome inhibitor PS-341. Oncologist 2002, 7, 9-16.
    • (2002) Oncologist , vol.7 , pp. 9-16
    • Adams, J.1
  • 5
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • Ciechanover, A.; Orian, A.; Schwartz, A. L. Ubiquitin-mediated proteolysis: biological regulation via destruction. BioEssays 2000, 22, 442-451.
    • (2000) BioEssays , vol.22 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 6
    • 0034967925 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and proteasome inhibitors
    • (a) Myung, J.; Kim, K. B.; Crews, C. M. The ubiquitin-proteasome pathway and proteasome inhibitors. Med. Res. Rev. 2001, 21, 245-73.
    • (2001) Med. Res. Rev , vol.21 , pp. 245-273
    • Myung, J.1    Kim, K.B.2    Crews, C.M.3
  • 8
    • 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.; Rando, O. J.; Goldberg, A. L.; Maniatis, T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 1994, 78, 773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 9
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors
    • (a) Bogyo, M.; McMaster, J. S.; Gaczynska, M.; Tortorella, D.; Goldberg, A. L.; Ploegh, H. Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 6629-6634.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 6629-6634
    • Bogyo, M.1    McMaster, J.S.2    Gaczynska, M.3    Tortorella, D.4    Goldberg, A.L.5    Ploegh, H.6
  • 10
    • 0032103006 scopus 로고    scopus 로고
    • Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes
    • (b) Bogyo, M.; Shin, S.; McMaster, J. S.; Ploegh, H. L. Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes. Chem. Biol. 1998, 5, 307-320.
    • (1998) Chem. Biol , vol.5 , pp. 307-320
    • Bogyo, M.1    Shin, S.2    McMaster, J.S.3    Ploegh, H.L.4
  • 11
    • 0026065338 scopus 로고    scopus 로고
    • Omura, S.; Fujimoto, T.; Otoguro, K.; Matsuzaki, K.; Moriguchi, R.; Tanaka, H.; Sasaki, Y. Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells. J. Antibiot. (Tokyo) 1991, 44, 113-116.
    • Omura, S.; Fujimoto, T.; Otoguro, K.; Matsuzaki, K.; Moriguchi, R.; Tanaka, H.; Sasaki, Y. Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells. J. Antibiot. (Tokyo) 1991, 44, 113-116.
  • 12
    • 0027050714 scopus 로고    scopus 로고
    • Hanada, M.; Sugawara, K.; Kaneta, K.; Toda, S.; Nishiyama, Y.; Tomita, K.; Yamamoto, H.; Konishi, M.; Oki, T. Epoxomicin, a new antitumor agent of microbial origin. J. Antibiot. (Tokyo) 1992, 45, 1746-1752.
    • Hanada, M.; Sugawara, K.; Kaneta, K.; Toda, S.; Nishiyama, Y.; Tomita, K.; Yamamoto, H.; Konishi, M.; Oki, T. Epoxomicin, a new antitumor agent of microbial origin. J. Antibiot. (Tokyo) 1992, 45, 1746-1752.
  • 13
    • 0030981843 scopus 로고    scopus 로고
    • Epopromycins, novel cell wall synthesis inhibitors of plant protoplast produced by Streptomyces sp. NK04000
    • (a) Tsuchiya, K.; Kobayashi, S.; Nishikiori, T.; Nakagawa, T.; Tatsuta, K. Epopromycins, novel cell wall synthesis inhibitors of plant protoplast produced by Streptomyces sp. NK04000. J. Antibiot. (Tokyo) 1997, 50, 261-263.
    • (1997) J. Antibiot. (Tokyo) , vol.50 , pp. 261-263
    • Tsuchiya, K.1    Kobayashi, S.2    Nishikiori, T.3    Nakagawa, T.4    Tatsuta, K.5
  • 14
    • 0034105791 scopus 로고    scopus 로고
    • TMC-95A, B, C, and D, novel proteasome inhibitors produced by Apiospora montagnei Sacc. TC 1093. Taxonomy, production, isolation, and biological activities
    • (b) Koguchi, Y.; Kohno, J.; Nishio, M.; Takahashi, K.; Okuda, T.; Ohnuki, T.; Komatsubara, S. TMC-95A, B, C, and D, novel proteasome inhibitors produced by Apiospora montagnei Sacc. TC 1093. Taxonomy, production, isolation, and biological activities. J. Antibiot. (Tokyo) 2000, 53, 105-109.
    • (2000) J. Antibiot. (Tokyo) , vol.53 , pp. 105-109
    • Koguchi, Y.1    Kohno, J.2    Nishio, M.3    Takahashi, K.4    Okuda, T.5    Ohnuki, T.6    Komatsubara, S.7
  • 15
    • 0033375564 scopus 로고    scopus 로고
    • Koguchi, Y.; Kohno, J.; Suzuki, S.; Nishio, M.; Takahashi, K.; Ohnuki, T.; Komatsubara, S. TMC-86A, B and TMC-96, new proteasome inhibitors from Streptomyces sp. TC 1084 and Saccharothrix sp. TC 1094. I. Taxonomy, fermentation, isolation, and biological activities. J. Antibiot. (Tokyo) 1999, 52, 1069-76.
    • (c) Koguchi, Y.; Kohno, J.; Suzuki, S.; Nishio, M.; Takahashi, K.; Ohnuki, T.; Komatsubara, S. TMC-86A, B and TMC-96, new proteasome inhibitors from Streptomyces sp. TC 1084 and Saccharothrix sp. TC 1094. I. Taxonomy, fermentation, isolation, and biological activities. J. Antibiot. (Tokyo) 1999, 52, 1069-76.
  • 16
    • 0025015309 scopus 로고    scopus 로고
    • Sugawara, K.; Hatori, M.; Nishiyama, Y.; Tomita, K.; Kamei, H.; Konishi, M.; Oki, T. Eponemycin, a new antibiotic active against B16 melanoma. I. Production, isolation, structure and biological activity. J. Antibiot. (Tokyo) 1990, 43, 8-18.
    • (d) Sugawara, K.; Hatori, M.; Nishiyama, Y.; Tomita, K.; Kamei, H.; Konishi, M.; Oki, T. Eponemycin, a new antibiotic active against B16 melanoma. I. Production, isolation, structure and biological activity. J. Antibiot. (Tokyo) 1990, 43, 8-18.
  • 17
    • 0035736099 scopus 로고    scopus 로고
    • The proteasome: A new target for novel drug therapies
    • Elliott, P. J.; Ross, J. S. The proteasome: a new target for novel drug therapies. Am. J. Clin. Pathol. 2001, 116, 637-646.
    • (2001) Am. J. Clin. Pathol , vol.116 , pp. 637-646
    • Elliott, P.J.1    Ross, J.S.2
  • 18
    • 0031985626 scopus 로고    scopus 로고
    • Role of proteasomes in T cell activation and proliferation
    • Wang, X.; Luo, H.; Chen, H.; Duguid, W.; Wu, J. Role of proteasomes in T cell activation and proliferation. J. Immunol. 1998, 160, 788-801.
    • (1998) J. Immunol , vol.160 , pp. 788-801
    • Wang, X.1    Luo, H.2    Chen, H.3    Duguid, W.4    Wu, J.5
  • 19
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • (a) Fenteany, G.; Standaert, R. F.; Lane, W. S.; Choi, S.; Corey, E. J.; Schreiber, S. L. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 1995, 268, 726-731.
    • (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
  • 20
    • 0034636585 scopus 로고    scopus 로고
    • Cdc25A stability is controlled by the ubiquitin-proteasome pathway during cell cycle progression and terminal differentiation
    • (b) Bernardi, R.; Liebermann, D. A.; Hoffman, B. Cdc25A stability is controlled by the ubiquitin-proteasome pathway during cell cycle progression and terminal differentiation. Oncogene 2000, 19, 2447-2454.
    • (2000) Oncogene , vol.19 , pp. 2447-2454
    • Bernardi, R.1    Liebermann, D.A.2    Hoffman, B.3
  • 21
    • 0030724422 scopus 로고    scopus 로고
    • Roles of ubiquitin-mediated proteolysis in cell cycle control
    • (c) Hershko, A. Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr. Opin. Cell Biol. 1997, 9, 788-799.
    • (1997) Curr. Opin. Cell Biol , vol.9 , pp. 788-799
    • Hershko, A.1
  • 22
    • 0035123105 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis of vertebrate G1- and S-phase regulators
    • (a) Yew, P. R. Ubiquitin-mediated proteolysis of vertebrate G1- and S-phase regulators. J. Cell. Physiol. 2001, 187, 1-10.
    • (2001) J. Cell. Physiol , vol.187 , pp. 1-10
    • Yew, P.R.1
  • 23
    • 0020961333 scopus 로고    scopus 로고
    • Evans, T.; Rosenthal, E. T.; Youngblom, J.; Distel, D.; Hunt, T. Cyclin: a protein specified by maternal mRNA in sea urchin eggs that is destroyed at each cleavage division. Cell 1983, 33, 389-396.
    • (b) Evans, T.; Rosenthal, E. T.; Youngblom, J.; Distel, D.; Hunt, T. Cyclin: a protein specified by maternal mRNA in sea urchin eggs that is destroyed at each cleavage division. Cell 1983, 33, 389-396.
  • 24
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • (c) Glotzer, M.; Murray, A. W.; Kirschner, M. W. Cyclin is degraded by the ubiquitin pathway. Nature 1991, 349, 132-138.
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 26
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
    • (b) Pagano, M.; Tam, S. W.; Theodoras, A. M.; Beer-Romero, P.; Del Sal, G.; Chau, V.; Yew, P. R.; Draetta, G. F.; Rolfe, M. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 1995, 269, 682-685.
    • (1995) Science , vol.269 , pp. 682-685
    • Pagano, M.1    Tam, S.W.2    Theodoras, A.M.3    Beer-Romero, P.4    Del Sal, G.5    Chau, V.6    Yew, P.R.7    Draetta, G.F.8    Rolfe, M.9
  • 27
    • 1342272916 scopus 로고    scopus 로고
    • How the cyclin became a cyclin: Regulated proteolysis in the cell cycle
    • (a) Koepp, D. M.; Harper, J. W.; Elledge, S. J. How the cyclin became a cyclin: regulated proteolysis in the cell cycle. Cell 1999, 97, 431-434.
    • (1999) Cell , vol.97 , pp. 431-434
    • Koepp, D.M.1    Harper, J.W.2    Elledge, S.J.3
  • 28
    • 17044370346 scopus 로고    scopus 로고
    • Regulation of the cell cycle by SCF-type ubiquitin ligases
    • (b) Nakayama, K. I.; Nakayama, K. Regulation of the cell cycle by SCF-type ubiquitin ligases. Semin. Cell Dev. Biol. 2005, 16, 323-333.
    • (2005) Semin. Cell Dev. Biol , vol.16 , pp. 323-333
    • Nakayama, K.I.1    Nakayama, K.2
  • 29
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat, M. H.; Jones, S. N.; Vousden, K. H. Regulation of p53 stability by Mdm2. Nature 1997, 387, 299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 30
    • 33646757232 scopus 로고    scopus 로고
    • The complexity of p53 stabilization and activation
    • Lavin, M. F.; Gueven, N. The complexity of p53 stabilization and activation. Cell Death Differ. 2006, 13, 941-950.
    • (2006) Cell Death Differ , vol.13 , pp. 941-950
    • Lavin, M.F.1    Gueven, N.2
  • 32
    • 31544457877 scopus 로고    scopus 로고
    • p53 ubiquitination: Mdm2 and beyond
    • (b) Brooks, C. L.; Gu, W. p53 ubiquitination: Mdm2 and beyond. Mol. Cell 2006, 21, 307-315.
    • (2006) Mol. Cell , vol.21 , pp. 307-315
    • Brooks, C.L.1    Gu, W.2
  • 33
    • 0032841656 scopus 로고    scopus 로고
    • Proteasome inhibitors induce p53/p21-independent apoptosis in human glioma cells
    • Wagenknecht, B.; Hermisson, M.; Eitel, K.; Weller, M. Proteasome inhibitors induce p53/p21-independent apoptosis in human glioma cells. Cell. Physiol. Biochem. 1999, 9, 117-125.
    • (1999) Cell. Physiol. Biochem , vol.9 , pp. 117-125
    • Wagenknecht, B.1    Hermisson, M.2    Eitel, K.3    Weller, M.4
  • 34
    • 0036483901 scopus 로고    scopus 로고
    • Deadly encounter: Ubiquitin meets apoptosis
    • (a) Jesenberger, V.; Jentsch, S. Deadly encounter: ubiquitin meets apoptosis. Nat. Rev. Mol. Cell Biol. 2002, 3, 112-121.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 112-121
    • Jesenberger, V.1    Jentsch, S.2
  • 35
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • (b) Cory, S.; Adams, J. M. The Bcl2 family: regulators of the cellular life-or-death switch. Nat. Rev. Cancer 2002, 2, 647-656.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 36
    • 1942534018 scopus 로고    scopus 로고
    • Regulation of apoptosis proteins in cancer cells by ubiquitin
    • Zhang, H. G.; Wang, J.; Yang, X.; Hsu, H. C.; Mountz, J. D. Regulation of apoptosis proteins in cancer cells by ubiquitin. Oncogene 2004, 23, 2009-2015.
    • (2004) Oncogene , vol.23 , pp. 2009-2015
    • Zhang, H.G.1    Wang, J.2    Yang, X.3    Hsu, H.C.4    Mountz, J.D.5
  • 37
    • 0035284812 scopus 로고    scopus 로고
    • Proteasomes modulate balance among proapoptotic and antiapoptotic Bcl-2 family members and compromise functioning of the electron transport chain in leukemic cells
    • Marshansky, V.; Wang, X.; Bertrand, R.; Luo, H.; Duguid, W.; Chinnadurai, G.; Kanaan, N.; Vu, M. D.; Wu, J. Proteasomes modulate balance among proapoptotic and antiapoptotic Bcl-2 family members and compromise functioning of the electron transport chain in leukemic cells. J. Immunol. 2001, 166, 3130-3142.
    • (2001) J. Immunol , vol.166 , pp. 3130-3142
    • Marshansky, V.1    Wang, X.2    Bertrand, R.3    Luo, H.4    Duguid, W.5    Chinnadurai, G.6    Kanaan, N.7    Vu, M.D.8    Wu, J.9
  • 38
    • 0034647563 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of the proapoptotic active form of bid. A functional consequence on apoptosis induction
    • Breitschopf, K.; Zeiher, A. M.; Dimmeier, S. Ubiquitin-mediated degradation of the proapoptotic active form of bid. A functional consequence on apoptosis induction. J. Biol. Chem. 2000, 275, 21648-21652.
    • (2000) J. Biol. Chem , vol.275 , pp. 21648-21652
    • Breitschopf, K.1    Zeiher, A.M.2    Dimmeier, S.3
  • 39
    • 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. 2000, 97, 3850-3855.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 3850-3855
    • Li, B.1    Dou, Q.P.2
  • 40
    • 0032506698 scopus 로고    scopus 로고
    • Inhibition of Bak-induced apoptosis by HPV-18 E6
    • Thomas, M.; Banks, L. Inhibition of Bak-induced apoptosis by HPV-18 E6. Oncogene 1998, 17, 2943-2954.
    • (1998) Oncogene , vol.17 , pp. 2943-2954
    • Thomas, M.1    Banks, L.2
  • 41
    • 18044383342 scopus 로고    scopus 로고
    • Dietary flavonoids as proteasome inhibitors and apoptosis inducers in human leukemia cells
    • (a) Chen, D.; Daniel, K. G.; Chen, M. S.; Kuhn, D. J.; Landis-Piwowar, K. R.; Dou, Q. P. Dietary flavonoids as proteasome inhibitors and apoptosis inducers in human leukemia cells. Biochem. Pharmacol. 2005, 69, 1421-1432.
    • (2005) Biochem. Pharmacol , vol.69 , pp. 1421-1432
    • Chen, D.1    Daniel, K.G.2    Chen, M.S.3    Kuhn, D.J.4    Landis-Piwowar, K.R.5    Dou, Q.P.6
  • 43
    • 33846454701 scopus 로고    scopus 로고
    • The tumor proteasome is a primary target for the natural anticancer compound Withaferin A isolated from Indian winter cherry
    • (c) Yang, H.; Shi, G.; Dou, Q. P. The tumor proteasome is a primary target for the natural anticancer compound Withaferin A isolated from "Indian winter cherry. Mol. Pharmacol. 2007, 71, 426-437.
    • (2007) Mol. Pharmacol , vol.71 , pp. 426-437
    • Yang, H.1    Shi, G.2    Dou, Q.P.3
  • 44
    • 33646406554 scopus 로고    scopus 로고
    • Yang, H.; Chen, D.; Cui, Q. C.; Yuan, X.; Dou, Q. P. Celastrol, a triterpene extracted from the Chinese Thunder of God Vine, is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice. Cancer Res. 2006, 66, 4758-4765.
    • (d) Yang, H.; Chen, D.; Cui, Q. C.; Yuan, X.; Dou, Q. P. Celastrol, a triterpene extracted from the Chinese "Thunder of God Vine", is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice. Cancer Res. 2006, 66, 4758-4765.
  • 45
    • 0042261670 scopus 로고    scopus 로고
    • Inhibition of the proteasome activity, a novel mechanism associated with the tumor cell apoptosis-inducing ability of genistein
    • (e) Kazi, A.; Daniel, K. G.; Smith, D. M.; Kumar, N. B.; Dou, Q. P. Inhibition of the proteasome activity, a novel mechanism associated with the tumor cell apoptosis-inducing ability of genistein. Biochem. Pharmacol. 2003, 66, 965-976.
    • (2003) Biochem. Pharmacol , vol.66 , pp. 965-976
    • Kazi, A.1    Daniel, K.G.2    Smith, D.M.3    Kumar, N.B.4    Dou, Q.P.5
  • 46
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-[kappa]B activity
    • Karin, M.; Ben-Neriah, Y. Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu. Rev. Immunol. 2000, 18, 621-663.
    • (2000) Annu. Rev. Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 47
    • 0036327139 scopus 로고    scopus 로고
    • NFkappaB-dependent chemoresistance in solid tumors
    • (a) Arlt, A.; Schafer, H. NFkappaB-dependent chemoresistance in solid tumors. Int. J. Clin. Pharmacol. Ther. 2002, 40, 336-347.
    • (2002) Int. J. Clin. Pharmacol. Ther , vol.40 , pp. 336-347
    • Arlt, A.1    Schafer, H.2
  • 48
    • 0033177897 scopus 로고    scopus 로고
    • NF-kappa B and chemoresistance: Potentiation of cancer drugs via inhibition of NF-kappa B
    • (b) Cusack, J. C.; Liu, R.; Baldwin, A. S. NF-kappa B and chemoresistance: potentiation of cancer drugs via inhibition of NF-kappa B. Drug Resist. Updates 1999, 2, 271-273.
    • (1999) Drug Resist. Updates , vol.2 , pp. 271-273
    • Cusack, J.C.1    Liu, R.2    Baldwin, A.S.3
  • 49
    • 0035328584 scopus 로고    scopus 로고
    • Cusack, J. C., Jr.; Liu, R.; Houston, M.; Abendroth, K.; Elliott, P. J.; Adams, J.; Baldwin, A. S., Jr. Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS-341: implications for systemic nuclear factor-kappaB inhibition. Cancer Res. 2001, 61, 3535-3540.
    • Cusack, J. C., Jr.; Liu, R.; Houston, M.; Abendroth, K.; Elliott, P. J.; Adams, J.; Baldwin, A. S., Jr. Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS-341: implications for systemic nuclear factor-kappaB inhibition. Cancer Res. 2001, 61, 3535-3540.
  • 50
    • 33748036736 scopus 로고    scopus 로고
    • Bone morphogenetic protein signal transduction in bone
    • (a) ten Dijke, P. Bone morphogenetic protein signal transduction in bone. Curr. Med. Res. Opin. 2006, 22, S7-S11.
    • (2006) Curr. Med. Res. Opin , vol.22
    • ten Dijke, P.1
  • 51
    • 27644494876 scopus 로고    scopus 로고
    • Smad transcription factors
    • (b) Massague, J.; Seoane, J.; Wotton, D. Smad transcription factors. Genes Dev. 2005, 19, 2783-2810.
    • (2005) Genes Dev , vol.19 , pp. 2783-2810
    • Massague, J.1    Seoane, J.2    Wotton, D.3
  • 52
    • 34250019537 scopus 로고
    • Bone: Formation by autoinduction
    • Urist, M. R. Bone: formation by autoinduction. Science 1965, 150, 893-899.
    • (1965) Science , vol.150 , pp. 893-899
    • Urist, M.R.1
  • 54
    • 24644482494 scopus 로고    scopus 로고
    • The BMP signaling and in vivo bone formation
    • Cao, X.; Chen, D. The BMP signaling and in vivo bone formation. Gene 2005, 357, 1-8.
    • (2005) Gene , vol.357 , pp. 1-8
    • Cao, X.1    Chen, D.2
  • 55
    • 0029616567 scopus 로고
    • Competition between noggin and bone morphogenetic protein 4 activities may regulate dorsalization during Xenopus development
    • Re'em-Kalma, Y.; Lamb, T.; Frank, D. Competition between noggin and bone morphogenetic protein 4 activities may regulate dorsalization during Xenopus development. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 12141-12145.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 12141-12145
    • Re'em-Kalma, Y.1    Lamb, T.2    Frank, D.3
  • 58
    • 17744412856 scopus 로고    scopus 로고
    • The 26S proteasome system in the signaling pathways of TGF-beta superfamily
    • (a) Wang, T. The 26S proteasome system in the signaling pathways of TGF-beta superfamily. Front. Biosci. 2003, 8, d1109-d1127.
    • (2003) Front. Biosci , vol.8
    • Wang, T.1
  • 59
    • 0035824568 scopus 로고    scopus 로고
    • Proteasomal degradation of Smad1 induced by bone morphogenetic proteins
    • (b) Gruendler, C.; Lin, Y.; Farley, J.; Wang, T. Proteasomal degradation of Smad1 induced by bone morphogenetic proteins. J. Biol. Chem. 2001, 276, 46533-46543.
    • (2001) J. Biol. Chem , vol.276 , pp. 46533-46543
    • Gruendler, C.1    Lin, Y.2    Farley, J.3    Wang, T.4
  • 60
    • 1842477311 scopus 로고    scopus 로고
    • Smurf1 inhibits osteoblast differentiation and bone formation in vitro and in vivo
    • (c) Zhao, M.; Qiao, M.; Harris, S. E.; Oyajobi, B. O.; Mundy, G. R.; Chen, D. Smurf1 inhibits osteoblast differentiation and bone formation in vitro and in vivo. J. Biol. Chem. 2004, 279, 12854-12859.
    • (2004) J. Biol. Chem , vol.279 , pp. 12854-12859
    • Zhao, M.1    Qiao, M.2    Harris, S.E.3    Oyajobi, B.O.4    Mundy, G.R.5    Chen, D.6
  • 61
    • 0030014641 scopus 로고    scopus 로고
    • The antitumor drug aclacinomycin A, which inhibits the degradation of ubiquitinated proteins, shows selectivity for the chymotrypsin-like activity of the bovine pituitary 20 S proteasome
    • (a) Figueiredo-Pereira, M. E.; Chen, W. E.; Li, J.; Johdo, O. The antitumor drug aclacinomycin A, which inhibits the degradation of ubiquitinated proteins, shows selectivity for the chymotrypsin-like activity of the bovine pituitary 20 S proteasome. J. Biol. Chem. 1996, 271, 16455-16459.
    • (1996) J. Biol. Chem , vol.271 , pp. 16455-16459
    • Figueiredo-Pereira, M.E.1    Chen, W.E.2    Li, J.3    Johdo, O.4
  • 62
    • 33646841837 scopus 로고    scopus 로고
    • Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate
    • (b) Kisselev, A. F.; Callard, A.; Goldberg, A. L. Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate. J. Biol. Chem. 2006, 281, 8582-8590.
    • (2006) J. Biol. Chem , vol.281 , pp. 8582-8590
    • Kisselev, A.F.1    Callard, A.2    Goldberg, A.L.3
  • 64
  • 65
    • 27744461250 scopus 로고    scopus 로고
    • Mishto, M.; Bellavista, E.; Santoro, A.; Stolzing, A.; Ligorio, C.; Nacmias, B.; Spazzafumo, L.; Chiappelli, M.; Licastro, F.; Sorbi, S.; Pession, A.; Ohm, T.; Grune, T.; Franceschi, C. Immunoproteasome and LMP2 polymorphism in aged and Alzheimer's disease brains. Neurobiol. Aging 2006, 27, 54-66.
    • (c) Mishto, M.; Bellavista, E.; Santoro, A.; Stolzing, A.; Ligorio, C.; Nacmias, B.; Spazzafumo, L.; Chiappelli, M.; Licastro, F.; Sorbi, S.; Pession, A.; Ohm, T.; Grune, T.; Franceschi, C. Immunoproteasome and LMP2 polymorphism in aged and Alzheimer's disease brains. Neurobiol. Aging 2006, 27, 54-66.
  • 67
    • 34247190754 scopus 로고    scopus 로고
    • LMP2-specific inhibitors: Novel chemical genetic tools for proteasome biology
    • (e) Ho, Y. K.; Bargagna-Mohan, P.; Mohan, R.; Kim, K. B. LMP2-specific inhibitors: novel chemical genetic tools for proteasome biology. Chem. Biol. 2007, 14, 419-430.
    • (2007) Chem. Biol , vol.14 , pp. 419-430
    • Ho, Y.K.1    Bargagna-Mohan, P.2    Mohan, R.3    Kim, K.B.4


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