메뉴 건너뛰기




Volumn 1816, Issue 2, 2011, Pages 147-157

Ubiquitin-independent proteasomal degradation during oncogenic viral infections

Author keywords

Oncogenic viruses; Proteasome; Ubiquitin independent

Indexed keywords

DOUBLE STRANDED DNA; PROTEASOME; PROTEIN P53; PROTEINASE INHIBITOR; RNA DIRECTED DNA POLYMERASE INHIBITOR; SINGLE STRANDED DNA; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; VIRUS DNA;

EID: 79959265889     PISSN: 0304419X     EISSN: 18792561     Source Type: Journal    
DOI: 10.1016/j.bbcan.2011.05.005     Document Type: Review
Times cited : (39)

References (165)
  • 1
    • 78049366283 scopus 로고    scopus 로고
    • Proteasome function determines cellular homeostasis and the rate of aging
    • N. Chondrogianni, E.S. Gonos, Proteasome function determines cellular homeostasis and the rate of aging, Adv. Exp. Med. Biol. 694 (2010) 38-46.
    • (2010) Adv. Exp. Med. Biol. , vol.694 , pp. 38-46
    • Chondrogianni, N.1    Gonos, E.S.2
  • 2
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • D.J. Klionsky, S.D. Emr, Autophagy as a regulated pathway of cellular degradation, Science 290 (2000) 1717-1721.
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 3
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • B. Levine, G. Kroemer, Autophagy in the pathogenesis of disease, Cell 132 (2008) 27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 4
    • 33745816760 scopus 로고    scopus 로고
    • Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
    • S.H. Lecker, A.L. Goldberg, W.E. Mitch, Protein degradation by the ubiquitin-proteasome pathway in normal and disease states, J. Am. Soc. Nephrol. 17 (2006) 1807-1819.
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 1807-1819
    • Lecker, S.H.1    Goldberg, A.L.2    Mitch, W.E.3
  • 5
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • K.L. Rock, C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, A.L. Goldberg, Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules, Cell 78 (1994) 761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 7
    • 33646345376 scopus 로고    scopus 로고
    • Ubiquitin ligases: cell-cycle control and cancer
    • K.I. Nakayama, K. Nakayama, Ubiquitin ligases: cell-cycle control and cancer, Nat. Rev. Cancer 6 (2006) 369-381.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 369-381
    • Nakayama, K.I.1    Nakayama, K.2
  • 8
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • M. Muratani, W.P. Tansey, How the ubiquitin-proteasome system controls transcription, Nat. Rev. Mol. Cell Biol. 4 (2003) 192-201.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 10
    • 0032919345 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasome pathway in apoptosis
    • R.Z. Orlowski, The role of the ubiquitin-proteasome pathway in apoptosis, Cell Death Differ. 6 (1999) 303-313.
    • (1999) Cell Death Differ , vol.6 , pp. 303-313
    • Orlowski, R.Z.1
  • 11
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: a suitable antineoplastic target
    • J. Adams, The proteasome: a suitable antineoplastic target, Nat. Rev. Cancer 4 (2004) 349-360.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 13
    • 59349088768 scopus 로고    scopus 로고
    • Manipulation of the ubiquitin-proteasome pathway by small DNA tumor viruses
    • P. Blanchette, P.E. Branton, Manipulation of the ubiquitin-proteasome pathway by small DNA tumor viruses, Virology 384 (2009) 317-323.
    • (2009) Virology , vol.384 , pp. 317-323
    • Blanchette, P.1    Branton, P.E.2
  • 14
    • 54249104026 scopus 로고    scopus 로고
    • The ubiquitin system, disease, and drug discovery
    • M. Petroski, The ubiquitin system, disease, and drug discovery, BMC Biochem. 9 (2008) S7.
    • (2008) BMC Biochem , vol.9
    • Petroski, M.1
  • 15
    • 33751506565 scopus 로고    scopus 로고
    • Antigen presentation and the ubiquitin-proteasome system in host-pathogen interactions
    • W.A. Frederick (Ed.), Academic Press
    • J. Loureiro, H.L. Ploegh, Antigen presentation and the ubiquitin-proteasome system in host-pathogen interactions, in: W.A. Frederick (Ed.), Advances in Immunology, vol. 92, Academic Press, 2006, pp. 225-305.
    • (2006) Advances in Immunology , vol.92 , pp. 225-305
    • Loureiro, J.1    Ploegh, H.L.2
  • 16
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • M.H. Glickman, A. Ciechanover, The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction, Physiol. Rev. 82 (2002) 373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 17
    • 56249108370 scopus 로고    scopus 로고
    • Ubiquitin-independent degra- dation of proteins by the proteasome
    • I. Jariel-Encontre, G. Bossis, M. Piechaczyk, Ubiquitin-independent degra- dation of proteins by the proteasome, Biochim. Biophys. Acta 1786 (2008) 153-177.
    • (2008) Biochim. Biophys. Acta , vol.1786 , pp. 153-177
    • Jariel-Encontre, I.1    Bossis, G.2    Piechaczyk, M.3
  • 22
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors
    • M. Rechsteiner, C.P. Hill, Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors, Trends Cell Biol. 15 (2005) 27-33.
    • (2005) Trends Cell Biol , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 24
    • 0031105037 scopus 로고    scopus 로고
    • Structural and functional properties of proteasome activator PA28
    • L. Kuehn, B. Dahlmann, Structural and functional properties of proteasome activator PA28, Mol. Biol. Rep. 24 (1997) 89-93.
    • (1997) Mol. Biol. Rep. , vol.24 , pp. 89-93
    • Kuehn, L.1    Dahlmann, B.2
  • 25
    • 77649243592 scopus 로고    scopus 로고
    • Structureof a Blm10 complex reveals common mechanisms for proteasome binding and gate opening
    • K.Sadre-Bazzaz, F.G.Whitby, H.Robinson, T. Formosa, C.P. Hill, Structureof a Blm10 complex reveals common mechanisms for proteasome binding and gate opening, Mol. Cell 37 (2010) 728-735.
    • (2010) Mol. Cell , vol.37 , pp. 728-735
    • Sadre-Bazzaz, K.1    Whitby, F.G.2    Robinson, H.3    Formosa, T.4    Hill, C.P.5
  • 28
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • M. Koegl, T. Hoppe, S. Schlenker, H.D. Ulrich, T.U. Mayer, S. Jentsch, A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly, Cell 96 (1999) 635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 30
  • 31
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • D. Finley, Recognition and processing of ubiquitin-protein conjugates by the proteasome, Annu. Rev. Biochem. 78 (2009) 477-513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 32
    • 78649289427 scopus 로고    scopus 로고
    • ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation
    • A. Peth, T. Uchiki, A.L. Goldberg, ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation, Mol. Cell 40 (2010) 671-681.
    • (2010) Mol. Cell , vol.40 , pp. 671-681
    • Peth, A.1    Uchiki, T.2    Goldberg, A.L.3
  • 33
    • 77953154024 scopus 로고    scopus 로고
    • The development and pharmacol- ogy of proteasome inhibitors for the management and treatment of cancer
    • S.J. Enna, W. Michael (Eds.), Academic Press
    • B. Ruggeri, S. Miknyoczki, B. Dorsey, A.-M. Hui, The development and pharmacol- ogy of proteasome inhibitors for the management and treatment of cancer, in: S.J. Enna, W. Michael (Eds.), Advances in Pharmacology, vol. 57, Academic Press, 2009, pp. 91-135.
    • (2009) Advances in Pharmacology , vol.57 , pp. 91-135
    • Ruggeri, B.1    Miknyoczki, S.2    Dorsey, B.3    Hui, A.-M.4
  • 36
    • 77954955259 scopus 로고    scopus 로고
    • Human papillomavirus oncoproteins: pathways to transformation
    • C.A. Moody, L.A. Laimins, Human papillomavirus oncoproteins: pathways to transformation, Nat. Rev. Cancer 10 (2010) 550-560.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 550-560
    • Moody, C.A.1    Laimins, L.A.2
  • 37
    • 18244375016 scopus 로고    scopus 로고
    • Mechanisms of persistent NF-kappaB activation by HTLV-I tax
    • E.W. Harhaj, N.S. Harhaj, Mechanisms of persistent NF-kappaB activation by HTLV-I tax, IUBMB Life 57 (2005) 83-91.
    • (2005) IUBMB Life , vol.57 , pp. 83-91
    • Harhaj, E.W.1    Harhaj, N.S.2
  • 39
    • 42149145636 scopus 로고    scopus 로고
    • Pathogen evasion strategies for the major histocompat- ibility complex class I assembly pathway
    • A.N. Antoniou, S.J. Powis, Pathogen evasion strategies for the major histocompat- ibility complex class I assembly pathway, Immunology 124 (2008) 1-12.
    • (2008) Immunology , vol.124 , pp. 1-12
    • Antoniou, A.N.1    Powis, S.J.2
  • 41
    • 0346243936 scopus 로고    scopus 로고
    • MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation
    • Y. Jin,H. Lee,S .X. Zeng, M.-S. Dai, H. Lu, MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation, EMBO J. 22 (2003) 6365-6377.
    • (2003) EMBO J , vol.22 , pp. 6365-6377
    • Jin, Y.1    Lee, H.2    Zeng, S.X.3    Dai, M.-S.4    Lu, H.5
  • 43
    • 0345701307 scopus 로고    scopus 로고
    • Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate
    • M. Zhang, C.M. Pickart, P. Cofno, Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate, EMBO J. 22 (2003) 1488-1496.
    • (2003) EMBO J , vol.22 , pp. 1488-1496
    • Zhang, M.1    Pickart, C.M.2    Cofno, P.3
  • 44
    • 40449121214 scopus 로고    scopus 로고
    • Structural elements of the ubiquitin- independent proteasome degron of ornithine decarboxylase
    • J. Takeuchi, H. Chen, M.A. Hoyt, P. Cofno, Structural elements of the ubiquitin- independent proteasome degron of ornithine decarboxylase, Biochem. J. 410 (2008) 401-407.
    • (2008) Biochem. J. , vol.410 , pp. 401-407
    • Takeuchi, J.1    Chen, H.2    Hoyt, M.A.3    Cofno, P.4
  • 45
    • 31044449824 scopus 로고    scopus 로고
    • The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP- independent manner by the REGgamma proteasome
    • X. Li, D.M. Lonard, S.Y. Jung, A. Malovannaya, Q. Feng, J. Qin, S.Y. Tsai, M.J. Tsai, B.W. O'Malley, The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP- independent manner by the REGgamma proteasome, Cell 124 (2006) 381-392.
    • (2006) Cell , vol.124 , pp. 381-392
    • Li, X.1    Lonard, D.M.2    Jung, S.Y.3    Malovannaya, A.4    Feng, Q.5    Qin, J.6    Tsai, S.Y.7    Tsai, M.J.8    O'Malley, B.W.9
  • 46
    • 34250339984 scopus 로고    scopus 로고
    • Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGgamma-proteasome pathway
    • X. Li, L. Amazit, W. Long, D.M. Lonard, J.J. Monaco, B.W. O'Malley, Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGgamma-proteasome pathway, Mol. Cell 26 (2007) 831-842.
    • (2007) Mol. Cell , vol.26 , pp. 831-842
    • Li, X.1    Amazit, L.2    Long, W.3    Lonard, D.M.4    Monaco, J.J.5    O'Malley, B.W.6
  • 47
    • 34250342888 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome
    • X. Chen, L.F. Barton, Y. Chi, B.E. Clurman, J.M. Roberts, Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome, Mol. Cell 26 (2007) 843-852.
    • (2007) Mol. Cell , vol.26 , pp. 843-852
    • Chen, X.1    Barton, L.F.2    Chi, Y.3    Clurman, B.E.4    Roberts, J.M.5
  • 51
    • 78649489748 scopus 로고    scopus 로고
    • Why do viruses cause cancer? Highlights of the rst century of human tumour virology
    • P.S. Moore, Y. Chang, Why do viruses cause cancer? Highlights of the rst century of human tumour virology, Nat. Rev. Cancer 10 (2010) 878-889.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 878-889
    • Moore, P.S.1    Chang, Y.2
  • 52
    • 59349121140 scopus 로고    scopus 로고
    • Papillomaviruses in the causation of human cancers - a brief historical account
    • H. zur Hausen, Papillomaviruses in the causation of human cancers - a brief historical account, Virology 384 (2009) 260-265.
    • (2009) Virology , vol.384 , pp. 260-265
    • zur Hausen, H.1
  • 53
    • 58249118272 scopus 로고    scopus 로고
    • The story of human cytomegalovirus and cancer: increasing evidence and open questions
    • M. Michaelis, H.W. Doerr, J. Cinatl, The story of human cytomegalovirus and cancer: increasing evidence and open questions, Neoplasia 11 (2009) 1-9.
    • (2009) Neoplasia , vol.11 , pp. 1-9
    • Michaelis, M.1    Doerr, H.W.2    Cinatl, J.3
  • 54
    • 1242351241 scopus 로고    scopus 로고
    • Oncomodulatory signals by regulatory proteins encoded by human cytomegalovirus: a novel role for viral infection in tumor progression
    • J. Cinatl Jr., J.U. Vogel, R. Kotchetkov, H. Wilhelm Doerr, Oncomodulatory signals by regulatory proteins encoded by human cytomegalovirus: a novel role for viral infection in tumor progression, FEMS Microbiol. Rev. 28 (2004) 59-77.
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 59-77
    • Cinatl, Jr.J.1    Vogel, J.U.2    Kotchetkov, R.3    Wilhelm Doerr, H.4
  • 55
    • 0034600355 scopus 로고    scopus 로고
    • Papillomaviruses causing cancer: evasion from host-cell control in early events in carcinogenesis
    • H. zur Hausen, Papillomaviruses causing cancer: evasion from host-cell control in early events in carcinogenesis, J. Natl. Cancer Inst. 92 (2000) 690-698.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 690-698
    • zur Hausen, H.1
  • 56
    • 0029834371 scopus 로고    scopus 로고
    • E7 protein of human papilloma virus-16 induces degradation of retinoblastoma protein through the ubiquitin-proteasome path- way
    • S.N. Boyer, D.E. Wazer, V. Band, E7 protein of human papilloma virus-16 induces degradation of retinoblastoma protein through the ubiquitin-proteasome path- way, Cancer Research 56 (1996) 4620-4624.
    • (1996) Cancer Research , vol.56 , pp. 4620-4624
    • Boyer, S.N.1    Wazer, D.E.2    Band, V.3
  • 57
    • 33748039092 scopus 로고    scopus 로고
    • Retinoblastoma family proteins as key targets of the small DNA virus oncoproteins
    • A. Felsani, A.M. Mileo, M.G. Paggi, Retinoblastoma family proteins as key targets of the small DNA virus oncoproteins, Oncogene 25 (2006) 5277-5285.
    • (2006) Oncogene , vol.25 , pp. 5277-5285
    • Felsani, A.1    Mileo, A.M.2    Paggi, M.G.3
  • 58
    • 0027468543 scopus 로고
    • Human papillomavirus type 16 E7 regulates E2F and contributes to mitogenic signalling
    • J.D. Morris, T. Crook, L.R. Bandara, R. Davies, N.B. LaThangue, K.H. Vousden, Human papillomavirus type 16 E7 regulates E2F and contributes to mitogenic signalling, Oncogene 8 (1993) 893-898.
    • (1993) Oncogene , vol.8 , pp. 893-898
    • Morris, J.D.1    Crook, T.2    Bandara, L.R.3    Davies, R.4    LaThangue, N.B.5    Vousden, K.H.6
  • 59
    • 34848876774 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E7 oncoprotein associates with the cullin 2 ubiquitin ligase complex, which contributes to degradation of the retinoblastoma tumor suppressor
    • K. Huh, X. Zhou, H. Hayakawa, J.-Y. Cho, T.A. Libermann, J. Jin, J. Wade Harper, K. Munger, Human papillomavirus type 16 E7 oncoprotein associates with the cullin 2 ubiquitin ligase complex, which contributes to degradation of the retinoblastoma tumor suppressor, J. Virol. 81 (2007) 9737-9747.
    • (2007) J. Virol. , vol.81 , pp. 9737-9747
    • Huh, K.1    Zhou, X.2    Hayakawa, H.3    Cho, J.-Y.4    Libermann, T.A.5    Jin, J.6    Wade Harper, J.7    Munger, K.8
  • 60
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
    • M. Scheffner, B. Werness, J. Huibregtse, A. Levine, P. Howley, The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53, Cell 63 (1990) 1129-1136.
    • (1990) Cell , vol.63 , pp. 1129-1136
    • Scheffner, M.1    Werness, B.2    Huibregtse, J.3    Levine, A.4    Howley, P.5
  • 61
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: the cell's response to p53
    • K.H. Vousden, X. Lu, Live or let die: the cell's response to p53, Nat. Rev. Cancer 2 (2002) 594-604.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 62
    • 0025876591 scopus 로고
    • The p53 tumour suppressor gene
    • A.J. Levine, J. Momand, C.A. Finlay, The p53 tumour suppressor gene, Nature 351 (1991) 453-456.
    • (1991) Nature , vol.351 , pp. 453-456
    • Levine, A.J.1    Momand, J.2    Finlay, C.A.3
  • 65
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Y. Haupt, R. Maya, A. Kazaz, M. Oren, Mdm2 promotes the rapid degradation of p53, Nature 387 (1997) 296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 66
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • M. Scheffner, J. Huibregtse, R. Vierstra, P. Howley, The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53, Cell 75 (1993) 495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.2    Vierstra, R.3    Howley, P.4
  • 67
    • 34247221276 scopus 로고    scopus 로고
    • Ubiquitin- independent degradation of p53 mediated by high-risk human papillomavirus protein E6
    • S. Camus, S. Menendez, C.F. Cheok, L.F. Stevenson, S. Lain, D.P. Lane, Ubiquitin- independent degradation of p53 mediated by high-risk human papillomavirus protein E6, Oncogene 26 (2007) 4059-4070.
    • (2007) Oncogene , vol.26 , pp. 4059-4070
    • Camus, S.1    Menendez, S.2    Cheok, C.F.3    Stevenson, L.F.4    Lain, S.5    Lane, D.P.6
  • 68
    • 8944239884 scopus 로고    scopus 로고
    • High-risk human papillomavirus E6 protein has two distinct binding sites within p53, of which only one determinesdegradation
    • X.Li,P.Cofno, High-risk human papillomavirus E6 protein has two distinct binding sites within p53, of which only one determinesdegradation, J.Virol.70(1996) 4509-4516.
    • (1996) J. Virol. , vol.70 , pp. 4509-4516
    • Li, X.1    Cofno, P.2
  • 70
    • 34548158284 scopus 로고    scopus 로고
    • Cytomegaloviruses
    • D.M. Knipe, P.M. Howley (Eds.), Philadelphia
    • E.S. Mocarski, T. Shenk, R.F. Pass, Cytomegaloviruses, in: D.M. Knipe, P.M. Howley (Eds.), Fields Virology, Lippincott, Philadelphia, 2007, pp. 2701-2772.
    • (2007) Fields Virology, Lippincott , pp. 2701-2772
    • Mocarski, E.S.1    Shenk, T.2    Pass, R.F.3
  • 72
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • D. Hanahan, R.A. Weinberg, Hallmarks of cancer: the next generation, Cell 144 (2011) 646-674.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 74
    • 48849114064 scopus 로고    scopus 로고
    • Human cytomegalovirus modulation of signal transduction
    • A.D. Yurochko, Human cytomegalovirus modulation of signal transduction, Curr. Top. Microbiol. Immunol. 325 (2008) 205-220.
    • (2008) Curr. Top. Microbiol. Immunol. , vol.325 , pp. 205-220
    • Yurochko, A.D.1
  • 76
    • 61349118084 scopus 로고    scopus 로고
    • Regulation of the retinoblastoma proteins by the human herpesviruses
    • A.J. Hume, R.F. Kalejta, Regulation of the retinoblastoma proteins by the human herpesviruses, Cell Div. 4 (2009) 1.
    • (2009) Cell Div , vol.4 , pp. 1
    • Hume, A.J.1    Kalejta, R.F.2
  • 77
    • 77950469982 scopus 로고    scopus 로고
    • Modulation of host innate and adaptive immune defenses by cytomegalovirus: timing is everything
    • A. Loewendorf, C.A. Benedict, Modulation of host innate and adaptive immune defenses by cytomegalovirus: timing is everything, J. Int. Med. 267 (2010) 483-501.
    • (2010) J. Int. Med. , vol.267 , pp. 483-501
    • Loewendorf, A.1    Benedict, C.A.2
  • 78
    • 59649121998 scopus 로고    scopus 로고
    • Immunobiology of human cytomegalovirus: from bench to bedside
    • T. Crough, R. Khanna, Immunobiology of human cytomegalovirus: from bench to bedside, Clin. Microbiol. Rev. 22 (2009) 76-98.
    • (2009) Clin. Microbiol. Rev. , vol.22 , pp. 76-98
    • Crough, T.1    Khanna, R.2
  • 80
    • 48849108427 scopus 로고    scopus 로고
    • Manifestations of human cytomegalovirus infection: proposed mechanisms of acute and chronic disease
    • W. Britt, Manifestations of human cytomegalovirus infection: proposed mechanisms of acute and chronic disease, Curr. Top. Microbiol. Immunol. 325 (2008) 417-470.
    • (2008) Curr. Top. Microbiol. Immunol. , vol.325 , pp. 417-470
    • Britt, W.1
  • 82
    • 76049130197 scopus 로고    scopus 로고
    • ActivationofEGFRonmonocytesis required for human cytomegalovirus entry and mediates cellular motility
    • G.Chan, M.T. Nogalski, A.D. Yurochko, ActivationofEGFRonmonocytesis required for human cytomegalovirus entry and mediates cellular motility, Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 22369-22374.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 22369-22374
    • Chan, G.1    Nogalski, M.T.2    Yurochko, A.D.3
  • 83
    • 79955032415 scopus 로고    scopus 로고
    • The role of cytomegalovirus in angiogenesis
    • P. Caposio, S.L. Orloff, D.N. Streblow, The role of cytomegalovirus in angiogenesis, Virus Res. 157 (2010) 204-211.
    • (2010) Virus Res , vol.157 , pp. 204-211
    • Caposio, P.1    Orloff, S.L.2    Streblow, D.N.3
  • 85
    • 0030611773 scopus 로고    scopus 로고
    • Human cytomegalovirus IE1 and IE2 proteins are mutagenic and mediate "hit-and-run" oncogenic transformation in cooperation with the adenovirus E1A proteins
    • Y. Shen, H. Zhu, T. Shenk, Human cytomegalovirus IE1 and IE2 proteins are mutagenic and mediate "hit-and-run" oncogenic transformation in cooperation with the adenovirus E1A proteins, Proc. Natl. Acad. Sci. 94 (1997) 3341-3345.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 3341-3345
    • Shen, Y.1    Zhu, H.2    Shenk, T.3
  • 86
    • 76249106205 scopus 로고    scopus 로고
    • HumancytomegalovirusUL76induces chromosome aberrations
    • V.K. Siew, C.Y. Duh, S.K. Wang, HumancytomegalovirusUL76induces chromosome aberrations, J. Biomed. Sci. 16 (2009) 107.
    • (2009) J. Biomed. Sci. , vol.16 , pp. 107
    • Siew, V.K.1    Duh, C.Y.2    Wang, S.K.3
  • 87
    • 79955043158 scopus 로고    scopus 로고
    • Inhibition of programmed cell death by cytomegaloviruses
    • W. Brune, Inhibition of programmed cell death by cytomegaloviruses, Virus Res. 157 (2010) 144-150.
    • (2010) Virus Res , vol.157 , pp. 144-150
    • Brune, W.1
  • 88
    • 79958108811 scopus 로고    scopus 로고
    • Human cytomegalovirus induces the activity and expression of acetyl-CoA carboxylase, a fatty acid biosynthetic enzyme whose inhibition attenuates viral replication
    • C.M. Spencer, X.L. Schafer, N.J. Moorman, J. Munger, Human cytomegalovirus induces the activity and expression of acetyl-CoA carboxylase, a fatty acid biosynthetic enzyme whose inhibition attenuates viral replication, J. Virol. 85 (2011) 5814-5824.
    • (2011) J. Virol. , vol.85 , pp. 5814-5824
    • Spencer, C.M.1    Schafer, X.L.2    Moorman, N.J.3    Munger, J.4
  • 89
    • 75449105003 scopus 로고    scopus 로고
    • Glutamine metabolism is essential for human cytomegalovirus infection
    • J.W. Chambers, T.G. Maguire, J.C. Alwine, Glutamine metabolism is essential for human cytomegalovirus infection, J. Virol. 84 (2010) 1867-1873.
    • (2010) J. Virol. , vol.84 , pp. 1867-1873
    • Chambers, J.W.1    Maguire, T.G.2    Alwine, J.C.3
  • 90
    • 44949213015 scopus 로고    scopus 로고
    • Tegument proteins of human cytomegalovirus
    • R.F. Kalejta, Tegument proteins of human cytomegalovirus, Microbiol. Mol. Biol. Rev. 72 (2008) 249-265.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 249-265
    • Kalejta, R.F.1
  • 91
    • 0036091745 scopus 로고    scopus 로고
    • Functional interaction between the pp 71 protein of human cytomegalovirus and the PML-interacting protein human Daxx
    • H. Hofmann, H. Sindre, T. Stamminger, Functional interaction between the pp 71 protein of human cytomegalovirus and the PML-interacting protein human Daxx, J. Virol. 76 (2002) 5769-5783.
    • (2002) J. Virol. , vol.76 , pp. 5769-5783
    • Hofmann, H.1    Sindre, H.2    Stamminger, T.3
  • 92
    • 19944382805 scopus 로고    scopus 로고
    • Interaction between the human cytomega- lovirus UL82 gene product (pp71) and hDaxx regulates immediate-early gene expression and viral replication
    • S. R. Cantrell, W. A. Bresnahan, Interaction between the human cytomega- lovirus UL82 gene product (pp71) and hDaxx regulates immediate-early gene expression and viral replication, J. Virol. 79 (2005) 7792-7802.
    • (2005) J. Virol. , vol.79 , pp. 7792-7802
    • Cantrell, S.R.1    Bresnahan, W.A.2
  • 94
    • 0037373383 scopus 로고    scopus 로고
    • Human cytomegalovirus pp71 stimulates cell cycle progression by inducing the proteasome-dependent degradation of the retinoblastoma family of tumor suppressors
    • R.F. Kalejta, J.T. Bechtel, T. Shenk, Human cytomegalovirus pp71 stimulates cell cycle progression by inducing the proteasome-dependent degradation of the retinoblastoma family of tumor suppressors, Mol. Cell. Biol. 23 (2003) 1885-1895.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1885-1895
    • Kalejta, R.F.1    Bechtel, J.T.2    Shenk, T.3
  • 95
    • 33645757807 scopus 로고    scopus 로고
    • Inactivating a cellular intrinsic immune defense mediated by Daxx is the mechanism through which the human cytomegalovirus pp71 protein stimulates viral immediate-early gene expression
    • R.T. Saffert, R.F. Kalejta, Inactivating a cellular intrinsic immune defense mediated by Daxx is the mechanism through which the human cytomegalovirus pp71 protein stimulates viral immediate-early gene expression, J. Virol. 80 (2006) 3863-3871.
    • (2006) J. Virol. , vol.80 , pp. 3863-3871
    • Saffert, R.T.1    Kalejta, R.F.2
  • 96
    • 44049107548 scopus 로고    scopus 로고
    • Phosphorylation of retinoblastoma protein by viral protein with cyclin- dependent kinase function
    • A.J.Hume,J.S.Finkel,J.P.Kamil,D.M.Coen,M.R.Culbertson,R.F.Kalejta, Phosphorylation of retinoblastoma protein by viral protein with cyclin- dependent kinase function, Science 320 (2008) 797-799.
    • (2008) Science , vol.320 , pp. 797-799
    • Hume, A.J.1    Finkel, J.S.2    Kamil, J.P.3    Coen, D.M.4    Culbertson, M.R.5    Kalejta, R.F.6
  • 97
    • 0037452979 scopus 로고    scopus 로고
    • Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71p rotein
    • R.F. Kalejta, T. Shenk, Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71p rotein, Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 3263-3268.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 3263-3268
    • Kalejta, R.F.1    Shenk, T.2
  • 98
    • 34848835708 scopus 로고    scopus 로고
    • Proteasome-dependent, ubiquitin-independent degradation of Daxx by the viral pp71 protein in human cytomegalovirus- infected cells
    • J. Hwang, R.F. Kalejta, Proteasome-dependent, ubiquitin-independent degradation of Daxx by the viral pp71 protein in human cytomegalovirus- infected cells, Virology 367 (2007) 334-338.
    • (2007) Virology , vol.367 , pp. 334-338
    • Hwang, J.1    Kalejta, R.F.2
  • 99
    • 0038708117 scopus 로고    scopus 로고
    • X. Grana, SKP2 associates with p130 and accelerates p130 ubiquitylation and degradation in human cells
    • S.Bhattacharya, J. Garriga, J. Calbo, T. Yong, D.S. Haines, X. Grana,SKP2 associates with p130 and accelerates p130 ubiquitylation and degradation in human cells, Oncogene 22 (2003) 2443-2451.
    • (2003) Oncogene , vol.22 , pp. 2443-2451
    • Bhattacharya, S.1    Garriga, J.2    Calbo, J.3    Yong, T.4    Haines, D.S.5
  • 100
    • 34248379575 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins in protein regulation
    • J. Herrmann, L.O. Lerman, A. Lerman, Ubiquitin and ubiquitin-like proteins in protein regulation, Circ. Res. 100 (2007) 1276-1291.
    • (2007) Circ. Res. , vol.100 , pp. 1276-1291
    • Herrmann, J.1    Lerman, L.O.2    Lerman, A.3
  • 101
    • 67449089255 scopus 로고    scopus 로고
    • Human cytomegalovirus protein pp71 induces Daxx SUMOylation
    • J. Hwang, R.F. Kalejta, Human cytomegalovirus protein pp71 induces Daxx SUMOylation, J. Virol. 83 (2009) 6591-6598.
    • (2009) J. Virol. , vol.83 , pp. 6591-6598
    • Hwang, J.1    Kalejta, R.F.2
  • 102
    • 27744492409 scopus 로고    scopus 로고
    • Mechanisms of protein degradation: an odyssey with ODC
    • C. Kahana, G. Asher, Y. Shaul, Mechanisms of protein degradation: an odyssey with ODC, Cell Cycle 4 (2005) 1461-1464.
    • (2005) Cell Cycle , vol.4 , pp. 1461-1464
    • Kahana, C.1    Asher, G.2    Shaul, Y.3
  • 103
    • 72849131562 scopus 로고    scopus 로고
    • Human cytomegalovirus gene UL21a encodes a short-lived cytoplasmic protein and facilitates virus replication in broblasts
    • A.R. Fehr, D. Yu, Human cytomegalovirus gene UL21a encodes a short-lived cytoplasmic protein and facilitates virus replication in broblasts, J. Virol. 84 (2010) 291-302.
    • (2010) J. Virol. , vol.84 , pp. 291-302
    • Fehr, A.R.1    Yu, D.2
  • 104
    • 70450234993 scopus 로고    scopus 로고
    • The intrinsically disordered n-terminal domain of thymidylate synthase targets the enzyme to the ubiquitin-independent proteasomal degradation path- way
    • M.M.O. Peña, S.P. Melo, Y.-Y. Xing, K. White, K.W. Barbour, F.G. Berger, The intrinsically disordered n-terminal domain of thymidylate synthase targets the enzyme to the ubiquitin-independent proteasomal degradation path- way, J. Biol. Chem. 284 (2009) 31597-31607.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31597-31607
    • Peña, M.M.O.1    Melo, S.P.2    Xing, Y.-Y.3    White, K.4    Barbour, K.W.5    Berger, F.G.6
  • 105
    • 75449084620 scopus 로고    scopus 로고
    • Murine cytomegalovirus US22 protein pM140 protects its binding partner, pM141, from proteasome-dependent but ubiquitin-independent degradation
    • L.L. Bolin, L.K. Hanson, J.S. Slater, J.A. Kerry, A.E. Campbell, Murine cytomegalovirus US22 protein pM140 protects its binding partner, pM141, from proteasome-dependent but ubiquitin-independent degradation, J. Virol. 84 (2010) 2164-2168.
    • (2010) J. Virol. , vol.84 , pp. 2164-2168
    • Bolin, L.L.1    Hanson, L.K.2    Slater, J.S.3    Kerry, J.A.4    Campbell, A.E.5
  • 107
    • 0034979385 scopus 로고    scopus 로고
    • Products of US22 genes M140 and M141 confer efcient replication of murine cytomegalovirus in macrophages and spleen
    • L.K. Hanson, J.S. Slater, Z. Karabekian, G. Ciocco-Schmitt, A.E. Campbell, Products of US22 genes M140 and M141 confer efcient replication of murine cytomegalovirus in macrophages and spleen, J. Virol. 75 (2001) 6292-6302.
    • (2001) J. Virol. , vol.75 , pp. 6292-6302
    • Hanson, L.K.1    Slater, J.S.2    Karabekian, Z.3    Ciocco-Schmitt, G.4    Campbell, A.E.5
  • 108
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • M. Rechsteiner, S.W. Rogers, PEST sequences and regulation by proteolysis, Trends Biochem. Sci. 21 (1996) 267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 109
    • 0025143774 scopus 로고
    • Molecular biology and pathogenicity of human and animal parvoviruses
    • G. Siegl, Molecular biology and pathogenicity of human and animal parvoviruses, Behring Inst. Mitt. (1990) 6-13.
    • (1990) Behring Inst. Mitt. , pp. 6-13
    • Siegl, G.1
  • 110
    • 78651278905 scopus 로고    scopus 로고
    • Production, purication and characterization of adeno-associated vectors
    • E. Ayuso, F. Mingozzi, F. Bosch, Production, purication and characterization of adeno-associated vectors, Curr. Gene Ther. 10 (2010) 423-436.
    • (2010) Curr. Gene Ther. , vol.10 , pp. 423-436
    • Ayuso, E.1    Mingozzi, F.2    Bosch, F.3
  • 111
    • 0035811841 scopus 로고    scopus 로고
    • The NS2 protein generated by the parvovirus minute virus of mice is degraded by the proteasome in a manner independent of ubiquitin chain elongation or activation
    • C.L. Miller, D.J. Pintel, The NS2 protein generated by the parvovirus minute virus of mice is degraded by the proteasome in a manner independent of ubiquitin chain elongation or activation, Virology 285 (2001) 346-355.
    • (2001) Virology , vol.285 , pp. 346-355
    • Miller, C.L.1    Pintel, D.J.2
  • 112
    • 0025251614 scopus 로고
    • Thesmallnonstructuralprotein(NS2)oftheparvovirus minute virus of mice is required for efcient DNA replication and infectious virus production in a cell-type-specic manner
    • L.K. Naeger, J. Cater, D.J. Pinte Thesmallnonstructuralprotein(NS2)oftheparvovirus minute virus of mice is required for efcient DNA replication and infectious virus production in a cell-type-specic manner, J. Virol. 64 (1990) 6166-6175.
    • (1990) J. Virol. , vol.64 , pp. 6166-6175
    • Naeger, L.K.1    Cater, J.2    Pinte, D.J.3
  • 113
    • 0030993261 scopus 로고    scopus 로고
    • The NS2 polypeptide of parvovirus MVM is required for capsid assembly in murine cells
    • S.F. Cotmore, A.M. D'Abramo Jr., L.F. Carbonell, J. Bratton, P. Tattersall, The NS2 polypeptide of parvovirus MVM is required for capsid assembly in murine cells, Virology 231 (1997) 267-280.
    • (1997) Virology , vol.231 , pp. 267-280
    • Cotmore, S.F.1    D'Abramo Jr., A.M.2    Carbonell, L.F.3    Bratton, J.4    Tattersall, P.5
  • 114
    • 77955712659 scopus 로고    scopus 로고
    • Hepatitis B virus-related hepatocarci- nogenesis: molecular oncogenic potential of clear or occult infections
    • M.S. De Mitri, R. Cassini, M. Bernardi, Hepatitis B virus-related hepatocarci- nogenesis: molecular oncogenic potential of clear or occult infections, Eur. J. Cancer 46 (2010) 2178-2186.
    • (2010) Eur. J. Cancer , vol.46 , pp. 2178-2186
    • De Mitri, M.S.1    Cassini, R.2    Bernardi, M.3
  • 115
    • 0030041821 scopus 로고    scopus 로고
    • Hepadnaviral X protein: review of recent progress
    • T.S. Yen, Hepadnaviral X protein: review of recent progress, J. Biomed. Sci. 3 (1996) 20-30.
    • (1996) J. Biomed. Sci. , vol.3 , pp. 20-30
    • Yen, T.S.1
  • 116
    • 8644274040 scopus 로고    scopus 로고
    • The enigmatic X gene of hepatitis B virus
    • M.J. Bouchard, R.J. Schneider, The enigmatic X gene of hepatitis B virus, J. Virol. 78 (2004) 12725-12734.
    • (2004) J. Virol. , vol.78 , pp. 12725-12734
    • Bouchard, M.J.1    Schneider, R.J.2
  • 117
    • 0025907983 scopus 로고
    • HBx gene of hepatitis B virus induces liver cancer in transgenic mice
    • C.M. Kim, K. Koike, I. Saito, T. Miyamura, G. Jay, HBx gene of hepatitis B virus induces liver cancer in transgenic mice, Nature 351 (1991) 317-320.
    • (1991) Nature , vol.351 , pp. 317-320
    • Kim, C.M.1    Koike, K.2    Saito, I.3    Miyamura, T.4    Jay, G.5
  • 118
    • 0032816238 scopus 로고    scopus 로고
    • Hepatitis B virus X protein is both a substrate and a potential inhibitor of the proteasome complex
    • Z. Hu, Z. Zhang, E. Doo, O. Coux, A.L. Goldberg, T.J. Liang, Hepatitis B virus X protein is both a substrate and a potential inhibitor of the proteasome complex, J. Virol. 73 (1999) 7231-7240.
    • (1999) J. Virol. , vol.73 , pp. 7231-7240
    • Hu, Z.1    Zhang, Z.2    Doo, E.3    Coux, O.4    Goldberg, A.L.5    Liang, T.J.6
  • 119
    • 37649020435 scopus 로고    scopus 로고
    • Ubiquitin-dependent and -independent proteasomal degradation of hepatitis B virus X protein
    • J.H. Kim, S.Y. Sohn, T.S. Benedict Yen, B.Y. Ahn, Ubiquitin-dependent and -independent proteasomal degradation of hepatitis B virus X protein, Biochem. Biophys. Res. Commun. 366 (2008) 1036-1042.
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 1036-1042
    • Kim, J.H.1    Sohn, S.Y.2    Benedict Yen, T.S.3    Ahn, B.Y.4
  • 120
    • 0037226227 scopus 로고    scopus 로고
    • Hepatitis B virus HBx peptide 116-138 and proteasome activator PA28 compete for binding to the proteasome alpha4/MC6 subunit
    • R. Stohwasser, H.G. Holzhutter, U. Lehmann, P. Henklein, P.M. Kloetzel, Hepatitis B virus HBx peptide 116-138 and proteasome activator PA28 compete for binding to the proteasome alpha4/MC6 subunit, Biol. Chem. 384 (2003) 39-49.
    • (2003) Biol. Chem. , vol.384 , pp. 39-49
    • Stohwasser, R.1    Holzhutter, H.G.2    Lehmann, U.3    Henklein, P.4    Kloetzel, P.M.5
  • 121
    • 0034685805 scopus 로고    scopus 로고
    • Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex
    • Z. Zhang, N. Torii, A. Furusaka, N. Malayaman, Z. Hu, T.J. Liang, Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex, J. Biol. Chem. 275 (2000) 15157-15165.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15157-15165
    • Zhang, Z.1    Torii, N.2    Furusaka, A.3    Malayaman, N.4    Hu, Z.5    Liang, T.J.6
  • 122
    • 0035946294 scopus 로고    scopus 로고
    • HBV X protein targets HIV Tat-binding protein 1
    • O. Barak, A. Aronheim, Y. Shaul, HBV X protein targets HIV Tat-binding protein 1, Virology 283 (2001) 110-120.
    • (2001) Virology , vol.283 , pp. 110-120
    • Barak, O.1    Aronheim, A.2    Shaul, Y.3
  • 123
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: con- servation and adaptation of chaperone function
    • M.E. Cheetham, A.J. Caplan, Structure, function and evolution of DnaJ: con- servation and adaptation of chaperone function, Cell Stress Chaperones 3 (1998) 28-36.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 125
    • 33746368686 scopus 로고    scopus 로고
    • Turnover of hepatitis B virus X protein is facilitated by Hdj1, a human Hsp40/DnaJ protein
    • S.Y. Sohn, J.H. Kim, K.W. Baek, W.S. Ryu, B.Y. Ahn, Turnover of hepatitis B virus X protein is facilitated by Hdj1, a human Hsp40/DnaJ protein, Biochem. Biophys. Res. Commun. 347 (2006) 764-768.
    • (2006) Biochem. Biophys. Res. Commun. , vol.347 , pp. 764-768
    • Sohn, S.Y.1    Kim, J.H.2    Baek, K.W.3    Ryu, W.S.4    Ahn, B.Y.5
  • 126
    • 0001389495 scopus 로고    scopus 로고
    • Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae
    • D.H. Lee, M.Y. Sherman, A.L. Goldberg, Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae, Mol. Cell. Biol. 16 (1996) 4773-4781.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4773-4781
    • Lee, D.H.1    Sherman, M.Y.2    Goldberg, A.L.3
  • 127
    • 0036630405 scopus 로고    scopus 로고
    • Human retroviruses after 20 years: a perspective from the past and prospects for their future control
    • R.C. Gallo, Human retroviruses after 20 years: a perspective from the past and prospects for their future control, Immunol. Rev. 185 (2002) 236-265.
    • (2002) Immunol. Rev. , vol.185 , pp. 236-265
    • Gallo, R.C.1
  • 128
    • 79551614790 scopus 로고    scopus 로고
    • HIV infection, inammation, immunosenescence, and aging
    • S.G. Deeks, HIV infection, inammation, immunosenescence, and aging, Annu. Rev. Med. 62 (2011) 141-155.
    • (2011) Annu. Rev. Med. , vol.62 , pp. 141-155
    • Deeks, S.G.1
  • 129
    • 79955473602 scopus 로고    scopus 로고
    • HIV, EBV and KSHV: viral cooperation in the pathogenesis of human malignancies
    • S. Ramos da Silva, D. Elgui de Oliveira, HIV, EBV and KSHV: viral cooperation in the pathogenesis of human malignancies, Cancer Lett. 305 (2011) 175-185.
    • (2011) Cancer Lett , vol.305 , pp. 175-185
    • Ramos da Silva, S.1    Elgui de Oliveira, D.2
  • 130
    • 0033920260 scopus 로고    scopus 로고
    • Tat modies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunode- ciency virus type 1 transcription
    • M. Zhou, M.A. Halanski, M.F. Radonovich, F. Kashanchi, J. Peng, D.H. Price, J.N. Brady, Tat modies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunode- ciency virus type 1 transcription, Mol. Cell. Biol. 20 (2000) 5077-5086.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5077-5086
    • Zhou, M.1    Halanski, M.A.2    Radonovich, M.F.3    Kashanchi, F.4    Peng, J.5    Price, D.H.6    Brady, J.N.7
  • 134
    • 58149115206 scopus 로고    scopus 로고
    • REGgamma, a proteasome activator and beyond?
    • I. Mao, J. Liu, X. Li, H. Luo, REGgamma, a proteasome activator and beyond? Cell Mol. Life Sci. 65 (2008) 3971-3980.
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 3971-3980
    • Mao, I.1    Liu, J.2    Li, X.3    Luo, H.4
  • 135
    • 0141682702 scopus 로고    scopus 로고
    • Human immunodeciency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits
    • G.S. Apcher, S. Heink, D. Zantopf, P.M. Kloetzel, H.P. Schmid, R.J. Mayer, E. Kruger, Human immunodeciency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits, FEBS Lett. 553 (2003) 200-204.
    • (2003) FEBS Lett , vol.553 , pp. 200-204
    • Apcher, G.S.1    Heink, S.2    Zantopf, D.3    Kloetzel, P.M.4    Schmid, H.P.5    Mayer, R.J.6    Kruger, E.7
  • 136
    • 0025339890 scopus 로고
    • A cDNA for a protein that interacts with the human immunodeciency virus Tat transactivator
    • P. Nelbock, P. Dillon, A. Perkins, C. Rosen, A cDNA for a protein that interacts with the human immunodeciency virus Tat transactivator, Science 248 (1990) 1650-1653.
    • (1990) Science , vol.248 , pp. 1650-1653
    • Nelbock, P.1    Dillon, P.2    Perkins, A.3    Rosen, C.4
  • 137
    • 33947578030 scopus 로고    scopus 로고
    • Human T-cell leukaemia virus type 1 (HTLV-1) infectivity and cellular transformation
    • M.M Atsuoka, K.-T. Jeang, Human T-cell leukaemia virus type 1 (HTLV-1) infectivity and cellular transformation, Nat. Rev. Cancer 7 (2007) 270-280.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 270-280
    • Atsuoka, M.M.1    Jeang, K.-T.2
  • 138
    • 79953033524 scopus 로고    scopus 로고
    • Human T-cell leukemia virus type 1 (HTLV-1) and leukemic transformation: viral infectivity, Tax, HBZ and therapy
    • M. Matsuoka, K.T. Jeang, Human T-cell leukemia virus type 1 (HTLV-1) and leukemic transformation: viral infectivity, Tax, HBZ and therapy, Oncogene 30 (2011) 1379-1389.
    • (2011) Oncogene , vol.30 , pp. 1379-1389
    • Matsuoka, M.1    Jeang, K.T.2
  • 139
    • 77949273352 scopus 로고    scopus 로고
    • The HTLV-1 Tax protein: Revealing mechanisms of transcriptional activation through histone acetylation and nucleosome disassembly
    • J.K. Nyborg, D. Egan, N. Sharma, The HTLV-1 Tax protein: Revealing mechanisms of transcriptional activation through histone acetylation and nucleosome disassembly, Biochim. Biophys. Acta (BBA) - Gene Regul. Mech. 1799 (2010) 266-274.
    • (2010) Biochim. Biophys. Acta (BBA) - Gene Regul. Mech , vol.1799 , pp. 266-274
    • Nyborg, J.K.1    Egan, D.2    Sharma, N.3
  • 140
    • 0032549585 scopus 로고    scopus 로고
    • A human T-cell leukemia virus Tax variant incapable of activating NF-κB retains its immortalizing potential for primary T-lymphocytes
    • O. Rosin, C. Koch, I. Schmitt, O.J. Semmes, K.-T. Jeang, R. Grassmann, A human T-cell leukemia virus Tax variant incapable of activating NF-κB retains its immortalizing potential for primary T-lymphocytes, J. Biol. Chem. 273 (1998) 6698-6703.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6698-6703
    • Rosin, O.1    Koch, C.2    Schmitt, I.3    Semmes, O.J.4    Jeang, K.-T.5    Grassmann, R.6
  • 141
    • 0032993635 scopus 로고    scopus 로고
    • Immortalization of CD4+ and CD8+ T lymphocytes by human T-cell leukemia virus type 1 Tax mutants expressed in a functional molecular clone
    • M.D. Robek, L. Ratner, Immortalization of CD4+ and CD8+ T lymphocytes by human T-cell leukemia virus type 1 Tax mutants expressed in a functional molecular clone, J. Virol. 73 (1999) 4856-4865.
    • (1999) J. Virol. , vol.73 , pp. 4856-4865
    • Robek, M.D.1    Ratner, L.2
  • 142
    • 0025037838 scopus 로고
    • The human T-lymphotropic virus type I tax gene can cooperate with the ras oncogene to induce neoplastic transformation of cells
    • R. Pozzatti, J. Vogel, G. Jay, The human T-lymphotropic virus type I tax gene can cooperate with the ras oncogene to induce neoplastic transformation of cells, Mol. Cell. Biol. 10 (1990) 413-417.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 413-417
    • Pozzatti, R.1    Vogel, J.2    Jay, G.3
  • 143
    • 0033596125 scopus 로고    scopus 로고
    • Persistent activation of NF-kappaB by the tax transforming protein of HTLV-1: hijacking cellular IkappaB kinases
    • S.C. Sun, D.W. Ballard, Persistent activation of NF-kappaB by the tax transforming protein of HTLV-1: hijacking cellular IkappaB kinases, Oncogene 18 (1999) 6948-6958.
    • (1999) Oncogene , vol.18 , pp. 6948-6958
    • Sun, S.C.1    Ballard, D.W.2
  • 144
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-kappaB transcription factors
    • H.L. Pahl, Activators and target genes of Rel/NF-kappaB transcription factors, Oncogene 18 (1999) 6853-6866.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 145
    • 0036771765 scopus 로고    scopus 로고
    • Two pathways to NF-[kappa]B
    • J.L. Pomerantz, D. Baltimore, Two pathways to NF-[kappa]B, Mol. Cell 10 (2002) 693-695.
    • (2002) Mol. Cell , vol.10 , pp. 693-695
    • Pomerantz, J.L.1    Baltimore, D.2
  • 146
    • 0028929371 scopus 로고
    • Coupling of a signal response domain in I kappa B alpha to multiple pathways for NF-kappa B activation
    • J.A. Brockman, D.C. Scherer, T.A. McKinsey, S.M. Hall, X. Qi, W.Y. Lee, D.W. Ballard, Coupling of a signal response domain in I kappa B alpha to multiple pathways for NF-kappa B activation, Mol. Cell. Biol. 15 (1995) 2809-2818.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2809-2818
    • Brockman, J.A.1    Scherer, D.C.2    McKinsey, T.A.3    Hall, S.M.4    Qi, X.5    Lee, W.Y.6    Ballard, D.W.7
  • 148
    • 0032488219 scopus 로고    scopus 로고
    • Association between HTLV-1 Tax and I kappa B alpha is dependent on the I kappa B alpha phosphorylation state
    • L. Petropoulos, J. Hiscott, Association between HTLV-1 Tax and I kappa B alpha is dependent on the I kappa B alpha phosphorylation state, Virology 252 (1998) 189-199.
    • (1998) Virology , vol.252 , pp. 189-199
    • Petropoulos, L.1    Hiscott, J.2
  • 149
    • 0029902650 scopus 로고    scopus 로고
    • Effects on NF-kappa B1/p105 processing of the interaction between the HTLV-1 transactivator Tax and the proteasome
    • R. Rousset, C. Desbois, F. Bantignies, P. Jalinot, Effects on NF-kappa B1/p105 processing of the interaction between the HTLV-1 transactivator Tax and the proteasome, Nature 381 (1996) 328-331.
    • (1996) Nature , vol.381 , pp. 328-331
    • Rousset, R.1    Desbois, C.2    Bantignies, F.3    Jalinot, P.4
  • 151
    • 78649992830 scopus 로고    scopus 로고
    • The human rhinovirus: human-pathological impact, mechanisms of antirhinoviral agents, and strategies for their discovery
    • J.M. Rollinger, M. Schmidtke, The human rhinovirus: human-pathological impact, mechanisms of antirhinoviral agents, and strategies for their discovery, Med. Res. Rev. 31 (2011) 42-92.
    • (2011) Med. Res. Rev. , vol.31 , pp. 42-92
    • Rollinger, J.M.1    Schmidtke, M.2
  • 154
    • 17344381535 scopus 로고    scopus 로고
    • Hepatitis C virus biology
    • C. Giannini, C. Brechot, Hepatitis C virus biology, Cell Death Differ. 10 (Suppl 1) (2003) S27-S38.
    • (2003) Cell Death Differ , vol.10 , Issue.SUPPL. 1
    • Giannini, C.1    Brechot, C.2
  • 156
    • 60049095596 scopus 로고    scopus 로고
    • Proteasomal turnover of hepatitis C virus core protein is regulated by two distinct mechanisms: a ubiquitin-dependent mechanism and a ubiquitin-independent but PA28gamma-dependent mechanism
    • R. Suzuki, K. Moriishi, K. Fukuda, M. Shirakura, K. Ishii, I. Shoji, T. Wakita, T. Miyamura, Y. Matsuura, T. Suzuki, Proteasomal turnover of hepatitis C virus core protein is regulated by two distinct mechanisms: a ubiquitin-dependent mechanism and a ubiquitin-independent but PA28gamma-dependent mechanism, J. Virol. 83 (2009) 2389-2392.
    • (2009) J. Virol. , vol.83 , pp. 2389-2392
    • Suzuki, R.1    Moriishi, K.2    Fukuda, K.3    Shirakura, M.4    Ishii, K.5    Shoji, I.6    Wakita, T.7    Miyamura, T.8    Matsuura, Y.9    Suzuki, T.10
  • 158
    • 58149517677 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of hepatitis C virus F protein
    • K. Yuksek, W.L. Chen, D. Chien, J.H. Ou, Ubiquitin-independent degradation of hepatitis C virus F protein, J. Virol. 83 (2009) 612-621.
    • (2009) J. Virol. , vol.83 , pp. 612-621
    • Yuksek, K.1    Chen, W.L.2    Chien, D.3    Ou, J.H.4
  • 161
    • 33845604018 scopus 로고    scopus 로고
    • Antiviralactivityofproteasomeinhibitorsinherpes simplex virus-1 infection: role of nuclear factor-kappaB
    • S. LaFrazia, C. Amici, M.G. Santoro, Antiviralactivityofproteasomeinhibitorsinherpes simplex virus-1 infection: role of nuclear factor-kappaB, Antivir. Ther. 11 (2006) 995-1004.
    • (2006) Antivir. Ther. , vol.11 , pp. 995-1004
    • LaFrazia, S.1    Amici, C.2    Santoro, M.G.3
  • 163
    • 0348223942 scopus 로고    scopus 로고
    • Proteasome inhibitors: a novel tool to suppress human cytomegalovirus replication and virus-induced immune modulation
    • S. Prosch, C. Priemer, C. Hoich, C. Liebenthaf, N. Babel, D.H. Kruger, H.D. Volk, Proteasome inhibitors: a novel tool to suppress human cytomegalovirus replication and virus-induced immune modulation, Antivir. Ther. 8 (2003) 555-567.
    • (2003) Antivir. Ther. , vol.8 , pp. 555-567
    • Prosch, S.1    Priemer, C.2    Hoich, C.3    Liebenthaf, C.4    Babel, N.5    Kruger, D.H.6    Volk, H.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.