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Volumn 14, Issue 16, 2015, Pages 2688-2700

The G1 phase E3 ubiquitin ligase TRUSS that gets deregulated in human cancers is a novel substrate of the S-phase E3 ubiquitin ligase Skp2

Author keywords

c Myc; Cell cycle; E3 ubiquitin ligase; HBx; Skp2; TRUSS; Ubiquitination

Indexed keywords

HEPATITIS B VIRUS X PROTEIN; MYC PROTEIN; S PHASE KINASE ASSOCIATED PROTEIN 2; SMALL INTERFERING RNA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED UBIQUITOUS SCAFFOLDING AND SIGNALING PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; MYC PROTEIN, HUMAN; PROTEIN BINDING; S PHASE KINASE ASSOCIATED PROTEIN; TRANSACTIVATOR PROTEIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL C; TRPC4AP PROTEIN, HUMAN;

EID: 84943787999     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.1080/15384101.2015.1056946     Document Type: Article
Times cited : (21)

References (48)
  • 1
    • 61449156563 scopus 로고    scopus 로고
    • Targeting proteins for destruction by the ubiquitin system: Implications for human pathobiology
    • PMID: 18834306
    • Schwartz AL, Ciechanover A. Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology. Annu Rev Pharmacol Toxicol 2009; 49: 73-96; PMID: 18834306; http://dx. doi. org/10. 1146/annurev. pharmtox. 051208. 165340.
    • (2009) Annu Rev Pharmacol Toxicol , vol.49 , pp. 73-96
    • Schwartz, A.L.1    Ciechanover, A.2
  • 2
    • 33646345376 scopus 로고    scopus 로고
    • Ubiquitin ligases: Cellcycle control and cancer
    • PMID: 16633365
    • Nakayama KI, Nakayama K. Ubiquitin ligases: cellcycle control and cancer. Nat Rev Cancer 2006; 6: 369-81; PMID: 16633365; http://dx. doi. org/10. 1038/nrc1881.
    • (2006) Nat Rev Cancer , vol.6 , pp. 369-381
    • Nakayama, K.I.1    Nakayama, K.2
  • 3
    • 67650657199 scopus 로고    scopus 로고
    • Ubiquitin-mediated control of oncogene and tumor suppressor gene products
    • PMID: 19459846
    • Kitagawa K, Kotake Y, Kitagawa M. Ubiquitin-mediated control of oncogene and tumor suppressor gene products. Cancer Sci 2009; 100: 1374-81; PMID: 19459846; http://dx. doi. org/10. 1111/j. 1349-7006. 2009. 01196. x.
    • (2009) Cancer Sci , vol.100 , pp. 1374-1381
    • Kitagawa, K.1    Kotake, Y.2    Kitagawa, M.3
  • 4
    • 44349122993 scopus 로고    scopus 로고
    • Deregulated proteolysis by the Fbox proteins SKP2 and beta-TrCP: Tipping the scales of cancer
    • PMID: 18500245
    • Frescas D, Pagano M. Deregulated proteolysis by the Fbox proteins SKP2 and beta-TrCP: tipping the scales of cancer. Nat Rev Cancer 2008; 8: 438-49; PMID: 18500245; http://dx. doi. org/10. 1038/nrc2396.
    • (2008) Nat Rev Cancer , vol.8 , pp. 438-449
    • Frescas, D.1    Pagano, M.2
  • 5
    • 38549086019 scopus 로고    scopus 로고
    • FBW7 ubiquitin ligase: A tumour suppressor at the crossroads of cell division, growth and differentiation
    • PMID: 18094723
    • WelckerM, Clurman BE. FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation. Nat Rev Cancer 2008; 8: 83-93; PMID: 18094723; http://dx. doi. org/10. 1038/nrc2290.
    • (2008) Nat Rev Cancer , vol.8 , pp. 83-93
    • Welcker, M.1    Clurman, B.E.2
  • 6
    • 34250318465 scopus 로고    scopus 로고
    • DCAFs, the missing link of the CUL4-DDB1 ubiquitin ligase
    • PMID: 17588513
    • Lee J, Zhou P. DCAFs, the missing link of the CUL4-DDB1 ubiquitin ligase. Mol Cell 2007; 26: 775-80; PMID: 17588513.
    • (2007) Mol Cell , vol.26 , pp. 775-780
    • Lee, J.1    Zhou, P.2
  • 7
    • 70350359679 scopus 로고    scopus 로고
    • CRL4s: The CUL4-RING E3 ubiquitin ligases
    • PMID: 19818632
    • Jackson S, Xiong Y. CRL4s: the CUL4-RING E3 ubiquitin ligases. Trends Biochem Sci 2009; 34: 562-70; PMID: 19818632; http://dx. doi. org/10. 1016/j. tibs. 2009. 07. 002.
    • (2009) Trends Biochem Sci , vol.34 , pp. 562-570
    • Jackson, S.1    Xiong, Y.2
  • 8
    • 21044442126 scopus 로고    scopus 로고
    • UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex
    • PMID: 15882621
    • Sugasawa K, Okuda Y, Saijo M, Nishi R, Matsuda N, Chu G, Mori T, Iwai S, Tanaka K, Tanaka K, et al. UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex. Cell 2005; 121: 387-00; PMID: 15882621; http://dx. doi. org/10. 1016/j. cell. 2005. 02. 035.
    • (2005) Cell , vol.121 , pp. 387-400
    • Sugasawa, K.1    Okuda, Y.2    Saijo, M.3    Nishi, R.4    Matsuda, N.5    Chu, G.6    Mori, T.7    Iwai, S.8    Tanaka, K.9    Tanaka, K.10
  • 9
    • 0034813575 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group E gene product DDB2 is a specific target of cullin 4A in mammalian cells
    • PMID: 11564859
    • Nag A, Bondar T, Shiv S, Raychaudhuri P. The xeroderma pigmentosum group E gene product DDB2 is a specific target of cullin 4A in mammalian cells. Mol Cell Biol 2001; 21: 6738-47; PMID: 11564859; http://dx. doi. org/10. 1128/MCB. 21. 20. 6738-6747. 2001.
    • (2001) Mol Cell Biol , vol.21 , pp. 6738-6747
    • Nag, A.1    Bondar, T.2    Shiv, S.3    Raychaudhuri, P.4
  • 10
    • 33744781568 scopus 로고    scopus 로고
    • Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage
    • PMID: 16678110
    • Wang H, Zhai L, Xu J, Joo HY, Jackson S, Erdjument-Bromage H, Tempst P, Xiong Y, Zhang Y. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol Cell 2006; 22: 383-94; PMID: 16678110; http://dx. doi. org/10. 1016/j. molcel. 2006. 03. 035.
    • (2006) Mol Cell , vol.22 , pp. 383-394
    • Wang, H.1    Zhai, L.2    Xu, J.3    Joo, H.Y.4    Jackson, S.5    Erdjument-Bromage, H.6    Tempst, P.7    Xiong, Y.8    Zhang, Y.9
  • 11
    • 33644536070 scopus 로고    scopus 로고
    • The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites
    • PMID: 16473935
    • Kapetanaki MG, Guerrero-Santoro J, Bisi DC, Hsieh CL, Rapić-Otrin V, Levine AS. The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites. Proc Natl Acad Sci U SA 2006; 103: 2588-93; PMID: 16473935; http://dx. doi. org/10. 1073/pnas. 0511160103.
    • (2006) Proc Natl Acad Sci U SA , vol.103 , pp. 2588-2593
    • Kapetanaki, M.G.1    Guerrero-Santoro, J.2    Bisi, D.C.3    Hsieh, C.L.4    Rapić-Otrin, V.5    Levine, A.S.6
  • 12
    • 77953934816 scopus 로고    scopus 로고
    • Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells
    • PMID: 20551172
    • Choi SH, Wright JB, Gerber SA, Cole MD. Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells. Genes Dev 2010; 24: 1236-41; PMID: 20551172; http://dx. doi. org/10. 1101/gad. 1920310.
    • (2010) Genes Dev , vol.24 , pp. 1236-1241
    • Choi, S.H.1    Wright, J.B.2    Gerber, S.A.3    Cole, M.D.4
  • 13
    • 0033551374 scopus 로고    scopus 로고
    • MYC oncogenes and human neoplastic disease
    • PMID: 10378696
    • Nesbit CE, Tersak JM, Prochownik EV. MYC oncogenes and human neoplastic disease. Oncogene 1999; 18: 3004-16; PMID: 10378696; http://dx. doi. org/10. 1038/sj. onc. 1202746.
    • (1999) Oncogene , vol.18 , pp. 3004-3016
    • Nesbit, C.E.1    Tersak, J.M.2    Prochownik, E.V.3
  • 14
    • 33748192942 scopus 로고    scopus 로고
    • The Myc oncoprotein as a therapeutic target for human cancer
    • PMID: 16934487
    • Vita M, Henriksson M. The Myc oncoprotein as a therapeutic target for human cancer. Semin Cancer Biol 2006; 16: 318-30; PMID: 16934487; http://dx. doi. org/10. 1016/j. semcancer. 2006. 07. 015.
    • (2006) Semin Cancer Biol , vol.16 , pp. 318-330
    • Vita, M.1    Henriksson, M.2
  • 15
    • 0036827626 scopus 로고    scopus 로고
    • The p127 subunit (DDB1) of the UV-DNA damage repair binding protein is essential for the targeted degradation of STAT1 by the V protein of the paramyxovirus simian virus 5
    • PMID: 12388698
    • Andrejeva J, Poole E, Young DF, Goodbourn S, Randall RE. The p127 subunit (DDB1) of the UV-DNA damage repair binding protein is essential for the targeted degradation of STAT1 by the V protein of the paramyxovirus simian virus 5. J Virol 2002; 76: 11379-86; PMID: 12388698; http://dx. doi. org/10. 1128/JVI. 76. 22. 11379-11386. 2002.
    • (2002) J Virol , vol.76 , pp. 11379-11386
    • Andrejeva, J.1    Poole, E.2    Young, D.F.3    Goodbourn, S.4    Randall, R.E.5
  • 16
    • 0036942290 scopus 로고    scopus 로고
    • Paramyxoviruses SV5 and HPIV2 assemble STAT protein ubiquitin ligase complexes from cellular components
    • PMID: 12504558
    • Ulane CM, Horvath CM. Paramyxoviruses SV5 and HPIV2 assemble STAT protein ubiquitin ligase complexes from cellular components. Virology 2002; 304: 160-66; PMID: 12504558; http://dx. doi. org/10. 1006/viro. 2002. 1773.
    • (2002) Virology , vol.304 , pp. 160-166
    • Ulane, C.M.1    Horvath, C.M.2
  • 17
    • 0038664389 scopus 로고    scopus 로고
    • STAT3 ubiquitylation and degradation by mumps virus suppress cytokine and oncogene signaling
    • PMID: 12743296
    • Ulane CM, Rodriguez JJ, Parisien JP, Horvath CM. STAT3 ubiquitylation and degradation by mumps virus suppress cytokine and oncogene signaling. J Virol 2003; 77: 6385-93; PMID: 12743296; http://dx. doi. org/10. 1128/JVI. 77. 11. 6385-6393. 2003.
    • (2003) J Virol , vol.77 , pp. 6385-6393
    • Ulane, C.M.1    Rodriguez, J.J.2    Parisien, J.P.3    Horvath, C.M.4
  • 18
    • 15244357567 scopus 로고    scopus 로고
    • Hepatitis B virus X protein stimulates viral genome replication via a DDB1-dependent pathway distinct from that leading to cell death
    • PMID: 15767425
    • Leupin O, Bontron S, Strubin M. Hepatitis B virus X protein stimulates viral genome replication via a DDB1-dependent pathway distinct from that leading to cell death. J Virol 2005; 79: 4238-45; PMID: 15767425; http://dx. doi. org/10. 1128/JVI. 79. 7. 4238-4245. 2005.
    • (2005) J Virol , vol.79 , pp. 4238-4245
    • Leupin, O.1    Bontron, S.2    Strubin, M.3
  • 19
    • 0038365225 scopus 로고    scopus 로고
    • Hepatitis B virus X protein and simian virus 5 V protein exhibit similar UV-DDB1 binding properties to mediate distinct activities
    • PMID: 12743284
    • Leupin O, Bontron S, Strubin M. Hepatitis B virus X protein and simian virus 5 V protein exhibit similar UV-DDB1 binding properties to mediate distinct activities. J Virol 2003; 77: 6274-83; PMID: 12743284; http://dx. doi. org/10. 1128/JVI. 77. 11. 6274-6283. 2003.
    • (2003) J Virol , vol.77 , pp. 6274-6283
    • Leupin, O.1    Bontron, S.2    Strubin, M.3
  • 20
    • 30644461154 scopus 로고    scopus 로고
    • The X protein of hepatitis B virus binds to the F box protein Skp2 and inhibits the ubiquitination and proteasomal degradation of c-Myc
    • PMID: 16376880
    • Kalra N, Kumar V. The X protein of hepatitis B virus binds to the F box protein Skp2 and inhibits the ubiquitination and proteasomal degradation of c-Myc. FEBS Lett 2006; 580: 431-36; PMID: 16376880; http://dx. doi. org/10. 1016/j. febslet. 2005. 12. 034.
    • (2006) FEBS Lett , vol.580 , pp. 431-436
    • Kalra, N.1    Kumar, V.2
  • 21
    • 1642378661 scopus 로고    scopus 로고
    • Control of the SCF (Skp2-Cks1) ubiquitin ligase by the APC/C (Cdh1) ubiquitin ligase
    • PMID: 15014502
    • Bashir T, Dorrello NV, Amador V, Guardavaccaro D, Pagano M. Control of the SCF (Skp2-Cks1) ubiquitin ligase by the APC/C (Cdh1) ubiquitin ligase. Nature 2004; 11: 190-93; PMID: 15014502; http://dx. doi. org/10. 1038/nature02330.
    • (2004) Nature , vol.11 , pp. 190-193
    • Bashir, T.1    Dorrello, N.V.2    Amador, V.3    Guardavaccaro, D.4    Pagano, M.5
  • 23
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: Insights into a molecular machine
    • PMID: 15340381
    • Cardozo T, Pagano M. The SCF ubiquitin ligase: insights into a molecular machine. Nat Rev Mol Cell Biol 2004; 5: 739-51; PMID: 15340381; http://dx. doi. org/10. 1038/nrm1471.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 24
    • 12444264823 scopus 로고    scopus 로고
    • The F-box protein Skp2 participates in c-Myc proteosomal degradation and acts as a cofactor for c-Myc-regulated transcription
    • PMID: 12769844
    • von der Lehr N, Johansson S, Wu S, Bahram F, Castell A, Cetinkaya C, Hydbring P, Weidung I, Nakayama K, Nakayama KI et al. The F-box protein Skp2 participates in c-Myc proteosomal degradation and acts as a cofactor for c-Myc-regulated transcription. Mol Cell 2003; 11: 1189-00; PMID: 12769844; http://dx. doi. org/10. 1016/S1097-2765(03)00193-X.
    • (2003) Mol Cell , vol.11 , pp. 1189-1200
    • von der Lehr, N.1    Johansson, S.2    Wu, S.3    Bahram, F.4    Castell, A.5    Cetinkaya, C.6    Hydbring, P.7    Weidung, I.8    Nakayama, K.9    Nakayama, K.I.10
  • 25
    • 0033176887 scopus 로고    scopus 로고
    • Skp2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • PMID: 10559916
    • Carrano AC, Eytan E, Hershko A, Pagano M. Skp2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat Cell Biol 1999; 1: 193-99; PMID: 10559916; http://dx. doi. org/10. 1038/12013.
    • (1999) Nat Cell Biol , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 26
    • 0037112174 scopus 로고    scopus 로고
    • The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2)
    • PMID: 12435635
    • Tedesco D, Lukas J, Reed SI. The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2). Genes Dev 2002; 16: 2946-57; PMID: 12435635; http://dx. doi. org/10. 1101/gad. 1011202.
    • (2002) Genes Dev , vol.16 , pp. 2946-2957
    • Tedesco, D.1    Lukas, J.2    Reed, S.I.3
  • 27
    • 0038152755 scopus 로고    scopus 로고
    • Role of the SCFSkp2 ubiquitin ligase in the degradation of p21Cip1 in S phase
    • PMID: 12730199
    • Bornstein G, Bloom J, Sitry-Shevah D, Nakayama K, Pagano M, Hershko A. Role of the SCFSkp2 ubiquitin ligase in the degradation of p21Cip1 in S phase. J Biol Chem 2003; 278: 25752-57; PMID: 12730199; http://dx. doi. org/10. 1074/jbc. M301774200.
    • (2003) J Biol Chem , vol.278 , pp. 25752-25757
    • Bornstein, G.1    Bloom, J.2    Sitry-Shevah, D.3    Nakayama, K.4    Pagano, M.5    Hershko, A.6
  • 28
    • 0041836324 scopus 로고    scopus 로고
    • Degradation of p57Kip2 mediated by SCFSkp2-dependent ubiquitylation
    • PMID: 12925736
    • Kamura T, Hara T, Kotoshiba S, Yada M, Ishida N, Nakayama KI. Degradation of p57Kip2 mediated by SCFSkp2-dependent ubiquitylation. Proc Natl Acad Sci U SA 2003; 100: 10231-36; PMID: 12925736; http://dx. doi. org/10. 1073/pnas. 1831009100.
    • (2003) Proc Natl Acad Sci U SA , vol.100 , pp. 10231-10236
    • Kamura, T.1    Hara, T.2    Kotoshiba, S.3    Yada, M.4    Ishida, N.5    Nakayama, K.I.6
  • 29
    • 0036208817 scopus 로고    scopus 로고
    • Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication
    • PMID: 11931757
    • Mendez J, Zou-Yang XH, Kim SY, Hidaka M, Stillman B. Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication. Mol Cell 2002; 9: 481-91; PMID: 11931757; http://dx. doi. org/10. 1016/S1097-2765(02)00467-7.
    • (2002) Mol Cell , vol.9 , pp. 481-491
    • Mendez, J.1    Zou-Yang, X.H.2    Kim, S.Y.3    Hidaka, M.4    Stillman, B.5
  • 30
    • 0043234476 scopus 로고    scopus 로고
    • The SCF(Skp2) ubiquitin ligase complex interacts with the human replication licensing factor Cdt1 and regulates Cdt1 degradation
    • PMID: 12840033
    • Li X, Zhao Q, Liao R, Sun P, Wu X. The SCF(Skp2) ubiquitin ligase complex interacts with the human replication licensing factor Cdt1 and regulates Cdt1 degradation. J Bio Chem 2003; 278: 30854-58; PMID: 12840033; http://dx. doi. org/10. 1074/jbc. C300251200.
    • (2003) J Bio Chem , vol.278 , pp. 30854-30858
    • Li, X.1    Zhao, Q.2    Liao, R.3    Sun, P.4    Wu, X.5
  • 31
    • 0034595292 scopus 로고    scopus 로고
    • Targeted disruption of Skp2 results in accumulation of cyclin E and p27(Kip1), polyploidy and centrosome overduplication
    • PMID: 10790373
    • Nakayama K, Nagahama H, Minamishima YA, Matsumoto M, Nakamichi I, Hatakeyama S. Targeted disruption of Skp2 results in accumulation of cyclin E and p27(Kip1), polyploidy and centrosome overduplication. EMBO J 2000; 19: 2069-81; PMID: 10790373; http://dx. doi. org/10. 1093/emboj/19. 9. 2069.
    • (2000) EMBO J , vol.19 , pp. 2069-2081
    • Nakayama, K.1    Nagahama, H.2    Minamishima, Y.A.3    Matsumoto, M.4    Nakamichi, I.5    Hatakeyama, S.6
  • 32
    • 0033130137 scopus 로고    scopus 로고
    • Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation
    • PMID: 10559858
    • Marti A, Wirbelauer C, Scheffner M, Krek W. Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation. Nat Cell Biol 1999; 1: 14-19; PMID: 10559858; http://dx. doi. org/10. 1038/8984.
    • (1999) Nat Cell Biol , vol.1 , pp. 14-19
    • Marti, A.1    Wirbelauer, C.2    Scheffner, M.3    Krek, W.4
  • 33
    • 84906251455 scopus 로고    scopus 로고
    • The role of homeostatic regulation between tumor suppressor DAB2IP and oncogenic Skp2 in prostate cancer growth
    • PMID: 25115390
    • Tsai YS, Lai CL, Lai CH, Chang KH, Wu K, Tseng SF, Fazli L, Gleave M, Xiao G, Gandee L, et al. The role of homeostatic regulation between tumor suppressor DAB2IP and oncogenic Skp2 in prostate cancer growth. Oncotarget 2014; 5: 6425-36; PMID: 25115390.
    • (2014) Oncotarget , vol.5 , pp. 6425-6436
    • Tsai, Y.S.1    Lai, C.L.2    Lai, C.H.3    Chang, K.H.4    Wu, K.5    Tseng, S.F.6    Fazli, L.7    Gleave, M.8    Xiao, G.9    Gandee, L.10
  • 35
    • 1342275414 scopus 로고    scopus 로고
    • Human de-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase
    • PMID: 14739464
    • Wertz IE, O'Rourke KM, Zhang Z, Dornan D, Arnott D, Deshaies RJ, Dixit VM. Human de-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase. Science 2004; 303: 1371-74; PMID: 14739464; http://dx. doi. org/10. 1126/science. 1093549.
    • (2004) Science , vol.303 , pp. 1371-1374
    • Wertz, I.E.1    O'Rourke, K.M.2    Zhang, Z.3    Dornan, D.4    Arnott, D.5    Deshaies, R.J.6    Dixit, V.M.7
  • 36
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • PMID: 8221889
    • 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: 495-05; PMID: 8221889; http://dx. doi. org/10. 1016/0092-8674(93)90384-3.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 37
    • 0034754443 scopus 로고    scopus 로고
    • Rhabdoviruses and the cellular ubiquitin-proteasome system: A budding interaction
    • PMID: 11602704
    • Harty RN, Brown ME, McGettigan JP, Wang G, Jayakar HR, Huibregtse JM, Whitt MA, Schnell MJ. Rhabdoviruses and the cellular ubiquitin-proteasome system: a budding interaction. J Virol 2011; 75: 10623-29; PMID: 11602704; http://dx. doi. org/10. 1128/JVI. 75. 22. 10623-10629. 2001.
    • (2011) J Virol , vol.75 , pp. 10623-10629
    • Harty, R.N.1    Brown, M.E.2    McGettigan, J.P.3    Wang, G.4    Jayakar, H.R.5    Huibregtse, J.M.6    Whitt, M.A.7    Schnell, M.J.8
  • 38
    • 0033756590 scopus 로고    scopus 로고
    • Latent Membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases
    • PMID: 11046148
    • Winberg G, Matskova L, Chen F, Plant P, Rotin D, Pawson T. Latent Membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases. Mol Cell Biol 2002; 20: 8526-35; PMID: 11046148; http://dx. doi. org/10. 1128/MCB. 20. 22. 8526-8535. 2000.
    • (2002) Mol Cell Biol , vol.20 , pp. 8526-8535
    • Winberg, G.1    Matskova, L.2    Chen, F.3    Plant, P.4    Rotin, D.5    Pawson, T.6
  • 39
    • 0035945349 scopus 로고    scopus 로고
    • A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition
    • PMID: 11756476
    • Coscoy L, Sanchez DJ, Ganem D. A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition. J Cell Biol 2001; 155: 1265-73; PMID: 11756476; http://dx. doi. org/10. 1083/jcb. 200111010.
    • (2001) J Cell Biol , vol.155 , pp. 1265-1273
    • Coscoy, L.1    Sanchez, D.J.2    Ganem, D.3
  • 40
    • 0035844173 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCPmediated degradation of Ikappa B
    • PMID: 11278695
    • Bour S, Perrin C, Akari H, Strebel K. The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCPmediated degradation of Ikappa B. J Biol Chem 2001; 276: 15920-28; PMID: 11278695; http://dx. doi. org/10. 1074/jbc. M010533200.
    • (2001) J Biol Chem , vol.276 , pp. 15920-15928
    • Bour, S.1    Perrin, C.2    Akari, H.3    Strebel, K.4
  • 41
    • 4444252349 scopus 로고    scopus 로고
    • Hepatitis B virus X protein (HBx): Structure-function relationship and role in viral pathogenesis
    • Triezenberg SJ, Kaufman J, Gossen M, Eds., Germany: Springer-Verlag
    • Kumar V, Sarkar DP. Hepatitis B virus X protein (HBx): structure-function relationship and role in viral pathogenesis. in: Handbook of Experimental Pharmacology. Triezenberg SJ, Kaufman J, Gossen M, Eds., Germany: Springer-Verlag; 2004, pp. 377-407.
    • (2004) Handbook of Experimental Pharmacology , pp. 377-407
    • Kumar, V.1    Sarkar, D.P.2
  • 42
    • 0032559971 scopus 로고    scopus 로고
    • Cytosol is the prime compartment of hepatitis B virus X protein where it colocalizes with the proteasome
    • PMID: 9572486
    • SirmaH, Weil R, RosmorducO, UrbanS, Israel A, Brechot C. Cytosol is the prime compartment of hepatitis B virus X protein where it colocalizes with the proteasome. Oncogene 1998; 16: 2051-63; PMID: 9572486; http://dx. doi. org/10. 1038/sj. onc. 1201737.
    • (1998) Oncogene , vol.16 , pp. 2051-2063
    • Sirma, H.1    Weil, R.2    Rosmorduc, O.3    Urban, S.4    Israel, A.5    Brechot, C.6
  • 43
    • 84867098526 scopus 로고    scopus 로고
    • HBx and c-myc cooperate in the up-regulation of ribosome biogenesis and in cellular transformation
    • PMID: 22889122
    • Shukla SK, Kumar V. HBx and c-myc cooperate in the up-regulation of ribosome biogenesis and in cellular transformation. FEBS J 2012; 279: 3859-71; PMID: 22889122; http://dx. doi. org/10. 1111/j. 1742-4658. 2012. 08745. x.
    • (2012) FEBS J , vol.279 , pp. 3859-3871
    • Shukla, S.K.1    Kumar, V.2
  • 44
    • 0029937060 scopus 로고    scopus 로고
    • A truncated mutant (residues 58-140) of the hepatitis B virus X protein retains transactivation function
    • PMID: 8643631
    • Kumar V, Jayasuryan N, Kumar R. A truncated mutant (residues 58-140) of the hepatitis B virus X protein retains transactivation function. Proc Natl Acad Sci U S A 1996; 93: 5647-52; PMID: 8643631; http://dx. doi. org/10. 1073/pnas. 93. 11. 5647.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 5647-5652
    • Kumar, V.1    Jayasuryan, N.2    Kumar, R.3
  • 45
    • 79955977893 scopus 로고    scopus 로고
    • Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry
    • PMID: 21596315
    • Huang X, Summers MK, Pham V, Lill JR, Liu J, Lee G, Kirkpatrick DS, Jackson PK, Fang G, Dixit VM. Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry. Mol Cell 2011; 20: 511-23; PMID: 21596315; http://dx. doi. org/10. 1016/j. molcel. 2011. 03. 027.
    • (2011) Mol Cell , vol.20 , pp. 511-523
    • Huang, X.1    Summers, M.K.2    Pham, V.3    Lill, J.R.4    Liu, J.5    Lee, G.6    Kirkpatrick, D.S.7    Jackson, P.K.8    Fang, G.9    Dixit, V.M.10
  • 46
    • 78449288145 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination of NP protein regulates influenza A virus RNA replication
    • PMID: 20924359
    • Liao TL, Wu CY, Su WC, Jeng KS, Lai MM. Ubiquitination and deubiquitination of NP protein regulates influenza A virus RNA replication. EMBO J 2010; 29: 3879-90; PMID: 20924359; http://dx. doi. org/10. 1038/emboj. 2010. 250.
    • (2010) EMBO J , vol.29 , pp. 3879-3890
    • Liao, T.L.1    Wu, C.Y.2    Su, W.C.3    Jeng, K.S.4    Lai, M.M.5
  • 47
    • 0031804912 scopus 로고    scopus 로고
    • A monoclonal antibody against the X protein of hepatitis B virus: Fine mapping of its epitope and application in a quantitative ELISA of the X protein in sera of hepatitis B patients
    • PMID: 9627056
    • Kumar V, Jayasuryan N, Reddi H, Sahal D, Panda SK. A monoclonal antibody against the X protein of hepatitis B virus: fine mapping of its epitope and application in a quantitative ELISA of the X protein in sera of hepatitis B patients. Hybridoma 1998; 17: 157-64; PMID: 9627056; http://dx. doi. org/10. 1089/hyb. 1998. 17. 157.
    • (1998) Hybridoma , vol.17 , pp. 157-164
    • Kumar, V.1    Jayasuryan, N.2    Reddi, H.3    Sahal, D.4    Panda, S.K.5
  • 48
    • 77952948681 scopus 로고    scopus 로고
    • p65 negatively regulate transcription of the cyclin E gene
    • PMID: 20385564
    • Janbandhu VC, Singh AK, Mukherji A, Kumar V. p65 negatively regulate transcription of the cyclin E gene. J Biol Chem 2010; 285: 17453-64; PMID: 20385564; http://dx. doi. org/10. 1074/jbc. M109. 058974.
    • (2010) J Biol Chem , vol.285 , pp. 17453-17464
    • Janbandhu, V.C.1    Singh, A.K.2    Mukherji, A.3    Kumar, V.4


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