메뉴 건너뛰기




Volumn 18, Issue 6, 2017, Pages 362-377

Importin β1 targeting by hepatitis C virus NS3/4A protein restricts IRF3 and NF-κB signaling of IFNB1 antiviral response

Author keywords

HCV; importin ; importin ; IMP 1 KPNB1; innate antiviral immunity; interferon ; IRF3; microscopy based high content screening; NF B p65; NPC; NS3 4A protein; nuclear pore complex; nuclear translocation; nucleocytoplasmic transport; RNAi screen; SeV; virus host interaction

Indexed keywords

BETA1 INTERFERON; DICER; ELONGATION FACTOR 1ALPHA; HEPACIVIRIN; IMPORTIN BETA1; INTERFERON REGULATORY FACTOR 3; KARYOPHERIN BETA; MESSENGER RNA; SHORT HAIRPIN RNA; TRANSCRIPTION FACTOR RELA; UNCLASSIFIED DRUG; VIRAL PROTEIN; ANTIVIRUS AGENT; CARRIER PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; KARYOPHERIN; KPNB1 PROTEIN, HUMAN; NS3 PROTEIN, HEPATITIS C VIRUS; NS4A COFACTOR PEPTIDE, HEPATITIS C VIRUS; PROTEINASE INHIBITOR; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 85018979408     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12480     Document Type: Article
Times cited : (26)

References (63)
  • 1
    • 84891771728 scopus 로고    scopus 로고
    • Elucidating novel hepatitis C virus-host interactions using combined mass spectrometry and functional genomics approaches
    • Germain MA, Chatel-Chaix L, Gagné B et al. Elucidating novel hepatitis C virus-host interactions using combined mass spectrometry and functional genomics approaches. Mol Cell Proteomics. 2014;13:184-203.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 184-203
    • Germain, M.A.1    Chatel-Chaix, L.2    Gagné, B.3
  • 2
    • 39349097864 scopus 로고    scopus 로고
    • Identification of host proteins required for HIV infection through a functional genomic screen
    • Brass AL, Dykxhoorn DM, Benita Y, et al. Identification of host proteins required for HIV infection through a functional genomic screen. Science. 2008;319:921-926.
    • (2008) Science , vol.319 , pp. 921-926
    • Brass, A.L.1    Dykxhoorn, D.M.2    Benita, Y.3
  • 3
    • 76749090540 scopus 로고    scopus 로고
    • Genome-wide RNAi screen identifies human host factors crucial for influenza virus replication
    • Karlas A, Machuy N, Shin Y, et al. Genome-wide RNAi screen identifies human host factors crucial for influenza virus replication. Nature. 2010;463:818-822.
    • (2010) Nature , vol.463 , pp. 818-822
    • Karlas, A.1    Machuy, N.2    Shin, Y.3
  • 4
    • 52949130695 scopus 로고    scopus 로고
    • Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication
    • Konig R, Zhou Y, Elleder D, et al. Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication. Cell. 2008;135:49-60.
    • (2008) Cell , vol.135 , pp. 49-60
    • Konig, R.1    Zhou, Y.2    Elleder, D.3
  • 5
    • 77956517897 scopus 로고    scopus 로고
    • A host of factors regulating influenza virus replication
    • Mehle A, Doudna JA. A host of factors regulating influenza virus replication. Viruses. 2010;2:566-573.
    • (2010) Viruses , vol.2 , pp. 566-573
    • Mehle, A.1    Doudna, J.A.2
  • 6
    • 84915748288 scopus 로고    scopus 로고
    • Functional characterization of nuclear localization and export signals in hepatitis C virus proteins and their role in the membranous web
    • Levin A, Neufeldt CJ, Pang D, et al. Functional characterization of nuclear localization and export signals in hepatitis C virus proteins and their role in the membranous web. PLoS One. 2014;9:e114629.
    • (2014) PLoS One , vol.9
    • Levin, A.1    Neufeldt, C.J.2    Pang, D.3
  • 7
    • 84887275344 scopus 로고    scopus 로고
    • Hepatitis C virus-induced cytoplasmic organelles use the nuclear transport machinery to establish an environment conducive to virus replication
    • Neufeldt CJ, Joyce MA, Levin A, et al. Hepatitis C virus-induced cytoplasmic organelles use the nuclear transport machinery to establish an environment conducive to virus replication. PLoS Pathog. 2013;9:e1003744.
    • (2013) PLoS Pathog , vol.9
    • Neufeldt, C.J.1    Joyce, M.A.2    Levin, A.3
  • 8
    • 33747625216 scopus 로고    scopus 로고
    • A picornavirus protein interacts with Ran-GTPase and disrupts nucleocytoplasmic transport
    • Porter FW, Bochkov YA, Albee AJ, Wiese C, Palmenberg AC. A picornavirus protein interacts with Ran-GTPase and disrupts nucleocytoplasmic transport. Proc Natl Acad Sci USA. 2006;103:12417-12422.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12417-12422
    • Porter, F.W.1    Bochkov, Y.A.2    Albee, A.J.3    Wiese, C.4    Palmenberg, A.C.5
  • 9
    • 84866672766 scopus 로고    scopus 로고
    • Human nucleoporins promote HIV-1 docking at the nuclear pore, nuclear import and integration
    • Di Nunzio F, Danckaert A, Fricke T, et al. Human nucleoporins promote HIV-1 docking at the nuclear pore, nuclear import and integration. PLoS One. 2012;7:e46037.
    • (2012) PLoS One , vol.7
    • Di Nunzio, F.1    Danckaert, A.2    Fricke, T.3
  • 10
    • 77955922760 scopus 로고    scopus 로고
    • Transportin 3 and importin alpha are required for effective nuclear import of HIV-1 integrase in virus-infected cells
    • Levin A, Hayouka Z, Friedler A, Loyter A. Transportin 3 and importin alpha are required for effective nuclear import of HIV-1 integrase in virus-infected cells. Nucleus. 2010;1:422-431.
    • (2010) Nucleus , vol.1 , pp. 422-431
    • Levin, A.1    Hayouka, Z.2    Friedler, A.3    Loyter, A.4
  • 11
    • 80055069036 scopus 로고    scopus 로고
    • Identification of a functional, CRM-1-dependent nuclear export signal in hepatitis C virus core protein
    • Cerutti A, Maillard P, Minisini R, et al. Identification of a functional, CRM-1-dependent nuclear export signal in hepatitis C virus core protein. PLoS One. 2011;6:e25854.
    • (2011) PLoS One , vol.6
    • Cerutti, A.1    Maillard, P.2    Minisini, R.3
  • 12
    • 19944428289 scopus 로고    scopus 로고
    • Molecular determinants for subcellular localization of hepatitis C virus core protein
    • Suzuki R, Sakamoto S, Tsutsumi T, et al. Molecular determinants for subcellular localization of hepatitis C virus core protein. J Virol. 2005;79:1271-1281.
    • (2005) J Virol , vol.79 , pp. 1271-1281
    • Suzuki, R.1    Sakamoto, S.2    Tsutsumi, T.3
  • 13
    • 84959562427 scopus 로고    scopus 로고
    • The hepatitis C virus-induced membranous web and associated nuclear transport machinery limit access of pattern recognition receptors to viral replication sites
    • Neufeldt CJ, Joyce MA, Van Buuren N, et al. The hepatitis C virus-induced membranous web and associated nuclear transport machinery limit access of pattern recognition receptors to viral replication sites. PLoS Pathog. 2016;12:e1005428.
    • (2016) PLoS Pathog , vol.12
    • Neufeldt, C.J.1    Joyce, M.A.2    Van Buuren, N.3
  • 14
    • 84991736601 scopus 로고    scopus 로고
    • Roles of nuclear trafficking in infection by cytoplasmic negative-strand RNA viruses: paramyxoviruses and beyond
    • Audsley MD, Jans DA, Moseley GW. Roles of nuclear trafficking in infection by cytoplasmic negative-strand RNA viruses: paramyxoviruses and beyond. J Gen Virol. 2016;97:2463-2481.
    • (2016) J Gen Virol , vol.97 , pp. 2463-2481
    • Audsley, M.D.1    Jans, D.A.2    Moseley, G.W.3
  • 15
    • 33846907343 scopus 로고    scopus 로고
    • Influenza virus targets the mRNA export machinery and the nuclear pore complex
    • Satterly N, Tsai PL, van Deursen J, et al. Influenza virus targets the mRNA export machinery and the nuclear pore complex. Proc Natl Acad Sci USA. 2007;104:1853-1858.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1853-1858
    • Satterly, N.1    Tsai, P.L.2    van Deursen, J.3
  • 16
    • 84980340170 scopus 로고    scopus 로고
    • NXT1, a novel influenza A NP binding protein, promotes the nuclear export of NP via a CRM1-dependent pathway
    • Chutiwitoonchai N, Aida Y. NXT1, a novel influenza A NP binding protein, promotes the nuclear export of NP via a CRM1-dependent pathway. Viruses. 2016;8(8).
    • (2016) Viruses , vol.8 , Issue.8
    • Chutiwitoonchai, N.1    Aida, Y.2
  • 17
    • 18144378011 scopus 로고    scopus 로고
    • Nuclear localization of the Nipah virus W protein allows for inhibition of both virus- and toll-like receptor 3-triggered signaling pathways
    • Shaw ML, Cardenas WB, Zamarin D, Palese P, Basler CF. Nuclear localization of the Nipah virus W protein allows for inhibition of both virus- and toll-like receptor 3-triggered signaling pathways. J Virol. 2005;79:6078-6088.
    • (2005) J Virol , vol.79 , pp. 6078-6088
    • Shaw, M.L.1    Cardenas, W.B.2    Zamarin, D.3    Palese, P.4    Basler, C.F.5
  • 18
    • 37149040796 scopus 로고    scopus 로고
    • Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily karyopherin alpha proteins with activated STAT1
    • Reid SP, Valmas C, Martinez O, Sanchez FM, Basler CF. Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily karyopherin alpha proteins with activated STAT1. J Virol. 2007;81:13469-13477.
    • (2007) J Virol , vol.81 , pp. 13469-13477
    • Reid, S.P.1    Valmas, C.2    Martinez, O.3    Sanchez, F.M.4    Basler, C.F.5
  • 19
    • 84908332680 scopus 로고    scopus 로고
    • Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of phosphorylated STAT1
    • Xu W, Edwards MR, Borek DM, et al. Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of phosphorylated STAT1. Cell Host Microbe. 2014;16:187-200.
    • (2014) Cell Host Microbe , vol.16 , pp. 187-200
    • Xu, W.1    Edwards, M.R.2    Borek, D.M.3
  • 21
    • 77956511212 scopus 로고    scopus 로고
    • Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease
    • Park N, Skern T, Gustin KE. Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease. J Biol Chem. 2010;285:28796-28805.
    • (2010) J Biol Chem , vol.285 , pp. 28796-28805
    • Park, N.1    Skern, T.2    Gustin, K.E.3
  • 22
    • 38849138626 scopus 로고    scopus 로고
    • Differential targeting of nuclear pore complex proteins in poliovirus-infected cells
    • Park N, Katikaneni P, Skern T, Gustin KE. Differential targeting of nuclear pore complex proteins in poliovirus-infected cells. J Virol. 2008;82:1647-1655.
    • (2008) J Virol , vol.82 , pp. 1647-1655
    • Park, N.1    Katikaneni, P.2    Skern, T.3    Gustin, K.E.4
  • 23
    • 70350367733 scopus 로고    scopus 로고
    • RNA nuclear export is blocked by poliovirus 2A protease and is concomitant with nucleoporin cleavage
    • Castello A, Izquierdo JM, Welnowska E, Carrasco L. RNA nuclear export is blocked by poliovirus 2A protease and is concomitant with nucleoporin cleavage. J Cell Sci. 2009;122:3799-3809.
    • (2009) J Cell Sci , vol.122 , pp. 3799-3809
    • Castello, A.1    Izquierdo, J.M.2    Welnowska, E.3    Carrasco, L.4
  • 24
    • 84876335362 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus Nsp1beta inhibits interferon-activated JAK/STAT signal transduction by inducing karyopherin-alpha1 degradation
    • Wang R, Nan Y, Yu Y, Zhang YJ. Porcine reproductive and respiratory syndrome virus Nsp1beta inhibits interferon-activated JAK/STAT signal transduction by inducing karyopherin-alpha1 degradation. J Virol. 2013;87:5219-5228.
    • (2013) J Virol , vol.87 , pp. 5219-5228
    • Wang, R.1    Nan, Y.2    Yu, Y.3    Zhang, Y.J.4
  • 25
    • 35348845802 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane
    • Frieman M, Yount B, Heise M, Kopecky-Bromberg SA, Palese P, Baric RS. Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane. J Virol. 2007;81:9812-9824.
    • (2007) J Virol , vol.81 , pp. 9812-9824
    • Frieman, M.1    Yount, B.2    Heise, M.3    Kopecky-Bromberg, S.A.4    Palese, P.5    Baric, R.S.6
  • 26
    • 84991497424 scopus 로고    scopus 로고
    • The selective permeability barrier in the nuclear pore complex
    • Li C, Goryaynov A, Yang W. The selective permeability barrier in the nuclear pore complex. Nucleus. 2016;7:430-446.
    • (2016) Nucleus , vol.7 , pp. 430-446
    • Li, C.1    Goryaynov, A.2    Yang, W.3
  • 27
    • 84921797642 scopus 로고    scopus 로고
    • Components and regulation of nuclear transport processes
    • Cautain B, Hill R, de Pedro N, Link W. Components and regulation of nuclear transport processes. FEBS J. 2015;282:445-462.
    • (2015) FEBS J , vol.282 , pp. 445-462
    • Cautain, B.1    Hill, R.2    de Pedro, N.3    Link, W.4
  • 28
    • 84861384878 scopus 로고    scopus 로고
    • Functional architecture of the nuclear pore complex
    • Grossman E, Medalia O, Zwerger M. Functional architecture of the nuclear pore complex. Annu Rev Biophys. 2012;41:557-584.
    • (2012) Annu Rev Biophys , vol.41 , pp. 557-584
    • Grossman, E.1    Medalia, O.2    Zwerger, M.3
  • 29
    • 79959423595 scopus 로고    scopus 로고
    • The structure of the nuclear pore complex
    • Hoelz A, Debler EW, Blobel G. The structure of the nuclear pore complex. Annu Rev Biochem. 2011;80:613-643.
    • (2011) Annu Rev Biochem , vol.80 , pp. 613-643
    • Hoelz, A.1    Debler, E.W.2    Blobel, G.3
  • 30
    • 84902650683 scopus 로고    scopus 로고
    • Biological significance of the importin-beta family-dependent nucleocytoplasmic transport pathways
    • Kimura M, Imamoto N. Biological significance of the importin-beta family-dependent nucleocytoplasmic transport pathways. Traffic. 2014;15:727-748.
    • (2014) Traffic , vol.15 , pp. 727-748
    • Kimura, M.1    Imamoto, N.2
  • 31
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-beta bound to the IBB domain of importin-alpha
    • Cingolani G, Petosa C, Weis K, Muller CW. Structure of importin-beta bound to the IBB domain of importin-alpha. Nature. 1999;399:221-229.
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 32
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp
    • Chook YM, Blobel G. Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp. Nature. 1999;399:230-237.
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 33
    • 0033522118 scopus 로고    scopus 로고
    • Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport
    • Vetter IR, Nowak C, Nishimoto T, Kuhlmann J, Wittinghofer A. Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature. 1999;398:39-46.
    • (1999) Nature , vol.398 , pp. 39-46
    • Vetter, I.R.1    Nowak, C.2    Nishimoto, T.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 34
    • 0034616910 scopus 로고    scopus 로고
    • Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking
    • Bayliss R, Littlewood T, Stewart M. Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking. Cell. 2000;102:99-108.
    • (2000) Cell , vol.102 , pp. 99-108
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 35
    • 55849144420 scopus 로고    scopus 로고
    • Individual binding pockets of importin-beta for FG-nucleoporins have different binding properties and different sensitivities to RanGTP
    • Otsuka S, Iwasaka S, Yoneda Y, Takeyasu K, Yoshimura SH. Individual binding pockets of importin-beta for FG-nucleoporins have different binding properties and different sensitivities to RanGTP. Proc Natl Acad Sci USA. 2008;105:16101-16106.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 16101-16106
    • Otsuka, S.1    Iwasaka, S.2    Yoneda, Y.3    Takeyasu, K.4    Yoshimura, S.H.5
  • 36
    • 0028834428 scopus 로고
    • Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach M, Blobel G. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell. 1995;83:683-692.
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 37
    • 84879539109 scopus 로고    scopus 로고
    • Genome-wide RNAi screen reveals a new role of a WNT/CTNNB1 signaling pathway as negative regulator of virus-induced innate immune responses
    • Baril M, Es-Saad S, Chatel-Chaix L, et al. Genome-wide RNAi screen reveals a new role of a WNT/CTNNB1 signaling pathway as negative regulator of virus-induced innate immune responses. PLoS Pathog. 2013;9:e1003416.
    • (2013) PLoS Pathog , vol.9
    • Baril, M.1    Es-Saad, S.2    Chatel-Chaix, L.3
  • 38
    • 59749085907 scopus 로고    scopus 로고
    • MAVS dimer is a crucial signaling component of innate immunity and the target of hepatitis C virus NS3/4A protease
    • Baril M, Racine ME, Penin F, Lamarre D. MAVS dimer is a crucial signaling component of innate immunity and the target of hepatitis C virus NS3/4A protease. J Virol. 2009;83:1299-1311.
    • (2009) J Virol , vol.83 , pp. 1299-1311
    • Baril, M.1    Racine, M.E.2    Penin, F.3    Lamarre, D.4
  • 39
    • 14544280209 scopus 로고    scopus 로고
    • Immune evasion by hepatitis C virus NS3/4A protease-mediated cleavage of the Toll-like receptor 3 adaptor protein TRIF
    • Li K, Foy E, Ferreon JC, et al. Immune evasion by hepatitis C virus NS3/4A protease-mediated cleavage of the Toll-like receptor 3 adaptor protein TRIF. Proc Natl Acad Sci USA. 2005;102:2992-2997.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2992-2997
    • Li, K.1    Foy, E.2    Ferreon, J.C.3
  • 40
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E, Curran J, Hofmann K, et al. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature. 2005;437:1167-1172.
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3
  • 41
    • 0031893220 scopus 로고    scopus 로고
    • Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation
    • Lin R, Heylbroeck C, Pitha PM, Hiscott J. Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation. Mol Cell Biol. 1998;18:2986-2996.
    • (1998) Mol Cell Biol , vol.18 , pp. 2986-2996
    • Lin, R.1    Heylbroeck, C.2    Pitha, P.M.3    Hiscott, J.4
  • 42
    • 36749081534 scopus 로고    scopus 로고
    • Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport
    • Terry LJ, Shows EB, Wente SR. Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport. Science. 2007;318:1412-1416.
    • (2007) Science , vol.318 , pp. 1412-1416
    • Terry, L.J.1    Shows, E.B.2    Wente, S.R.3
  • 43
    • 18144426719 scopus 로고    scopus 로고
    • NF-(kappa)B is transported into the nucleus by importin {alpha}3 and importin {alpha}4
    • Fagerlund R, Kinnunen L, Kohler M, Julkunen I, Melen K. NF-{kappa}B is transported into the nucleus by importin {alpha}3 and importin {alpha}4. J Biol Chem. 2005;280:15942-15951.
    • (2005) J Biol Chem , vol.280 , pp. 15942-15951
    • Fagerlund, R.1    Kinnunen, L.2    Kohler, M.3    Julkunen, I.4    Melen, K.5
  • 44
    • 45449112571 scopus 로고    scopus 로고
    • NF-kappaB p52, RelB and c-Rel are transported into the nucleus via a subset of importin alpha molecules
    • Fagerlund R, Melen K, Cao X, Julkunen I. NF-kappaB p52, RelB and c-Rel are transported into the nucleus via a subset of importin alpha molecules. Cell Signal. 2008;20:1442-1451.
    • (2008) Cell Signal , vol.20 , pp. 1442-1451
    • Fagerlund, R.1    Melen, K.2    Cao, X.3    Julkunen, I.4
  • 45
    • 0034111332 scopus 로고    scopus 로고
    • Regulated nuclear-cytoplasmic localization of interferon regulatory factor 3, a subunit of double-stranded RNA-activated factor 1
    • Kumar KP, McBride KM, Weaver BK, Dingwall C, Reich NC. Regulated nuclear-cytoplasmic localization of interferon regulatory factor 3, a subunit of double-stranded RNA-activated factor 1. Mol Cell Biol. 2000;20:4159-4168.
    • (2000) Mol Cell Biol , vol.20 , pp. 4159-4168
    • Kumar, K.P.1    McBride, K.M.2    Weaver, B.K.3    Dingwall, C.4    Reich, N.C.5
  • 46
    • 84885383167 scopus 로고    scopus 로고
    • KPNB1, XPO7 and IPO8 mediate the translocation ofNF-kappaB/p65 into the nucleus
    • Liang P, Zhang H, Wang G, et al. KPNB1, XPO7 and IPO8 mediate the translocation ofNF-kappaB/p65 into the nucleus. Traffic. 2013;14:1132-1143.
    • (2013) Traffic , vol.14 , pp. 1132-1143
    • Liang, P.1    Zhang, H.2    Wang, G.3
  • 47
    • 84858120416 scopus 로고    scopus 로고
    • The nucleoporin-like protein NLP1 (hCG1) promotes CRM1-dependent nuclear protein export
    • Waldmann I, Spillner C, Kehlenbach RH. The nucleoporin-like protein NLP1 (hCG1) promotes CRM1-dependent nuclear protein export. J Cell Sci. 2012;125:144-154.
    • (2012) J Cell Sci , vol.125 , pp. 144-154
    • Waldmann, I.1    Spillner, C.2    Kehlenbach, R.H.3
  • 48
    • 0344201903 scopus 로고    scopus 로고
    • An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virus
    • Lamarre D, Anderson PC, Bailey M, et al. An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virus. Nature. 2003;426:186-189.
    • (2003) Nature , vol.426 , pp. 186-189
    • Lamarre, D.1    Anderson, P.C.2    Bailey, M.3
  • 49
    • 0030670639 scopus 로고    scopus 로고
    • Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1
    • Sekimoto T, Imamoto N, Nakajima K, Hirano T, Yoneda Y. Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1. EMBO J. 1997;16:7067-7077.
    • (1997) EMBO J , vol.16 , pp. 7067-7077
    • Sekimoto, T.1    Imamoto, N.2    Nakajima, K.3    Hirano, T.4    Yoneda, Y.5
  • 50
    • 29144462494 scopus 로고    scopus 로고
    • Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity
    • Li XD, Sun L, Seth RB, Pineda G, Chen ZJ. Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity. Proc Natl Acad Sci USA. 2005;102:17717-17722.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17717-17722
    • Li, X.D.1    Sun, L.2    Seth, R.B.3    Pineda, G.4    Chen, Z.J.5
  • 51
    • 84930943161 scopus 로고    scopus 로고
    • Rapid and highly efficient mammalian cell engineering via Cas9 protein transfection
    • Liang X, Potter J, Kumar S, et al. Rapid and highly efficient mammalian cell engineering via Cas9 protein transfection. J Biotechnol. 2015;208:44-53.
    • (2015) J Biotechnol , vol.208 , pp. 44-53
    • Liang, X.1    Potter, J.2    Kumar, S.3
  • 52
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherin beta 2
    • Lee BJ, Cansizoglu AE, Suel KE, Louis TH, Zhang Z, Chook YM. Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell. 2006;126:543-558.
    • (2006) Cell , vol.126 , pp. 543-558
    • Lee, B.J.1    Cansizoglu, A.E.2    Suel, K.E.3    Louis, T.H.4    Zhang, Z.5    Chook, Y.M.6
  • 53
    • 0034760338 scopus 로고    scopus 로고
    • RanBP3 influences interactions between CRM1 and its nuclear protein export substrates
    • Englmeier L, Fornerod M, Bischoff FR, Petosa C, Mattaj IW, Kutay U. RanBP3 influences interactions between CRM1 and its nuclear protein export substrates. EMBO Rep. 2001;2:926-932.
    • (2001) EMBO Rep , vol.2 , pp. 926-932
    • Englmeier, L.1    Fornerod, M.2    Bischoff, F.R.3    Petosa, C.4    Mattaj, I.W.5    Kutay, U.6
  • 54
    • 0035954439 scopus 로고    scopus 로고
    • Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export
    • Lindsay ME, Holaska JM, Welch K, Paschal BM, Macara IG. Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J Cell Biol. 2001;153:1391-1402.
    • (2001) J Cell Biol , vol.153 , pp. 1391-1402
    • Lindsay, M.E.1    Holaska, J.M.2    Welch, K.3    Paschal, B.M.4    Macara, I.G.5
  • 55
    • 0037192823 scopus 로고    scopus 로고
    • Signaling molecules of the NF-kappa B pathway shuttle constitutively between cytoplasm and nucleus
    • Birbach A, Gold P, Binder BR, Hofer E, de Martin R, Schmid JA. Signaling molecules of the NF-kappa B pathway shuttle constitutively between cytoplasm and nucleus. J Biol Chem. 2002;277:10842-10851.
    • (2002) J Biol Chem , vol.277 , pp. 10842-10851
    • Birbach, A.1    Gold, P.2    Binder, B.R.3    Hofer, E.4    de Martin, R.5    Schmid, J.A.6
  • 56
    • 0033998441 scopus 로고    scopus 로고
    • Cytoplasmic sequestration of rel proteins by IkappaBalpha requires CRM1-dependent nuclear export
    • Tam WF, Lee LH, Davis L, Sen R. Cytoplasmic sequestration of rel proteins by IkappaBalpha requires CRM1-dependent nuclear export. Mol Cell Biol. 2000;20:2269-2284.
    • (2000) Mol Cell Biol , vol.20 , pp. 2269-2284
    • Tam, W.F.1    Lee, L.H.2    Davis, L.3    Sen, R.4
  • 57
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook A, Bono F, Jinek M, Conti E. Structural biology of nucleocytoplasmic transport. Annu Rev Biochem. 2007;76:647-671.
    • (2007) Annu Rev Biochem , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 58
    • 84890101190 scopus 로고    scopus 로고
    • Integrated structural analysis of the human nuclear pore complex scaffold
    • Bui KH, von Appen A, DiGuilio AL, et al. Integrated structural analysis of the human nuclear pore complex scaffold. Cell. 2013;155:1233-1243.
    • (2013) Cell , vol.155 , pp. 1233-1243
    • Bui, K.H.1    von Appen, A.2    DiGuilio, A.L.3
  • 59
    • 49049098057 scopus 로고    scopus 로고
    • Tumor marker nucleoporin 88 kDa regulates nucleocytoplasmic transport of NF-kappaB
    • Takahashi N, van Kilsdonk JW, Ostendorf B, et al. Tumor marker nucleoporin 88 kDa regulates nucleocytoplasmic transport of NF-kappaB. Biochem Biophys Res Commun. 2008;374:424-430.
    • (2008) Biochem Biophys Res Commun , vol.374 , pp. 424-430
    • Takahashi, N.1    van Kilsdonk, J.W.2    Ostendorf, B.3
  • 60
    • 0342276108 scopus 로고    scopus 로고
    • Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor
    • Kutay U, Bischoff FR, Kostka S, Kraft R, Gorlich D. Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor. Cell. 1997;90:1061-1071.
    • (1997) Cell , vol.90 , pp. 1061-1071
    • Kutay, U.1    Bischoff, F.R.2    Kostka, S.3    Kraft, R.4    Gorlich, D.5
  • 61
    • 84897508835 scopus 로고    scopus 로고
    • 3Cpro of foot-and-mouth disease virus antagonizes the interferon signaling pathway by blocking STAT1/STAT2 nuclear translocation
    • Du Y, Bi J, Liu J, et al. 3Cpro of foot-and-mouth disease virus antagonizes the interferon signaling pathway by blocking STAT1/STAT2 nuclear translocation. J Virol. 2014;88:4908-4920.
    • (2014) J Virol , vol.88 , pp. 4908-4920
    • Du, Y.1    Bi, J.2    Liu, J.3
  • 62
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da W, Sherman BT, Lempicki RA. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc. 2009;4:44-57.
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 63
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
    • Huang da W, Sherman BT, Lempicki RA. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 2009;37:1-13.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1-13
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.