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Volumn 2, Issue 6, 2003, Pages 623-629

Targeting E3 ubiquitin ligases for cancer therapy

(1)  Sun, Yi a  

a NONE

Author keywords

Apoptosis; Cancer targets; Drug discovery; E3 ubiquitin ligases; High throughput screening; Protein degradation

Indexed keywords

ANTINEOPLASTIC AGENT; CYSTEINE PROTEINASE; ENZYME INHIBITOR; LIGASE; MULTIENZYME COMPLEX; PROTEASOME; UBIQUITIN;

EID: 2642559887     PISSN: 15384047     EISSN: 15558576     Source Type: Journal    
DOI: 10.4161/cbt.2.6.677     Document Type: Review
Times cited : (137)

References (106)
  • 1
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • DOI 10.1093/emboj/17.24.7151
    • Ciechanover A. The ubiquitin-proteasome pathway: On protein death and cell life. EMBO J 1998; 17:7151-60. (Pubitemid 29002684)
    • (1998) EMBO Journal , vol.17 , Issue.24 , pp. 7151-7160
    • Ciechanover, A.1
  • 3
    • 0037719729 scopus 로고    scopus 로고
    • The N-end rule and regulation of apoptosis
    • Varshavsky A. The N-end rule and regulation of apoptosis. Nat Cell Biol 2003; 5:373-6.
    • (2003) Nat Cell Biol , vol.5 , pp. 373-376
    • Varshavsky, A.1
  • 4
    • 0030632048 scopus 로고    scopus 로고
    • The N-end rule pathway of protein degradation
    • Varshavsky A. The N-end rule pathway of protein degradation. Genes Cells 1997; 2:13-28. (Pubitemid 127688555)
    • (1997) Genes to Cells , vol.2 , Issue.1 , pp. 13-28
    • Varshavsky, A.1
  • 5
    • 0037936841 scopus 로고    scopus 로고
    • Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis
    • DOI 10.1038/ncb984
    • Ditzel M, Wilson R, Tenev T, Zachariou A, Paul A, Deas E, et al. Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis. Nat Cell Biol 2003; 5:467-73. (Pubitemid 36592271)
    • (2003) Nature Cell Biology , vol.5 , Issue.5 , pp. 467-473
    • Ditzel, M.1    Wilson, R.2    Tenev, T.3    Zachariou, A.4    Paul, A.5    Deas, E.6    Meier, P.7
  • 6
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • DOI 10.1016/0092-8674(93)90384-3
    • Scheffner M, Huibregtse JM, Vierstra RD, Howley PM. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 1993; 75:495-505. (Pubitemid 23335075)
    • (1993) Cell , vol.75 , Issue.3 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 7
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner M, Nuber U, Huibregtse JM. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature 1995; 373:81-3.
    • (1995) Nature , vol.373 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 8
    • 0032524621 scopus 로고    scopus 로고
    • Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7
    • DOI 10.1074/jbc.273.20.12148
    • Schwarz SE, Rosa JL, Scheffner M. Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. J Biol Chem 1998; 273:12148-54. (Pubitemid 28240577)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.20 , pp. 12148-12154
    • Schwarz, S.E.1    Rosa, J.L.2    Scheffner, M.3
  • 9
    • 0033961923 scopus 로고    scopus 로고
    • RING for destruction?
    • Freemont PS. RING for destruction? Curr Biol 2000; 10:R84-7.
    • (2000) Curr Biol , vol.10
    • Freemont, P.S.1
  • 13
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro CA, Weissman AM. RING finger proteins: Mediators of ubiquitin ligase activity. Cell 2000; 102:549-52.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 14
    • 0037331103 scopus 로고    scopus 로고
    • RING finger ubiquitin protein ligases: Implications for tumorigenesis, metastasis and for molecular targets in cancer
    • DOI 10.1016/S1044-579X(02)00095-0, PII S1044579X02000950
    • Fang S, Lorick KL, Jensen JP, Weissman AM. RING finger ubiquitin protein ligases: Implications for tumorigenesis, metastasis and for molecular targets in cancer. Semin Cancer Biol 2003; 13:5-14. (Pubitemid 36269176)
    • (2003) Seminars in Cancer Biology , vol.13 , Issue.1 , pp. 5-14
    • Fang, S.1    Lorick, K.L.2    Jensen, J.P.3    Weissman, A.M.4
  • 15
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger - A common domain in ubiquitination
    • Aravind L, Koonin EV. The U box is a modified RING finger - a common domain in ubiquitination. Curr Biol 2000; 10:R132-4.
    • (2000) Curr Biol , vol.10
    • Aravind, L.1    Koonin, E.V.2
  • 16
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • Jiang J, Ballinger CA, Wu Y, Dai Q, Cyr DM, Hohfeld J, et al. CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation. J Biol Chem 2001; 276:42938-44.
    • (2001) J Biol Chem , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6
  • 18
    • 0036279167 scopus 로고    scopus 로고
    • The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2
    • DOI 10.1016/S1097-2765(02)00519-1
    • Lu Z, Xu S, Joazeiro C, Cobb MH, Hunter T. The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2. Mol Cell 2002; 9:945-56. (Pubitemid 34626666)
    • (2002) Molecular Cell , vol.9 , Issue.5 , pp. 945-956
    • Lu, Z.1    Xu, S.2    Joazeiro, C.3    Cobb, M.H.4    Hunter, T.5
  • 19
    • 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
  • 20
    • 0023339504 scopus 로고
    • Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line
    • Cahilly-Snyder L, Yang-Feng T, Francke U, George DL. Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line. Somat Cell Mol Genet 1987; 13:235-44.
    • (1987) Somat Cell Mol Genet , vol.13 , pp. 235-244
    • Cahilly-Snyder, L.1    Yang-Feng, T.2    Francke, U.3    George, D.L.4
  • 22
    • 0034044571 scopus 로고    scopus 로고
    • MDM2 oncogene as a novel target for human cancer therapy
    • Zhang, Wang H. MDM2 oncogene as a novel target for human cancer therapy. Curr Pharm Des 2000; 6:393-416.
    • (2000) Curr Pharm des , vol.6 , pp. 393-416
    • Zhang1    Wang, H.2
  • 24
    • 0028071555 scopus 로고
    • Mutations in the p53 tumor suppressor gene: Clues to cancer etiology and molecular pathogenesis
    • Greenblatt MS, Bennett WP, Hollstein M, Harris CC. Mutations in the p53 tumor suppressor gene: Clues to cancer etiology and molecular pathogenesis. Cancer Res 1994; 54:4855-78. (Pubitemid 24289415)
    • (1994) Cancer Research , vol.54 , Issue.18 , pp. 4855-4878
    • Greenblatt, M.S.1    Bennett, W.P.2    Hollstein, M.3    Harris, C.C.4
  • 25
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: Emerging patterns from divergent signals
    • Giaccia AJ, Kastan MB. The complexity of p53 modulation: Emerging patterns from divergent signals. Genes Dev 1998; 12:2973-83. (Pubitemid 28469299)
    • (1998) Genes and Development , vol.12 , Issue.19 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 27
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • DOI 10.1038/387296a0
    • Haupt Y, Maya R, Kazaz A, Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997; 387:296-9. (Pubitemid 27220766)
    • (1997) Nature , vol.387 , Issue.6630 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 28
  • 29
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • DOI 10.1016/S0014-5793(97)01480-4, PII S0014579397014804
    • Honda R, Tanaka H, Yasuda H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett 1997; 420:25-7. (Pubitemid 28037193)
    • (1997) FEBS Letters , vol.420 , Issue.1 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 30
    • 0034624678 scopus 로고    scopus 로고
    • Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase
    • Honda R, Yasuda H. Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase. Oncogene 2000; 19:1473-6. (Pubitemid 30171179)
    • (2000) Oncogene , vol.19 , Issue.11 , pp. 1473-1476
    • Honda, R.1    Yasuda, H.2
  • 31
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R, Wagner DS, Lozano G. Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 1995; 378:203-6.
    • (1995) Nature , vol.378 , pp. 203-206
    • Montes De Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 32
    • 0034704923 scopus 로고    scopus 로고
    • The loss of mdm2 induces p53 mediated apoptosis
    • de Rozieres S, Maya R, Oren M, Lozano G. The loss of mdm2 induces p53-mediated apoptosis. Oncogene 2000; 19:1691-7. (Pubitemid 30200971)
    • (2000) Oncogene , vol.19 , Issue.13 , pp. 1691-1697
    • De Rozieres, S.1    Maya, R.2    Oren, M.3    Lozano, G.4
  • 33
    • 0034644506 scopus 로고    scopus 로고
    • Opposing effects of Ras on p53: Transcriptional activation of mdm2 and induction of p19ARF
    • Ries S, Biederer C, Woods D, Shifman O, Shirasawa S, Sasazuki T, et al. Opposing effects of Ras on p53: Transcriptional activation of mdm2 and induction of p19ARF. Cell 2000; 103:321-30.
    • (2000) Cell , vol.103 , pp. 321-330
    • Ries, S.1    Biederer, C.2    Woods, D.3    Shifman, O.4    Shirasawa, S.5    Sasazuki, T.6
  • 34
    • 0032893878 scopus 로고    scopus 로고
    • Regulation of the p53 protein by the MDM2 oncoprotein - Thirty-eighth G. H. A. Clowes Memorial Award lecture
    • Freedman DA, Levine AJ. Regulation of the p53 protein by the MDM2 oncoprotein - thirty-eighth G.H.A. Clowes Memorial Award Lecture. Cancer Res 1999; 59:1-7. (Pubitemid 29062945)
    • (1999) Cancer Research , vol.59 , Issue.1 , pp. 1-7
    • Freedman, D.A.1    Levine, A.J.2
  • 36
    • 0037423446 scopus 로고    scopus 로고
    • Binding of an inhibitor of the p53/MDM2 interaction to MDM2
    • Duncan SJ, Cooper MA, Williams DH. Binding of an inhibitor of the p53/MDM2 interaction to MDM2. Chem Commun (Camb) 2003: 316-7. (Pubitemid 36207694)
    • (2003) Chemical Communications , Issue.3 , pp. 316-317
    • Duncan, S.J.1    Cooper, M.A.2    Williams, D.H.3
  • 37
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways
    • DOI 10.1016/S0092-8674(00)81401-4
    • Zhang Y, Xiong Y, Yarbrough WG. ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways. Cell 1998; 92:725-34. (Pubitemid 28155312)
    • (1998) Cell , vol.92 , Issue.6 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3
  • 38
    • 0034603897 scopus 로고    scopus 로고
    • An N-terminal p14(ARF) peptide blocks Mdm2-dependent ubiquinitation in vitro and can activate p53 in vivo
    • Midgley CA, Desterro JM, Saville MK, Howard S, Sparks A, Hay RT, et al. An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo. Oncogene 2000; 19:2312-23. (Pubitemid 30307207)
    • (2000) Oncogene , vol.19 , Issue.19 , pp. 2312-2323
    • Midgley, C.A.1    Desterro, J.M.2    Saville, M.K.3    Howard, S.4    Sparks, A.5    Hay, R.T.6    Lane, D.P.7
  • 39
    • 0036042573 scopus 로고    scopus 로고
    • Anti-tumor efficacy of a novel antisense anti-MDM2 mixed-backbone oligonucleotide in human colon cancer models: p53-dependent and p53-independent mechanisms
    • Wang H, Nan L, Yu D, Lindsey JR, Agrawal S, Zhang R. Anti-tumor efficacy of a novel antisense anti-MDM2 mixed-backbone oligonucleotide in human colon cancer models: p53-dependent and p53- independent mechanisms. Mol Med 2002; 8:185-99. (Pubitemid 35013750)
    • (2002) Molecular Medicine , vol.8 , Issue.4 , pp. 185-199
    • Wang, H.1    Nan, L.2    Yu, D.3    Lindsey, J.R.4    Agrawal, S.5    Zhang, R.6
  • 40
    • 0037441417 scopus 로고    scopus 로고
    • Experimental therapy of human prostate cancer by inhibiting MDM2 expression with novel mixed-backbone antisense oligonucleotides: In vitro and in vivo activities and mechanisms
    • DOI 10.1002/pros.10187
    • Wang H, Yu D, Agrawal S, Zhang R. Experimental therapy of human prostate cancer by inhibiting MDM2 expression with novel mixed-backbone antisense oligonucleotides: In vitro and in vivo activities and mechanisms. Prostate 2003; 54:194-205. (Pubitemid 36120317)
    • (2003) Prostate , vol.54 , Issue.3 , pp. 194-205
    • Wang, H.1    Yu, D.2    Agrawal, S.3    Zhang, R.4
  • 44
    • 0029028354 scopus 로고
    • Interaction between the retinoblastoma protein and the oncoprotein MDM2
    • Xiao ZX, Chen J, Levine AJ, Modjtahedi N, Xing J, Sellers WR, et al. Interaction between the retinoblastoma protein and the oncoprotein MDM2. Nature 1995; 375:694-8.
    • (1995) Nature , vol.375 , pp. 694-698
    • Xiao, Z.X.1    Chen, J.2    Levine, A.J.3    Modjtahedi, N.4    Xing, J.5    Sellers, W.R.6
  • 45
  • 47
    • 0042530220 scopus 로고    scopus 로고
    • Mdm2 ligase dead mutants did not act in a dominant negative manner to re-activate p53, but promoted tumor cell growth
    • Swaroop M, Sun Y. Mdm2 ligase dead mutants did not act in a dominant negative manner to reactivate p53, but promoted tumor cell growth. Anticancer Res 2003; 23:3167-74. (Pubitemid 36975410)
    • (2003) Anticancer Research , vol.23 , Issue.4 , pp. 3167-3174
    • Swaroop, M.1    Sun, Y.2
  • 48
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins - Suppressors of apoptosis
    • Deveraux QL, Reed JC. IAP family proteins - suppressors of apoptosis. Genes Dev 1999; 13:239-52. (Pubitemid 29095796)
    • (1999) Genes and Development , vol.13 , Issue.3 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 49
    • 0034278085 scopus 로고    scopus 로고
    • The IAP family: Endogenous caspase inhibitors with multiple biological activities
    • Yang YL, Li XM. The IAP family: Endogenous caspase inhibitors with multiple biological activities. Cell Res 2000; 10:169-77.
    • (2000) Cell Res , vol.10 , pp. 169-177
    • Yang, Y.L.1    Li, X.M.2
  • 51
    • 0035917851 scopus 로고    scopus 로고
    • Two splicing variants of a new inhibitor of apoptosis gene with different biological properties and tissue distribution pattern
    • DOI 10.1016/S0014-5793(01)02366-3, PII S0014579301023663
    • Ashhab Y, Alian A, Polliack A, Panet A, Yehuda DB. Two splicing variants of a new inhibitor of apoptosis gene with different biological properties and tissue distribution pattern. FEBS Lett 2001; 495:56-60. (Pubitemid 32367973)
    • (2001) FEBS Letters , vol.495 , Issue.1-2 , pp. 56-60
    • Ashhab, Y.1    Alian, A.2    Polliack, A.3    Panet, A.4    Yehuda, D.B.5
  • 52
    • 0034597630 scopus 로고    scopus 로고
    • ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas
    • Vucic D, Stennicke HR, Pisabarro MT, Salvesen GS, Dixit VM. ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas. Curr Biol 2000; 10:1359-66.
    • (2000) Curr Biol , vol.10 , pp. 1359-1366
    • Vucic, D.1    Stennicke, H.R.2    Pisabarro, M.T.3    Salvesen, G.S.4    Dixit, V.M.5
  • 53
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • DOI 10.1016/S1097-2765(02)00482-3
    • Shi Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol Cell 2002; 9:459-70. (Pubitemid 34273778)
    • (2002) Molecular Cell , vol.9 , Issue.3 , pp. 459-470
    • Shi, Y.1
  • 54
    • 0035920126 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and - 7 in distinct modes
    • Suzuki Y, Nakabayashi Y, Nakata K, Reed JC, Takahashi R. X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and - 7 in distinct modes. J Biol Chem 2001; 276:27058-63.
    • (2001) J Biol Chem , vol.276 , pp. 27058-27063
    • Suzuki, Y.1    Nakabayashi, Y.2    Nakata, K.3    Reed, J.C.4    Takahashi, R.5
  • 55
    • 0035902601 scopus 로고    scopus 로고
    • Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death
    • DOI 10.1073/pnas.161506698
    • Suzuki Y, Nakabayashi Y, Takahashi R. Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. Proc Natl Acad Sci USA 2001; 98:8662-7. (Pubitemid 32678084)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.15 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 56
    • 0034282432 scopus 로고    scopus 로고
    • The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7
    • Huang H, Joazeiro CA, Bonfoco E, Kamada S, Leverson JD, Hunter T. The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7. J Biol Chem 2000; 275:26661-4.
    • (2000) J Biol Chem , vol.275 , pp. 26661-26664
    • Huang, H.1    Joazeiro, C.A.2    Bonfoco, E.3    Kamada, S.4    Leverson, J.D.5    Hunter, T.6
  • 57
    • 0037267333 scopus 로고    scopus 로고
    • Validating survivin as a cancer therapeutic target
    • DOI 10.1038/nrc968
    • Altieri DC. Validating survivin as a cancer therapeutic target. Nat Rev Cancer 2003; 3:46-54. (Pubitemid 37328886)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.1 , pp. 46-54
    • Altieri, D.C.1
  • 58
    • 0034905394 scopus 로고    scopus 로고
    • XIAP: Apoptotic brake and promising therapeutic target
    • DOI 10.1023/A:1011379307472
    • Holcik M, Gibson H, Korneluk RG. XIAP: Apoptotic brake and promising therapeutic target. Apoptosis 2001; 6:253-61. (Pubitemid 32708519)
    • (2001) Apoptosis , vol.6 , Issue.4 , pp. 253-261
    • Holcik, M.1    Gibson, H.2    Korneluk, R.G.3
  • 59
    • 0036733756 scopus 로고    scopus 로고
    • Expression of cIAP1, a target for 11q22 amplification, correlates with resistance of cervical cancers to radiotherapy
    • Imoto I, Tsuda H, Hirasawa A, Miura M, Sakamoto M, Hirohashi S, et al. Expression of cIAP1, a target for 11q22 amplification, correlates with resistance of cervical cancers to radiotherapy. Cancer Res 2002; 2:4860-6. (Pubitemid 34984404)
    • (2002) Cancer Research , vol.62 , Issue.17 , pp. 4860-4866
    • Imoto, I.1    Tsuda, H.2    Hirasawa, A.3    Miura, M.4    Sakamoto, M.5    Hirohashi, S.6    Inazawa, J.7
  • 60
    • 0034700491 scopus 로고    scopus 로고
    • Structural basis of IAP recognition by Smac/DIABLO
    • DOI 10.1038/35050012
    • Wu G, Chai J, Suber TL, Wu JW, Du C, Wang X, Shi Y. Structural basis of IAP recognition by Smac/DIABLO. Nature 2000; 08:1008-12. (Pubitemid 32101651)
    • (2000) Nature , vol.408 , Issue.6815 , pp. 1008-1012
    • Wu, G.1    Chai, J.2    Suber, T.L.3    Wu, J.-W.4    Du, C.5    Wang, X.6    Shi, Y.7
  • 61
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • DOI 10.1038/35022514
    • Chai J, Du C, Wu JW, Kyin S, Wang X, Shi Y. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 2000; 06:855-62. (Pubitemid 30664254)
    • (2000) Nature , vol.406 , Issue.6798 , pp. 855-862
    • Chai, J.1    Du, C.2    Wu, J.-W.3    Kyin, S.4    Wang, X.5    Shi, Y.6
  • 62
    • 0037855783 scopus 로고    scopus 로고
    • Cellular inhibitor of apoptosis 1 and 2 are ubiquitin ligases for the apoptosis inducer Smac/DIABLO
    • DOI 10.1074/jbc.M207197200
    • Hu S, Yang X. Cellular Inhibitor of Apoptosis 1 and 2 Are Ubiquitin Ligases for the Apoptosis Inducer Smac/DIABLO. J Biol Chem 2003; 78:10055-60. (Pubitemid 36800260)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.12 , pp. 10055-10060
    • Hu, S.1    Yang, X.2
  • 63
    • 0037184113 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro
    • MacFarlane M, Merrison W, Bratton SB, Cohen GM. Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro. J Biol Chem 2002; 77:36611-6.
    • (2002) J Biol Chem , vol.77 , pp. 36611-36616
    • MacFarlane, M.1    Merrison, W.2    Bratton, S.B.3    Cohen, G.M.4
  • 64
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • DOI 10.1126/science.288.5467.874
    • Yang Y, Fang S, Jensen JP, Weissman AM, Ashwell JD. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 2000; 88:874-7. (Pubitemid 30257739)
    • (2000) Science , vol.288 , Issue.5467 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 66
    • 0034667372 scopus 로고    scopus 로고
    • Down-regulation of X-linked inhibitor of apoptosis protein induces apoptosis in chemoresistant human ovarian cancer cells
    • 0
    • Sasaki H, Sheng Y, Kotsuji F, Tsang BK. Down-regulation of X-linked inhibitor of apoptosis protein induces apoptosis in chemoresistant human ovarian cancer cells. Cancer Res 2000; 0:5659-66.
    • (2000) Cancer Res , pp. 5659-5666
    • Sasaki, H.1    Sheng, Y.2    Kotsuji, F.3    Tsang, B.K.4
  • 68
    • 0342657718 scopus 로고    scopus 로고
    • A novel antisense oligonucleotide targeting survivin expression induces apoptosis and sensitizes lung cancer cells to chemotherapy
    • Olie RA, Simoes-Wust AP, Baumann B, Leech SH, Fabbro D, Stahel RA, et al. A novel antisense oligonucleotide targeting survivin expression induces apoptosis and sensitizes lung cancer cells to chemotherapy. Cancer Res 2000; 60:2805-9. (Pubitemid 30395796)
    • (2000) Cancer Research , vol.60 , Issue.11 , pp. 2805-2809
    • Olie, R.A.1    Simoes-Wust, A.P.2    Baumann, B.3    Leech, S.H.4    Fabbro, D.5    Stahel, R.A.6    Zangemeister-Wittke, U.7
  • 69
    • 0037478904 scopus 로고    scopus 로고
    • Antisense oligonucleotides targeting XIAP induce apoptosis and enhance chemotherapeutic activity against human lung cancer cells in vitro and in vivo
    • Hu Y, Cherton-Horvat G, Dragowska V, Baird S, Korneluk RG, Durkin JP, et al. ntisense oligonucleotides targeting XIAP induce apoptosis and enhance chemotherapeutic activity against human lung cancer cells in vitro and in vivo. Clin Cancer Res 2003; 9:2826-36. (Pubitemid 36842129)
    • (2003) Clinical Cancer Research , vol.9 , Issue.7 , pp. 2826-2836
    • Hu, Y.P.1    Cherton-Horvat, G.2    Dragowska, V.3    Baird, S.4    Korneluk, R.G.5    Durkin, J.P.6    Mayer, L.D.7    LaCasse, E.C.8
  • 70
    • 0036341291 scopus 로고    scopus 로고
    • Smac agonists sensitize for Apo2L/TRAIL- Or anticancer drug-induced apoptosis and induce regression of malignant glioma in vivo
    • Fulda S, Wick W, Weller M, Debatin KM. Smac agonists sensitize for Apo2L/TRAIL- or anticancer drug-induced apoptosis and induce regression of malignant glioma in vivo. Nat Med 2002; 8:808-15.
    • (2002) Nat Med , vol.8 , pp. 808-815
    • Fulda, S.1    Wick, W.2    Weller, M.3    Debatin, K.M.4
  • 71
    • 0347895102 scopus 로고    scopus 로고
    • Synthetic Smac/DIABLO peptides enhance the effects of chemotherapeutic agents by binding XIAP and cIAP1 in situ
    • DOI 10.1074/jbc.M207578200
    • Arnt CR, Chiorean MV, Heldebrant MP, Gores GJ, Kaufmann SH. Synthetic Smac/DIABLO peptides enhance the effects of chemotherapeutic agents by binding XIAP and cIAP1 in situ. J Biol Chem 2002; 277:44236-43. (Pubitemid 36157856)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 44236-44243
    • Arnt, C.R.1    Chiorean, M.V.2    Heldebrant, M.P.3    Gores, G.J.4    Kaufmann, S.H.5
  • 72
    • 0036565885 scopus 로고    scopus 로고
    • Ectopic overexpression of second mitochondria-derived activator of caspases (Smac/DIABLO) or cotreatment with N-terminus of Smac/DIABLO peptide potentiates epothilone B derivative-(BMS 247550) and Apo-2L/TRAIL-induced apoptosis
    • DOI 10.1182/blood.V99.9.3419
    • Guo F, Nimmanapalli R, Paranawithana S, Wittman S, Griffin D, Bali P, et al. Ectopic overexpression of second mitochondria-derived activator of caspases (Smac/DIABLO) or cotreatment with N-terminus of Smac/DIABLO peptide potentiates epothilone B derivative-(BMS 247550) and Apo-2L/TRAIL-induced apoptosis. Blood 2002; 99:3419-26. (Pubitemid 34525325)
    • (2002) Blood , vol.99 , Issue.9 , pp. 3419-3426
    • Quo, F.1    Nimmanapalli, R.2    Paranawithana, S.3    Wittman, S.4    Griffin, D.5    Bali, P.6    O'Bryan, E.7    Fumero, C.8    Wang, H.G.9    Bhalla, K.10
  • 74
  • 75
    • 0034871084 scopus 로고    scopus 로고
    • SAG/ROC/Rbx/Hrt, a zinc RING finger gene family: Molecular cloning, biochemical properties, and biological functions
    • Sun Y, Tan M, Duan H, Swaroop M. SAG/ROC/Rbx/Hrt, a zinc RING finger gene family: Molecular cloning, biochemical properties, and biological functions. Antioxid Redox Signal 2001; 3:635-50. (Pubitemid 32785986)
    • (2001) Antioxidants and Redox Signaling , vol.3 , Issue.4 , pp. 635-650
    • Sun, Y.1    Tan, M.2    Duan, H.3    Swaroop, M.4
  • 83
    • 0036847690 scopus 로고    scopus 로고
    • Elevated Skp2 protein expression in human prostate cancer: Association with loss of the cyclin-dependent kinase inhibitor p27 and PTEN and with reduced recurrence-free survival
    • Yang G, Ayala G, Marzo AD, Tian W, Frolov A, Wheeler TM, et al. Elevated Skp2 protein expression in human prostate cancer: Association with loss of the cyclin-dependent kinase inhibitor p27 and PTEN and with reduced recurrence-free survival. Clin Cancer Res 2002; 8:3419-26. (Pubitemid 35340716)
    • (2002) Clinical Cancer Research , vol.8 , Issue.11 , pp. 3419-3426
    • Yang, G.1    Ayala, G.2    De Marzo, A.3    Tian, W.4    Frolov, A.5    Wheeler, T.M.6    Thompson, T.C.7    Harper, J.W.8
  • 84
    • 0035340719 scopus 로고    scopus 로고
    • Kip1 and of its ubiquitin ligase subunit Skp2 in colorectal carcinomas
    • DOI 10.1002/1097-0142(20010501)91:9<1745::AID-CNCR1193>3.0.CO;2-H
    • Hershko D, Bornstein G, Ben-Izhak O, Carrano A, Pagano M, Krausz MM, et al. Inverse relation between levels of p27(Kip1) and of its ubiquitin ligase subunit Skp2 in colorectal carcinomas. Cancer 2001; 91:1745-51. (Pubitemid 32377961)
    • (2001) Cancer , vol.91 , Issue.9 , pp. 1745-1751
    • Hershko, D.1    Bornstein, G.2    Ben-Izhak, O.3    Carrano, A.4    Pagano, M.5    Krausz, M.M.6    Hershko, A.7
  • 85
    • 0036645405 scopus 로고    scopus 로고
    • Clinical and biological significance of S-phase kinase-associated protein 2 (Skp2) gene expression in gastric carcinoma: Modulation of malignant phenotype by Skp2 overexpression, possibly via p27 proteolysis
    • Masuda TA, Inoue H, Sonoda H, Mine S, Yoshikawa Y, Nakayama K, et al. Clinical and biological significance of S-phase kinase-associated protein 2 (Skp2) gene expression in gastric carcinoma: Modulation of malignant phenotype by Skp2 overexpression, possibly via p27 proteolysis. Cancer Res 2002; 62:3819-25. (Pubitemid 34728867)
    • (2002) Cancer Research , vol.62 , Issue.13 , pp. 3819-3825
    • Masuda, T.-A.1    Inoue, H.2    Sonoda, H.3    Mine, S.4    Yoshikawa, Y.5    Nakayama, K.6    Nakayama, K.-I.7    Mori, M.8
  • 86
    • 0035476237 scopus 로고    scopus 로고
    • High expression of S-phase kinase-interacting protein 2, human F-box protein, correlates with poor prognosis in oral squamous cell carcinomas
    • Kudo Y, Kitajima S, Sato S, Miyauchi M, Ogawa I, Takata T. High expression of S-phase kinase-interacting protein 2, human F-box protein, correlates with poor prognosis in oral squamous cell carcinomas. Cancer Res 2001; 61:7044-7. (Pubitemid 32946493)
    • (2001) Cancer Research , vol.61 , Issue.19 , pp. 7044-7047
    • Kudo, Y.1    Kitajima, S.2    Sato, S.3    Miyauchi, M.4    Ogawa, I.5    Takata, T.6
  • 87
    • 0035921849 scopus 로고    scopus 로고
    • Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line
    • DOI 10.1038/35095076
    • Strohmaier H, Spruck CH, Kaiser P, Won KA, Sangfelt O, Reed SI. Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature 2001; 413:316-22. (Pubitemid 32905853)
    • (2001) Nature , vol.413 , Issue.6853 , pp. 316-322
    • Strohmaier, H.1    Spruck, C.H.2    Kaiser, P.3    Won, K.-A.4    Sangfelt, O.5    Reed, S.I.6
  • 89
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney JD, Hochstrasser M. Substrate targeting in the ubiquitin system. Cell 1999; 97:427-30.
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 90
    • 0037186196 scopus 로고    scopus 로고
    • Mouse homologue of HOS (mHOS) is overexpressed in skin tumors and implicated in constitutive activation of NF-kappaB
    • Bhatia N, Herter JR, Slaga TJ, Fuchs SY, Spiegelman VS. Mouse homologue of HOS (mHOS) is overexpressed in skin tumors and implicated in constitutive activation of NF-kappaB. Oncogene 2002; 21:1501-9.
    • (2002) Oncogene , vol.21 , pp. 1501-1509
    • Bhatia, N.1    Herter, J.R.2    Slaga, T.J.3    Fuchs, S.Y.4    Spiegelman, V.S.5
  • 92
    • 0035145738 scopus 로고    scopus 로고
    • Elevated expression of SAG/ROC2/Rbx2/Hrt2 in human colon carcinomas: SAG does not induce neoplastic transformation, but antisense SAG transfection inhibits tumor cell growth
    • DOI 10.1002/1098-2744(200101)30:1<62::AID-MC1014>3.0.CO;2-A
    • Huang Y, Duan H, Sun Y. Elevated expression of SAG/ROC2/Rbx2/Hrt2 in human colon carcinomas: SAG does not induce neoplastic transformation, but its antisense transfection inhibits tumor cell growth. Mol Carcinog 2001; 30:62-70. (Pubitemid 32127351)
    • (2001) Molecular Carcinogenesis , vol.30 , Issue.1 , pp. 62-70
    • Huang, Y.1    Duan, H.2    Sun, Y.3
  • 94
    • 0037379776 scopus 로고    scopus 로고
    • Expression of the F-Box Protein SKP2 Induces Hyperplasia, Dysplasia, and Low-Grade Carcinoma in the Mouse Prostate
    • Shim EH, Johnson L, Noh HL, Kim YJ, Sun H, Zeiss C, Zhang H. Expression of the F-Box Protein SKP2 Induces Hyperplasia, Dysplasia, and Low-Grade Carcinoma in the Mouse Prostate. Cancer Res 2003; 63:1583-8.
    • (2003) Cancer Res , vol.63 , pp. 1583-1588
    • Shim, E.H.1    Johnson, L.2    Noh, H.L.3    Kim, Y.J.4    Sun, H.5    Zeiss, C.6    Zhang, H.7
  • 95
    • 0032877005 scopus 로고    scopus 로고
    • Alterations of SAG mRNA in human cancer cell lines: Requirement for the RING finger domain for apoptosis protection
    • DOI 10.1093/carcin/20.10.1899
    • Sun Y. Alteration of SAG mRNA in human cancer cell lines: Requirement for the RING finger domain for apoptosis protection. Carcinogenesis 1999; 20:1899-1903. (Pubitemid 29476114)
    • (1999) Carcinogenesis , vol.20 , Issue.10 , pp. 1899-1903
    • Sun, Y.1
  • 97
    • 0037348330 scopus 로고    scopus 로고
    • SAG attenuates apoptotic cell death caused by simulated ischaemia/reoxygenation in rat cardiomyocytes
    • DOI 10.1016/S0022-2828(03)00003-8
    • Chanalaris A, Sun Y, Latchman DS, Stephanou A. SAG attenuates apoptotic cell death caused by simulated ischaemia/reoxygenation in rat cardiomyocytes. J Mol Cell Cardiol 2003; 35:257-64. (Pubitemid 36379169)
    • (2003) Journal of Molecular and Cellular Cardiology , vol.35 , Issue.3 , pp. 257-264
    • Chanalaris, A.1    Sun, Y.2    Latchman, D.S.3    Stephanou, A.4
  • 98
    • 0035143141 scopus 로고    scopus 로고
    • Promotion of S-phase entry and cell growth under serum starvation by SAG/ROC2/Rbx2/Hrt2, an E3 ubiquitin ligase component: Association with inhibition of p27 accumulation
    • Duan H, Tsvetkov LM, Liu Y, Song Y, Swaroop M, Wen R, et al. Sun Y. Promotion of S-phase entry and cell growth under serum starvation by SAG/ROC2/Rbx2/Hrt2, an E3 ubiquitin ligase component: Association with inhibition of p27 accumulation. Mol Carcinog 2001; 30:37-46.
    • (2001) Mol Carcinog , vol.30 , pp. 37-46
    • Duan, H.1    Tsvetkov, L.M.2    Liu, Y.3    Song, Y.4    Swaroop, M.5    Wen, R.6    Sun, Y.7
  • 99
    • 0033956753 scopus 로고    scopus 로고
    • The SCF(HOS/beta-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct domains within CUL1 for substrate targeting and ubiquitin ligation
    • DOI 10.1128/MCB.20.4.1382-1393.2000
    • Wu K, Fuchs SY, Chen A, Tan P, Gomez C, Ronai Z, et al. The SCF(HOS/beta-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct domains within CUL1 for substrate targeting and ubiquitin ligation. Mol Cell Biol 2000; 20:1382-93. (Pubitemid 30069258)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.4 , pp. 1382-1393
    • Wu, K.1    Fuchs, S.Y.2    Chen, A.3    Tan, P.4    Gomez, C.5    Ronai, Z.6    Pan, Z.-Q.7
  • 100
    • 0037013260 scopus 로고    scopus 로고
    • Activation of UBC5 ubiquitin-conjugating enzyme by the RING finger of ROC1 and assembly of active ubiquitin ligases by all cullins
    • DOI 10.1074/jbc.M108565200
    • Furukawa M, Ohta T, Xiong Y. Activation of UBC5 ubiquitin-conjugating enzyme by the RING finger of ROC1 and assembly of active ubiquitin ligases by all cullins. J Biol Chem 2002; 277:15758-65. (Pubitemid 34967851)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15758-15765
    • Furukawa, M.1    Ohta, T.2    Xiong, Y.3
  • 101
    • 0034213598 scopus 로고    scopus 로고
    • Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth, but not for germination: Chip profiling implicates its role in cell cycle regulation
    • Swaroop M, Wang Y, Miller P, Duan H, Jatkoe T, Madore S, et al. Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth, but not for germination: Chip profiling implicates its role in cell cycle regulation. Oncogene 2000; 19:2855-2866.
    • (2000) Oncogene , vol.19 , pp. 2855-2866
    • Swaroop, M.1    Wang, Y.2    Miller, P.3    Duan, H.4    Jatkoe, T.5    Madore, S.6
  • 103
    • 0033769797 scopus 로고    scopus 로고
    • Development of a ubiquitin transfer assay for high throughput screening by fluorescence resonance energy transfer
    • Boisclair MD, McClure C, Josiah S, Glass S, Bottomley S, Kamerkar S, et al. Development of a ubiquitin transfer assay for high throughput screening by fluorescence resonance energy transfer. J Biomol Screen 2000; 5:319-28.
    • (2000) J Biomol Screen , vol.5 , pp. 319-328
    • Boisclair, M.D.1    McClure, C.2    Josiah, S.3    Glass, S.4    Bottomley, S.5    Kamerkar, S.6
  • 104
    • 85009046504 scopus 로고    scopus 로고
    • Speedy approvals for new cancer treatments
    • Speedy approvals for new cancer treatments. FDA Consum 2003; 37:36.
    • (2003) FDA Consum , vol.37 , pp. 36
  • 105
    • 0035215395 scopus 로고    scopus 로고
    • Proteasome inhibition in cancer: Development of PS-341
    • Adams J. Proteasome inhibition in cancer: Development of PS-341. Semin Oncol 2001; 28:613-9. (Pubitemid 33134421)
    • (2001) Seminars in Oncology , vol.28 , Issue.6 , pp. 613-619
    • Adams, J.1
  • 106
    • 0037376230 scopus 로고    scopus 로고
    • Potential for proteasome inhibition in the treatment of cancer
    • DOI 10.1016/S1359-6446(03)02647-3, PII S1359644603026473
    • Adams J. Potential for proteasome inhibition in the treatment of cancer. Drug Discov Today 2003; 8:307-15. (Pubitemid 36332222)
    • (2003) Drug Discovery Today , vol.8 , Issue.7 , pp. 307-315
    • Adams, J.1


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