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Journal of Virology
Volumn 89, Issue 14, 2015, Pages 7064-7078
Heterogeneous nuclear ribonucleoprotein M facilitates enterovirus infection
Author keywords

[No Author keywords available]
Indexed keywords

HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN M; MESSENGER RNA; SMALL INTERFERING RNA; VIRUS RNA; 3C PROTEASES; CYSTEINE PROTEINASE; VIRUS PROTEIN;
EID: 84931077175     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02977-14     Document Type: Article
Times cited : (47)
References (72)
  • 1
    • 84859366447 scopus 로고    scopus 로고
    • Protease signaling: the cutting edge
    • Turk B, Turk D, Turk V. 2012. Protease signaling: the cutting edge. EMBO J 31:1630-1643. http://dx.doi.org/10.1038/emboj.2012.42.
    • (2012) EMBO J , vol.31 , pp. 1630-1643
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 3
    • 84902682736 scopus 로고    scopus 로고
    • Differential restriction patterns of mRNA decay factor AUF1 during picornavirus infections
    • Cathcart AL, Semler BL. 2014. Differential restriction patterns of mRNA decay factor AUF1 during picornavirus infections. J Gen Virol 95:1488-1492. http://dx.doi.org/10.1099/vir.0.064501-0.
    • (2014) J Gen Virol , vol.95 , pp. 1488-1492
    • Cathcart, A.L.1    Semler, B.L.2
  • 4
    • 84894521803 scopus 로고    scopus 로고
    • Inhibition of poliovirus-induced cleavage of cellular protein PCBP2 reduces the levels of viral RNA replication
    • Chase AJ, Daijogo S, Semler BL. 2014. Inhibition of poliovirus-induced cleavage of cellular protein PCBP2 reduces the levels of viral RNA replication. J Virol 88:3192-3201. http://dx.doi.org/10.1128/JVI.02503-13.
    • (2014) J Virol , vol.88 , pp. 3192-3201
    • Chase, A.J.1    Daijogo, S.2    Semler, B.L.3
  • 5
    • 54449095457 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonuclear protein K interacts with the enterovirus 71 5' untranslated region and participates in virus replication
    • Lin JY, Li ML, Huang PN, Chien KY, Horng JT, Shih SR. 2008. Heterogeneous nuclear ribonuclear protein K interacts with the enterovirus 71 5' untranslated region and participates in virus replication. J Gen Virol 89:2540-2549. http://dx.doi.org/10.1099/vir.0.2008/003673-0.
    • (2008) J Gen Virol , vol.89 , pp. 2540-2549
    • Lin, J.Y.1    Li, M.L.2    Huang, P.N.3    Chien, K.Y.4    Horng, J.T.5    Shih, S.R.6
  • 6
    • 66149116780 scopus 로고    scopus 로고
    • hnRNP A1 interacts with the 5' untranslated regions of enterovirus 71 and Sindbis virus RNA and is required for viral replication
    • Lin JY, Shih SR, Pan M, Li C, Lue CF, Stollar V, Li ML. 2009. hnRNP A1 interacts with the 5' untranslated regions of enterovirus 71 and Sindbis virus RNA and is required for viral replication. J Virol 83:6106-6114. http://dx.doi.org/10.1128/JVI.02476-08.
    • (2009) J Virol , vol.83 , pp. 6106-6114
    • Lin, J.Y.1    Shih, S.R.2    Pan, M.3    Li, C.4    Lue, C.F.5    Stollar, V.6    Li, M.L.7
  • 7
    • 34548179796 scopus 로고    scopus 로고
    • Cellular protein modification by poliovirus: the two faces of poly(rC)-binding protein
    • Perera R, Daijogo S, Walter BL, Nguyen JH, Semler BL. 2007. Cellular protein modification by poliovirus: the two faces of poly(rC)-binding protein. J Virol 81:8919-8932. http://dx.doi.org/10.1128/JVI.01013-07.
    • (2007) J Virol , vol.81 , pp. 8919-8932
    • Perera, R.1    Daijogo, S.2    Walter, B.L.3    Nguyen, J.H.4    Semler, B.L.5
  • 9
    • 84879680033 scopus 로고    scopus 로고
    • Cytoplasmic redistribution and cleavage of AUF1 during coxsackievirus infection enhance the stability of its viral genome
    • Wong J, Si X, Angeles A, Zhang J, Shi J, Fung G, Jagdeo J, Wang T, Zhong Z, Jan E, Luo H. 2013. Cytoplasmic redistribution and cleavage of AUF1 during coxsackievirus infection enhance the stability of its viral genome. FASEB J 27:2777-2787. http://dx.doi.org/10.1096/fj.12-226498.
    • (2013) FASEB J , vol.27 , pp. 2777-2787
    • Wong, J.1    Si, X.2    Angeles, A.3    Zhang, J.4    Shi, J.5    Fung, G.6    Jagdeo, J.7    Wang, T.8    Zhong, Z.9    Jan, E.10    Luo, H.11
  • 10
    • 0032889314 scopus 로고    scopus 로고
    • Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro
    • Joachims M, Van Breugel PC, Lloyd RE. 1999. Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro. J Virol 73:718-727.
    • (1999) J Virol , vol.73 , pp. 718-727
    • Joachims, M.1    Van Breugel, P.C.2    Lloyd, R.E.3
  • 11
    • 0036171240 scopus 로고    scopus 로고
    • Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease
    • Kuyumcu-Martinez NM, Joachims M, Lloyd RE. 2002. Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease. J Virol 76:2062-2074. http://dx.doi.org/10.1128/jvi.76.5.2062-2074.2002.
    • (2002) J Virol , vol.76 , pp. 2062-2074
    • Kuyumcu-Martinez, N.M.1    Joachims, M.2    Lloyd, R.E.3
  • 12
    • 0020356106 scopus 로고
    • Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex
    • Etchison D, Milburn SC, Edery I, Sonenberg N, Hershey JW. 1982. Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex. J Biol Chem 257:14806-14810.
    • (1982) J Biol Chem , vol.257 , pp. 14806-14810
    • Etchison, D.1    Milburn, S.C.2    Edery, I.3    Sonenberg, N.4    Hershey, J.W.5
  • 13
    • 0027182923 scopus 로고
    • Mapping the cleavage site in protein synthesis initiation factor eIF-4γ of the 2A proteases from human coxsackievirus and rhinovirus
    • Lamphear BJ, Yan R, Yang F, Waters D, Liebig HD, Klump H, Kuechler E, Skern T, Rhoads RE. 1993. Mapping the cleavage site in protein synthesis initiation factor eIF-4γ of the 2A proteases from human coxsackievirus and rhinovirus. J Biol Chem 268:19200-19203.
    • (1993) J Biol Chem , vol.268 , pp. 19200-19203
    • Lamphear, B.J.1    Yan, R.2    Yang, F.3    Waters, D.4    Liebig, H.D.5    Klump, H.6    Kuechler, E.7    Skern, T.8    Rhoads, R.E.9
  • 14
    • 0032889326 scopus 로고    scopus 로고
    • Cleavage of Poly(A)-binding protein by coxsackievirus 2A protease in vitro and in vivo: another mechanism for host protein synthesis shutoff?
    • Kerekatte V, Keiper BD, Badorff C, Cai A, Knowlton KU, Rhoads RE. 1999. Cleavage of Poly(A)-binding protein by coxsackievirus 2A protease in vitro and in vivo: another mechanism for host protein synthesis shutoff? J Virol 73:709-717.
    • (1999) J Virol , vol.73 , pp. 709-717
    • Kerekatte, V.1    Keiper, B.D.2    Badorff, C.3    Cai, A.4    Knowlton, K.U.5    Rhoads, R.E.6
  • 15
    • 0015192576 scopus 로고
    • The synthesis of protein by mammalian RNA viruses. In: strategy of the viral genome
    • Baltimore D, Huang A, Manly KF, Rekosh D, Stampfer M. 1971. The synthesis of protein by mammalian RNA viruses. In: strategy of the viral genome. Ciba Found Symp 1971:101-110.
    • (1971) Ciba Found Symp , vol.1971 , pp. 101-110
    • Baltimore, D.1    Huang, A.2    Manly, K.F.3    Rekosh, D.4    Stampfer, M.5
  • 16
    • 0014331325 scopus 로고
    • Polypeptide cleavages in the formation of poliovirus proteins
    • Jacobson MF, Baltimore D. 1968. Polypeptide cleavages in the formation of poliovirus proteins. Proc Natl Acad Sci USA 61:77-84. http://dx.doi.org/10.1073/pnas.61.1.77.
    • (1968) Proc Natl Acad Sci USA , vol.61 , pp. 77-84
    • Jacobson, M.F.1    Baltimore, D.2
  • 17
    • 0023720048 scopus 로고
    • Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA
    • Pelletier J, Sonenberg N. 1988. Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA. Nature 334:320-325. http://dx.doi.org/10.1038/334320a0.
    • (1988) Nature , vol.334 , pp. 320-325
    • Pelletier, J.1    Sonenberg, N.2
  • 18
    • 0023758546 scopus 로고
    • A segment of the 5' nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation
    • Jang SK, Krausslich HG, Nicklin MJ, Duke GM, Palmenberg AC, Wimmer E. 1988. A segment of the 5' nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation. J Virol 62:2636-2643.
    • (1988) J Virol , vol.62 , pp. 2636-2643
    • Jang, S.K.1    Krausslich, H.G.2    Nicklin, M.J.3    Duke, G.M.4    Palmenberg, A.C.5    Wimmer, E.6
  • 20
    • 0023043280 scopus 로고
    • A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein
    • Toyoda H, Nicklin MJ, Murray MG, Anderson CW, Dunn JJ, Studier FW, Wimmer E. 1986. A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein. Cell 45:761-770. http://dx.doi.org/10.1016/0092-8674(86)90790-7.
    • (1986) Cell , vol.45 , pp. 761-770
    • Toyoda, H.1    Nicklin, M.J.2    Murray, M.G.3    Anderson, C.W.4    Dunn, J.J.5    Studier, F.W.6    Wimmer, E.7
  • 21
    • 0023213565 scopus 로고
    • Poliovirus polypeptide precursors: expression in vitro and processing by exogenous 3C and 2A proteinases
    • Nicklin MJ, Krausslich HG, Toyoda H, Dunn JJ, Wimmer E. 1987. Poliovirus polypeptide precursors: expression in vitro and processing by exogenous 3C and 2A proteinases. Proc Natl Acad Sci USA 84:4002-4006. http://dx.doi.org/10.1073/pnas.84.12.4002.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4002-4006
    • Nicklin, M.J.1    Krausslich, H.G.2    Toyoda, H.3    Dunn, J.J.4    Wimmer, E.5
  • 22
    • 0019971712 scopus 로고
    • Proteolytic processing of poliovirus polypeptides: antibodies to polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs
    • Hanecak R, Semler BL, Anderson CW, Wimmer E. 1982. Proteolytic processing of poliovirus polypeptides: antibodies to polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs. Proc Natl Acad Sci USA 79:3973-3977. http://dx.doi.org/10.1073/pnas.79.13.3973.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 3973-3977
    • Hanecak, R.1    Semler, B.L.2    Anderson, C.W.3    Wimmer, E.4
  • 23
    • 0026729556 scopus 로고
    • Determinants of substrate recognition by poliovirus 2A proteinase
    • Hellen CU, Lee CK, Wimmer E. 1992. Determinants of substrate recognition by poliovirus 2A proteinase. J Virol 66:3330-3338.
    • (1992) J Virol , vol.66 , pp. 3330-3338
    • Hellen, C.U.1    Lee, C.K.2    Wimmer, E.3
  • 26
    • 0025907748 scopus 로고
    • Development of synthetic peptide substrates for the poliovirus 3C proteinase
    • Weidner JR, Dunn BM. 1991. Development of synthetic peptide substrates for the poliovirus 3C proteinase. Arch Biochem Biophys 286:402-408. http://dx.doi.org/10.1016/0003-9861(91)90058-Q.
    • (1991) Arch Biochem Biophys , vol.286 , pp. 402-408
    • Weidner, J.R.1    Dunn, B.M.2
  • 27
    • 0024297314 scopus 로고
    • Structural domains of the poliovirus polyprotein are major determinants for proteolytic cleavage at Gln-Gly pairs
    • Ypma-Wong MF, Filman DJ, Hogle JM, Semler BL. 1988. Structural domains of the poliovirus polyprotein are major determinants for proteolytic cleavage at Gln-Gly pairs. J Biol Chem 263:17846-17856.
    • (1988) J Biol Chem , vol.263 , pp. 17846-17856
    • Ypma-Wong, M.F.1    Filman, D.J.2    Hogle, J.M.3    Semler, B.L.4
  • 28
    • 34247640056 scopus 로고    scopus 로고
    • Inhibition of U snRNP assembly by a virus-encoded proteinase
    • Almstead LL, Sarnow P. 2007. Inhibition of U snRNP assembly by a virus-encoded proteinase. Genes Dev 21:1086-1097. http://dx.doi.org/10.1101/gad.1535607.
    • (2007) Genes Dev , vol.21 , pp. 1086-1097
    • Almstead, L.L.1    Sarnow, P.2
  • 29
    • 0027535652 scopus 로고
    • Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro
    • Clark ME, Lieberman PM, Berk AJ, Dasgupta A. 1993. Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro. Mol Cell Biol 13:1232-1237.
    • (1993) Mol Cell Biol , vol.13 , pp. 1232-1237
    • Clark, M.E.1    Lieberman, P.M.2    Berk, A.J.3    Dasgupta, A.4
  • 30
    • 47749151829 scopus 로고    scopus 로고
    • Cleavage of eukaryotic initiation factor eIF5B by enterovirus 3C proteases
    • de Breyne S, Bonderoff JM, Chumakov KM, Lloyd RE, Hellen CU. 2008. Cleavage of eukaryotic initiation factor eIF5B by enterovirus 3C proteases. Virology 378:118-122. http://dx.doi.org/10.1016/j.virol.2008.05.019.
    • (2008) Virology , vol.378 , pp. 118-122
    • de Breyne, S.1    Bonderoff, J.M.2    Chumakov, K.M.3    Lloyd, R.E.4    Hellen, C.U.5
  • 31
    • 2642552969 scopus 로고    scopus 로고
    • Proteolytic cleavage of the catalytic subunit ofDNA-dependentprotein kinase during poliovirus infection
    • Graham KL, Gustin KE, Rivera C, Kuyumcu-Martinez NM, Choe SS, Lloyd RE, Sarnow P, Utz PJ. 2004. Proteolytic cleavage of the catalytic subunit ofDNA-dependentprotein kinase during poliovirus infection. J Virol 78:6313-6321. http://dx.doi.org/10.1128/JVI.78.12.6313-6321.2004.
    • (2004) J Virol , vol.78 , pp. 6313-6321
    • Graham, K.L.1    Gustin, K.E.2    Rivera, C.3    Kuyumcu-Martinez, N.M.4    Choe, S.S.5    Lloyd, R.E.6    Sarnow, P.7    Utz, P.J.8
  • 32
    • 21244499051 scopus 로고    scopus 로고
    • Proteolytic cleavage of the p65-RelA subunit of NF-B during poliovirus infection
    • Neznanov N, Chumakov KM, Neznanova L, Almasan A, Banerjee AK, Gudkov AV. 2005. Proteolytic cleavage of the p65-RelA subunit of NF-B during poliovirus infection. J Biol Chem 280:24153-24158. http://dx.doi.org/10.1074/jbc.M502303200.
    • (2005) J Biol Chem , vol.280 , pp. 24153-24158
    • Neznanov, N.1    Chumakov, K.M.2    Neznanova, L.3    Almasan, A.4    Banerjee, A.K.5    Gudkov, A.V.6
  • 34
    • 84856617250 scopus 로고    scopus 로고
    • Cleavage of serum response factor mediated by enteroviral protease 2A contributes to impaired cardiac function
    • Wong J, Zhang J, Yanagawa B, Luo Z, Yang X, Chang J, McManus B, Luo H. 2012. Cleavage of serum response factor mediated by enteroviral protease 2A contributes to impaired cardiac function. Cell Res 22:360-371. http://dx.doi.org/10.1038/cr.2011.114.
    • (2012) Cell Res , vol.22 , pp. 360-371
    • Wong, J.1    Zhang, J.2    Yanagawa, B.3    Luo, Z.4    Yang, X.5    Chang, J.6    McManus, B.7    Luo, H.8
  • 36
    • 35848929915 scopus 로고    scopus 로고
    • Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase
    • White JP, Cardenas AM, Marissen WE, Lloyd RE. 2007. Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase. Cell Host Microbe 2:295-305. http://dx.doi.org/10.1016/j.chom.2007.08.006.
    • (2007) Cell Host Microbe , vol.2 , pp. 295-305
    • White, J.P.1    Cardenas, A.M.2    Marissen, W.E.3    Lloyd, R.E.4
  • 38
    • 77956687928 scopus 로고    scopus 로고
    • Functional diversity of the hnRNPs: past, present and perspectives
    • Han SP, Tang YH, Smith R. 2010. Functional diversity of the hnRNPs: past, present and perspectives. Biochem J 430:379-392. http://dx.doi.org/10.1042/BJ20100396.
    • (2010) Biochem J , vol.430 , pp. 379-392
    • Han, S.P.1    Tang, Y.H.2    Smith, R.3
  • 41
    • 80053404377 scopus 로고    scopus 로고
    • Identifying and quantifying proteolytic events and the natural N terminome by terminal amine isotopic labeling of substrates
    • Kleifeld O, Doucet A, Prudova A, Auf Dem Keller U, Gioia M, Kizhakkedathu JN, Overall CM. 2011. Identifying and quantifying proteolytic events and the natural N terminome by terminal amine isotopic labeling of substrates. Nature protocols 6:1578-1611. http://dx.doi.org/10.1038/nprot.2011.382.
    • (2011) Nature protocols , vol.6 , pp. 1578-1611
    • Kleifeld, O.1    Doucet, A.2    Prudova, A.3    Auf Dem Keller, U.4    Gioia, M.5    Kizhakkedathu, J.N.6    Overall, C.M.7
  • 42
    • 79955545315 scopus 로고    scopus 로고
    • Mechanistic control of carcinoembryonic antigen-related cell adhesion molecule-1 (CEACAM1) splice isoforms by the heterogeneous nuclear ribonuclear proteins hnRNP L, hnRNP A1, and hnRNP M
    • Dery KJ, Gaur S, Gencheva M, Yen Y, Shively JE, Gaur RK. 2011. Mechanistic control of carcinoembryonic antigen-related cell adhesion molecule-1 (CEACAM1) splice isoforms by the heterogeneous nuclear ribonuclear proteins hnRNP L, hnRNP A1, and hnRNP M. J Biol Chem 286:16039-16051. http://dx.doi.org/10.1074/jbc.M110.204057.
    • (2011) J Biol Chem , vol.286 , pp. 16039-16051
    • Dery, K.J.1    Gaur, S.2    Gencheva, M.3    Yen, Y.4    Shively, J.E.5    Gaur, R.K.6
  • 43
    • 37549039473 scopus 로고    scopus 로고
    • Heterogeneous ribonucleoprotein m is a splicing regulatory protein that can enhance or silence splicing of alternatively spliced exons
    • Hovhannisyan RH, Carstens RP. 2007. Heterogeneous ribonucleoprotein m is a splicing regulatory protein that can enhance or silence splicing of alternatively spliced exons. J Biol Chem 282:36265-36274. http://dx.doi.org/10.1074/jbc.M704188200.
    • (2007) J Biol Chem , vol.282 , pp. 36265-36274
    • Hovhannisyan, R.H.1    Carstens, R.P.2
  • 44
    • 0034283557 scopus 로고    scopus 로고
    • The 72/74-kDa polypeptides of the 70-110 S large heterogeneous nuclear ribonucleoprotein complex (LH-nRNP) represent a discrete subset of the hnRNPMprotein family
    • Kafasla P, Patrinou-Georgoula M, Guialis A. 2000. The 72/74-kDa polypeptides of the 70-110 S large heterogeneous nuclear ribonucleoprotein complex (LH-nRNP) represent a discrete subset of the hnRNPMprotein family. Biochem J 350(Pt 2):495-503.
    • (2000) Biochem J , vol.350 , pp. 495-503
    • Kafasla, P.1    Patrinou-Georgoula, M.2    Guialis, A.3
  • 45
    • 0036566191 scopus 로고    scopus 로고
    • Association of the 72/74-kDa proteins, members of the heterogeneous nuclear ribonucleoproteinMgroup, with the pre-mRNA at early stages of spliceosome assembly
    • Kafasla P, Patrinou-Georgoula M, Lewis JD, Guialis A. 2002. Association of the 72/74-kDa proteins, members of the heterogeneous nuclear ribonucleoproteinMgroup, with the pre-mRNA at early stages of spliceosome assembly. Biochem J 363:793-799. http://dx.doi.org/10.1042/0264-6021:3630793.
    • (2002) Biochem J , vol.363 , pp. 793-799
    • Kafasla, P.1    Patrinou-Georgoula, M.2    Lewis, J.D.3    Guialis, A.4
  • 46
    • 77953122318 scopus 로고    scopus 로고
    • Direct interaction between hnRNP-M and CDC5L/PLRG1 proteins affects alternative splice site choice
    • Lleres D, Denegri M, Biggiogera M, Ajuh P, Lamond AI. 2010. Direct interaction between hnRNP-M and CDC5L/PLRG1 proteins affects alternative splice site choice. EMBO Rep 11:445-451. http://dx.doi.org/10.1038/embor.2010.64.
    • (2010) EMBO Rep , vol.11 , pp. 445-451
    • Lleres, D.1    Denegri, M.2    Biggiogera, M.3    Ajuh, P.4    Lamond, A.I.5
  • 47
    • 79960135469 scopus 로고    scopus 로고
    • Regulatory roles of heterogeneous nuclear ribonucleoprotein M and Nova-1 protein in alternative splicing of dopamine D2 receptor pre-mRNA
    • Park E, Iaccarino C, Lee J, Kwon I, Baik SM, Kim M, Seong JY, Son GH, Borrelli E, Kim K. 2011. Regulatory roles of heterogeneous nuclear ribonucleoprotein M and Nova-1 protein in alternative splicing of dopamine D2 receptor pre-mRNA. J Biol Chem 286:25301-25308. http://dx.doi.org/10.1074/jbc.M110.206540.
    • (2011) J Biol Chem , vol.286 , pp. 25301-25308
    • Park, E.1    Iaccarino, C.2    Lee, J.3    Kwon, I.4    Baik, S.M.5    Kim, M.6    Seong, J.Y.7    Son, G.H.8    Borrelli, E.9    Kim, K.10
  • 48
    • 0027238531 scopus 로고
    • The human hnRNP M proteins: identification of a methionine/arginine-rich repeat motif in ribonucleoproteins
    • Datar KV, Dreyfuss G, Swanson MS. 1993. The human hnRNP M proteins: identification of a methionine/arginine-rich repeat motif in ribonucleoproteins. Nucleic Acids Res 21:439-446. http://dx.doi.org/10.1093/nar/21.3.439.
    • (1993) Nucleic Acids Res , vol.21 , pp. 439-446
    • Datar, K.V.1    Dreyfuss, G.2    Swanson, M.S.3
  • 49
    • 0024077061 scopus 로고
    • Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor
    • Ypma-Wong MF, Dewalt PG, Johnson VH, Lamb JG, Semler BL. 1988. Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor. Virology 166:265-270. http://dx.doi.org/10.1016/0042-6822(88)90172-9.
    • (1988) Virology , vol.166 , pp. 265-270
    • Ypma-Wong, M.F.1    Dewalt, P.G.2    Johnson, V.H.3    Lamb, J.G.4    Semler, B.L.5
  • 52
    • 0029100156 scopus 로고
    • Two immunologically related polypeptides of 72/74 kDa specify a novel 70-100S heterogeneous nuclear RNP
    • Aidinis V, Sekeris CE, Guialis A. 1995. Two immunologically related polypeptides of 72/74 kDa specify a novel 70-100S heterogeneous nuclear RNP. Nucleic Acids Res 23:2742-2753. http://dx.doi.org/10.1093/nar/23.14.2742.
    • (1995) Nucleic Acids Res , vol.23 , pp. 2742-2753
    • Aidinis, V.1    Sekeris, C.E.2    Guialis, A.3
  • 53
    • 0035863125 scopus 로고    scopus 로고
    • Effects of poliovirus infection on nucleocytoplasmic trafficking and nuclear pore complex composition
    • Gustin KE, Sarnow P. 2001. Effects of poliovirus infection on nucleocytoplasmic trafficking and nuclear pore complex composition. EMBO J 20:240-249. http://dx.doi.org/10.1093/emboj/20.1.240.
    • (2001) EMBO J , vol.20 , pp. 240-249
    • Gustin, K.E.1    Sarnow, P.2
  • 54
    • 0025976987 scopus 로고
    • An RNA hairpin at the extreme 5' end of the poliovirus RNA genome modulates viral translation in human cells
    • Simoes EA, Sarnow P. 1991. An RNA hairpin at the extreme 5' end of the poliovirus RNA genome modulates viral translation in human cells. J Virol 65:913-921.
    • (1991) J Virol , vol.65 , pp. 913-921
    • Simoes, E.A.1    Sarnow, P.2
  • 56
    • 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. 2009. RNA nuclear export is blocked by poliovirus 2A protease and is concomitant with nucleoporin cleavage. J Cell Sci 122:3799-3809. http://dx.doi.org/10.1242/jcs.055988.
    • (2009) J Cell Sci , vol.122 , pp. 3799-3809
    • Castello, A.1    Izquierdo, J.M.2    Welnowska, E.3    Carrasco, L.4
  • 57
    • 38849138626 scopus 로고    scopus 로고
    • Differential targeting of nuclear pore complex proteins in poliovirus-infected cells
    • Park N, Katikaneni P, Skern T, Gustin KE. 2008. Differential targeting of nuclear pore complex proteins in poliovirus-infected cells. J Virol 82: 1647-1655. http://dx.doi.org/10.1128/JVI.01670-07.
    • (2008) J Virol , vol.82 , pp. 1647-1655
    • Park, N.1    Katikaneni, P.2    Skern, T.3    Gustin, K.E.4
  • 58
    • 77956511212 scopus 로고    scopus 로고
    • Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease
    • Park N, Skern T, Gustin KE. 2010. Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease. J Biol Chem 285:28796-28805. http://dx.doi.org/10.1074/jbc.M110.143404.
    • (2010) J Biol Chem , vol.285 , pp. 28796-28805
    • Park, N.1    Skern, T.2    Gustin, K.E.3
  • 59
    • 1542345709 scopus 로고    scopus 로고
    • Nuclear entry of poliovirus protease-polymerase precursor 3CD: implications for host cell transcription shut-off
    • Sharma R, Raychaudhuri S, Dasgupta A. 2004. Nuclear entry of poliovirus protease-polymerase precursor 3CD: implications for host cell transcription shut-off. Virology 320:195-205. http://dx.doi.org/10.1016/j.virol.2003.10.020.
    • (2004) Virology , vol.320 , pp. 195-205
    • Sharma, R.1    Raychaudhuri, S.2    Dasgupta, A.3
  • 60
    • 16844374636 scopus 로고    scopus 로고
    • Hrp59, an hnRNP M protein in Chironomus and Drosophila, binds to exonic splicing enhancers and is required for expression of a subset of mRNAs
    • Kiesler E, Hase ME, Brodin D, Visa N. 2005. Hrp59, an hnRNP M protein in Chironomus and Drosophila, binds to exonic splicing enhancers and is required for expression of a subset of mRNAs. J Cell Biol 168: 1013-1025. http://dx.doi.org/10.1083/jcb.200407173.
    • (2005) J Cell Biol , vol.168 , pp. 1013-1025
    • Kiesler, E.1    Hase, M.E.2    Brodin, D.3    Visa, N.4
  • 61
    • 84896983805 scopus 로고    scopus 로고
    • hnRNP M facilitates exon 7 inclusion of SMN2 premRNA in spinal muscular atrophy by targeting an enhancer on exon 7
    • Cho S, Moon H, Loh TJ, Oh HK, Choy HE, Song WK, Chun JS, Zheng X, Shen H. 2014. hnRNP M facilitates exon 7 inclusion of SMN2 premRNA in spinal muscular atrophy by targeting an enhancer on exon 7. Biochim Biophys Acta 1839:306-315. http://dx.doi.org/10.1016/j.bbagrm.2014.02.006.
    • (2014) Biochim Biophys Acta , vol.1839 , pp. 306-315
    • Cho, S.1    Moon, H.2    Loh, T.J.3    Oh, H.K.4    Choy, H.E.5    Song, W.K.6    Chun, J.S.7    Zheng, X.8    Shen, H.9
  • 62
    • 84897533665 scopus 로고    scopus 로고
    • Selective interactions of hnRNP M isoforms with the TET proteins TAF15 and TLS/FUS
    • Marko M, Leichter M, Patrinou-Georgoula M, Guialis A. 2014. Selective interactions of hnRNP M isoforms with the TET proteins TAF15 and TLS/FUS. Mol Biol Rep 41:2687-2695. http://dx.doi.org/10.1007/s11033-014-3128-3.
    • (2014) Mol Biol Rep , vol.41 , pp. 2687-2695
    • Marko, M.1    Leichter, M.2    Patrinou-Georgoula, M.3    Guialis, A.4
  • 63
    • 0035903139 scopus 로고    scopus 로고
    • Heterogeneous RNA-binding protein M4 is a receptor for carcinoembryonic antigen in Kupffer cells
    • Bajenova OV, Zimmer R, Stolper E, Salisbury-Rowswell J, Nanji A, Thomas P. 2001. Heterogeneous RNA-binding protein M4 is a receptor for carcinoembryonic antigen in Kupffer cells. J Biol Chem 276:31067-31073. http://dx.doi.org/10.1074/jbc.M104093200.
    • (2001) J Biol Chem , vol.276 , pp. 31067-31073
    • Bajenova, O.V.1    Zimmer, R.2    Stolper, E.3    Salisbury-Rowswell, J.4    Nanji, A.5    Thomas, P.6
  • 64
    • 0029934811 scopus 로고    scopus 로고
    • The human hnRNP-M proteins: structure and relation with early heat shock-induced splicing arrest and chromosome mapping
    • Gattoni R, Mahe D, Mahl P, Fischer N, Mattei MG, Stevenin J, Fuchs JP. 1996. The human hnRNP-M proteins: structure and relation with early heat shock-induced splicing arrest and chromosome mapping. Nucleic Acids Res 24:2535-2542. http://dx.doi.org/10.1093/nar/24.13.2535.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2535-2542
    • Gattoni, R.1    Mahe, D.2    Mahl, P.3    Fischer, N.4    Mattei, M.G.5    Stevenin, J.6    Fuchs, J.P.7
  • 65
    • 80054079869 scopus 로고    scopus 로고
    • Alternative splicing, a new target to block cellular gene expression by poliovirus 2A protease
    • Alvarez E, Castello A, Carrasco L, Izquierdo JM. 2011. Alternative splicing, a new target to block cellular gene expression by poliovirus 2A protease. Biochem Biophys Res Commun 414:142-147. http://dx.doi.org/10.1016/j.bbrc.2011.09.040.
    • (2011) Biochem Biophys Res Commun , vol.414 , pp. 142-147
    • Alvarez, E.1    Castello, A.2    Carrasco, L.3    Izquierdo, J.M.4
  • 66
    • 84903467004 scopus 로고    scopus 로고
    • Cytoplasmic viral RNAdependent RNA polymerase disrupts the intracellular splicing machinery by entering the nucleus and interfering with Prp8
    • Liu YC, Kuo RL, Lin JY, Huang PN, Huang Y, Liu H, Arnold JJ, Chen SJ, Wang RY, Cameron CE, Shih SR. 2014. Cytoplasmic viral RNAdependent RNA polymerase disrupts the intracellular splicing machinery by entering the nucleus and interfering with Prp8. PLoS Pathog 10: e1004199. http://dx.doi.org/10.1371/journal.ppat.1004199.
    • (2014) PLoS Pathog , vol.10
    • Liu, Y.C.1    Kuo, R.L.2    Lin, J.Y.3    Huang, P.N.4    Huang, Y.5    Liu, H.6    Arnold, J.J.7    Chen, S.J.8    Wang, R.Y.9    Cameron, C.E.10    Shih, S.R.11
  • 67
    • 44649108325 scopus 로고    scopus 로고
    • Analysis of the interaction of influenza virus polymerase complex with human cell factors
    • Jorba N, Juarez S, Torreira E, Gastaminza P, Zamarreno N, Albar JP, Ortin J. 2008. Analysis of the interaction of influenza virus polymerase complex with human cell factors. Proteomics 8:2077-2088. http://dx.doi.org/10.1002/pmic.200700508.
    • (2008) Proteomics , vol.8 , pp. 2077-2088
    • Jorba, N.1    Juarez, S.2    Torreira, E.3    Gastaminza, P.4    Zamarreno, N.5    Albar, J.P.6    Ortin, J.7
  • 68
    • 84883292987 scopus 로고    scopus 로고
    • Magnetic fractionation and proteomic dissection of cellular organelles occupied by the late replication complexes of Semliki Forest virus
    • Varjak M, Saul S, Arike L, Lulla A, Peil L, Merits A. 2013. Magnetic fractionation and proteomic dissection of cellular organelles occupied by the late replication complexes of Semliki Forest virus. J Virol 87:10295-10312. http://dx.doi.org/10.1128/JVI.01105-13.
    • (2013) J Virol , vol.87 , pp. 10295-10312
    • Varjak, M.1    Saul, S.2    Arike, L.3    Lulla, A.4    Peil, L.5    Merits, A.6
  • 69
    • 84899744133 scopus 로고    scopus 로고
    • Generation of unique poliovirus RNA replication organelles
    • Richards AL, Soares-Martins JA, Riddell GT, Jackson WT. 2014. Generation of unique poliovirus RNA replication organelles. mBio 5:e00833-13. http://dx.doi.org/10.1128/mBio.00833-13.
    • (2014) mBio , vol.5
    • Richards, A.L.1    Soares-Martins, J.A.2    Riddell, G.T.3    Jackson, W.T.4
  • 70
    • 78650069922 scopus 로고    scopus 로고
    • Poliovirus-mediated disruption of cytoplasmic processing bodies
    • Dougherty JD, White JP, Lloyd RE. 2011. Poliovirus-mediated disruption of cytoplasmic processing bodies. J Virol 85:64-75. http://dx.doi.org/10.1128/JVI.01657-10.
    • (2011) J Virol , vol.85 , pp. 64-75
    • Dougherty, J.D.1    White, J.P.2    Lloyd, R.E.3

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