메뉴 건너뛰기




Volumn 3, Issue 10, 2005, Pages 799-808

TRIM family proteins: Retroviral restriction and antiviral defence

Author keywords

[No Author keywords available]

Indexed keywords

PROMYELOCYTIC LEUKEMIA PROTEIN; TRIPARTITE PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; NUCLEAR PROTEIN; PML PROTEIN, HUMAN; PROTEIN; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR; TRIM22 PROTEIN, HUMAN; TRIM32 PROTEIN, HUMAN; TRIM5(ALPHA) PROTEIN, RHESUS MONKEY; TUMOR PROTEIN; TUMOR SUPPRESSOR PROTEIN;

EID: 27244444559     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro1248     Document Type: Review
Times cited : (635)

References (128)
  • 1
    • 0002441585 scopus 로고
    • Mode of action of interferon
    • Isaacs, A. & Burke, D. C. Mode of action of interferon. Nature 182, 1073-1074 (1958).
    • (1958) Nature , vol.182 , pp. 1073-1074
    • Isaacs, A.1    Burke, D.C.2
  • 2
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov, R., Preston-Hurlburt, P. & Janeway, C. A. Jr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 388, 394-397 (1997).
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 3
    • 10944260126 scopus 로고    scopus 로고
    • Retrovirus restriction factors
    • Goff, S. P. Retrovirus restriction factors. Mol. Cell 16, 849-859 (2004).
    • (2004) Mol. Cell , vol.16 , pp. 849-859
    • Goff, S.P.1
  • 4
    • 8544241736 scopus 로고    scopus 로고
    • Retroviral restriction by APOBEC proteins
    • Harris, R. S. & Liddament, M. T. Retroviral restriction by APOBEC proteins. Nature Rev. Immunol. 4, 868-877 (2004).
    • (2004) Nature Rev. Immunol. , vol.4 , pp. 868-877
    • Harris, R.S.1    Liddament, M.T.2
  • 5
    • 14344252157 scopus 로고    scopus 로고
    • Induction and suppression of RNA silencing: Insights from viral infections
    • Voinnet, O. Induction and suppression of RNA silencing: Insights from viral infections. Nature Rev. Genet. 6, 206-220 (2005).
    • (2005) Nature Rev. Genet. , vol.6 , pp. 206-220
    • Voinnet, O.1
  • 6
    • 0037031709 scopus 로고    scopus 로고
    • Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein
    • Gao, G., Guo, X. & Goff, S. P. Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein. Science 297, 1703-1706 (2002).
    • (2002) Science , vol.297 , pp. 1703-1706
    • Gao, G.1    Guo, X.2    Goff, S.P.3
  • 7
    • 0025999551 scopus 로고
    • The cloning and characterization of a maternally expressed novel zinc finger nuclear phosphoprotein (xnf7) in Xenopus laevis
    • Reddy, B. A., Kloc, M. & Etkin, L. The cloning and characterization of a maternally expressed novel zinc finger nuclear phosphoprotein (xnf7) in Xenopus laevis. Dev. Biol. 148, 107-116 (1991).
    • (1991) Dev. Biol. , vol.148 , pp. 107-116
    • Reddy, B.A.1    Kloc, M.2    Etkin, L.3
  • 8
    • 17744371839 scopus 로고    scopus 로고
    • The tripartite motif family identifies cell compartments
    • Reymond, A. et al. The tripartite motif family identifies cell compartments. EMBO J. 20, 2140-2151 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2140-2151
    • Reymond, A.1
  • 9
    • 9144252038 scopus 로고    scopus 로고
    • Complete sequencing and characterization of 21,243 full-length human cDNAs
    • Ota, T. et al. Complete sequencing and characterization of 21,243 full-length human cDNAs. Nature Genet. 36, 40-45 (2004).
    • (2004) Nature Genet. , vol.36 , pp. 40-45
    • Ota, T.1
  • 10
    • 0037168586 scopus 로고    scopus 로고
    • Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences
    • Strausberg, R. L. et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl Acad. Sci. USA 99, 16899-16903 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16899-16903
    • Strausberg, R.L.1
  • 11
    • 0036453682 scopus 로고    scopus 로고
    • RING finger, B-box, and coiled-coil (RBCC) protein expression in branchial elpithelial cells of Japanese eel, Anguilla japonica
    • Miyamoto, K. et al. RING finger, B-box, and coiled-coil (RBCC) protein expression in branchial elpithelial cells of Japanese eel, Anguilla japonica. Eur. J. Biochem. 269, 6152-6161 (2002).
    • (2002) Eur. J. Biochem. , vol.269 , pp. 6152-6161
    • Miyamoto, K.1
  • 12
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of the nematode C. elegans: A platform for investigating biology
    • C. elegans Sequencing Consortium
    • C. elegans Sequencing Consortium. Genome sequence of the nematode C. elegans: A platform for investigating biology. Science 282, 2012-2018 (1998).
    • (1998) Science , vol.282 , pp. 2012-2018
  • 14
    • 0027394788 scopus 로고
    • Identification and preliminary characterization of a protein motif related to the zinc finger
    • Levering, R. et al. Identification and preliminary characterization of a protein motif related to the zinc finger. Proc. Natl Acad. Sci. USA 90, 2112-2116 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2112-2116
    • Levering, R.1
  • 15
    • 0034602928 scopus 로고    scopus 로고
    • RING domains: Master builders of molecular scaffolds?
    • Borden, K. L. RING domains: Master builders of molecular scaffolds? J. Mol. Biol. 295, 1103-1112 (2000).
    • (2000) J. Mol. Biol. , vol.295 , pp. 1103-1112
    • Borden, K.L.1
  • 16
    • 0033961923 scopus 로고    scopus 로고
    • RING for destruction?
    • Freemont, P. S. RING for destruction? Curr. Biol. 10, R84-R87 (2000).
    • (2000) Curr. Biol. , vol.10
    • Freemont, P.S.1
  • 17
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro, C. A. & Weissman, A. M. RING finger proteins: Mediators of ubiquitin ligase activity. Cell 102, 549-552 (2000).
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 18
    • 0038148965 scopus 로고    scopus 로고
    • BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5δ
    • Xu, L. et al. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5δ. Exp. Cell Res. 288, 84-93 (2003).
    • (2003) Exp. Cell Res. , vol.288 , pp. 84-93
    • Xu, L.1
  • 19
    • 0035184651 scopus 로고    scopus 로고
    • MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation
    • Trockenbacher, A. et al. MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation. Nature Genet. 29, 287-294 (2001).
    • (2001) Nature Genet. , vol.29 , pp. 287-294
    • Trockenbacher, A.1
  • 20
    • 0037142070 scopus 로고    scopus 로고
    • σ for proteolysis and promotes breast tumour growth
    • σ for proteolysis and promotes breast tumour growth. Nature 417, 871-875 (2002).
    • (2002) Nature , vol.417 , pp. 871-875
    • Urano, T.1
  • 21
    • 10744221161 scopus 로고    scopus 로고
    • RING protein Trim32 associated with skin carcinogenesis has anti-apoptotic and E3-ubiquitin ligase properties
    • Horn, E. J. et al. RING protein Trim32 associated with skin carcinogenesis has anti-apoptotic and E3-ubiquitin ligase properties. Carcinogenesis, 25, 157-167 (2004).
    • (2004) Carcinogenesis , vol.25 , pp. 157-167
    • Horn, E.J.1
  • 22
    • 13844320524 scopus 로고    scopus 로고
    • E3 ubiquitin ligase activity of the trifunctional ARD1 ADP-ribosylation factor domain protein 1)
    • Vichi, A., Payne, D. M., Pacheco-Rodriguez, G., Moss, J. & Vaughan, M. E3 ubiquitin ligase activity of the trifunctional ARD1 ADP-ribosylation factor domain protein 1). Proc. Natl Acad. Sci. USA 102, 1945-1950 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1945-1950
    • Vichi, A.1    Payne, D.M.2    Pacheco-Rodriguez, G.3    Moss, J.4    Vaughan, M.5
  • 23
    • 0026782376 scopus 로고
    • A novel zinc finger coiled-coil domain in a family of nuclear proteins
    • Reddy, B. A., Etkin, L. D. & Freemont, P. S. A novel zinc finger coiled-coil domain in a family of nuclear proteins. Trends Biochem. Sci. 17, 344-345 (1992).
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 344-345
    • Reddy, B.A.1    Etkin, L.D.2    Freemont, P.S.3
  • 24
    • 0029918562 scopus 로고    scopus 로고
    • In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML
    • Borden, K. L. et al. In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML. Proc. Natl Acad. Sci. USA 93, 1601-1606 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1601-1606
    • Borden, K.L.1
  • 25
    • 0030751654 scopus 로고    scopus 로고
    • Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution
    • Cao, T., Borden, K. L., Freemont, P. S. & Etkin, L. D. Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution. J. Cell Sci. 110, 1563-1571 (1997).
    • (1997) J. Cell Sci. , vol.110 , pp. 1563-1571
    • Cao, T.1    Borden, K.L.2    Freemont, P.S.3    Etkin, L.D.4
  • 26
    • 0028932963 scopus 로고
    • The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML
    • Borden, K. L. et al. The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML. EMBO J. 14, 1532-1541 (1995).
    • (1995) EMBO J. , vol.14 , pp. 1532-1541
    • Borden, K.L.1
  • 27
    • 0034602922 scopus 로고    scopus 로고
    • Reconstitution of the KRAB-KAP-1 repressor complex: A model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interactions
    • Peng, H. et al. Reconstitution of the KRAB-KAP-1 repressor complex: A model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interactions. J. Mol. Biol. 295, 1139-1162 (2000).
    • (2000) J. Mol. Biol. , vol.295 , pp. 1139-1162
    • Peng, H.1
  • 29
    • 0031773260 scopus 로고    scopus 로고
    • B30.2-like domain proteins: Update and new insights into a rapidly expanding family of proteins
    • Henry, J., Mather, I. H., McDermott, M. F. & Pontarotti, P. B30.2-like domain proteins: Update and new insights into a rapidly expanding family of proteins. Mol. Biol. Evol. 15, 1696-1705 (1998).
    • (1998) Mol. Biol. Evol. , vol.15 , pp. 1696-1705
    • Henry, J.1    Mather, I.H.2    McDermott, M.F.3    Pontarotti, P.4
  • 30
    • 0027484261 scopus 로고
    • Evolutionary study of multigenic families mapping close to the human MHC class I region
    • Vernet, C. et al. Evolutionary study of multigenic families mapping close to the human MHC class I region. J. Mol. Evol. 37, 600-612 (1993).
    • (1993) J. Mol. Evol. , vol.37 , pp. 600-612
    • Vernet, C.1
  • 31
    • 13144258732 scopus 로고    scopus 로고
    • Twenty proteins containing a C-terminal SOCS box form five structural classes
    • Hilton, D. J. et al. Twenty proteins containing a C-terminal SOCS box form five structural classes. Proc. Natl Acad. Sci. USA 95, 114-119 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 114-119
    • Hilton, D.J.1
  • 32
    • 0028861418 scopus 로고
    • The PHD finger: Implications for chromatin-mediated transcriptional regulation
    • Aasland, R., Gibson, T. J. & Stewart, A. F. The PHD finger: Implications for chromatin-mediated transcriptional regulation. Trends Blochem. Sci. 20, 513-59 (1995).
    • (1995) Trends Blochem. Sci. , vol.20 , pp. 513-559
    • Aasland, R.1    Gibson, T.J.2    Stewart, A.F.3
  • 33
    • 0029841744 scopus 로고    scopus 로고
    • A possible involvement of TIF1 α and TIL 1 β in the epigenetic control of transcription by nuclear receptors
    • Le Douarin, B. et al. A possible involvement of TIF1 α and TIL 1 β in the epigenetic control of transcription by nuclear receptors. EMBO J. 15, 6701-6715 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6701-6715
    • Le Douarin, B.1
  • 34
    • 0033521759 scopus 로고    scopus 로고
    • TIF 1 γ, a novel member of the transcriptional intermediary factor 1 family
    • Venturini, L. et al. TIF 1 γ, a novel member of the transcriptional intermediary factor 1 family. Oncogene 18, 1209-1217 (1999).
    • (1999) Oncogene , vol.18 , pp. 1209-1217
    • Venturini, L.1
  • 35
    • 16944365196 scopus 로고    scopus 로고
    • A candidate gene for familial Mediterranean fever
    • The French FMF Consortium
    • The French FMF Consortium. A candidate gene for familial Mediterranean fever Nature Genet. 17, 25-31 (1997).
    • (1997) Nature Genet. , vol.17 , pp. 25-31
  • 36
    • 16944365777 scopus 로고    scopus 로고
    • Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22
    • Quaderi, N. A. et al. Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22. Nature Genet. 17, 285-291 (1997).
    • (1997) Nature Genet. , vol.17 , pp. 285-291
    • Quaderi, N.A.1
  • 37
    • 0036179479 scopus 로고    scopus 로고
    • Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene
    • Frosk, P. et al. Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene. Am. J. Hum. Genet. 70, 663-672 (2002).
    • (2002) Am. J. Hum. Genet. , vol.70 , pp. 663-672
    • Frosk, P.1
  • 38
    • 0033918327 scopus 로고    scopus 로고
    • Gene encoding a new RING-B-box-coiled-coil protein is mutated in mulibrey nanism
    • Avela, K. et al. Gene encoding a new RING-B-box-coiled-coil protein is mutated in mulibrey nanism. Nature Genet. 25, 298-301 (2000).
    • (2000) Nature Genet. , vol.25 , pp. 298-301
    • Avela, K.1
  • 39
    • 0025875679 scopus 로고
    • The PML-RARα fusion mRNA generated by the t(15; 17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
    • de The, H. et al. The PML-RARα fusion mRNA generated by the t(15; 17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66, 675-684 (1991).
    • (1991) Cell , vol.66 , pp. 675-684
    • de The, H.1
  • 40
    • 0025780876 scopus 로고
    • Chromosomal translocation t(15; 17) in human acute promyelocytic leukemia fuses RARα with a novel putative transcription factor, PML
    • Kakizuka, A. et al. Chromosomal translocation t(15; 17) in human acute promyelocytic leukemia fuses RARα with a novel putative transcription factor, PML. Cell 66, 663-674 (1991).
    • (1991) Cell , vol.66 , pp. 663-674
    • Kakizuka, A.1
  • 41
    • 0026326963 scopus 로고
    • Characterization of a zinc finger gene disrupted by the t(15; 17) in acute promyelocytic leukemia
    • Goddard, A. D., Borrow, J., Freemont, P. S. & Solomon, E. Characterization of a zinc finger gene disrupted by the t(15; 17) in acute promye
    • (1991) Science , vol.254 , pp. 1371-1374
    • Goddard, A.D.1    Borrow, J.2    Freemont, P.S.3    Solomon, E.4
  • 42
    • 0023875393 scopus 로고
    • Developmentally regulated expression of a human 'finger'-containing gene encoded by the 5′ half of the ret transforming gene
    • Takahashi, M., Inaguma, Y., Hiai, H. & Hirose, F. Developmentally regulated expression of a human 'finger'-containing gene encoded by the 5′ half of the ret transforming gene. Mol. Cell Biol. 8, 1853-1856 (1988).
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1853-1856
    • Takahashi, M.1    Inaguma, Y.2    Hiai, H.3    Hirose, F.4
  • 43
    • 0029030016 scopus 로고
    • The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18
    • Le Douarin, B. et al. The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18. EMBO J. 14, 2020-2033 (1995).
    • (1995) EMBO J. , vol.14 , pp. 2020-2033
    • Le Douarin, B.1
  • 44
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys
    • Stremlau, M. et al. The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys. Nature 427, 848-853 (2004).
    • (2004) Nature , vol.427 , pp. 848-853
    • Stremlau, M.1
  • 46
    • 3242670402 scopus 로고    scopus 로고
    • The human and African green monkey TRIM5α genes encode Ref1 and Lv1 retroviral restriction factor activities
    • Keckesova, Z., Ylihen, L. M. & Towers, G. J. The human and African green monkey TRIM5α genes encode Ref1 and Lv1 retroviral restriction factor activities. Proc. Natl Acad. Sci. USA 101, 10780-10785 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10780-10785
    • Keckesova, Z.1    Ylihen, L.M.2    Towers, G.J.3
  • 47
    • 4143132245 scopus 로고    scopus 로고
    • TRIM5α mediates the postentry block to N-tropic murine leukemia viruses in human cells
    • Perron, M. J. et al. TRIM5α mediates the postentry block to N-tropic murine leukemia viruses in human cells. Proc. Natl Acad. Sci. USA 101, 11827-11832 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11827-11832
    • Perron, M.J.1
  • 48
    • 3242720240 scopus 로고    scopus 로고
    • Trim5α protein restricts both HIV-1 and murine leukemia virus
    • Yap, M. W., Nisole, S., Lynch, C. & Stoye, J. P. Trim5α protein restricts both HIV-1 and murine leukemia virus. Proc. Natl Acad. Sci. USA 101, 10786-10791 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10786-10791
    • Yap, M.W.1    Nisole, S.2    Lynch, C.3    Stoye, J.P.4
  • 49
    • 0029015347 scopus 로고
    • Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression
    • Tissot, C. & Mechti, N. Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression. J. Biol. Chem. 270, 14891-14898 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 14891-14898
    • Tissot, C.1    Mechti, N.2
  • 50
    • 0346147033 scopus 로고    scopus 로고
    • Body language: The function of PML nuclear bodies in apoptosis regulation
    • Hofmann, T. G. & Will, H. Body language: The function of PML nuclear bodies in apoptosis regulation. Cell Death Differ. 10, 1290-1299 (2003).
    • (2003) Cell Death Differ. , vol.10 , pp. 1290-1299
    • Hofmann, T.G.1    Will, H.2
  • 51
    • 0035965139 scopus 로고    scopus 로고
    • The RING domains of the promyelocytic leukemia protein PML and the arenaviral protein Z repress translation by directly inhibiting translation initiation factor elF4E
    • Kentsis, A. et al. The RING domains of the promyelocytic leukemia protein PML and the arenaviral protein Z repress translation by directly inhibiting translation initiation factor elF4E. J. Mol. Biol. 312, 609-623 (2001).
    • (2001) J. Mol. Biol. , vol.312 , pp. 609-623
    • Kentsis, A.1
  • 52
    • 0034644274 scopus 로고    scopus 로고
    • PML regulates p53 acetylation and premature senescence induced by oncogenic Ras
    • Pearson, M. et al. PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 406, 207-210 (2000).
    • (2000) Nature , vol.406 , pp. 207-210
    • Pearson, M.1
  • 53
    • 0000237552 scopus 로고    scopus 로고
    • Role of PML in cell growth and the retinoic acid pathway
    • Wang, Z. G. et al. Role of PML in cell growth and the retinoic acid pathway. Science 279, 1547-1551 (1998).
    • (1998) Science , vol.279 , pp. 1547-1551
    • Wang, Z.G.1
  • 54
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF-β signalling
    • Lin, H. K., Bergmann, S. & Pandolfi, P. P. Cytoplasmic PML function in TGF-β signalling. Nature 431, 205-211 (2004).
    • (2004) Nature , vol.431 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 55
    • 0028293945 scopus 로고
    • The t(15; 17) translocation alters a nuclear body in a retinoic acid-reversible fashion
    • Koken, M. H. et al. The t(15; 17) translocation alters a nuclear body in a retinoic acid-reversible fashion. EMBO J. 13, 1073-1083 (1994).
    • (1994) EMBO J. , vol.13 , pp. 1073-1083
    • Koken, M.H.1
  • 56
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller, S., Matunis, M. J. & Dejean, A. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17, 61-70 (1998).
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 57
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1
    • Ishov, A. M. et al. PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1. J. Cell Biol. 147, 221-234 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 221-234
    • Ishov, A.M.1
  • 58
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1
    • Sternsdorf, T., Jensen, K. & Will, H. Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol. 139, 1621-1634 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 59
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • Dyck, J. A. et al. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76, 333-343 (1994).
    • (1994) Cell , vol.76 , pp. 333-343
    • Dyck, J.A.1
  • 60
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RARα in acute promyelocytic leukemia cells
    • Weis, K. et al. Retinoic acid regulates aberrant nuclear localization of PML-RARα in acute promyelocytic leukemia cells. Cell 76, 345-356 (1994).
    • (1994) Cell , vol.76 , pp. 345-356
    • Weis, K.1
  • 62
    • 0030890942 scopus 로고    scopus 로고
    • Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia
    • Zhu, J. et al. Arsenic-induced PML targeting onto nuclear bodies: implications for the treatment of acute promyelocytic leukemia. Proc. Natl Acad. Sci. USA 94, 3978-3983 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3978-3983
    • Zhu, J.1
  • 63
    • 0035908032 scopus 로고    scopus 로고
    • 3-induced PML or PML/retinoic acid receptor α degradation
    • 3-induced PML or PML/retinoic acid receptor α degradation. J. Exp. Med. 193, 1361-1371 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 1361-1371
    • Lallemand-Breitenbach, V.1
  • 64
    • 0042709466 scopus 로고    scopus 로고
    • PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatorv protein ICP0
    • Boutell, C., Orr, A. & Everett, R. D. PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatorv protein ICP0. J. Virol, 77, 8686-8694 (2003).
    • (2003) J. Virol. , vol.77 , pp. 8686-8694
    • Boutell, C.1    Orr, A.2    Everett, R.D.3
  • 65
    • 0036318221 scopus 로고    scopus 로고
    • Pondering the promyelocytic leukemia protein (PML) puzzle: Possible functions for PML nuclear bodies
    • Borden, K. L. Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies. Mol. Cell Biol. 22, 5259-5269 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5259-5269
    • Borden, K.L.1
  • 66
    • 0029560027 scopus 로고
    • Transcriptional induction of the PML growth suppressor gene by interferons is mediated through an ISRE and a GAS element
    • Stadler, M. et al. Transcriptional induction of the PML growth suppressor gene by interferons is mediated through an ISRE and a GAS element. Oncogene 11, 2565-2573 (1995).
    • (1995) Oncogene , vol.11 , pp. 2565-2573
    • Stadler, M.1
  • 67
    • 0029618165 scopus 로고
    • Induction of the PML protein by interferons in normal and APL cells
    • Chelbi-Alix, M. K. et al. Induction of the PML protein by interferons in normal and APL cells. Leukemia 9, 2027-2033 (1995).
    • (1995) Leukemia , vol.9 , pp. 2027-2033
    • Chelbi-Alix, M.K.1
  • 68
    • 0028979594 scopus 로고
    • The acute promyelocytic leukaemia-associated PML gene is induced by interferon
    • Lavau, C. et al. The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene 11, 871-876 (1995).
    • (1995) Oncogene , vol.11 , pp. 871-876
    • Lavau, C.1
  • 69
    • 0036715591 scopus 로고    scopus 로고
    • Viruses and interferon: A fight for supremacy
    • Katze, M. G., He, Y. & Gale, M. Jr. Viruses and interferon: A fight for supremacy. Nature Rev. Immunol. 2, 675-687 (2002).
    • (2002) Nature Rev. Immunol. , vol.2 , pp. 675-687
    • Katze, M.G.1    He, Y.2    Gale Jr., M.3
  • 70
    • 0031907092 scopus 로고    scopus 로고
    • Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein
    • Chelbi-Alix, M. K., Quignon, F., Pelicano, L., Koken, M. H. & de The, H. Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein. J. Virol. 72, 1043-1051 (1998).
    • (1998) J. Virol. , vol.72 , pp. 1043-1051
    • Chelbi-Alix, M.K.1    Quignon, F.2    Pelicano, L.3    Koken, M.H.4    de The, H.5
  • 71
    • 1542347736 scopus 로고    scopus 로고
    • Inhibition of different Lassa virus strains by α and γ interferons and comparison with a less pathogenic arenavirus
    • Asper, M. et al. Inhibition of different Lassa virus strains by α and γ interferons and comparison with a less pathogenic arenavirus. J. Virol. 78, 3162-3169 (2004).
    • (2004) J. Virol. , vol.78 , pp. 3162-3169
    • Asper, M.1
  • 72
    • 0034973563 scopus 로고    scopus 로고
    • Cytoplasmic recruitment of INI1 and PML on incoming HIV preintegration complexes: Interference with early steps of viral replication
    • Turelli, P. et al. Cytoplasmic recruitment of INI1 and PML on incoming HIV preintegration complexes: Interference with early steps of viral replication. Mol. Cell 7, 1245-1254 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 1245-1254
    • Turelli, P.1
  • 73
    • 0034898078 scopus 로고    scopus 로고
    • Accumulation and intranuclear distribution of unintegrated human immunodeficiency virus type 1 DNA
    • Bell, P., Montaner, L. J. & Maul, G. G. Accumulation and intranuclear distribution of unintegrated human immunodeficiency virus type 1 DNA. J. Virol. 75, 7683-7691 (2001).
    • (2001) J. Virol. , vol.75 , pp. 7683-7691
    • Bell, P.1    Montaner, L.J.2    Maul, G.G.3
  • 74
    • 0344089327 scopus 로고    scopus 로고
    • 3 enhances retroviral reverse transcription and counteracts Ref1 antiviral activity
    • 3 enhances retroviral reverse transcription and counteracts Ref1 antiviral activity. J. Virol. 77, 3167-3180 (2003).
    • (2003) J. Virol. , vol.77 , pp. 3167-3180
    • Berthoux, L.1
  • 75
    • 0035796503 scopus 로고    scopus 로고
    • PML mediates the interferon-induced antiviral state against a complex retrovirus via its association with the viral transactivator
    • Regad, T. et al. PML mediates the interferon-induced antiviral state against a complex retrovirus via its association with the viral transactivator. EMBO J. 20, 3495-3505 (2001).
    • (2001) EMBO J. , vol.20 , pp. 3495-3505
    • Regad, T.1
  • 76
    • 0037301503 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein does not mediate foamy virus latency in vitro
    • Meiering, C. D. & Linial, M. L. The promyelocytic leukemia protein does not mediate foamy virus latency in vitro. J. Virol. 77, 2207-2213 (2003).
    • (2003) J. Virol. , vol.77 , pp. 2207-2213
    • Meiering, C.D.1    Linial, M.L.2
  • 77
    • 2642670320 scopus 로고    scopus 로고
    • An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm
    • Borden, K. L., Campbell Dwyer, E. J. & Salvato, M. S. An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm. J. Virol. 72, 758-766 (1998).
    • (1998) J. Virol. , vol.72 , pp. 758-766
    • Borden, K.L.1    Campbell Dwyer, E.J.2    Salvato, M.S.3
  • 78
    • 18744379736 scopus 로고    scopus 로고
    • Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies
    • Blondel, D. et al. Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies. Oncogene 21, 7957-7970 (2002).
    • (2002) Oncogene , vol.21 , pp. 7957-7970
    • Blondel, D.1
  • 79
    • 0027769358 scopus 로고
    • Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICPO)
    • Maul, G. G., Guldner, H. H. & Spivack, J. G. Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICPO). J. Gen. Virol. 74, 2679-2690 (1993).
    • (1993) J. Gen. Virol. , vol.74 , pp. 2679-2690
    • Maul, G.G.1    Guldner, H.H.2    Spivack, J.G.3
  • 80
    • 0028039189 scopus 로고
    • HSV-1 IE protein Vmw110 causes redistribution of PML
    • Everett, R. D. & Maul, G. G. HSV-1 IE protein Vmw110 causes redistribution of PML. EMBO J. 13, 5062-5069 (1994).
    • (1994) EMBO J. , vol.13 , pp. 5062-5069
    • Everett, R.D.1    Maul, G.G.2
  • 81
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix, M. K. & de The, H. Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 18, 935-941 (1999).
    • (1999) Oncogene , vol.18 , pp. 935-941
    • Chelbi-Alix, M.K.1    de The, H.2
  • 82
    • 0344299239 scopus 로고    scopus 로고
    • Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption
    • Muller, S. & Dejean, A. Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J. Virol. 73, 5137-5143 (1999).
    • (1999) J. Virol. , vol.73 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 83
    • 0036138854 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro
    • Boutell, C., Sadis, S. & Everett, R. D. Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro. J. Virol. 76, 841-850 (2002).
    • (2002) J. Virol. , vol.76 , pp. 841-850
    • Boutell, C.1    Sadis, S.2    Everett, R.D.3
  • 84
    • 0037062483 scopus 로고    scopus 로고
    • Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0
    • Hagglund, R. & Roizman, B. Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0. Proc. Natl Acad. Sci. USA 99, 7889-7894 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7889-7894
    • Hagglund, R.1    Roizman, B.2
  • 85
    • 0141704201 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 interacts with and ubiquitinates p53
    • Boutell, C. & Everett, R. D. The herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 interacts with and ubiquitinates p53. J. Biol. Chem. 278, 36596-36602 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 36596-36602
    • Boutell, C.1    Everett, R.D.2
  • 86
    • 0042808481 scopus 로고    scopus 로고
    • The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a
    • Gu, H. & Roizman, B. The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a. Proc. Natl Acad. Sci. USA 100, 8963-8968 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8963-8968
    • Gu, H.1    Roizman, B.2
  • 87
    • 0036720433 scopus 로고    scopus 로고
    • Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effect on accumulation of infectious herpes simplex virus 1 or its proteins
    • Lopez, P., Jacob, R. J. & Roizman, B. Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effect on accumulation of infectious herpes simplex virus 1 or its proteins. J. Virol. 76, 9355-9367 (2002).
    • (2002) J. Virol. , vol.76 , pp. 9355-9367
    • Lopez, P.1    Jacob, R.J.2    Roizman, B.3
  • 88
    • 0037941647 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects
    • Chee, A. V., Lopez, P., Pandolfi, P. P. & Roizman, B. Promyelocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects. J. Virol. 77, 7101-7105 (2003).
    • (2003) J. Virol. , vol.77 , pp. 7101-7105
    • Chee, A.V.1    Lopez, P.2    Pandolfi, P.P.3    Roizman, B.4
  • 89
    • 0033779805 scopus 로고    scopus 로고
    • αherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins
    • Parkinson, J. & Everett, R. D. αherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins. J. Virol. 74, 10006-10017 (2000).
    • (2000) J. Virol. , vol.74 , pp. 10006-10017
    • Parkinson, J.1    Everett, R.D.2
  • 90
    • 0014824519 scopus 로고
    • Fv-2: Identification and location of a second gene governing the spleen focus response to Friend leukemia virus in mice
    • Lilly, F. Fv-2: Identification and location of a second gene governing the spleen focus response to Friend leukemia virus in mice. J. Natl Cancer Inst. 45, 163-169 (1970).
    • (1970) J. Natl. Cancer Inst. , vol.45 , pp. 163-169
    • Lilly, F.1
  • 91
    • 0014740351 scopus 로고
    • Host-range restrictions of murine leukemia viruses in mouse embryo cell cultures
    • Hartley, J. W., Rowe, W. P. & Huebner, R. J. Host-range restrictions of murine leukemia viruses in mouse embryo cell cultures. J. Virol. 5, 221-225 (1970).
    • (1970) J. Virol. , vol.5 , pp. 221-225
    • Hartley, J.W.1    Rowe, W.P.2    Huebner, R.J.3
  • 92
    • 0021079815 scopus 로고
    • Physical mapping of the Fv-1 tropism host range determinant of BALB/c murine leukemia viruses
    • DesGroseillers, F. & Jolicoeur, P. Physical mapping of the Fv-1 tropism host range determinant of BALB/c murine leukemia viruses. J. Virol. 48, 685-696 (1983).
    • (1983) J. Virol. , vol.48 , pp. 685-696
    • DesGroseillers, F.1    Jolicoeur, P.2
  • 93
    • 0030588980 scopus 로고    scopus 로고
    • Single amino acid changes in the murine leukemia virus capsid protein gene define the target of Fv1 resistance
    • Kozak, C. A. & Chakraborti, A. Single amino acid changes in the murine leukemia virus capsid protein gene define the target of Fv1 resistance. Virology 225, 300-305 (1996).
    • (1996) Virology , vol.225 , pp. 300-305
    • Kozak, C.A.1    Chakraborti, A.2
  • 94
    • 0032036690 scopus 로고    scopus 로고
    • Fv1, the mouse retrovirus resistance gene
    • Stoye, J. P. Fv1, the mouse retrovirus resistance gene. Rev. Sci. Tech. 17, 269-277 (1998).
    • (1998) Rev. Sci. Tech. , vol.17 , pp. 269-277
    • Stoye, J.P.1
  • 95
    • 0029763293 scopus 로고    scopus 로고
    • Positional cloning of the mouse retrovirus restriction gene Fv1
    • Best, S., Le Tissier, P., Towers, G. & Stoye, J. P. Positional cloning of the mouse retrovirus restriction gene Fv1. Nature 382, 826-829 (1996).
    • (1996) Nature , vol.382 , pp. 826-829
    • Best, S.1    Le Tissier, P.2    Towers, G.3    Stoye, J.P.4
  • 96
    • 0029129017 scopus 로고
    • Isolation of novel human endogenous retrovirus-like elements with foamy virus-related pol sequence
    • Cordonnier, A., Casella, J.-F. & Heidmann, T. Isolation of novel human endogenous retrovirus-like elements with foamy virus-related pol sequence. J. Virol. 69, 5890-5897 (1995).
    • (1995) J. Virol. , vol.69 , pp. 5890-5897
    • Cordonnier, A.1    Casella, J.-F.2    Heidmann, T.3
  • 97
    • 0030572654 scopus 로고    scopus 로고
    • Operating under a Gag order: A block against incoming virus by the Fv1 gene
    • Goff, S. P. Operating under a Gag order: A block against incoming virus by the Fv1 gene. Cell 86, 691-693 (1996).
    • (1996) Cell , vol.86 , pp. 691-693
    • Goff, S.P.1
  • 98
    • 0030997681 scopus 로고    scopus 로고
    • Cloning of a new murine endogenous retrovirus, MuERV-L, with strong similarity to the human HERV-L element and with a gag coding sequence closely related to the Fv1 restriction gene
    • Benit, L. et al. Cloning of a new murine endogenous retrovirus, MuERV-L, with strong similarity to the human HERV-L element and with a gag coding sequence closely related to the Fv1 restriction gene. J. Virol. 71, 5652-5657 (1997).
    • (1997) J. Virol. , vol.71 , pp. 5652-5657
    • Benit, L.1
  • 99
    • 0034710884 scopus 로고    scopus 로고
    • A conserved mechanism of retrovirus restriction in mammals
    • Towers, G. et al. A conserved mechanism of retrovirus restriction in mammals. Proc. Natl Acad. Sci. USA 97, 12295-12299 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12295-12299
    • Towers, G.1
  • 100
    • 0345599025 scopus 로고    scopus 로고
    • Characterization of murine leukemia virus restriction in mammals
    • Besnier, C. et al. Characterization of murine leukemia virus restriction in mammals. J. Virol. 77, 13403-13406 (2003).
    • (2003) J. Virol. , vol.77 , pp. 13403-13406
    • Besnier, C.1
  • 101
    • 0032708384 scopus 로고    scopus 로고
    • Species-specific, postentry barriers to primate immunodeficiency virus infection
    • Hofmann, W. et al. Species-specific, postentry barriers to primate immunodeficiency virus infection. J. Virol. 73, 10020-10028 (1999).
    • (1999) J. Virol. , vol.73 , pp. 10020-10028
    • Hofmann, W.1
  • 103
    • 0037015007 scopus 로고    scopus 로고
    • Cellular inhibitors with Fv1-like activity restrict human and simian immunodeficiency virus tropism
    • Cowan, S. et al. Cellular inhibitors with Fv1-like activity restrict human and simian immunodeficiency virus tropism. Proc. Natl Acad. Sci. USA 99, 11914-11919 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11914-11919
    • Cowan, S.1
  • 104
    • 0037108977 scopus 로고    scopus 로고
    • A dominant block to HIV-1 replication at reverse transcription in simian cells
    • Munk, C., Brandt, S. M., Lucero, G. & Landau, N. R. A dominant block to HIV-1 replication at reverse transcription in simian cells. Proc. Natl Acad. Sci USA 99, 13843-13848 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13843-13848
    • Munk, C.1    Brandt, S.M.2    Lucero, G.3    Landau, N.R.4
  • 105
    • 11844278251 scopus 로고    scopus 로고
    • A single amino acid change in the SPRY domain of human Trim5α leads to HIV-1 restriction
    • Yap, M. W., Nisole, S. & Stoye, J. P. A single amino acid change in the SPRY domain of human Trim5α leads to HIV-1 restriction. Curr. Biol. 15, 73-78 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 73-78
    • Yap, M.W.1    Nisole, S.2    Stoye, J.P.3
  • 106
    • 13944259674 scopus 로고    scopus 로고
    • Species-specific variation in the B30.2(SPRY) domain of TRIM5α determines the potency of human immunodeficiency virus restriction
    • Stremlau, M., Perron, M., Welikala, S. & Sodroski, J. Species-specific variation in the B30.2(SPRY) domain of TRIM5α determines the potency of human immunodeficiency virus restriction. J. Virol. 79, 3139-3145 (2005).
    • (2005) J. Virol. , vol.79 , pp. 3139-3145
    • Stremlau, M.1    Perron, M.2    Welikala, S.3    Sodroski, J.4
  • 108
    • 14544281087 scopus 로고    scopus 로고
    • Positive selection of primate TRIM5α identifies a critical species-specific retroviral restriction domain
    • Sawyer, S. L., Wu, L. I., Emerman, M. & Malik, H. S. Positive selection of primate TRIM5α identifies a critical species-specific retroviral restriction domain. Proc. Natl Acad. Sci. USA 102, 2832-2837 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2832-2837
    • Sawyer, S.L.1    Wu, L.I.2    Emerman, M.3    Malik, H.S.4
  • 109
    • 10944259799 scopus 로고    scopus 로고
    • The B30.2(SPRY) domain of the retroviral restriction factor TRIM5α exhibits lineage-specific length and sequence variation in primates
    • Song, B. et al. The B30.2(SPRY) domain of the retroviral restriction factor TRIM5α exhibits lineage-specific length and sequence variation in primates. J. Virol. 79, 6111-6121 (2005).
    • (2005) J. Virol. , vol.79 , pp. 6111-6121
    • Song, B.1
  • 110
    • 0018766503 scopus 로고
    • The Fv-1 gene of the mouse and its control of murine leukemia virus replication
    • Jolicoeur, P. The Fv-1 gene of the mouse and its control of murine leukemia virus replication. Curr. Top. Microbiol. Immunol. 86, 67-122 (1979).
    • (1979) Curr. Top. Microbiol. Immunol. , vol.86 , pp. 67-122
    • Jolicoeur, P.1
  • 111
    • 0017335655 scopus 로고
    • Loss of Fv-1 restriction in Balb/3T3 cells following infection with a single N tropic murine leukemia particle
    • Duran-Troise, G., Bassin, R. H., Rein, A. & Gerwin, B. I. Loss of Fv-1 restriction in Balb/3T3 cells following infection with a single N tropic murine leukemia particle. Cell 10, 479-488 (1977).
    • (1977) Cell , vol.10 , pp. 479-488
    • Duran-Troise, G.1    Bassin, R.H.2    Rein, A.3    Gerwin, B.I.4
  • 112
    • 0037347206 scopus 로고    scopus 로고
    • Intracellular localisation of Fv1
    • Yap, M. W. & Stoye, J. P. Intracellular localisation of Fv1. Virology 307, 76-89 (2003).
    • (2003) Virology , vol.307 , pp. 76-89
    • Yap, M.W.1    Stoye, J.P.2
  • 113
    • 4444241947 scopus 로고    scopus 로고
    • A Trim5-cyclophilin A fusion protein found in owl monkey kidney cells can restrict HIV-1
    • Nisole, S., Lynch, C., Stoye, J. P. & Yap, M. W. A Trim5-cyclophilin A fusion protein found in owl monkey kidney cells can restrict HIV-1. Proc. Natl Acad. Sci. USA 101, 13324-13328 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13324-13328
    • Nisole, S.1    Lynch, C.2    Stoye, J.P.3    Yap, M.W.4
  • 114
    • 3242876747 scopus 로고    scopus 로고
    • Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1
    • Sayah, D. M., Sokolskaja, E., Berthoux, L. & Luban, J. Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1. Nature 430, 569-573 (2004).
    • (2004) Nature , vol.430 , pp. 569-573
    • Sayah, D.M.1    Sokolskaja, E.2    Berthoux, L.3    Luban, J.4
  • 115
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B
    • Luban, J., Bossolt, K. L., Franke, E. K., Kalpana, G. V. & Goff, S. P. Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell 73, 1067-1078 (1993).
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 116
    • 0030448994 scopus 로고    scopus 로고
    • Crvstal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • Gamble, T. R. et al. Crvstal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell 87, 1285-1294 (1996).
    • (1996) Cell , vol.87 , pp. 1285-1294
    • Gamble, T.R.1
  • 117
    • 0141796317 scopus 로고    scopus 로고
    • Cyclophilin A modulates the sensitivity of HIV-1 to host restriction factors
    • Towers, G. J. et al. Cyclophilin A modulates the sensitivity of HIV-1 to host restriction factors. Nature Med. 9, 1138-1143 (2003).
    • (2003) Nature Med. , vol.9 , pp. 1138-1143
    • Towers, G.J.1
  • 118
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey, B. M., von Schwedler, U., Sundquist, W. I. & Aiken, S. C. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J. Virol. 76, 5667-5677 (2002).
    • (2002) J. Virol. , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    von Schwedler, U.2    Sundquist, W.I.3    Aiken, S.C.4
  • 119
    • 23244435611 scopus 로고    scopus 로고
    • Capsid processing requirements for abrogation of Fv1 and ref1 restriction
    • Dodding, M. P., Bock, M., Yap, M. W. & Stoye, J. P. Capsid processing requirements for abrogation of Fv1 and ref1 restriction. J. Virol. 79, 10571-10577 (2005).
    • (2005) J. Virol. , vol.79 , pp. 10571-10577
    • Dodding, M.P.1    Bock, M.2    Yap, M.W.3    Stoye, J.P.4
  • 120
    • 4644301808 scopus 로고    scopus 로고
    • High-resolution structure of a retroviral capsid hexameric amino-terminal domain
    • Mortuza, G. B. et al. High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature 431, 481-485 (2004).
    • (2004) Nature , vol.431 , pp. 481-485
    • Mortuza, G.B.1
  • 121
    • 6344262057 scopus 로고    scopus 로고
    • Lv1 inhibition of human immunodeficiency virus type 1 is counteracted by factors that stimulate synthesis or nuclear translocation of viral cDNA
    • Berthoux, F., Sebastian, S., Sokolskaja, E. & Luban, J. Lv1 inhibition of human immunodeficiency virus type 1 is counteracted by factors that stimulate synthesis or nuclear translocation of viral cDNA. J. Virol. 78, 11739-11750 (2004).
    • (2004) J. Virol. , vol.78 , pp. 11739-11750
    • Berthoux, F.1    Sebastian, S.2    Sokolskaja, E.3    Luban, J.4
  • 122
    • 4344652071 scopus 로고    scopus 로고
    • Early steps of retrovirus replicative cycle
    • Nisole, S. & Saib, A. Early steps of retrovirus replicative cycle. Retrovirology 1, 9 (2004).
    • (2004) Retrovirology , vol.1 , pp. 9
    • Nisole, S.1    Saib, A.2
  • 123
    • 0029055286 scopus 로고
    • Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins
    • Fridell, R. A., Harding, F. S., Bogerd, H. P. & Cullen, B. R. Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins. Virology 209, 347-357 (1995).
    • (1995) Virology , vol.209 , pp. 347-357
    • Fridell, R.A.1    Harding, F.S.2    Bogerd, H.P.3    Cullen, B.R.4
  • 124
    • 0036678864 scopus 로고    scopus 로고
    • Cellular transciptional profiling in influenza A virus-infected lung epithelial cells: The role of the nonstructural NS1 protein in the evasion of the host innate defense and its potential contribution to pandemic influenza
    • Geiss, G. K. et al. Cellular transciptional profiling in influenza A virus-infected lung epithelial cells: The role of the nonstructural NS1 protein in the evasion of the host innate defense and its potential contribution to pandemic influenza. Proc. Natl Acad. Sci. USA 99, 107313-10741 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10736-10741
    • Geiss, G.K.1
  • 125
    • 4444301523 scopus 로고    scopus 로고
    • TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional activities of EIK-1 and AP-1
    • Wang, Y. et al. TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional activities of EIK-1 and AP-1. Biochem. Biophys. Res. Commun. 323, 9-16 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 9-16
    • Wang, Y.1
  • 126
    • 18344406436 scopus 로고    scopus 로고
    • Fools, virus infection inversely correlates with the overall expression levels of promyelocytic leukaemia (PML) protein in cultured cells
    • Bjorndal, A. S., Szekely, L. & Elgh, F. Fools, virus infection inversely correlates with the overall expression levels of promyelocytic leukaemia (PML) protein in cultured cells. BMC Microbiol. 3, 6 (2003).
    • (2003) BMC Microbiol. , vol.3 , pp. 6
    • Bjorndal, A.S.1    Szekely, L.2    Elgh, F.3
  • 127
    • 0036200416 scopus 로고    scopus 로고
    • Effects of promyelocytic leukemia protein on virus-host balance
    • Bonilla, W. V. et al. Effects of promyelocytic leukemia protein on virus-host balance. J. Virol. 76, 3810-3818 (2002).
    • (2002) J. Virol. , vol.76 , pp. 3810-3818
    • Bonilla, W.V.1
  • 128
    • 0034974380 scopus 로고    scopus 로고
    • Role of the promyelocytic leukemia protein PML in the interferon sensitivity of lymphocytic choriomeningitis virus
    • Djavani, M. et al. Role of the promyelocytic leukemia protein PML in the interferon sensitivity of lymphocytic choriomeningitis virus. J. Virol. 75, 6204-6208 (2001).
    • (2001) J. Virol. , vol.75 , pp. 6204-6208
    • Djavani, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.