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Volumn 85, Issue 22, 2011, Pages 11588-11600

Molecular characterization of the host defense activity of the barrier to autointegration factor against vaccinia virus

Author keywords

[No Author keywords available]

Indexed keywords

BARRIER TO AUTOINTEGRATION FACTOR; DOUBLE STRANDED DNA; EMERIN; VIRUS DNA;

EID: 80655146251     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00641-11     Document Type: Article
Times cited : (33)

References (45)
  • 1
    • 77955427185 scopus 로고    scopus 로고
    • The interaction of viruses with host immune defenses
    • doi:10.1016/j.mib.2010.07.001
    • Alcami, A. 2010. The interaction of viruses with host immune defenses. Curr. Opin. Microbiol. 13:501-502. doi:10.1016/j.mib.2010.07.001.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 501-502
    • Alcami, A.1
  • 2
    • 33644864100 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor phosphorylation on Ser-4 regulates emerin binding to lamin A in vitro and emerin localization in vivo
    • doi:10.1091/ mbc.E05-04-0356
    • Bengtsson, L., and K. L. Wilson. 2006. Barrier-to-autointegration factor phosphorylation on Ser-4 regulates emerin binding to lamin A in vitro and emerin localization in vivo. Mol. Biol. Cell 17:1154-1163. doi:10.1091/ mbc.E05-04-0356.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1154-1163
    • Bengtsson, L.1    Wilson, K.L.2
  • 3
    • 0842347704 scopus 로고    scopus 로고
    • Members of a novel family of mammalian protein kinases complement the DNA-negative phenotype of a vaccinia virus ts mutant defective in the B1 kinase
    • Boyle, K. A., and P. Traktman. 2004. Members of a novel family of mammalian protein kinases complement the DNA-negative phenotype of a vaccinia virus ts mutant defective in the B1 kinase. J. Virol. 78:1992-2005.
    • (2004) J. Virol. , vol.78 , pp. 1992-2005
    • Boyle, K.A.1    Traktman, P.2
  • 4
    • 27144484996 scopus 로고    scopus 로고
    • Structural basis for DNA bridging by barrier-to-autointegration factor
    • doi:10.1038/nsmb989
    • Bradley, C. M., D. R. Ronning, R. Ghirlando, R. Craigie, and F. Dyda. 2005. Structural basis for DNA bridging by barrier-to-autointegration factor. Nat. Struct. Mol. Biol. 12:935-936. doi:10.1038/nsmb989.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 935-936
    • Bradley, C.M.1    Ronning, D.R.2    Ghirlando, R.3    Craigie, R.4    Dyda, F.5
  • 5
    • 0031720496 scopus 로고    scopus 로고
    • Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration
    • doi:10.1038/2345
    • Cai, M., et al. 1998. Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration. Nat. Struct. Biol. 5:903-909. doi:10.1038/2345.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 903-909
    • Cai, M.1
  • 6
    • 12344305602 scopus 로고    scopus 로고
    • LAP2alpha and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly
    • doi:10.1242/jcs.01529
    • Dechat, T., et al. 2004. LAP2alpha and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly. J. Cell Sci. 117:6117-6128. doi:10.1242/jcs.01529.
    • (2004) J. Cell Sci. , vol.117 , pp. 6117-6128
    • Dechat, T.1
  • 7
    • 0033926099 scopus 로고    scopus 로고
    • Lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics
    • doi:10.1006/jsbi.2000.4212
    • Dechat, T., S. Vlcek, and R. Foisner. 2000. Lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics. J. Struct. Biol. 129:335-345. doi:10.1006/jsbi.2000.4212.
    • (2000) J. Struct. Biol. , vol.129 , pp. 335-345
    • Dechat, T.1    Vlcek, S.2    Foisner, R.3
  • 8
    • 12444289583 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organization in Drosophila
    • doi:10.1242/jcs.00682
    • Furukawa, K., et al. 2003. Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organization in Drosophila. J. Cell Sci. 116:3811-3823. doi:10.1242/jcs.00682.
    • (2003) J. Cell Sci. , vol.116 , pp. 3811-3823
    • Furukawa, K.1
  • 9
    • 33846195879 scopus 로고    scopus 로고
    • Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in post-mitotic nuclear envelope assembly
    • doi:10.1038/sj.emboj.7601470
    • Gorjanacz, M., et al. 2007. Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in post-mitotic nuclear envelope assembly. EMBO J. 26:132-143. doi:10.1038/sj.emboj.7601470.
    • (2007) EMBO J , vol.26 , pp. 132-143
    • Gorjanacz, M.1
  • 10
    • 50249107835 scopus 로고    scopus 로고
    • Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly
    • doi:10.1242/jcs.033597
    • Haraguchi, T., et al. 2008. Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly. J. Cell Sci. 121:2540-2554. doi:10.1242/jcs.033597.
    • (2008) J. Cell Sci. , vol.121 , pp. 2540-2554
    • Haraguchi, T.1
  • 11
    • 0035696958 scopus 로고    scopus 로고
    • BAF is required for emerin assembly into the reforming nuclear envelope
    • Haraguchi, T., et al. 2001. BAF is required for emerin assembly into the reforming nuclear envelope. J. Cell Sci. 114:4575-4585.
    • (2001) J. Cell Sci. , vol.114 , pp. 4575-4585
    • Haraguchi, T.1
  • 12
    • 0034671508 scopus 로고    scopus 로고
    • Both the structure and DNA binding function of the barrier-to-autointegration factor contribute to reconstitution of HIV type 1 integration in vitro
    • doi: 10.1074/jbc.M002626200
    • Harris, D., and A. Engelman. 2000. Both the structure and DNA binding function of the barrier-to-autointegration factor contribute to reconstitution of HIV type 1 integration in vitro. J. Biol. Chem. 275:39671-39677. doi: 10.1074/jbc.M002626200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39671-39677
    • Harris, D.1    Engelman, A.2
  • 13
    • 0037689535 scopus 로고    scopus 로고
    • Poxvirus immunomodulatory strategies: current perspectives
    • Johnston, J. B., and G. McFadden. 2003. Poxvirus immunomodulatory strategies: current perspectives. J. Virol. 77:6093-6100.
    • (2003) J. Virol. , vol.77 , pp. 6093-6100
    • Johnston, J.B.1    McFadden, G.2
  • 14
    • 34848865040 scopus 로고    scopus 로고
    • Colocalization of transcription and translation within cytoplasmic poxvirus factories coordinates viral expression and subjugates host functions
    • doi:10. 1016/ j. chom. 2007. 08.005
    • Katsafanas, G. C., and B. Moss. 2007. Colocalization of transcription and translation within cytoplasmic poxvirus factories coordinates viral expression and subjugates host functions. Cell Host Microbe 2:221-228. doi:10.1016/ j.chom.2007.08.005.
    • (2007) Cell Host Microbe , vol.2 , pp. 221-228
    • Katsafanas, G.C.1    Moss, B.2
  • 15
    • 36849090938 scopus 로고    scopus 로고
    • NHK- 1 phosphorylates BAF to allow karyosome formation in the Drosophila oocyte nucleus
    • doi:10.1083/jcb.200706067
    • Lancaster, O. M., C. F. Cullen, and H. Ohkura. 2007. NHK-1 phosphorylates BAF to allow karyosome formation in the Drosophila oocyte nucleus. J. Cell Biol. 179:817-824. doi:10.1083/jcb.200706067.
    • (2007) J. Cell Biol. , vol.179 , pp. 817-824
    • Lancaster, O.M.1    Cullen, C.F.2    Ohkura, H.3
  • 16
    • 0035694820 scopus 로고    scopus 로고
    • Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF
    • Lee, K. K., et al. 2001. Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF. J. Cell Sci. 114:4567-4573.
    • (2001) J. Cell Sci. , vol.114 , pp. 4567-4573
    • Lee, K.K.1
  • 17
    • 0032539631 scopus 로고    scopus 로고
    • A previously unidentified host protein protects retroviral DNA from autointegration Proc
    • Lee, M. S., and R. Craigie. 1998. A previously unidentified host protein protects retroviral DNA from autointegration Proc. Natl. Acad. Sci. U. S. A. 95:1528-1533.
    • (1998) Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1528-1533
    • Lee, M.S.1    Craigie, R.2
  • 18
    • 0344736902 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions
    • Mansharamani, M., et al. 2003. Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions. J. Virol. 77:13084-13092.
    • (2003) J. Virol. , vol.77 , pp. 13084-13092
    • Mansharamani, M.1
  • 19
    • 33947715599 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor-a BAFfling little protein
    • doi:10.1016/j.tcb.2007.02.004
    • Margalit, A., A. Brachner, J. Gotzmann, R. Foisner, and Y. Gruenbaum. 2007. Barrier-to-autointegration factor-a BAFfling little protein. Trends Cell Biol. 17:202-208. doi:10.1016/j.tcb.2007.02.004.
    • (2007) Trends Cell Biol. , vol.17 , pp. 202-208
    • Margalit, A.1    Brachner, A.2    Gotzmann, J.3    Foisner, R.4    Gruenbaum, Y.5
  • 20
    • 14744280620 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor is required to segregate and enclose chromosomes within the nuclear envelope and assemble the nuclear lamina
    • doi:10.1073/pnas.0408364102
    • Margalit, A., M. Segura-Totten, Y. Gruenbaum, and K. L. Wilson. 2005. Barrier-to-autointegration factor is required to segregate and enclose chromosomes within the nuclear envelope and assemble the nuclear lamina. Proc. Natl. Acad. Sci. U. S. A. 102:3290-3295. doi:10.1073/pnas.0408364102.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 3290-3295
    • Margalit, A.1    Segura-Totten, M.2    Gruenbaum, Y.3    Wilson, K.L.4
  • 21
    • 14544284014 scopus 로고    scopus 로고
    • Poxvirus tropism
    • doi: 10.1038/nrmicro1099
    • McFadden, G. 2005. Poxvirus tropism. Nat. Rev. Microbiol. 3:201-213. doi: 10.1038/nrmicro1099.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 201-213
    • McFadden, G.1
  • 22
    • 28844456962 scopus 로고    scopus 로고
    • Functional inaccessibility of quiescent herpes simplex virus genomes
    • doi:10.1186/ 1743-422X-2-85
    • Minaker, R. L., K. L. Mossman, and J. R. Smiley. 2005. Functional inaccessibility of quiescent herpes simplex virus genomes. Virol. J. 2:85. doi:10.1186/ 1743-422X-2-85.
    • (2005) Virol. J , vol.2 , pp. 85
    • Minaker, R.L.1    Mossman, K.L.2    Smiley, J.R.3
  • 23
    • 29144529317 scopus 로고    scopus 로고
    • Binding of barrier to autointegration factor (BAF) to histone H3 and selected linker histones including H1
    • doi:10.1074/ jbc.M509917200
    • Montes de Oca, R., K. K. Lee, and K. L. Wilson. 2005. Binding of barrier to autointegration factor (BAF) to histone H3 and selected linker histones including H1.1. J. Biol. Chem. 280:42252-42262. doi:10.1074/ jbc.M509917200.
    • (2005) 1. J. Biol. Chem. , vol.280 , pp. 42252-42262
    • Montes de Oca, R.1    Lee, K.K.2    Wilson, K.L.3
  • 24
    • 75549091918 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor proteome reveals chromatinregulatory partners
    • doi:10. 1371/journal. pone.0007050
    • Montes de Oca, R., C. J. Shoemaker, M. Gucek, R. N. Cole, and K. L. Wilson. 2009. Barrier-to-autointegration factor proteome reveals chromatinregulatory partners. PLoS One 4:e7050. doi:10.1371/journal.pone.0007050.
    • (2009) PLoS One , vol.4
    • Montes de Oca, R.1    Shoemaker, C.J.2    Gucek, M.3    Cole, R.N.4    Wilson, K.L.5
  • 25
    • 1542379726 scopus 로고    scopus 로고
    • Characterization of three paralogous members of the mammalian vaccinia related kinase family
    • doi:10.1074/jbc.M310813200
    • Nichols, R. J., and P. Traktman. 2004. Characterization of three paralogous members of the mammalian vaccinia related kinase family. J. Biol. Chem. 279:7934-7946. doi:10.1074/jbc.M310813200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7934-7946
    • Nichols, R.J.1    Traktman, P.2
  • 26
    • 33745450085 scopus 로고    scopus 로고
    • The vaccinia-related kinases phosphorylate the N' terminus of BAF, regulating its interaction with DNA and its retention in the nucleus
    • doi:10. 1091/mbc. E05-12-1179
    • Nichols, R. J., M. S. Wiebe, and P. Traktman. 2006. The vaccinia-related kinases phosphorylate the N' terminus of BAF, regulating its interaction with DNA and its retention in the nucleus. Mol. Biol. Cell 17:2451-2464. doi:10.1091/mbc.E05-12-1179.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2451-2464
    • Nichols, R.J.1    Wiebe, M.S.2    Traktman, P.3
  • 27
    • 26444501426 scopus 로고    scopus 로고
    • Host cell nuclear proteins are recruited to cytoplasmic vaccinia virus replication complexes
    • doi:10.1128/JVI.79.20.12852-12860.2005
    • Oh, J., and S. S. Broyles. 2005. Host cell nuclear proteins are recruited to cytoplasmic vaccinia virus replication complexes. J. Virol. 79:12852-12860. doi:10.1128/JVI.79.20.12852-12860.2005.
    • (2005) J. Virol , vol.79 , pp. 12852-12860
    • Oh, J.1    Broyles, S.S.2
  • 28
    • 70349260534 scopus 로고    scopus 로고
    • The interferon system and vaccinia virus evasion mechanisms
    • doi: 10.1089/jir.2009.0073
    • Perdiguero, B., and M. Esteban. 2009. The interferon system and vaccinia virus evasion mechanisms. J. Interferon Cytokine Res. 29:581-598. doi: 10.1089/jir.2009.0073.
    • (2009) J. Interferon Cytokine Res. , vol.29 , pp. 581-598
    • Perdiguero, B.1    Esteban, M.2
  • 29
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl, M. W. 2001. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29:e45.
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 30
    • 0013098971 scopus 로고    scopus 로고
    • Poxviruses and immune evasion
    • doi:10.1146/annurev.immunol.21.120601.141049
    • Seet, B. T., et al. 2003. Poxviruses and immune evasion. Annu. Rev. Immunol. 21:377-423. doi:10.1146/annurev.immunol.21.120601.141049.
    • (2003) Annu. Rev. Immunol. , vol.21 , pp. 377-423
    • Seet, B.T.1
  • 31
    • 0036330001 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly
    • doi:10.1083/jcb.200202019
    • Segura-Totten, M., A. K. Kowalski, R. Craigie, and K. L. Wilson. 2002. Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly. J. Cell Biol. 158:475-485. doi:10.1083/jcb.200202019.
    • (2002) J. Cell Biol. , vol.158 , pp. 475-485
    • Segura-Totten, M.1    Kowalski, A.K.2    Craigie, R.3    Wilson, K.L.4
  • 32
    • 70449562099 scopus 로고    scopus 로고
    • Predicted poxvirus FEN1-like nuclease required for homologous recombination, double-strand break repair and full-size genome formation
    • doi:10.1073/pnas.0909529106
    • Senkevich, T. G., E. V. Koonin, and B. Moss. 2009. Predicted poxvirus FEN1-like nuclease required for homologous recombination, double-strand break repair and full-size genome formation. Proc. Natl. Acad. Sci. U. S. A. 106:17921-17926. doi:10.1073/pnas.0909529106.
    • (2009) Proc. Natl. Acad. Sci. U. S. A , vol.106 , pp. 17921-17926
    • Senkevich, T.G.1    Koonin, E.V.2    Moss, B.3
  • 33
    • 42149145278 scopus 로고    scopus 로고
    • LAP2zeta binds BAF and suppresses LAP2betamediated transcriptional repression
    • doi: 10.1016/j.ejcb.2008.01.014
    • Shaklai, S., et al. 2008. LAP2zeta binds BAF and suppresses LAP2betamediated transcriptional repression. Eur. J. Cell Biol. 87:267-278. doi: 10.1016/j.ejcb.2008.01.014.
    • (2008) Eur. J. Cell Biol. , vol.87 , pp. 267-278
    • Shaklai, S.1
  • 34
    • 1842578717 scopus 로고    scopus 로고
    • Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyses in living HeLa cells
    • doi:10.1016/j.jsb.2003.11.013
    • Shimi, T., et al. 2004. Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyses in living HeLa cells. J. Struct. Biol. 147:31-41. doi:10.1016/j.jsb.2003.11.013.
    • (2004) J. Struct. Biol. , vol.147 , pp. 31-41
    • Shimi, T.1
  • 35
    • 33845788704 scopus 로고    scopus 로고
    • Wild-type levels of human immunodeficiency virus type 1 infectivity in the absence of cellular emerin protein
    • doi:10.1128/JVI.01953-06
    • Shun, M. C., J. E. Daigle, N. Vandegraaff, and A. Engelman. 2007. Wild-type levels of human immunodeficiency virus type 1 infectivity in the absence of cellular emerin protein. J. Virol. 81:166-172. doi:10.1128/JVI.01953-06.
    • (2007) J. Virol. , vol.81 , pp. 166-172
    • Shun, M.C.1    Daigle, J.E.2    Vandegraaff, N.3    Engelman, A.4
  • 36
    • 77949269567 scopus 로고    scopus 로고
    • Chromatin structure regulates human cytomegalovirus gene expression during latency, reactivation and lytic infection
    • doi:10. 1016/j. bbagrm. 2009. 08.001
    • Sinclair, J. 2010. Chromatin structure regulates human cytomegalovirus gene expression during latency, reactivation and lytic infection. Biochim. Biophys. Acta 1799:286-295. doi:10.1016/j.bbagrm.2009.08.001.
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 286-295
    • Sinclair, J.1
  • 37
    • 70349748587 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor (BAF) condenses DNA by looping
    • doi: 10.1073/pnas.0909077106
    • Skoko, D., et al. 2009. Barrier-to-autointegration factor (BAF) condenses DNA by looping. Proc. Natl. Acad. Sci. U. S. A. 106:16610-16615. doi: 10.1073/pnas.0909077106.
    • (2009) Proc. Natl. Acad. Sci. U. S. A , vol.106 , pp. 16610-16615
    • Skoko, D.1
  • 38
    • 10644230990 scopus 로고    scopus 로고
    • LAP2alpha and BAF collaborate to organize the Moloney murine leukemia virus preintegration complex
    • doi:10.1038/sj.emboj.7600452
    • Suzuki, Y., H. Yang, and R. Craigie. 2004. LAP2alpha and BAF collaborate to organize the Moloney murine leukemia virus preintegration complex. EMBO J. 23:4670-4678. doi:10.1038/sj.emboj.7600452.
    • (2004) EMBO J , vol.23 , pp. 4670-4678
    • Suzuki, Y.1    Yang, H.2    Craigie, R.3
  • 39
    • 0035157752 scopus 로고    scopus 로고
    • Vaccinia virus DNA replication occurs in endoplasmic reticulum-enclosed cytoplasmic mini-nuclei
    • Tolonen, N., L. Doglio, S. Schleich, and J. Krijnse Locker. 2001. Vaccinia virus DNA replication occurs in endoplasmic reticulum-enclosed cytoplasmic mini-nuclei. Mol. Biol. Cell 12:2031-2046.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2031-2046
    • Tolonen, N.1    Doglio, L.2    Schleich, S.3    Krijnse Locker, J.4
  • 40
    • 4043116119 scopus 로고    scopus 로고
    • Methods for analysis of poxvirus DNA replication
    • doi:10.1385/1-59259-789-0:169
    • Traktman, P., and K. Boyle. 2004. Methods for analysis of poxvirus DNA replication. Methods Mol. Biol. 269:169-186. doi:10.1385/1-59259-789-0:169.
    • (2004) Methods Mol. Biol. , vol.269 , pp. 169-186
    • Traktman, P.1    Boyle, K.2
  • 41
    • 0034622513 scopus 로고    scopus 로고
    • Structural basis of DNA bridging by barrier-to-autointegration factor
    • Umland, T. C., S. Q. Wei, R. Craigie, and D. R. Davies. 2000. Structural basis of DNA bridging by barrier-to-autointegration factor. Biochemistry 39:9130- 9138.
    • (2000) Biochemistry , vol.39 , pp. 9130-9138
    • Umland, T.C.1    Wei, S.Q.2    Craigie, R.3    Davies, D.R.4
  • 42
    • 18644386771 scopus 로고    scopus 로고
    • Barrier to autointegration factor interacts with the cone-rod homeobox and represses its transactivation function
    • doi:10.1074/jbc.M207952200
    • Wang, X., et al. 2002. Barrier to autointegration factor interacts with the cone-rod homeobox and represses its transactivation function. J. Biol. Chem. 277:43288-43300. doi:10.1074/jbc.M207952200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43288-43300
    • Wang, X.1
  • 43
    • 34248205172 scopus 로고    scopus 로고
    • Poxviral B1 kinase overcomes barrier to autointegration factor, a host defense against virus replication
    • doi:10. 1016/j. chom. 2007. 03
    • Wiebe, M. S., and P. Traktman. 2007. Poxviral B1 kinase overcomes barrier to autointegration factor, a host defense against virus replication. Cell Host Microbe 1:187-197. doi:10.1016/j.chom.2007.03.007.
    • (2007) Cell Host Microbe , vol.1 , pp. 187-197
    • Wiebe, M.S.1    Traktman, P.2
  • 44
    • 63449120803 scopus 로고    scopus 로고
    • The SET complex acts as a barrier to autointegration of HIV-1
    • doi:10.1371/journal.ppat.1000327
    • Yan, N., P. Cherepanov, J. E. Daigle, A. Engelman, and J. Lieberman. 2009. The SET complex acts as a barrier to autointegration of HIV-1. PLoS Pathog. 5:e1000327. doi:10.1371/journal.ppat.1000327.
    • (2009) PLoS Pathog. , vol.5
    • Yan, N.1    Cherepanov, P.2    Daigle, J.E.3    Engelman, A.4    Lieberman, J.5
  • 45
    • 0034255236 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex
    • doi:10.1073/pnas.150240197
    • Zheng, R., et al. 2000. Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex. Proc. Natl. Acad. Sci. U. S. A. 97:8997-9002. doi:10.1073/pnas.150240197.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 8997-9002
    • Zheng, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.