메뉴 건너뛰기




Volumn 7, Issue 9, 2011, Pages

Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting

Author keywords

[No Author keywords available]

Indexed keywords

EXPORTIN 1; GUANINE NUCLEOTIDE EXCHANGE FACTOR; LEPTOMYCIN B; PROTEIN; RCC1 PROTEIN; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG; CELL RECEPTOR; EXPORTIN 1 PROTEIN; KARYOPHERIN; NUCLEAR PROTEIN; RAN PROTEIN; UNSATURATED FATTY ACID; VIRUS RNA;

EID: 80053436121     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002187     Document Type: Article
Times cited : (58)

References (49)
  • 1
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import
    • Martin K, Helenius A, (1991) Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import. Cell 67: 117-130.
    • (1991) Cell , vol.67 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 2
    • 0030731422 scopus 로고    scopus 로고
    • Nuclear import and export of influenza virus nucleoprotein
    • Neumann G, Castrucci MR, Kawaoka Y, (1997) Nuclear import and export of influenza virus nucleoprotein. J Virol 71: 9690-9700.
    • (1997) J Virol , vol.71 , pp. 9690-9700
    • Neumann, G.1    Castrucci, M.R.2    Kawaoka, Y.3
  • 3
    • 0032472328 scopus 로고    scopus 로고
    • The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins
    • O'Neill RE, Talon J, Palese P, (1998) The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. EMBO J 17: 288-296.
    • (1998) EMBO J , vol.17 , pp. 288-296
    • O'Neill, R.E.1    Talon, J.2    Palese, P.3
  • 4
    • 0033946767 scopus 로고    scopus 로고
    • Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins
    • Bui M, Wills EG, Helenius A, Whittaker GR, (2000) Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins. J Virol 74: 1781-1786.
    • (2000) J Virol , vol.74 , pp. 1781-1786
    • Bui, M.1    Wills, E.G.2    Helenius, A.3    Whittaker, G.R.4
  • 5
    • 0034749515 scopus 로고    scopus 로고
    • Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway
    • Elton D, Simpson-Holley M, Archer K, Medcalf L, Hallam R, et al. (2001) Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway. J Virol 75: 408-419.
    • (2001) J Virol , vol.75 , pp. 408-419
    • Elton, D.1    Simpson-Holley, M.2    Archer, K.3    Medcalf, L.4    Hallam, R.5
  • 6
    • 0034929835 scopus 로고    scopus 로고
    • Inhibition of nuclear export of ribonucleoprotein complexes of influenza virus by leptomycin B
    • Watanabe K, Takizawa N, Katoh M, Hoshida K, Kobayashi N, et al. (2001) Inhibition of nuclear export of ribonucleoprotein complexes of influenza virus by leptomycin B. Virus Res 77: 31-42.
    • (2001) Virus Res , vol.77 , pp. 31-42
    • Watanabe, K.1    Takizawa, N.2    Katoh, M.3    Hoshida, K.4    Kobayashi, N.5
  • 7
    • 0033529866 scopus 로고    scopus 로고
    • Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region
    • Kudo N, Matsumori N, Taoka H, Fujiwara D, Schreiner EP, et al. (1999) Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region. Proc Natl Acad Sci U S A 96: 9112-9117.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 9112-9117
    • Kudo, N.1    Matsumori, N.2    Taoka, H.3    Fujiwara, D.4    Schreiner, E.P.5
  • 8
    • 0037139590 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic localization of influenza virus nucleoprotein depends on cell density and phosphorylation
    • Bui M, Myers JE, Whittaker GR, (2002) Nucleo-cytoplasmic localization of influenza virus nucleoprotein depends on cell density and phosphorylation. Virus Res 84: 37-44.
    • (2002) Virus Res , vol.84 , pp. 37-44
    • Bui, M.1    Myers, J.E.2    Whittaker, G.R.3
  • 9
    • 0141737104 scopus 로고    scopus 로고
    • Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)
    • Akarsu H, Burmeister WP, Petosa C, Petit I, Muller CW, et al. (2003) Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2). EMBO J 22: 4646-4655.
    • (2003) EMBO J , vol.22 , pp. 4646-4655
    • Akarsu, H.1    Burmeister, W.P.2    Petosa, C.3    Petit, I.4    Muller, C.W.5
  • 10
    • 9744248734 scopus 로고    scopus 로고
    • Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex
    • Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, et al. (2004) Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex. Mol Cell 16: 761-775.
    • (2004) Mol Cell , vol.16 , pp. 761-775
    • Petosa, C.1    Schoehn, G.2    Askjaer, P.3    Bauer, U.4    Moulin, M.5
  • 11
    • 0035947299 scopus 로고    scopus 로고
    • Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B
    • Nemergut ME, Mizzen CA, Stukenberg T, Allis CD, Macara IG, (2001) Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B. Science 292: 1540-1543.
    • (2001) Science , vol.292 , pp. 1540-1543
    • Nemergut, M.E.1    Mizzen, C.A.2    Stukenberg, T.3    Allis, C.D.4    Macara, I.G.5
  • 12
    • 0037124071 scopus 로고    scopus 로고
    • Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor
    • Nemergut ME, Lindsay ME, Brownawell AM, Macara IG, (2002) Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor. J Biol Chem 277: 17385-17388.
    • (2002) J Biol Chem , vol.277 , pp. 17385-17388
    • Nemergut, M.E.1    Lindsay, M.E.2    Brownawell, A.M.3    Macara, I.G.4
  • 13
    • 14744301997 scopus 로고    scopus 로고
    • Leucine-rich nuclear-export signals: born to be weak
    • Kutay U, Guttinger S, (2005) Leucine-rich nuclear-export signals: born to be weak. Trends Cell Biol 15: 121-124.
    • (2005) Trends Cell Biol , vol.15 , pp. 121-124
    • Kutay, U.1    Guttinger, S.2
  • 14
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton LF, Paschal BM, (2005) Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 6: 187-198.
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 15
    • 59749097063 scopus 로고    scopus 로고
    • Avian Influenza A virus polymerase association with nucleoprotein, but not polymerase assembly, is impaired in human cells during the course of infection
    • Rameix-Welti MA, Tomoiu A, Dos Santos Afonso E, van der Werf S, Naffakh N, (2009) Avian Influenza A virus polymerase association with nucleoprotein, but not polymerase assembly, is impaired in human cells during the course of infection. J Virol 83: 1320-1331.
    • (2009) J Virol , vol.83 , pp. 1320-1331
    • Rameix-Welti, M.A.1    Tomoiu, A.2    Dos Santos Afonso, E.3    van der Werf, S.4    Naffakh, N.5
  • 16
    • 70350125974 scopus 로고    scopus 로고
    • Nuclear dynamics of influenza A virus ribonucleoproteins revealed by live-cell imaging studies
    • Loucaides EM, von Kirchbach JC, Foeglein A, Sharps J, Fodor E, et al. (2009) Nuclear dynamics of influenza A virus ribonucleoproteins revealed by live-cell imaging studies. Virology 394: 154-163.
    • (2009) Virology , vol.394 , pp. 154-163
    • Loucaides, E.M.1    von Kirchbach, J.C.2    Foeglein, A.3    Sharps, J.4    Fodor, E.5
  • 17
    • 17444430403 scopus 로고    scopus 로고
    • Association of the influenza A virus RNA-dependent RNA polymerase with cellular RNA polymerase II
    • Engelhardt OG, Smith M, Fodor E, (2005) Association of the influenza A virus RNA-dependent RNA polymerase with cellular RNA polymerase II. J Virol 79: 5812-5818.
    • (2005) J Virol , vol.79 , pp. 5812-5818
    • Engelhardt, O.G.1    Smith, M.2    Fodor, E.3
  • 18
    • 33646057735 scopus 로고    scopus 로고
    • Association of functional influenza viral proteins and RNAs with nuclear chromatin and sub-chromatin structure
    • Takizawa N, Watanabe K, Nouno K, Kobayashi N, Nagata K, (2006) Association of functional influenza viral proteins and RNAs with nuclear chromatin and sub-chromatin structure. Microbes Infect 8: 823-833.
    • (2006) Microbes Infect , vol.8 , pp. 823-833
    • Takizawa, N.1    Watanabe, K.2    Nouno, K.3    Kobayashi, N.4    Nagata, K.5
  • 20
    • 61849170193 scopus 로고    scopus 로고
    • Genome-wide profiling of salt fractions maps physical properties of chromatin
    • Henikoff S, Henikoff JG, Sakai A, Loeb GB, Ahmad K, (2009) Genome-wide profiling of salt fractions maps physical properties of chromatin. Genome Res 19: 460-469.
    • (2009) Genome Res , vol.19 , pp. 460-469
    • Henikoff, S.1    Henikoff, J.G.2    Sakai, A.3    Loeb, G.B.4    Ahmad, K.5
  • 21
    • 0021250601 scopus 로고
    • Differential salt fractionation of active and inactive genomic domains in chicken erythrocyte
    • Rocha E, Davie JR, van Holde KE, Weintraub H, (1984) Differential salt fractionation of active and inactive genomic domains in chicken erythrocyte. J Biol Chem 259: 8558-8563.
    • (1984) J Biol Chem , vol.259 , pp. 8558-8563
    • Rocha, E.1    Davie, J.R.2    van Holde, K.E.3    Weintraub, H.4
  • 22
    • 70649087924 scopus 로고    scopus 로고
    • Mechanisms and functional implications of the degradation of host RNA polymerase II in influenza virus infected cells
    • Vreede FT, Chan AY, Sharps J, Fodor E, (2010) Mechanisms and functional implications of the degradation of host RNA polymerase II in influenza virus infected cells. Virology 396: 125-134.
    • (2010) Virology , vol.396 , pp. 125-134
    • Vreede, F.T.1    Chan, A.Y.2    Sharps, J.3    Fodor, E.4
  • 23
    • 34248397190 scopus 로고    scopus 로고
    • Influenza virus infection causes specific degradation of the largest subunit of cellular RNA polymerase II
    • Rodriguez A, Perez-Gonzalez A, Nieto A, (2007) Influenza virus infection causes specific degradation of the largest subunit of cellular RNA polymerase II. J Virol 81: 5315-5324.
    • (2007) J Virol , vol.81 , pp. 5315-5324
    • Rodriguez, A.1    Perez-Gonzalez, A.2    Nieto, A.3
  • 24
    • 25144479801 scopus 로고    scopus 로고
    • The generation of recombinant influenza A viruses expressing a PB2 fusion protein requires the conservation of a packaging signal overlapping the coding and noncoding regions at the 5′ end of the PB2 segment
    • Dos Santos Afonso E, Escriou N, Leclercq I, van der Werf S, Naffakh N, (2005) The generation of recombinant influenza A viruses expressing a PB2 fusion protein requires the conservation of a packaging signal overlapping the coding and noncoding regions at the 5′ end of the PB2 segment. Virology 341: 34-46.
    • (2005) Virology , vol.341 , pp. 34-46
    • Dos Santos Afonso, E.1    Escriou, N.2    Leclercq, I.3    van der Werf, S.4    Naffakh, N.5
  • 25
    • 77953107225 scopus 로고    scopus 로고
    • Dynamics of single mRNP nucleocytoplasmic transport and export through the nuclear pore in living cells
    • Mor A, Suliman S, Ben-Yishay R, Yunger S, Brody Y, et al. (2010) Dynamics of single mRNP nucleocytoplasmic transport and export through the nuclear pore in living cells. Nat Cell Biol 12: 543-552.
    • (2010) Nat Cell Biol , vol.12 , pp. 543-552
    • Mor, A.1    Suliman, S.2    Ben-Yishay, R.3    Yunger, S.4    Brody, Y.5
  • 26
    • 0014348152 scopus 로고
    • The role of lysine-rich histone in the maintenance of chromatin structure in metaphase chromosomes
    • Mirsky AE, Burdick CJ, Davidson EH, Littau VC, (1968) The role of lysine-rich histone in the maintenance of chromatin structure in metaphase chromosomes. Proc Natl Acad Sci U S A 61: 592-597.
    • (1968) Proc Natl Acad Sci U S A , vol.61 , pp. 592-597
    • Mirsky, A.E.1    Burdick, C.J.2    Davidson, E.H.3    Littau, V.C.4
  • 27
    • 0035836373 scopus 로고    scopus 로고
    • Nuclear export of influenza virus ribonucleoproteins: identification of an export intermediate at the nuclear periphery
    • Ma K, Roy AM, Whittaker GR, (2001) Nuclear export of influenza virus ribonucleoproteins: identification of an export intermediate at the nuclear periphery. Virology 282: 215-220.
    • (2001) Virology , vol.282 , pp. 215-220
    • Ma, K.1    Roy, A.M.2    Whittaker, G.R.3
  • 28
    • 25444530020 scopus 로고    scopus 로고
    • Genome gating'; polarized intranuclear trafficking of influenza virus RNPs
    • Elton D, Amorim MJ, Medcalf L, Digard P, (2005) 'Genome gating'; polarized intranuclear trafficking of influenza virus RNPs. Biol Lett 1: 113-117.
    • (2005) Biol Lett , vol.1 , pp. 113-117
    • Elton, D.1    Amorim, M.J.2    Medcalf, L.3    Digard, P.4
  • 29
    • 0026537584 scopus 로고
    • A normally masked nuclear matrix antigen that appears at mitosis on cytoskeleton filaments adjoining chromosomes, centrioles, and midbodies
    • Nickerson JA, Krockmalnic G, Wan KM, Turner CD, Penman S, (1992) A normally masked nuclear matrix antigen that appears at mitosis on cytoskeleton filaments adjoining chromosomes, centrioles, and midbodies. J Cell Biol 116: 977-987.
    • (1992) J Cell Biol , vol.116 , pp. 977-987
    • Nickerson, J.A.1    Krockmalnic, G.2    Wan, K.M.3    Turner, C.D.4    Penman, S.5
  • 30
    • 4444372435 scopus 로고    scopus 로고
    • Generation of influenza A virus NS2 (NEP) mutants with an altered nuclear export signal sequence
    • Iwatsuki-Horimoto K, Horimoto T, Fujii Y, Kawaoka Y, (2004) Generation of influenza A virus NS2 (NEP) mutants with an altered nuclear export signal sequence. J Virol 78: 10149-10155.
    • (2004) J Virol , vol.78 , pp. 10149-10155
    • Iwatsuki-Horimoto, K.1    Horimoto, T.2    Fujii, Y.3    Kawaoka, Y.4
  • 31
    • 0347003598 scopus 로고    scopus 로고
    • Heat shock protein 70 is related to thermal inhibition of nuclear export of the influenza virus ribonucleoprotein complex
    • Hirayama E, Atagi H, Hiraki A, Kim J, (2004) Heat shock protein 70 is related to thermal inhibition of nuclear export of the influenza virus ribonucleoprotein complex. J Virol 78: 1263-1270.
    • (2004) J Virol , vol.78 , pp. 1263-1270
    • Hirayama, E.1    Atagi, H.2    Hiraki, A.3    Kim, J.4
  • 32
    • 34447324079 scopus 로고    scopus 로고
    • Nuclear localization of enhanced green fluorescent protein homomultimers
    • Seibel NM, Eljouni J, Nalaskowski MM, Hampe W, (2007) Nuclear localization of enhanced green fluorescent protein homomultimers. Anal Biochem 368: 95-99.
    • (2007) Anal Biochem , vol.368 , pp. 95-99
    • Seibel, N.M.1    Eljouni, J.2    Nalaskowski, M.M.3    Hampe, W.4
  • 33
    • 33751524902 scopus 로고    scopus 로고
    • The nucleoporin Nup214 sequesters CRM1 at the nuclear rim and modulates NFkappaB activation in Drosophila
    • Xylourgidis N, Roth P, Sabri N, Tsarouhas V, Samakovlis C, (2006) The nucleoporin Nup214 sequesters CRM1 at the nuclear rim and modulates NFkappaB activation in Drosophila. J Cell Sci 119: 4409-4419.
    • (2006) J Cell Sci , vol.119 , pp. 4409-4419
    • Xylourgidis, N.1    Roth, P.2    Sabri, N.3    Tsarouhas, V.4    Samakovlis, C.5
  • 34
    • 0025365997 scopus 로고
    • The synthesis of influenza virus negative-strand RNA takes place in insoluble complexes present in the nuclear matrix fraction
    • Lopez-Turiso JA, Martinez C, Tanaka T, Ortin J, (1990) The synthesis of influenza virus negative-strand RNA takes place in insoluble complexes present in the nuclear matrix fraction. Virus Res 16: 325-337.
    • (1990) Virus Res , vol.16 , pp. 325-337
    • Lopez-Turiso, J.A.1    Martinez, C.2    Tanaka, T.3    Ortin, J.4
  • 35
    • 67649227447 scopus 로고    scopus 로고
    • NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome
    • Robb NC, Smith M, Vreede FT, Fodor E, (2009) NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome. J Gen Virol 90: 1398-1407.
    • (2009) J Gen Virol , vol.90 , pp. 1398-1407
    • Robb, N.C.1    Smith, M.2    Vreede, F.T.3    Fodor, E.4
  • 36
    • 77954912141 scopus 로고    scopus 로고
    • Influenza A virus-generated small RNAs regulate the switch from transcription to replication
    • Perez JT, Varble A, Sachidanandam R, Zlatev I, Manoharan M, et al. (2010) Influenza A virus-generated small RNAs regulate the switch from transcription to replication. Proc Natl Acad Sci U S A 107: 11525-11530.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 11525-11530
    • Perez, J.T.1    Varble, A.2    Sachidanandam, R.3    Zlatev, I.4    Manoharan, M.5
  • 37
    • 11844272621 scopus 로고    scopus 로고
    • Kinetic and molecular analysis of nuclear export factor CRM1 association with its cargo in vivo
    • Daelemans D, Costes SV, Lockett S, Pavlakis GN, (2005) Kinetic and molecular analysis of nuclear export factor CRM1 association with its cargo in vivo. Mol Cell Biol 25: 728-739.
    • (2005) Mol Cell Biol , vol.25 , pp. 728-739
    • Daelemans, D.1    Costes, S.V.2    Lockett, S.3    Pavlakis, G.N.4
  • 38
    • 70449448939 scopus 로고    scopus 로고
    • Dynamic localisation of Ran GTPase during the cell cycle
    • Hutchins JR, Moore WJ, Clarke PR, (2009) Dynamic localisation of Ran GTPase during the cell cycle. BMC Cell Biol 10: 66.
    • (2009) BMC Cell Biol , vol.10 , pp. 66
    • Hutchins, J.R.1    Moore, W.J.2    Clarke, P.R.3
  • 40
    • 0347990552 scopus 로고    scopus 로고
    • The dynamic association of RCC1 with chromatin is modulated by Ran-dependent nuclear transport
    • Cushman I, Stenoien D, Moore MS, (2004) The dynamic association of RCC1 with chromatin is modulated by Ran-dependent nuclear transport. Mol Biol Cell 15: 245-255.
    • (2004) Mol Biol Cell , vol.15 , pp. 245-255
    • Cushman, I.1    Stenoien, D.2    Moore, M.S.3
  • 41
    • 0030825146 scopus 로고    scopus 로고
    • Histones as a target for influenza virus matrix protein M1
    • Zhirnov OP, Klenk HD, (1997) Histones as a target for influenza virus matrix protein M1. Virology 235: 302-310.
    • (1997) Virology , vol.235 , pp. 302-310
    • Zhirnov, O.P.1    Klenk, H.D.2
  • 42
    • 34547947215 scopus 로고    scopus 로고
    • Distinct functions of the Drosophila Nup153 and Nup214 FG domains in nuclear protein transport
    • Sabri N, Roth P, Xylourgidis N, Sadeghifar F, Adler J, et al. (2007) Distinct functions of the Drosophila Nup153 and Nup214 FG domains in nuclear protein transport. J Cell Biol 178: 557-565.
    • (2007) J Cell Biol , vol.178 , pp. 557-565
    • Sabri, N.1    Roth, P.2    Xylourgidis, N.3    Sadeghifar, F.4    Adler, J.5
  • 43
    • 0035902446 scopus 로고    scopus 로고
    • Multiple vesiculoviral matrix proteins inhibit both nuclear export and import
    • Petersen JM, Her LS, Dahlberg JE, (2001) Multiple vesiculoviral matrix proteins inhibit both nuclear export and import. Proc Natl Acad Sci U S A 98: 8590-8595.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 8590-8595
    • Petersen, J.M.1    Her, L.S.2    Dahlberg, J.E.3
  • 45
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler G, Milstein C, (1975) Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256: 495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 46
    • 70449571952 scopus 로고    scopus 로고
    • Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication
    • Wunderlich K, Mayer D, Ranadheera C, Holler AS, Manz B, et al. (2009) Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication. PLoS One 4: e7517.
    • (2009) PLoS One , vol.4
    • Wunderlich, K.1    Mayer, D.2    Ranadheera, C.3    Holler, A.S.4    Manz, B.5
  • 47
    • 33847421368 scopus 로고    scopus 로고
    • Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches
    • Mayer D, Molawi K, Martinez-Sobrido L, Ghanem A, Thomas S, et al. (2007) Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches. J Proteome Res 6: 672-682.
    • (2007) J Proteome Res , vol.6 , pp. 672-682
    • Mayer, D.1    Molawi, K.2    Martinez-Sobrido, L.3    Ghanem, A.4    Thomas, S.5
  • 49
    • 77954590750 scopus 로고    scopus 로고
    • The anti-inflammatory prostaglandin 15-deoxy-delta(12,14)-PGJ2 inhibits CRM1-dependent nuclear protein export
    • Hilliard M, Frohnert C, Spillner C, Marcone S, Nath A, et al. (2010) The anti-inflammatory prostaglandin 15-deoxy-delta(12,14)-PGJ2 inhibits CRM1-dependent nuclear protein export. J Biol Chem 285: 22202-22210.
    • (2010) J Biol Chem , vol.285 , pp. 22202-22210
    • Hilliard, M.1    Frohnert, C.2    Spillner, C.3    Marcone, S.4    Nath, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.