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Journal of Virology
Volumn 90, Issue 8, 2016, Pages 4199-4214
SUN2 overexpression deforms nuclear shape and inhibits HIV
Author keywords

[No Author keywords available]
Indexed keywords

CYCLOPHILIN A; NUCLEAR PROTEIN; SUN2 PROTEIN; UNCLASSIFIED DRUG; INTERFERON; MEMBRANE PROTEIN; SIGNAL PEPTIDE; SUN2 PROTEIN, HUMAN;
EID: 84963813173     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03202-15     Document Type: Article
Times cited : (42)
References (106)
  • 1
    • 39349097864 scopus 로고    scopus 로고
    • Identification of host proteins required for HIV infection through a functional genomic screen
    • Brass AL, Dykxhoorn DM, Benita Y, Yan N, Engelman A, Xavier RJ, Lieberman J, Elledge SJ. 2008. Identification of host proteins required for HIV infection through a functional genomic screen. Science 319:921-926. http://dx.doi.org/10.1126/science.1152725.
    • (2008) Science , vol.319 , pp. 921-926
    • Brass, A.L.1    Dykxhoorn, D.M.2    Benita, Y.3    Yan, N.4    Engelman, A.5    Xavier, R.J.6    Lieberman, J.7    Elledge, S.J.8
  • 3
    • 67749148923 scopus 로고    scopus 로고
    • A genomewide short hairpin RNA screening of Jurkat T-cells for human proteins contributing to productive HIV-1 replication
    • Yeung ML, Houzet L, Yedavalli VSRK, Jeang K-T. 2009. A genomewide short hairpin RNA screening of Jurkat T-cells for human proteins contributing to productive HIV-1 replication. J Biol Chem 284:19463-19473. http://dx.doi.org/10.1074/jbc.M109.010033.
    • (2009) J Biol Chem , vol.284 , pp. 19463-19473
    • Yeung, M.L.1    Houzet, L.2    Yedavalli, V.S.R.K.3    Jeang, K.-T.4
  • 5
    • 84956585606 scopus 로고    scopus 로고
    • SnapShot: antiviral restriction factors
    • Kluge SF, Sauter D, Kirchhoff F. 2015. SnapShot: antiviral restriction factors. Cell 163:774-774.e1. http://dx.doi.org/10.1016/j.cell.2015.10.019.
    • (2015) Cell , vol.163 , pp. 774-774
    • Kluge, S.F.1    Sauter, D.2    Kirchhoff, F.3
  • 6
    • 84929907228 scopus 로고    scopus 로고
    • Intrinsic host restrictions to HIV-1 and mechanisms of viral escape
    • Simon V, Bloch N, Landau NR. 2015. Intrinsic host restrictions to HIV-1 and mechanisms of viral escape. Nat Immunol 16:546-553. http://dx.doi.org/10.1038/ni.3156.
    • (2015) Nat Immunol , vol.16 , pp. 546-553
    • Simon, V.1    Bloch, N.2    Landau, N.R.3
  • 7
    • 0037031709 scopus 로고    scopus 로고
    • Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein
    • Gao G, Guo X, Goff SP. 2002. Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein. Science 297:1703-1706. http://dx.doi.org/10.1126/science.1074276.
    • (2002) Science , vol.297 , pp. 1703-1706
    • Gao, G.1    Guo, X.2    Goff, S.P.3
  • 8
    • 33747010603 scopus 로고    scopus 로고
    • Inhibition of HIV-1 gene expression by a fragment of hnRNP U
    • Valente ST, Goff SP. 2006. Inhibition of HIV-1 gene expression by a fragment of hnRNP U. Mol Cell 23:597-605. http://dx.doi.org/10.1016/j.molcel.2006.07.021.
    • (2006) Mol Cell , vol.23 , pp. 597-605
    • Valente, S.T.1    Goff, S.P.2
  • 10
    • 18244397937 scopus 로고    scopus 로고
    • Overexpression of fasciculation and elongation protein zeta-1 (FEZ1) induces a postentry block to retroviruses in cultured cells
    • Naghavi MH, Hatziioannou T, Gao G, Goff SP. 2005. Overexpression of fasciculation and elongation protein zeta-1 (FEZ1) induces a postentry block to retroviruses in cultured cells. Genes Dev 19:1105-1115. http://dx.doi.org/10.1101/gad.1290005.
    • (2005) Genes Dev , vol.19 , pp. 1105-1115
    • Naghavi, M.H.1    Hatziioannou, T.2    Gao, G.3    Goff, S.P.4
  • 12
    • 84880348270 scopus 로고    scopus 로고
    • A carboxy-terminally truncated human CPSF6 lacking residues encoded by exon 6 inhibits HIV-1 cDNA synthesis and promotes capsid disassembly
    • Hori T, Takeuchi H, Saito H, Sakuma R, Inagaki Y, Yamaoka S. 2013. A carboxy-terminally truncated human CPSF6 lacking residues encoded by exon 6 inhibits HIV-1 cDNA synthesis and promotes capsid disassembly. J Virol 87:7726-7736. http://dx.doi.org/10.1128/JVI.00124-13.
    • (2013) J Virol , vol.87 , pp. 7726-7736
    • Hori, T.1    Takeuchi, H.2    Saito, H.3    Sakuma, R.4    Inagaki, Y.5    Yamaoka, S.6
  • 13
    • 79955542915 scopus 로고    scopus 로고
    • A diverse range of gene products are effectors of the type I interferon antiviral response
    • Schoggins JW, Wilson SJ, Panis M, Murphy MY, Jones CT, Bieniasz P, Rice CM. 2011. A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 472:481-485. http://dx.doi.org/10.1038/nature09907.
    • (2011) Nature , vol.472 , pp. 481-485
    • Schoggins, J.W.1    Wilson, S.J.2    Panis, M.3    Murphy, M.Y.4    Jones, C.T.5    Bieniasz, P.6    Rice, C.M.7
  • 14
    • 84863285086 scopus 로고    scopus 로고
    • Systematic identification of type I and type II interferon-induced antiviral factors
    • Liu S-Y, Sanchez DJ, Aliyari R, Lu S, Cheng G. 2012. Systematic identification of type I and type II interferon-induced antiviral factors. Proc Natl Acad Sci U S A 109:4239-4244. http://dx.doi.org/10.1073/pnas.1114981109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 4239-4244
    • Liu, S.-Y.1    Sanchez, D.J.2    Aliyari, R.3    Lu, S.4    Cheng, G.5
  • 18
    • 84890926341 scopus 로고    scopus 로고
    • A model for cofactor use during HIV-1 reverse transcription and nuclear entry
    • Hilditch L, Towers GJ. 2014. A model for cofactor use during HIV-1 reverse transcription and nuclear entry. Curr Opin Virol 4:32-36. http://dx.doi.org/10.1016/j.coviro.2013.11.003.
    • (2014) Curr Opin Virol , vol.4 , pp. 32-36
    • Hilditch, L.1    Towers, G.J.2
  • 19
    • 84937208681 scopus 로고    scopus 로고
    • HIV-1 capsid: the multifaceted key player in HIV-1 infection
    • Campbell EM, Hope TJ. 2015. HIV-1 capsid: the multifaceted key player in HIV-1 infection. Nat Rev Microbiol 13:471-483. http://dx.doi.org/10.1038/nrmicro3503.
    • (2015) Nat Rev Microbiol , vol.13 , pp. 471-483
    • Campbell, E.M.1    Hope, T.J.2
  • 20
    • 33750390377 scopus 로고    scopus 로고
    • Cyclophilin A interacts with diverse lentiviral capsids
    • Lin T-Y, Emerman M. 2006. Cyclophilin A interacts with diverse lentiviral capsids. Retrovirology 3:70. http://dx.doi.org/10.1186/1742-4690-3-70.
    • (2006) Retrovirology , vol.3 , pp. 70
    • Lin, T.-Y.1    Emerman, M.2
  • 21
    • 84899733286 scopus 로고    scopus 로고
    • Gene expression analysis of a panel of cell lines that differentially restrict HIV-1 CA mutants infection in a cyclophilin A-dependent manner
    • Shah VB, Aiken C. 2014. Gene expression analysis of a panel of cell lines that differentially restrict HIV-1 CA mutants infection in a cyclophilin A-dependent manner. PLoS One 9:e92724. http://dx.doi.org/10.1371/journal.pone.0092724.
    • (2014) PLoS One , vol.9
    • Shah, V.B.1    Aiken, C.2
  • 22
    • 84893204722 scopus 로고    scopus 로고
    • Cyclophilin A promotes HIV-1 reverse transcription but its effect on transduction correlates best with its effect on nuclear entry of viral cDNA
    • De Iaco A, Luban J. 2014. Cyclophilin A promotes HIV-1 reverse transcription but its effect on transduction correlates best with its effect on nuclear entry of viral cDNA. Retrovirology 11:11. http://dx.doi.org/10.1186/1742-4690-11-11.
    • (2014) Retrovirology , vol.11 , pp. 11
    • De Iaco, A.1    Luban, J.2
  • 25
    • 84924266757 scopus 로고    scopus 로고
    • The highly polymorphic cyclophilin A-binding loop in HIV-1 capsid modulates viral resistance to MxB
    • Liu Z, Pan Q, Liang Z, Qiao W, Cen S, Liang C. 2015. The highly polymorphic cyclophilin A-binding loop in HIV-1 capsid modulates viral resistance to MxB. Retrovirology 12:1. http://dx.doi.org/10.1186/s12977-014-0129-1.
    • (2015) Retrovirology , vol.12 , pp. 1
    • Liu, Z.1    Pan, Q.2    Liang, Z.3    Qiao, W.4    Cen, S.5    Liang, C.6
  • 26
    • 84897965284 scopus 로고    scopus 로고
    • HIV-1 uncoating: connection to nuclear entry and regulation by host proteins
    • Ambrose Z, Aiken C. 2014. HIV-1 uncoating: connection to nuclear entry and regulation by host proteins. Virology 454-455:371-379.
    • (2014) Virology , vol.454-455 , pp. 371-379
    • Ambrose, Z.1    Aiken, C.2
  • 27
    • 84888206251 scopus 로고    scopus 로고
    • New insights in the role of nucleoporins: a bridge leading to concerted steps from HIV-1 nuclear entry until integration
    • Di Nunzio F. 2013. New insights in the role of nucleoporins: a bridge leading to concerted steps from HIV-1 nuclear entry until integration. Virus Res 178:187-196. http://dx.doi.org/10.1016/j.virusres.2013.09.003.
    • (2013) Virus Res , vol.178 , pp. 187-196
    • Di Nunzio, F.1
  • 28
    • 84873720427 scopus 로고    scopus 로고
    • TNPO3 protects HIV-1 replication from CPSF6-mediated capsid stabilization in the host cell cytoplasm
    • De Iaco A, Santoni F, Vannier A, Guipponi M, Antonarakis S, Luban J. 2013. TNPO3 protects HIV-1 replication from CPSF6-mediated capsid stabilization in the host cell cytoplasm. Retrovirology 10:20. http://dx.doi.org/10.1186/1742-4690-10-20.
    • (2013) Retrovirology , vol.10 , pp. 20
    • De Iaco, A.1    Santoni, F.2    Vannier, A.3    Guipponi, M.4    Antonarakis, S.5    Luban, J.6
  • 30
    • 84952873645 scopus 로고    scopus 로고
    • Direct visualization of HIV-1 replication intermediates shows that capsid and CPSF6 modulate HIV-1 intranuclear invasion and integration
    • Chin CR, Perreira JM, Savidis G, Portmann JM, Aker AM, Feeley EM, Smith MC, Brass AL. 2015. Direct visualization of HIV-1 replication intermediates shows that capsid and CPSF6 modulate HIV-1 intranuclear invasion and integration. Cell Rep 13:1717-1731. http://dx.doi.org/10.1016/j.celrep.2015.10.036.
    • (2015) Cell Rep , vol.13 , pp. 1717-1731
    • Chin, C.R.1    Perreira, J.M.2    Savidis, G.3    Portmann, J.M.4    Aker, A.M.5    Feeley, E.M.6    Smith, M.C.7    Brass, A.L.8
  • 33
    • 0032772929 scopus 로고    scopus 로고
    • UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. elegans development
    • Malone CJ, Fixsen WD, Horvitz HR, Han M. 1999. UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. elegans development. Development 126:3171-3181.
    • (1999) Development , vol.126 , pp. 3171-3181
    • Malone, C.J.1    Fixsen, W.D.2    Horvitz, H.R.3    Han, M.4
  • 34
    • 2942533937 scopus 로고    scopus 로고
    • Sun2 is a novel mammalian inner nuclear membrane protein
    • Hodzic DM, Yeater DB, Bengtsson L, Otto H, Stahl PD. 2004. Sun2 is a novel mammalian inner nuclear membrane protein. J Biol Chem 279: 25805-25812. http://dx.doi.org/10.1074/jbc.M313157200.
    • (2004) J Biol Chem , vol.279 , pp. 25805-25812
    • Hodzic, D.M.1    Yeater, D.B.2    Bengtsson, L.3    Otto, H.4    Stahl, P.D.5
  • 36
    • 33846463849 scopus 로고    scopus 로고
    • Characterization of the structures involved in localization of the SUN proteins to the nuclear envelope and the centrosome
    • Wang Q, Du X, Cai Z, Greene MI. 2006. Characterization of the structures involved in localization of the SUN proteins to the nuclear envelope and the centrosome. DNA Cell Biol 25:554-562. http://dx.doi.org/10.1089/dna.2006.25.554.
    • (2006) DNA Cell Biol , vol.25 , pp. 554-562
    • Wang, Q.1    Du, X.2    Cai, Z.3    Greene, M.I.4
  • 37
    • 78049394356 scopus 로고    scopus 로고
    • Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges
    • Starr DA, Fridolfsson HN. 2010. Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges. Annu Rev Cell Dev Biol 26:421-444. http://dx.doi.org/10.1146/annurev-cellbio-100109-104037.
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 421-444
    • Starr, D.A.1    Fridolfsson, H.N.2
  • 38
    • 84920880008 scopus 로고    scopus 로고
    • Accessorizing and anchoring the LINC complex for multifunctionality
    • Chang W, Worman HJ, Gundersen GG. 2015. Accessorizing and anchoring the LINC complex for multifunctionality. J Cell Biol 208:11-22. http://dx.doi.org/10.1083/jcb.201409047.
    • (2015) J Cell Biol , vol.208 , pp. 11-22
    • Chang, W.1    Worman, H.J.2    Gundersen, G.G.3
  • 39
    • 84885846858 scopus 로고    scopus 로고
    • The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin
    • Rothballer A, Kutay U. 2013. The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin. Chromosoma 122: 415-429. http://dx.doi.org/10.1007/s00412-013-0417-x.
    • (2013) Chromosoma , vol.122 , pp. 415-429
    • Rothballer, A.1    Kutay, U.2
  • 40
    • 84878585819 scopus 로고    scopus 로고
    • Structural insights into LINC complexes
    • Sosa BA, Kutay U, Schwartz TU. 2013. Structural insights into LINC complexes. Curr Opin Struct Biol 23:285-291. http://dx.doi.org/10.1016/j.sbi.2013.03.005.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 285-291
    • Sosa, B.A.1    Kutay, U.2    Schwartz, T.U.3
  • 41
    • 0029115575 scopus 로고
    • Establishment of human microglial cell lines after transfection of primary cultures of embryonic microglial cells with the SV40 large T antigen
    • Janabi N, Peudenier S, Héron B, Ng KH, Tardieu M. 1995. Establishment of human microglial cell lines after transfection of primary cultures of embryonic microglial cells with the SV40 large T antigen. Neurosci Lett 195:105-108. http://dx.doi.org/10.1016/0304-3940(94)11792-H.
    • (1995) Neurosci Lett , vol.195 , pp. 105-108
    • Janabi, N.1    Peudenier, S.2    Héron, B.3    Ng, K.H.4    Tardieu, M.5
  • 42
    • 0028149419 scopus 로고
    • Human immunodeficiency virus Vpx is required for the early phase of replication in peripheral blood mononuclear cells
    • Kawamura M, Sakai H, Adachi A. 1994. Human immunodeficiency virus Vpx is required for the early phase of replication in peripheral blood mononuclear cells. Microbiol Immunol 38:871-878. http://dx.doi.org/10.1111/j.1348-0421.1994.tb02140.x.
    • (1994) Microbiol Immunol , vol.38 , pp. 871-878
    • Kawamura, M.1    Sakai, H.2    Adachi, A.3
  • 44
    • 0029018332 scopus 로고
    • Isolation and characterization of a syncytium-inducing, macrophage/T-cell linetropic human immunodeficiency virus type 1 isolate that readily infects chimpanzee cells in vitro and in vivo
    • Shibata R, Hoggan MD, Broscius C, Englund G, Theodore TS, Buckler-White A, Arthur LO, Israel Z, Schultz A, Lane HC. 1995. Isolation and characterization of a syncytium-inducing, macrophage/T-cell linetropic human immunodeficiency virus type 1 isolate that readily infects chimpanzee cells in vitro and in vivo. J Virol 69:4453-4462.
    • (1995) J Virol , vol.69 , pp. 4453-4462
    • Shibata, R.1    Hoggan, M.D.2    Broscius, C.3    Englund, G.4    Theodore, T.S.5    Buckler-White, A.6    Arthur, L.O.7    Israel, Z.8    Schultz, A.9    Lane, H.C.10
  • 45
    • 70349753255 scopus 로고    scopus 로고
    • Partial inhibition of human immunodeficiency virus replication by type I interferons: impact of cell-to-cell viral transfer
    • Vendrame D, Sourisseau M, Perrin V, Schwartz O, Mammano F. 2009. Partial inhibition of human immunodeficiency virus replication by type I interferons: impact of cell-to-cell viral transfer. J Virol 83:10527-10537. http://dx.doi.org/10.1128/JVI.01235-09.
    • (2009) J Virol , vol.83 , pp. 10527-10537
    • Vendrame, D.1    Sourisseau, M.2    Perrin, V.3    Schwartz, O.4    Mammano, F.5
  • 46
    • 54549099338 scopus 로고    scopus 로고
    • HIV-2 integrase gene polymorphism and phenotypic susceptibility of HIV-2 clinical isolates to the integrase inhibitors raltegravir and elvitegravir in vitro
    • Roquebert B, Damond F, Collin G, Matheron S, Peytavin G, Bénard A, Campa P, Chêne G, Brun-Vézinet F, Descamps D, French ANRS, HIV-2 Cohort (ANRS CO 05 VIH-2). 2008. HIV-2 integrase gene polymorphism and phenotypic susceptibility of HIV-2 clinical isolates to the integrase inhibitors raltegravir and elvitegravir in vitro. J Antimicrob Chemother 62:914-920. http://dx.doi.org/10.1093/jac/dkn335.
    • (2008) J Antimicrob Chemother , vol.62 , pp. 914-920
    • Roquebert, B.1    Damond, F.2    Collin, G.3    Matheron, S.4    Peytavin, G.5    Bénard, A.6    Campa, P.7    Chêne, G.8    Brun-Vézinet, F.9    Descamps, D.10
  • 48
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini L, Blömer U, Gallay P, Ory D, Mulligan R, Gage FH, Verma IM, Trono D. 1996. In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272:263-267. http://dx.doi.org/10.1126/science.272.5259.263.
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1    Blömer, U.2    Gallay, P.3    Ory, D.4    Mulligan, R.5    Gage, F.H.6    Verma, I.M.7    Trono, D.8
  • 49
    • 33744832621 scopus 로고    scopus 로고
    • With a little help from a friend: increasing HIV transduction of monocyte-derived dendritic cells with virion-like particles of SIV(MAC)
    • Goujon C, Jarrosson-Wuillème L, Bernaud J, Rigal D, Darlix JL, Cimarelli A. 2006. With a little help from a friend: increasing HIV transduction of monocyte-derived dendritic cells with virion-like particles of SIV(MAC). Gene Ther 13:991-994. http://dx.doi.org/10.1038/sj.gt.3302753.
    • (2006) Gene Ther , vol.13 , pp. 991-994
    • Goujon, C.1    Jarrosson-Wuillème, L.2    Bernaud, J.3    Rigal, D.4    Darlix, J.L.5    Cimarelli, A.6
  • 51
    • 0035025888 scopus 로고    scopus 로고
    • A quantitative assay for HIV DNA integration in vivo
    • Butler SL, Bushman FD. 2001. A quantitative assay for HIV DNA integration in vivo. Nat Med 7:631-634. http://dx.doi.org/10.1038/87979.
    • (2001) Nat Med , vol.7 , pp. 631-634
    • Butler, S.L.1    Bushman, F.D.2
  • 54
    • 33646573998 scopus 로고    scopus 로고
    • Genomic response to interferon-alpha in chimpanzees: implications of rapid downregulation for hepatitis C kinetics
    • Lanford RE, Guerra B, Lee H, Chavez D, Brasky KM, Bigger CB. 2006. Genomic response to interferon-alpha in chimpanzees: implications of rapid downregulation for hepatitis C kinetics. Hepatology 43:961-972. http://dx.doi.org/10.1002/hep.21167.
    • (2006) Hepatology , vol.43 , pp. 961-972
    • Lanford, R.E.1    Guerra, B.2    Lee, H.3    Chavez, D.4    Brasky, K.M.5    Bigger, C.B.6
  • 55
    • 27444431583 scopus 로고    scopus 로고
    • Human T-cell leukemia virus type I (HTLV-I) infection and the onset of adult T-cell leukemia (ATL)
    • Matsuoka M. 2005. Human T-cell leukemia virus type I (HTLV-I) infection and the onset of adult T-cell leukemia (ATL). Retrovirology 2:27. http://dx.doi.org/10.1186/1742-4690-2-27.
    • (2005) Retrovirology , vol.2 , pp. 27
    • Matsuoka, M.1
  • 58
    • 44749086091 scopus 로고    scopus 로고
    • Over-expression of GFP-FEZ1 causes generation of multi-lobulated nuclei mediated by microtubules in HEK293 cells
    • Lanza DCF, Trindade DM, Assmann EM, Kobarg J. 2008. Over-expression of GFP-FEZ1 causes generation of multi-lobulated nuclei mediated by microtubules in HEK293 cells. Exp Cell Res 314:2028-2039. http://dx.doi.org/10.1016/j.yexcr.2008.02.012.
    • (2008) Exp Cell Res , vol.314 , pp. 2028-2039
    • Lanza, D.C.F.1    Trindade, D.M.2    Assmann, E.M.3    Kobarg, J.4
  • 59
    • 14644433076 scopus 로고    scopus 로고
    • Multi-lobulation of the nucleus in prolonged S phase by nuclear expression of Chk tyrosine kinase
    • Nakayama Y, Yamaguchi N. 2005. Multi-lobulation of the nucleus in prolonged S phase by nuclear expression of Chk tyrosine kinase. Exp Cell Res 304:570-581. http://dx.doi.org/10.1016/j.yexcr.2004.11.027.
    • (2005) Exp Cell Res , vol.304 , pp. 570-581
    • Nakayama, Y.1    Yamaguchi, N.2
  • 65
    • 84908664449 scopus 로고    scopus 로고
    • Cytoplasmic dynein promotes HIV-1 uncoating
    • Pawlica P, Berthoux L. 2014. Cytoplasmic dynein promotes HIV-1 uncoating. Viruses 6:4195-4211. http://dx.doi.org/10.3390/v6114195.
    • (2014) Viruses , vol.6 , pp. 4195-4211
    • Pawlica, P.1    Berthoux, L.2
  • 66
    • 84908676379 scopus 로고    scopus 로고
    • HIV-1 uncoating is facilitated by dynein and kinesin 1
    • Lukic Z, Dharan A, Fricke T, Diaz-Griffero F, Campbell EM. 2014. HIV-1 uncoating is facilitated by dynein and kinesin 1. J Virol 88:13613-13625. http://dx.doi.org/10.1128/JVI.02219-14.
    • (2014) J Virol , vol.88 , pp. 13613-13625
    • Lukic, Z.1    Dharan, A.2    Fricke, T.3    Diaz-Griffero, F.4    Campbell, E.M.5
  • 67
    • 84897563528 scopus 로고    scopus 로고
    • KASHing up with the nucleus: novel functional roles of KASH proteins at the cytoplasmic surface of the nucleus
    • Luxton GG, Starr DA. 2014. KASHing up with the nucleus: novel functional roles of KASH proteins at the cytoplasmic surface of the nucleus. Curr Opin Cell Biol 28:69-75. http://dx.doi.org/10.1016/j.ceb.2014.03.002.
    • (2014) Curr Opin Cell Biol , vol.28 , pp. 69-75
    • Luxton, G.G.1    Starr, D.A.2
  • 68
    • 84936771673 scopus 로고    scopus 로고
    • Single-cell and single-cycle analysis of HIV-1 replication
    • Holmes M, Zhang F, Bieniasz PD. 2015. Single-cell and single-cycle analysis of HIV-1 replication. PLoS Pathog 11:e1004961. http://dx.doi.org/10.1371/journal.ppat.1004961.
    • (2015) PLoS Pathog , vol.11
    • Holmes, M.1    Zhang, F.2    Bieniasz, P.D.3
  • 69
    • 67650860274 scopus 로고    scopus 로고
    • Characterization of the behavior of functional viral genomes during the early steps of human immunodeficiency virus type 1 infection
    • Arfi V, Lienard J, Nguyen X-N, Berger G, Rigal D, Darlix J-L, Cimarelli A. 2009. Characterization of the behavior of functional viral genomes during the early steps of human immunodeficiency virus type 1 infection. J Virol 83:7524-7535. http://dx.doi.org/10.1128/JVI.00429-09.
    • (2009) J Virol , vol.83 , pp. 7524-7535
    • Arfi, V.1    Lienard, J.2    Nguyen, X.-N.3    Berger, G.4    Rigal, D.5    Darlix, J.-L.6    Cimarelli, A.7
  • 70
    • 79952369523 scopus 로고    scopus 로고
    • Effects of microtubule modulators on HIV-1 infection of transformed and resting CD4 T cells
    • Yoder A, Guo J, Yu D, Cui Z, Zhang XE, Wu Y. 2011. Effects of microtubule modulators on HIV-1 infection of transformed and resting CD4 T cells. J Virol 85:3020-3024. http://dx.doi.org/10.1128/JVI.02462-10.
    • (2011) J Virol , vol.85 , pp. 3020-3024
    • Yoder, A.1    Guo, J.2    Yu, D.3    Cui, Z.4    Zhang, X.E.5    Wu, Y.6
  • 71
    • 84925000178 scopus 로고    scopus 로고
    • Inhibition of microtubules and dynein rescues human immunodeficiency virus type 1 from owl monkey TRIMCyp-mediated restriction in a cellular context-specific fashion
    • Pawlica P, Dufour C, Berthoux L. 2015. Inhibition of microtubules and dynein rescues human immunodeficiency virus type 1 from owl monkey TRIMCyp-mediated restriction in a cellular context-specific fashion. J Gen Virol 96:874-886. http://dx.doi.org/10.1099/jgv.0.000018.
    • (2015) J Gen Virol , vol.96 , pp. 874-886
    • Pawlica, P.1    Dufour, C.2    Berthoux, L.3
  • 72
    • 84861426660 scopus 로고    scopus 로고
    • The trinity of the cortical actin in the initiation of HIV-1 infection
    • Spear M, Guo J, Wu Y. 2012. The trinity of the cortical actin in the initiation of HIV-1 infection. Retrovirology 9:45. http://dx.doi.org/10.1186/1742-4690-9-45.
    • (2012) Retrovirology , vol.9 , pp. 45
    • Spear, M.1    Guo, J.2    Wu, Y.3
  • 74
    • 84861543038 scopus 로고    scopus 로고
    • LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins
    • Sosa BA, Rothballer A, Kutay U, Schwartz TU. 2012. LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins. Cell 149:1035-1047. http://dx.doi.org/10.1016/j.cell.2012.03.046.
    • (2012) Cell , vol.149 , pp. 1035-1047
    • Sosa, B.A.1    Rothballer, A.2    Kutay, U.3    Schwartz, T.U.4
  • 76
    • 77954886484 scopus 로고    scopus 로고
    • A classical NLS and the SUN domain contribute to the targeting of SUN2 to the inner nuclear membrane
    • Turgay Y, Ungricht R, Rothballer A, Kiss A, Csucs G, Horvath P, Kutay U. 2010. A classical NLS and the SUN domain contribute to the targeting of SUN2 to the inner nuclear membrane. EMBO J 29:2262-2275. http://dx.doi.org/10.1038/emboj.2010.119.
    • (2010) EMBO J , vol.29 , pp. 2262-2275
    • Turgay, Y.1    Ungricht, R.2    Rothballer, A.3    Kiss, A.4    Csucs, G.5    Horvath, P.6    Kutay, U.7
  • 78
    • 84934977725 scopus 로고    scopus 로고
    • Host and viral determinants for MxB restriction of HIV-1 infection
    • Matreyek KA, Wang W, Serrao E, Singh P, Levin HL, Engelman A. 2014. Host and viral determinants for MxB restriction of HIV-1 infection. Retrovirology 11:90. http://dx.doi.org/10.1186/s12977-014-0090-z.
    • (2014) Retrovirology , vol.11 , pp. 90
    • Matreyek, K.A.1    Wang, W.2    Serrao, E.3    Singh, P.4    Levin, H.L.5    Engelman, A.6
  • 79
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • Gamble TR, Vajdos FF, Yoo S, Worthylake DK, Houseweart M, Sundquist WI, Hill CP. 1996. Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell 87:1285-1294. http://dx.doi.org/10.1016/S0092-8674(00)81823-1.
    • (1996) Cell , vol.87 , pp. 1285-1294
    • Gamble, T.R.1    Vajdos, F.F.2    Yoo, S.3    Worthylake, D.K.4    Houseweart, M.5    Sundquist, W.I.6    Hill, C.P.7
  • 80
    • 33845967100 scopus 로고    scopus 로고
    • Two binding partners cooperate to activate the molecular motor kinesin-1
    • Blasius TL, Cai D, Jih GT, Toret CP, Verhey KJ. 2007. Two binding partners cooperate to activate the molecular motor kinesin-1. J Cell Biol 176:11-17. http://dx.doi.org/10.1083/jcb.200605099.
    • (2007) J Cell Biol , vol.176 , pp. 11-17
    • Blasius, T.L.1    Cai, D.2    Jih, G.T.3    Toret, C.P.4    Verhey, K.J.5
  • 81
    • 69549111484 scopus 로고    scopus 로고
    • The brain-specific factor FEZ1 is a determinant of neuronal susceptibility to HIV-1 infection
    • Haedicke J, Brown C, Naghavi MH. 2009. The brain-specific factor FEZ1 is a determinant of neuronal susceptibility to HIV-1 infection. Proc Natl Acad Sci U S A 106:14040-14045. http://dx.doi.org/10.1073/pnas.0900502106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14040-14045
    • Haedicke, J.1    Brown, C.2    Naghavi, M.H.3
  • 82
    • 33645116283 scopus 로고    scopus 로고
    • Laminopathies: multisystem dystrophy syndromes
    • Jacob KN, Garg A. 2006. Laminopathies: multisystem dystrophy syndromes. Mol Genet Metab 87:289-302. http://dx.doi.org/10.1016/j.ymgme.2005.10.018.
    • (2006) Mol Genet Metab , vol.87 , pp. 289-302
    • Jacob, K.N.1    Garg, A.2
  • 84
    • 84860327128 scopus 로고    scopus 로고
    • Accumulation of the inner nuclear envelope protein Sun1 is pathogenic in progeric and dystrophic laminopathies
    • Chen C-Y, Chi Y-H, Mutalif RA, Starost MF, Myers TG, Anderson SA, Stewart CL, Jeang K-T. 2012. Accumulation of the inner nuclear envelope protein Sun1 is pathogenic in progeric and dystrophic laminopathies. Cell 149:565-577. http://dx.doi.org/10.1016/j.cell.2012.01.059.
    • (2012) Cell , vol.149 , pp. 565-577
    • Chen, C.-Y.1    Chi, Y.-H.2    Mutalif, R.A.3    Starost, M.F.4    Myers, T.G.5    Anderson, S.A.6    Stewart, C.L.7    Jeang, K.-T.8
  • 85
    • 84898887269 scopus 로고    scopus 로고
    • Dysregulated interactions between lamin A and SUN1 induce abnormalities in the nuclear envelope and endoplasmic reticulum in progeric laminopathies
    • Chen Z-J, Wang W-P, Chen Y-C, Wang J-Y, Lin W-H, Tai L-A, Liou G-G, Yang C-S, Chi Y-H. 2014. Dysregulated interactions between lamin A and SUN1 induce abnormalities in the nuclear envelope and endoplasmic reticulum in progeric laminopathies. J Cell Sci 127:1792-1804. http://dx.doi.org/10.1242/jcs.139683.
    • (2014) J Cell Sci , vol.127 , pp. 1792-1804
    • Chen, Z.-J.1    Wang, W.-P.2    Chen, Y.-C.3    Wang, J.-Y.4    Lin, W.-H.5    Tai, L.-A.6    Liou, G.-G.7    Yang, C.-S.8    Chi, Y.-H.9
  • 87
    • 77449109551 scopus 로고    scopus 로고
    • Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes
    • Haque F, Mazzeo D, Patel JT, Smallwood DT, Ellis JA, Shanahan CM, Shackleton S. 2010. Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes. J Biol Chem 285:3487-3498. http://dx.doi.org/10.1074/jbc.M109.071910.
    • (2010) J Biol Chem , vol.285 , pp. 3487-3498
    • Haque, F.1    Mazzeo, D.2    Patel, J.T.3    Smallwood, D.T.4    Ellis, J.A.5    Shanahan, C.M.6    Shackleton, S.7
  • 88
    • 84866183378 scopus 로고    scopus 로고
    • Reversal of laminopathies: the curious case of SUN1
    • Chi Y-H, Chen C-Y, Jeang K-T. 2012. Reversal of laminopathies: the curious case of SUN1. Nucleus 3:418-421. http://dx.doi.org/10.4161/nucl.21714.
    • (2012) Nucleus , vol.3 , pp. 418-421
    • Chi, Y.-H.1    Chen, C.-Y.2    Jeang, K.-T.3
  • 89
    • 84866177329 scopus 로고    scopus 로고
    • Laminopathies: too much SUN is a bad thing
    • Starr DA. 2012. Laminopathies: too much SUN is a bad thing. Curr Biol 22:R678-R680. http://dx.doi.org/10.1016/j.cub.2012.06.070.
    • (2012) Curr Biol , vol.22 , pp. R678-R680
    • Starr, D.A.1
  • 90
    • 84934436859 scopus 로고    scopus 로고
    • The cyclosporin A washout assay to detect HIV-1 uncoating in infected cells
    • Hulme AE, Hope TJ. 2014. The cyclosporin A washout assay to detect HIV-1 uncoating in infected cells. Methods Mol Biol 1087:37-46. http://dx.doi.org/10.1007/978-1-62703-670-2_4.
    • (2014) Methods Mol Biol , vol.1087 , pp. 37-46
    • Hulme, A.E.1    Hope, T.J.2
  • 91
    • 84934437891 scopus 로고    scopus 로고
    • The fate of HIV-1 capsid: a biochemical assay for HIV-1 uncoating
    • Yang Y, Luban J, Diaz-Griffero F. 2014. The fate of HIV-1 capsid: a biochemical assay for HIV-1 uncoating. Methods Mol Biol 1087:29-36. http://dx.doi.org/10.1007/978-1-62703-670-2_3.
    • (2014) Methods Mol Biol , vol.1087 , pp. 29-36
    • Yang, Y.1    Luban, J.2    Diaz-Griffero, F.3
  • 98
    • 84924194959 scopus 로고    scopus 로고
    • BI-2 destabilizes HIV-1 cores during infection and prevents binding of CPSF6 to the HIV-1 capsid
    • Fricke T, Buffone C, Opp S, Valle-Casuso J, Diaz-Griffero F. 2014. BI-2 destabilizes HIV-1 cores during infection and prevents binding of CPSF6 to the HIV-1 capsid. Retrovirology 11:120. http://dx.doi.org/10.1186/s12977-014-0120-x.
    • (2014) Retrovirology , vol.11 , pp. 120
    • Fricke, T.1    Buffone, C.2    Opp, S.3    Valle-Casuso, J.4    Diaz-Griffero, F.5
  • 99
    • 84885090088 scopus 로고    scopus 로고
    • Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity
    • Matreyek KA, Yücel SS, Li X, Engelman A. 2013. Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity. PLoS Pathog 9:e1003693. http://dx.doi.org/10.1371/journal.ppat.1003693.
    • (2013) PLoS Pathog , vol.9
    • Matreyek, K.A.1    Yücel, S.S.2    Li, X.3    Engelman, A.4
  • 100
    • 84938937756 scopus 로고    scopus 로고
    • HIV-1 resistance to the capsid-targeting inhibitor PF74 results in altered dependence on host factors required for virus nuclear entry
    • Zhou J, Price AJ, Halambage UD, James LC, Aiken C. 2015. HIV-1 resistance to the capsid-targeting inhibitor PF74 results in altered dependence on host factors required for virus nuclear entry. J Virol 89:9068-9079. http://dx.doi.org/10.1128/JVI.00340-15.
    • (2015) J Virol , vol.89 , pp. 9068-9079
    • Zhou, J.1    Price, A.J.2    Halambage, U.D.3    James, L.C.4    Aiken, C.5
  • 103
    • 79957838252 scopus 로고    scopus 로고
    • Subcellular localization of SUN2 is regulated by lamin A and Rab5
    • Liang Y, Chiu PH, Yip KY, Chan SY. 2011. Subcellular localization of SUN2 is regulated by lamin A and Rab5. PLoS One 6:e20507. http://dx.doi.org/10.1371/journal.pone.0020507.
    • (2011) PLoS One , vol.6
    • Liang, Y.1    Chiu, P.H.2    Yip, K.Y.3    Chan, S.Y.4
  • 105
    • 84935097050 scopus 로고    scopus 로고
    • X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability
    • Gres AT, Kirby KA, KewalRamani VN, Tanner JJ, Pornillos O, Sarafianos SG. 2015. X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability. Science 349:99-103. http://dx.doi.org/10.1126/science.aaa5936.
    • (2015) Science , vol.349 , pp. 99-103
    • Gres, A.T.1    Kirby, K.A.2    KewalRamani, V.N.3    Tanner, J.J.4    Pornillos, O.5    Sarafianos, S.G.6

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