메뉴 건너뛰기




Volumn 17, Issue 1, 2010, Pages 4-13

Therapeutic strategies within the ubiquitin proteasome system

Author keywords

DUB; E3 ligase; proteasome; small molecule inhibitor; ubiquitin

Indexed keywords

BENZODIAZEPINE; BORTEZOMIB; CARFILZOMIB; CULLIN; ENZYME INHIBITOR; LIGASE; NEDD8 PROTEIN; NEREUS; NSC 632839; PROTEASOME; PROTEASOME INHIBITOR; SALINOSPORAMIDE A; SERDEMETAN; TDP 665759; UBIQUITIN; UBIQUITIN LIGASE E1; UBIQUITIN LIGASE E2; UNCLASSIFIED DRUG; UBIQUITIN PROTEIN LIGASE;

EID: 77449103325     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2009.82     Document Type: Review
Times cited : (102)

References (88)
  • 1
    • 33748336875 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in cell cycle control
    • DOI 10.1007/b136681, Cell Cycle Regulation
    • Reed SI. The ubiquitin-proteasome pathway in cell cycle control. Results Probl Cell Differ 2006; 42: 147-181. (Pubitemid 44856951)
    • (2006) Results and Problems in Cell Differentiation , vol.42 , pp. 147-181
    • Reed, S.I.1
  • 2
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NF-kappaB pathway
    • Chen ZJ. Ubiquitin signalling in the NF-kappaB pathway. Nat Cell Biol 2005; 7: 758-765.
    • (2005) Nat Cell Biol , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 3
    • 36248988054 scopus 로고    scopus 로고
    • Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation
    • DOI 10.1016/j.semcdb.2007.09.002, PII S1084952107001486, Degredation of Misfolded Glycoproteins
    • Kostova Z, Tsai YC, Weissman AM. Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation. Semin Cell Dev Biol 2007; 18: 770-779. (Pubitemid 350138452)
    • (2007) Seminars in Cell and Developmental Biology , vol.18 , Issue.6 , pp. 770-779
    • Kostova, Z.1    Tsai, Y.C.2    Weissman, A.M.3
  • 4
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • Vembar SS, Brodsky JL. One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 2008; 9: 944-957.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 5
    • 38049150586 scopus 로고    scopus 로고
    • The DNA damage response pathways: At the crossroad of protein modifications
    • Huen MS, Chen J. The DNA damage response pathways: at the crossroad of protein modifications. Cell Res 2008; 18: 8-16.
    • (2008) Cell Res , vol.18 , pp. 8-16
    • Huen, M.S.1    Chen, J.2
  • 6
    • 33750023437 scopus 로고    scopus 로고
    • Keeping Transcriptional Activators under Control
    • DOI 10.1016/j.cell.2006.10.002, PII S0092867406012839
    • Kodadek T, Sikder D, Nalley K. Keeping transcriptional activators under control. Cell 2006; 127: 261-264. (Pubitemid 44572383)
    • (2006) Cell , vol.127 , Issue.2 , pp. 261-264
    • Kodadek, T.1    Sikder, D.2    Nalley, K.3
  • 7
    • 34250011799 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases
    • Wang J, Maldonado MA. The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases. Cell Mol Immunol 2006; 3: 255-261.
    • (2006) Cell Mol Immunol , vol.3 , pp. 255-261
    • Wang, J.1    Maldonado, M.A.2
  • 8
    • 36849043810 scopus 로고    scopus 로고
    • The role of E3 ligases in autoimmunity and the regulation of autoreactive T cells
    • DOI 10.1016/j.coi.2007.10.002, PII S0952791507001720, Autoimmunity / Allergy and Hypersenditivity
    • Lin AE, Mak TW. The role of E3 ligases in autoimmunity and the regulation of autoreactive T cells. Curr Opin Immunol 2007; 19: 665-673. (Pubitemid 350236811)
    • (2007) Current Opinion in Immunology , vol.19 , Issue.6 , pp. 665-673
    • Lin, A.E.1    Mak, T.W.2
  • 9
    • 33748991453 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins in cancer pathogenesis
    • DOI 10.1038/nrc1994, PII NRC1994
    • Hoeller D, Hecker CM, Dikic I. Ubiquitin and ubiquitin-like proteins in cancer pathogenesis. Nat Rev Cancer 2006; 6: 776-788. (Pubitemid 44450466)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.10 , pp. 776-788
    • Hoeller, D.1    Hecker, C.-M.2    Dikic, I.3
  • 10
    • 27144512435 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and neurodegenerative disorders
    • Layfield R, Lowe J, Bedford L. The ubiquitin-proteasome system and neurodegenerative disorders. Essays Biochem 2005; 41: 157-171. (Pubitemid 41500977)
    • (2005) Essays in Biochemistry , vol.41 , pp. 157-171
    • Layfield, R.1    Lowe, J.2    Bedford, L.3
  • 11
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • DOI 10.1038/nature05291, PII NATURE05291
    • Rubinsztein DC. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006; 443: 780-786. (Pubitemid 44622682)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 780-786
    • Rubinsztein, D.C.1
  • 12
    • 56449118262 scopus 로고    scopus 로고
    • Ubiquitin-like protein involved in the proteasome pathway of mycobacterium tuberculosis
    • Pearce MJ, Mintseris J, Ferreyra J, Gygi SP, Darwin KH. Ubiquitin-like protein involved in the proteasome pathway of mycobacterium tuberculosis. Science 2008; 322: 1104-1107.
    • (2008) Science , vol.322 , pp. 1104-1107
    • Pearce, M.J.1    Mintseris, J.2    Ferreyra, J.3    Gygi, S.P.4    Darwin, K.H.5
  • 14
    • 59649103156 scopus 로고    scopus 로고
    • Involvement of linear polyubiquitylation of NEMO in NF-[kappa] B activation
    • Tokunaga F, Sakata S-i, Saeki Y, Satomi Y, Kirisako T, Kamei K et al. Involvement of linear polyubiquitylation of NEMO in NF-[kappa]B activation. Nat Cell Biol 2009; 11: 123-132.
    • (2009) Nat Cell Biol , vol.11 , pp. 123-132
    • Tokunaga, F.1    S-I, S.2    Saeki, Y.3    Satomi, Y.4    Kirisako, T.5    Kamei, K.6
  • 15
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • DOI 10.1016/j.ceb.2004.02.005, PII S0955067404000146
    • Sun L, Chen ZJ. The novel functions of ubiquitination in signaling. Curr Opin Cell Biol 2004; 16: 119-126. (Pubitemid 38757287)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.2 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 16
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • DOI 10.1038/35056583
    • Hicke L. Protein regulation by monoubiquitin. Nat Rev Mol Cell Biol 2001; 2: 195-201. (Pubitemid 33675744)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.3 , pp. 195-201
    • Hicke, L.1
  • 17
    • 33750497452 scopus 로고    scopus 로고
    • Mutual regulation of conventional protein kinase C and a ubiquitin ligase complex
    • DOI 10.1016/j.bbrc.2006.09.163, PII S0006291X06022236
    • Nakamura M, Tokunaga F, Sakata S-I, Iwai K. Mutual regulation of conventional protein kinase C and a ubiquitin ligase complex. Biochem Biophys Res Commun 2006; 351: 340-347. (Pubitemid 44666695)
    • (2006) Biochemical and Biophysical Research Communications , vol.351 , Issue.2 , pp. 340-347
    • Nakamura, M.1    Tokunaga, F.2    Sakata, S.-i.3    Iwai, K.4
  • 19
    • 41549142601 scopus 로고    scopus 로고
    • Reverse the curse - The role of deubiquitination in cell cycle control
    • Song L, Rape M. Reverse the curse-the role of deubiquitination in cell cycle control. Curr Opin Cell Biol 2008; 20: 156-163.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 156-163
    • Song, L.1    Rape, M.2
  • 20
    • 0032741446 scopus 로고    scopus 로고
    • Structure of an E6AP-UbcH7 complex: Insights into ubiquitination by the E2-E3 enzyme cascade
    • Huang L, Kinnucan E, Wang G, Beaudenon S, Howley PM, Huibregtse JM et al. Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science 1999; 286: 1321-1326.
    • (1999) Science , vol.286 , pp. 1321-1326
    • Huang, L.1    Kinnucan, E.2    Wang, G.3    Beaudenon, S.4    Howley, P.M.5    Huibregtse, J.M.6
  • 21
    • 0037249354 scopus 로고    scopus 로고
    • Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase
    • DOI 10.1016/S1097-2765(02)00774-8
    • Verdecia MA, Joazeiro CA, Wells NJ, Ferrer JL, Bowman ME, Hunter T et al. Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase. Mol Cell 2003; 11: 249-259. (Pubitemid 36126605)
    • (2003) Molecular Cell , vol.11 , Issue.1 , pp. 249-259
    • Verdecia, M.A.1    Joazeiro, C.A.P.2    Wells, N.J.3    Ferrer, J.-L.4    Bowman, M.E.5    Hunter, T.6    Noel, J.P.7
  • 23
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng N, Wang P, Jeffrey PD, Pavletich NP. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 2000; 102: 533-539.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 25
    • 0027239790 scopus 로고
    • The RING finger. A novel protein sequence motif related to the zinc finger
    • Freemont PS. The RING finger. A novel protein sequence motif related to the zinc finger. Ann NY Acad Sci 1993; 684: 174-192. (Pubitemid 23218950)
    • (1993) Annals of the New York Academy of Sciences , vol.684 , pp. 174-192
    • Freemont, P.S.1
  • 26
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • DOI 10.1038/nrm1547
    • Petroski MD, Deshaies RJ. Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 2005; 6: 9-20. (Pubitemid 40064895)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.1 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 27
    • 33947261954 scopus 로고    scopus 로고
    • Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells - Evidence for cullin dimerization
    • DOI 10.1016/j.cellsig.2006.12.002, PII S0898656806003238
    • Chew E-H, Poobalasingam T, Hawkey CJ, Hagen T. Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells - evidence for cullin dimerization. Cell Signal 2007; 19: 1071-1080. (Pubitemid 46436442)
    • (2007) Cellular Signalling , vol.19 , Issue.5 , pp. 1071-1080
    • Chew, E.-H.1    Poobalasingam, T.2    Hawkey, C.J.3    Hagen, T.4
  • 28
    • 42149105590 scopus 로고    scopus 로고
    • Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans
    • DOI 10.1038/sj.cdd.4402309, PII 4402309
    • Linke K, Mace PD, Smith CA, Vaux DL, Silke J, Day CL. Structure of the MDM2//MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans. Cell Death Differ 2008; 15: 841-848. (Pubitemid 351524426)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.5 , pp. 841-848
    • Linke, K.1    Mace, P.D.2    Smith, C.A.3    Vaux, D.L.4    Silke, J.5    Day, C.L.6
  • 29
    • 0037213013 scopus 로고    scopus 로고
    • PHD domains and E3 ubiquitin ligases: Viruses make the connection
    • DOI 10.1016/S0962-8924(02)00005-3, PII S0962892402000053
    • Coscoy L, Ganem D. PHD domains and E3 ubiquitin ligases: viruses make the connection. Trends Cell Biol 2003; 13: 7-12. (Pubitemid 35453890)
    • (2003) Trends in Cell Biology , vol.13 , Issue.1 , pp. 7-12
    • Coscoy, L.1    Ganem, D.2
  • 30
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger - A common domain in ubiquitination [1]
    • DOI 10.1016/S0960-9822(00)00398-5
    • Aravind L, Koonin EV. The U box is a modified RING finger - a common domain in ubiquitination. Curr Biol 2000; 10: R132-R134. (Pubitemid 30146770)
    • (2000) Current Biology , vol.10 , Issue.4
    • Aravind, L.1    Koonin, E.V.2
  • 31
  • 32
    • 33845270990 scopus 로고    scopus 로고
    • Regulating the p53 pathway: In vitro hypotheses, in vivo veritas
    • DOI 10.1038/nrc2012, PII NRC2012
    • Toledo F, Wahl GM. Regulating the p53 pathway: in vitro hypotheses, in vivo veritas. Nat Rev Cancer 2006; 6: 909-923. (Pubitemid 44862676)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.12 , pp. 909-923
    • Toledo, F.1    Wahl, G.M.2
  • 36
    • 28844496621 scopus 로고    scopus 로고
    • High-throughput screening for inhibitors of the E3 ubiquitin ligase APC
    • DOI 10.1016/S0076-6879(05)99049-6, PII S0076687905990496, 49, Ubiquitin and Protein Degradation, Part B
    • Huang J, Sheung J, Dong G, Coquilla C, Daniel-Issakani S, Payan DG. High-throughput screening for inhibitors of the e3 ubiquitin ligase APC. Methods Enzymol 2005; 399: 740-754. (Pubitemid 41772765)
    • (2005) Methods in Enzymology , vol.399 , pp. 740-754
    • Huang, J.1    Sheung, J.2    Dong, G.3    Coquilla, C.4    Daniel-Issakani, S.5    Payan, D.G.6
  • 37
    • 28844486027 scopus 로고    scopus 로고
    • β-Trcp1-mediated IκBα ubiquitination assay for high-throughput screen
    • DOI 10.1016/S0076-6879(05)99048-4, PII S0076687905990484, 48, Ubiquitin and Protein Degradation, Part B
    • Xu S, Patel P, Abbasian M, Giegel D, Xie W, Mercurio F et al. In vitro SCFbeta-Trcp1- mediated IkappaBalpha ubiquitination assay for high-throughput screen. Methods Enzymol 2005; 399: 729-740. (Pubitemid 41772764)
    • (2005) Methods in Enzymology , vol.399 , pp. 729-740
    • Xu, S.1    Patel, P.2    Abbasian, M.3    Giegel, D.4    Xie, W.5    Mercurio, F.6    Cox, S.7
  • 40
    • 33644873086 scopus 로고    scopus 로고
    • Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo
    • Koblish HK, Zhao S, Franks CF, Donatelli RR, Tominovich RM, LaFrance LV et al. Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo. Mol Cancer Therapeut 2006; 5: 160-169.
    • (2006) Mol Cancer Therapeut , vol.5 , pp. 160-169
    • Koblish, H.K.1    Zhao, S.2    Franks, C.F.3    Donatelli, R.R.4    Tominovich, R.M.5    Lafrance, L.V.6
  • 42
    • 34347329214 scopus 로고    scopus 로고
    • Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging
    • DOI 10.1038/nature05902, PII NATURE05902
    • Jin J, Li X, Gygi SP, Harper JW. Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging. Nature 2007; 447: 1135-1138. (Pubitemid 47014428)
    • (2007) Nature , vol.447 , Issue.7148 , pp. 1135-1138
    • Jin, J.1    Li, X.2    Gygi, S.P.3    Harper, J.W.4
  • 44
    • 34748884321 scopus 로고    scopus 로고
    • E1-L2 Activates Both Ubiquitin and FAT10
    • DOI 10.1016/j.molcel.2007.08.020, PII S1097276507005849
    • Chiu YH, Sun Q, Chen ZJ. E1-L2 activates both ubiquitin and FAT10. Mol Cell 2007; 27: 1014-1023. (Pubitemid 47488190)
    • (2007) Molecular Cell , vol.27 , Issue.6 , pp. 1014-1023
    • Chiu, Y.-H.1    Sun, Q.2    Chen, Z.J.3
  • 45
    • 20444456668 scopus 로고    scopus 로고
    • Crystal structure of a fragment of mouse ubiquitin-activating enzyme
    • DOI 10.1074/jbc.M502583200
    • Szczepanowski RH, Filipek R, Bochtler M. Crystal structure of a fragment of mouse ubiquitin-activating enzyme. J Biol Chem 2005; 280: 22006-22011. (Pubitemid 40827854)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.23 , pp. 22006-22011
    • Szczepanowski, R.H.1    Filipek, R.2    Bochtler, M.3
  • 48
    • 9644281548 scopus 로고    scopus 로고
    • Himeic acid A: A new ubiquitin-activating enzyme inhibitor isolated from a marine-derived fungus, Aspergillus sp
    • DOI 10.1016/j.bmcl.2004.10.012, PII S0960894X04012363
    • Tsukamoto S, Hirota H, Imachi M, Fujimuro M, Onuki H, Ohta T et al. Himeic acid A: a new ubiquitin-activating enzyme inhibitor isolated from a marine-derived fungus, Aspergillus sp. Bioorg Med Chem Lett 2005; 15: 191-194. (Pubitemid 39575810)
    • (2005) Bioorganic and Medicinal Chemistry Letters , vol.15 , Issue.1 , pp. 191-194
    • Tsukamoto, S.1    Hirota, H.2    Imachi, M.3    Fujimuro, M.4    Onuki, H.5    Ohta, T.6    Yokosawa, H.7
  • 50
    • 0037077232 scopus 로고    scopus 로고
    • Structural and functional analysis of the human mitotic-specific ubiquitin-conjugating enzyme, UbcH10
    • DOI 10.1074/jbc.M109398200
    • Lin Y, Hwang WC, Basavappa R. Structural and functional analysis of the human mitotic-specific ubiquitin-conjugating enzyme, UbcH10. J Biol Chem 2002; 277: 21913-21921. (Pubitemid 34952345)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21913-21921
    • Lin, Y.1    Hwang, W.C.2    Basavappa, R.3
  • 54
    • 53249154203 scopus 로고    scopus 로고
    • Function and regulation of protein neddylation 'Protein modifications: Beyond the usual suspects' review series
    • Rabut G, Peter M. Function and regulation of protein neddylation. 'Protein modifications: beyond the usual suspects' review series. EMBO Rep 2008; 9: 969-976.
    • (2008) EMBO Rep , vol.9 , pp. 969-976
    • Rabut, G.1    Peter, M.2
  • 55
    • 60549091914 scopus 로고    scopus 로고
    • E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification
    • Huang DT, Ayrault O, Hunt HW, Taherbhoy AM, Duda DM, Scott DC et al. E2-RING Expansion of the NEDD8 Cascade Confers Specificity to Cullin Modification. Mol Cell 2009; 33: 483-495.
    • (2009) Mol Cell , vol.33 , pp. 483-495
    • Huang, D.T.1    Ayrault, O.2    Hunt, H.W.3    Taherbhoy, A.M.4    Duda, D.M.5    Scott, D.C.6
  • 56
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell 2008; 134: 995-1006.
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 57
    • 53349121021 scopus 로고    scopus 로고
    • Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation
    • Saha A, Deshaies RJ. Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol Cell 2008; 32: 21-31.
    • (2008) Mol Cell , vol.32 , pp. 21-31
    • Saha, A.1    Deshaies, R.J.2
  • 59
    • 60649088334 scopus 로고    scopus 로고
    • Ginkgolic acid inhibits protein SUMOylation by blocking formation of the E1-SUMO intermediate
    • Fukuda I, Ito A, Hirai G, Nishimura S, Kawasaki H, Saitoh H et al. Ginkgolic acid inhibits protein SUMOylation by blocking formation of the E1-SUMO intermediate. Chem Biol 2009; 16: 133-140.
    • (2009) Chem Biol , vol.16 , pp. 133-140
    • Fukuda, I.1    Ito, A.2    Hirai, G.3    Nishimura, S.4    Kawasaki, H.5    Saitoh, H.6
  • 60
    • 33745728140 scopus 로고    scopus 로고
    • Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132
    • Crawford LJ, Walker B, Ovaa H, Chauhan D, Anderson KC, Morris TC et al. Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132. Cancer Res 2006; 66: 6379-6386.
    • (2006) Cancer Res , vol.66 , pp. 6379-6386
    • Crawford, L.J.1    Walker, B.2    Ovaa, H.3    Chauhan, D.4    Anderson, K.C.5    Morris, T.C.6
  • 62
    • 41549133200 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy: Lessons from the first decade
    • DOI 10.1158/1078-0432.CCR-07-2218
    • Orlowski RZ, Kuhn DJ. Proteasome inhibitors in cancer therapy: lessons from the first decade. Clin Cancer Res 2008; 14: 1649-1657. (Pubitemid 351469448)
    • (2008) Clinical Cancer Research , vol.14 , Issue.6 , pp. 1649-1657
    • Orlowski, R.Z.1    Kuhn, D.J.2
  • 64
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • DOI 10.1128/MCB.22.13.4902-4913.2002
    • Chen L, Madura K. Rad23 promotes the targeting of proteolytic substrates to the proteasome. Mol Cell Biol 2002; 22: 4902-4913. (Pubitemid 34620423)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.13 , pp. 4902-4913
    • Chen, L.1    Madura, K.2
  • 66
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • DOI 10.1016/j.cell.2004.06.014, PII S0092867404005835
    • Verma R, Oania R, Graumann J, Deshaies RJ. Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 2004; 118: 99-110. (Pubitemid 38902817)
    • (2004) Cell , vol.118 , Issue.1 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 68
    • 33749482993 scopus 로고    scopus 로고
    • Identification of new compounds that trigger apoptosome-independent caspase activation and apoptosis
    • DOI 10.1158/0008-5472.CAN-06-0702
    • Aleo E, Henderson CJ, Fontanini A, Solazzo B, Brancolini C. Identification of new compounds that trigger apoptosome-independent caspase activation and apoptosis. Cancer Res 2006; 66: 9235-9244. (Pubitemid 44521145)
    • (2006) Cancer Research , vol.66 , Issue.18 , pp. 9235-9244
    • Aleo, E.1    Henderson, C.J.2    Fontanini, A.3    Solazzo, B.4    Brancolini, C.5
  • 71
    • 1642575095 scopus 로고    scopus 로고
    • Degradation of target protein in living cells by small-molecule proteolysis inducer
    • DOI 10.1016/j.bmcl.2003.11.042
    • Zhang D, Baek SH, Ho A, Kim K. Degradation of target protein in living cells by smallmolecule proteolysis inducer. Bioorg Med Chem Lett 2004; 14: 645-648. (Pubitemid 38114844)
    • (2004) Bioorganic and Medicinal Chemistry Letters , vol.14 , Issue.3 , pp. 645-648
    • Zhang, D.1    Baek, S.-H.2    Ho, A.3    Kim, K.4
  • 72
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • DOI 10.1126/science.274.5289.948
    • Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ et al. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 1996; 274: 948-953. (Pubitemid 26398409)
    • (1996) Science , vol.274 , Issue.5289 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3    Elenbaas, B.4    Moreau, J.5    Levine, A.J.6    Pavletich, N.P.7
  • 73
    • 36248989248 scopus 로고    scopus 로고
    • The Nedd4-like family of E3 ubiquitin ligases and cancer
    • DOI 10.1007/s10555-007-9091-x, Forty Years of Metastasis Research: A Tribute to Dr. Isaiah J. Fidler
    • Chen C, Matesic LE. The Nedd4-like family of E3 ubiquitin ligases and cancer. Cancer Metastasis Rev 2007; 26: 587-604. (Pubitemid 350119775)
    • (2007) Cancer and Metastasis Reviews , vol.26 , Issue.3-4 , pp. 587-604
    • Chen, C.1    Matesic, L.E.2
  • 74
    • 21244451434 scopus 로고    scopus 로고
    • ARF-BP1/mule is a critical mediator of the ARF tumor suppressor
    • DOI 10.1016/j.cell.2005.03.037, PII S0092867405003569
    • Chen D, Kon N, Li M, Zhang W, Qin J, Gu W. ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 2005; 121: 1071-1083. (Pubitemid 40884397)
    • (2005) Cell , vol.121 , Issue.7 , pp. 1071-1083
    • Chen, D.1    Kon, N.2    Li, M.3    Zhang, W.4    Qin, J.5    Gu, W.6
  • 76
    • 54249105821 scopus 로고    scopus 로고
    • HPV E6 E6AP and cervical cancer
    • Beaudenon S, Huibregtse JM. HPV E6, E6AP and cervical cancer. BMC Biochem 2008; 9 (Suppl 1): S4.
    • (2008) BMC Biochem , vol.9 , Issue.SUPPL. 1
    • Beaudenon, S.1    Huibregtse, J.M.2
  • 78
    • 4444229048 scopus 로고    scopus 로고
    • Overexpression, genomic amplification and therapeutic potential of inhibiting the UbcH10 ubiquitin conjugase in human carcinomas of diverse anatomic origin
    • DOI 10.1038/sj.onc.1207861
    • Wagner KW, Sapinoso LM, El-Rifai W, Frierson HF, Butz N, Mestan J et al. Overexpression, genomic amplification and therapeutic potential of inhibiting the UbcH10 ubiquitin conjugase in human carcinomas of diverse anatomic origin. Oncogene 2004; 23: 6621-6629. (Pubitemid 39265525)
    • (2004) Oncogene , vol.23 , Issue.39 , pp. 6621-6629
    • Wagner, K.W.1    Sapinoso, L.M.2    El-Rifai, W.3    Frierson Jr., H.F.4    Butz, N.5    Mestan, J.6    Hofmann, F.7    Deveraux, Q.L.8    Hampton, G.M.9
  • 79
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • DOI 10.1016/S1097-2765(04)00157-1, PII S1097276504001571
    • Li M, Brooks CL, Kon N, Gu W. A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol Cell 2004; 13: 879-886. (Pubitemid 38438482)
    • (2004) Molecular Cell , vol.13 , Issue.6 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 84
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • DOI 10.1083/jcb.200401141
    • McCullough J, Clague MJ, Urbe S. AMSH is an endosome-associated ubiquitin isopeptidase. J Cell Biol 2004; 166: 487-492. (Pubitemid 39097168)
    • (2004) Journal of Cell Biology , vol.166 , Issue.4 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbe, S.3
  • 85
    • 17644421091 scopus 로고    scopus 로고
    • VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1α
    • DOI 10.1038/sj.embor.7400377
    • Li Z, Wang D, Messing EM, Wu G. VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha. EMBO Rep 2005; 6: 373-378. (Pubitemid 40561631)
    • (2005) EMBO Reports , vol.6 , Issue.4 , pp. 373-378
    • Li, Z.1    Wang, D.2    Messing, E.M.3    Wu, G.4
  • 87
    • 27944431658 scopus 로고    scopus 로고
    • Bortezomib, a novel proteasome inhibitor, in the treatment of hematologic malignancies
    • DOI 10.1016/j.ctrv.2005.10.001, PII S0305737205001994
    • Jackson G, Einsele H, Moreau P, Miguel JS. Bortezomib, a novel proteasome inhibitor, in the treatment of hematologic malignancies. Cancer Treat Rev 2005; 31: 591-602. (Pubitemid 41662886)
    • (2005) Cancer Treatment Reviews , vol.31 , Issue.8 , pp. 591-602
    • Jackson, G.1    Einsele, H.2    Moreau, P.3    San Miguel, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.