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Volumn 44, Issue 16, 2016, Pages 7511-7526

mRNA capping: Biological functions and applications

Author keywords

[No Author keywords available]

Indexed keywords

ACID HYDROLASE; DNA VACCINE; MESSENGER RNA; RNA GUANYLYLTRANSFERASE; RNA TRIPHOSPHATASE; RNA VACCINE; TRANSCRIPTOME; UNCLASSIFIED DRUG; VIRUS RNA; CAPPED RNA; NUCLEOTIDYLTRANSFERASE;

EID: 84988979122     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkw551     Document Type: Review
Times cited : (560)

References (183)
  • 3
    • 84908192020 scopus 로고    scopus 로고
    • The cytoplasmic capping complex assembles on adapter protein Nck1 bound to the Proline-rich C-terminus of mammalian capping enzyme
    • Mukherjee, C., Bakthavachalu, B. and Schoenberg, D.R. (2014) The cytoplasmic capping complex assembles on adapter protein Nck1 bound to the Proline-rich C-terminus of mammalian capping enzyme. PLoS Biol., 12, e1001933.
    • (2014) PLoS Biol. , vol.12 , pp. e1001933
    • Mukherjee, C.1    Bakthavachalu, B.2    Schoenberg, D.R.3
  • 5
    • 83855162132 scopus 로고    scopus 로고
    • Conventional and unconventional mechanisms for capping viral mRNA
    • Decroly, E., Ferron, F., Lescar, J. and Canard, B. (2012) Conventional and unconventional mechanisms for capping viral mRNA. Nat. Rev. Microbiol., 10, 51-65.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 51-65
    • Decroly, E.1    Ferron, F.2    Lescar, J.3    Canard, B.4
  • 6
    • 0033788228 scopus 로고    scopus 로고
    • The ends of the affair: Capping and polyadenylation
    • Shatkin, A.J. and Manley, J.L. (2000) The ends of the affair: capping and polyadenylation. Nat. Struct. Biol., 7, 838-842.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 838-842
    • Shatkin, A.J.1    Manley, J.L.2
  • 7
    • 0036753427 scopus 로고    scopus 로고
    • Functional coupling of capping and transcription of mRNA
    • Moteki, S. and Price, D. (2002) Functional coupling of capping and transcription of mRNA. Mol. Cell, 10, 599-609.
    • (2002) Mol. Cell , vol.10 , pp. 599-609
    • Moteki, S.1    Price, D.2
  • 10
    • 0030660264 scopus 로고    scopus 로고
    • Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
    • Yue, Z., Maldonado, E., Pillutla, R., Cho, H., Reinberg, D. and Shatkin, A.J. (1997) Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II. Proc. Natl. Acad. Sci. U.S.A., 94, 12898-12903.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12898-12903
    • Yue, Z.1    Maldonado, E.2    Pillutla, R.3    Cho, H.4    Reinberg, D.5    Shatkin, A.J.6
  • 11
    • 0033522898 scopus 로고    scopus 로고
    • Characterization of human, Schizosaccharomyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes
    • Saha, N., Schwer, B. and Shuman, S. (1999) Characterization of human, Schizosaccharomyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes. J. Biol. Chem., 274, 16553-16562.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16553-16562
    • Saha, N.1    Schwer, B.2    Shuman, S.3
  • 12
    • 77958508457 scopus 로고    scopus 로고
    • Characterization of hMTr1, a human Cap1 2′-O-ribose methyltransferase
    • Belanger, F., Stepinski, J., Darzynkiewicz, E. and Pelletier, J. (2010) Characterization of hMTr1, a human Cap1 2′-O-ribose methyltransferase. J. Biol. Chem., 285, 33037-33044.
    • (2010) J. Biol. Chem. , vol.285 , pp. 33037-33044
    • Belanger, F.1    Stepinski, J.2    Darzynkiewicz, E.3    Pelletier, J.4
  • 15
    • 0031453408 scopus 로고    scopus 로고
    • mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain
    • Cho, E.-J., Takagi, T., Moore, C.R. and Buratowski, S. (1997) mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev., 11, 3319-3326.
    • (1997) Genes Dev. , vol.11 , pp. 3319-3326
    • Cho, E.-J.1    Takagi, T.2    Moore, C.R.3    Buratowski, S.4
  • 16
    • 79960442655 scopus 로고    scopus 로고
    • Structural insights to how mammalian capping enzyme reads the CTD code
    • Ghosh, A., Shuman, S. and Lima, C.D. (2011) Structural insights to how mammalian capping enzyme reads the CTD code. Mol. Cell, 43, 299-310.
    • (2011) Mol. Cell , vol.43 , pp. 299-310
    • Ghosh, A.1    Shuman, S.2    Lima, C.D.3
  • 17
    • 73849107519 scopus 로고    scopus 로고
    • Regulation of mRNA cap methylation
    • Cowling, V.H. (2010) Regulation of mRNA cap methylation. Biochem. J., 425, 295-302.
    • (2010) Biochem. J. , vol.425 , pp. 295-302
    • Cowling, V.H.1
  • 18
    • 75849118597 scopus 로고    scopus 로고
    • Structure of the Saccharomyces cerevisiae Cet1-Ceg1 mRNA capping apparatus
    • Gu, M., Rajashankar, K.R. and Lima, C.D. (2010) Structure of the Saccharomyces cerevisiae Cet1-Ceg1 mRNA capping apparatus. Structure, 18, 216-227.
    • (2010) Structure , vol.18 , pp. 216-227
    • Gu, M.1    Rajashankar, K.R.2    Lima, C.D.3
  • 19
    • 84902519559 scopus 로고    scopus 로고
    • How an mRNA capping enzyme reads distinct RNA polymerase II and Spt5 CTD phosphorylation codes
    • Doamekpor, S.K., Sanchez, A.M., Schwer, B., Shuman, S. and Lima, C.D. (2014) How an mRNA capping enzyme reads distinct RNA polymerase II and Spt5 CTD phosphorylation codes. Genes Dev., 28, 1323-1336.
    • (2014) Genes Dev. , vol.28 , pp. 1323-1336
    • Doamekpor, S.K.1    Sanchez, A.M.2    Schwer, B.3    Shuman, S.4    Lima, C.D.5
  • 20
    • 0037121926 scopus 로고    scopus 로고
    • Human Dcp2: A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
    • van Dijk, E., Cougot, N., Meyer, S., Babajko, S., Wahle, E. and Seraphin, B. (2002) Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J., 21, 6915-6924.
    • (2002) EMBO J. , vol.21 , pp. 6915-6924
    • Van Dijk, E.1    Cougot, N.2    Meyer, S.3    Babajko, S.4    Wahle, E.5    Seraphin, B.6
  • 21
    • 27144515901 scopus 로고    scopus 로고
    • Movement of Eukaryotic mRNAs between polysomes and cytoplasmic processing bodies
    • Brengues, M. (2005) Movement of Eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science, 310, 486-489.
    • (2005) Science , vol.310 , pp. 486-489
    • Brengues, M.1
  • 22
    • 66049158810 scopus 로고    scopus 로고
    • Polysomes, P bodies and stress granules: States and fates of eukaryotic mRNAs
    • Balagopal, V. and Parker, R. (2009) Polysomes, P bodies and stress granules: states and fates of eukaryotic mRNAs. Curr. Opin. Cell Biol., 21, 403-408.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 403-408
    • Balagopal, V.1    Parker, R.2
  • 25
    • 64649087770 scopus 로고    scopus 로고
    • Identification of a cytoplasmic complex that adds a cap onto 5′-monophosphate RNA
    • Otsuka, Y., Kedersha, N.L. and Schoenberg, D.R. (2009) Identification of a cytoplasmic complex that adds a cap onto 5′-monophosphate RNA. Mol. Cell. Biol., 29, 2155-2167.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2155-2167
    • Otsuka, Y.1    Kedersha, N.L.2    Schoenberg, D.R.3
  • 27
    • 84921467394 scopus 로고    scopus 로고
    • Uncapped 5′ ends of mRNAs targeted by cytoplasmic capping map to the vicinity of downstream CAGE tags
    • Kiss, D.L., Oman, K., Bundschuh, R. and Schoenberg, D.R. (2015) Uncapped 5′ ends of mRNAs targeted by cytoplasmic capping map to the vicinity of downstream CAGE tags. FEBS Lett., 589, 279-284.
    • (2015) FEBS Lett. , vol.589 , pp. 279-284
    • Kiss, D.L.1    Oman, K.2    Bundschuh, R.3    Schoenberg, D.R.4
  • 30
    • 84866951989 scopus 로고    scopus 로고
    • Identification of cytoplasmic capping targets reveals a role for cap homeostasis in translation and mRNA stability
    • Mukherjee, C., Patil, D.P., Kennedy, B.A., Bakthavachalu, B., Bundschuh, R. and Schoenberg, D.R. (2012) Identification of cytoplasmic capping targets reveals a role for cap homeostasis in translation and mRNA stability. Cell Rep., 2, 674-684.
    • (2012) Cell Rep. , vol.2 , pp. 674-684
    • Mukherjee, C.1    Patil, D.P.2    Kennedy, B.A.3    Bakthavachalu, B.4    Bundschuh, R.5    Schoenberg, D.R.6
  • 31
    • 84876088413 scopus 로고    scopus 로고
    • A mammalian pre-mRNA 5′ end capping quality control mechanism and an unexpected link of capping to pre-mRNA processing
    • Jiao, X., Chang, J.H., Kilic, T., Tong, L. and Kiledjian, M. (2013) A mammalian pre-mRNA 5′ end capping quality control mechanism and an unexpected link of capping to pre-mRNA processing. Mol. Cell, 50, 104-115.
    • (2013) Mol. Cell , vol.50 , pp. 104-115
    • Jiao, X.1    Chang, J.H.2    Kilic, T.3    Tong, L.4    Kiledjian, M.5
  • 32
    • 77957340903 scopus 로고    scopus 로고
    • Identification of a quality-control mechanism for mRNA 5′-end capping
    • Jiao, X., Xiang, S., Oh, C., Martin, C.E., Tong, L. and Kiledjian, M. (2010) Identification of a quality-control mechanism for mRNA 5′-end capping. Nature, 467, 608-611.
    • (2010) Nature , vol.467 , pp. 608-611
    • Jiao, X.1    Xiang, S.2    Oh, C.3    Martin, C.E.4    Tong, L.5    Kiledjian, M.6
  • 33
    • 64749111945 scopus 로고    scopus 로고
    • Structure and function of the 5′->3′ exoribonuclease Rat1 and its activating partner Rai1
    • Xiang, S., Cooper-Morgan, A., Jiao, X., Kiledjian, M., Manley, J.L. and Tong, L. (2009) Structure and function of the 5′->3′ exoribonuclease Rat1 and its activating partner Rai1. Nature, 458, 784-788.
    • (2009) Nature , vol.458 , pp. 784-788
    • Xiang, S.1    Cooper-Morgan, A.2    Jiao, X.3    Kiledjian, M.4    Manley, J.L.5    Tong, L.6
  • 34
    • 84867229926 scopus 로고    scopus 로고
    • Dxo1 is a new type of eukaryotic enzyme with both decapping and 5′-3′ exoribonuclease activity
    • Chang, J.H., Jiao, X., Chiba, K., Oh, C., Martin, C.E., Kiledjian, M. and Tong, L. (2012) Dxo1 is a new type of eukaryotic enzyme with both decapping and 5′-3′ exoribonuclease activity. Nat. Struct. Mol. Biol., 19, 1011-1017.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 1011-1017
    • Chang, J.H.1    Jiao, X.2    Chiba, K.3    Oh, C.4    Martin, C.E.5    Kiledjian, M.6    Tong, L.7
  • 35
    • 0021747202 scopus 로고
    • Recognition of cap structure in splicing in vitro of mRNA precursors
    • Konarska, M.M., Padgett, R.A. and Sharp, P.A. (1984) Recognition of cap structure in splicing in vitro of mRNA precursors. Cell, 38, 731-736.
    • (1984) Cell , vol.38 , pp. 731-736
    • Konarska, M.M.1    Padgett, R.A.2    Sharp, P.A.3
  • 36
    • 0023394375 scopus 로고
    • Preferential excision of the 5′ proximal intron from mRNA precursors with two introns as mediated by the cap structure
    • Ohno, M., Sakamoto, H. and Shimura, Y. (1987) Preferential excision of the 5′ proximal intron from mRNA precursors with two introns as mediated by the cap structure. Proc. Natl. Acad. Sci. U.S.A., 84, 5187-5191.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 5187-5191
    • Ohno, M.1    Sakamoto, H.2    Shimura, Y.3
  • 37
    • 0024729178 scopus 로고
    • Effect of the cap structure on pre-mRNA splicing in Xenopus oocyte nuclei
    • Inoue, K., Ohno, M., Sakamoto, H. and Shimura, Y. (1989) Effect of the cap structure on pre-mRNA splicing in Xenopus oocyte nuclei. Genes Dev., 3, 1472-1479.
    • (1989) Genes Dev. , vol.3 , pp. 1472-1479
    • Inoue, K.1    Ohno, M.2    Sakamoto, H.3    Shimura, Y.4
  • 38
    • 0029951308 scopus 로고    scopus 로고
    • Conditional mutants of the yeast mRNA capping enzyme show that the cap enhances, but is not required for, mRNA splicing
    • Fresco, L.D. and Buratowski, S. (1996) Conditional mutants of the yeast mRNA capping enzyme show that the cap enhances, but is not required for, mRNA splicing. RNA, 2, 584-596.
    • (1996) RNA , vol.2 , pp. 584-596
    • Fresco, L.D.1    Buratowski, S.2
  • 42
    • 84880650073 scopus 로고    scopus 로고
    • The nuclear cap-binding complex interacts with the U4/U6U5 tri-snRNP and promotes spliceosome assembly in mammalian cells
    • Pabis, M., Neufeld, N., Steiner, M.C., Bojic, T., Shav-Tal, Y. and Neugebauer, K.M. (2013) The nuclear cap-binding complex interacts with the U4/U6U5 tri-snRNP and promotes spliceosome assembly in mammalian cells. RNA, 19, 1054-1063.
    • (2013) RNA , vol.19 , pp. 1054-1063
    • Pabis, M.1    Neufeld, N.2    Steiner, M.C.3    Bojic, T.4    Shav-Tal, Y.5    Neugebauer, K.M.6
  • 45
    • 0031954020 scopus 로고    scopus 로고
    • Transport of macromolecules between the nucleus and the cytoplasm
    • Izaurralde, E. and Adam, S. (1998) Transport of macromolecules between the nucleus and the cytoplasm. RNA, 4, 351-364.
    • (1998) RNA , vol.4 , pp. 351-364
    • Izaurralde, E.1    Adam, S.2
  • 46
    • 0035912782 scopus 로고    scopus 로고
    • Assembly and transport of a premessenger RNP particle
    • Daneholt, B. (2001) Assembly and transport of a premessenger RNP particle. Proc. Natl. Acad. Sci. U.S.A., 98, 7012-7017.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 7012-7017
    • Daneholt, B.1
  • 47
    • 34447527805 scopus 로고    scopus 로고
    • The interaction between cap-binding complex and RNA export factor is required for intronless mRNA export
    • Nojima, T., Hirose, T., Kimura, H. and Hagiwara, M. (2007) The interaction between cap-binding complex and RNA export factor is required for intronless mRNA export. J. Biol. Chem., 282, 15645-15651.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15645-15651
    • Nojima, T.1    Hirose, T.2    Kimura, H.3    Hagiwara, M.4
  • 48
    • 33845626622 scopus 로고    scopus 로고
    • Human mRNA export machinery recruited to the 5′ end of mRNA
    • Cheng, H., Dufu, K., Lee, C.-S., Hsu, J.L., Dias, A. and Reed, R. (2006) Human mRNA export machinery recruited to the 5′ end of mRNA. Cell, 127, 1389-1400.
    • (2006) Cell , vol.127 , pp. 1389-1400
    • Cheng, H.1    Dufu, K.2    Lee, C.-S.3    Hsu, J.L.4    Dias, A.5    Reed, R.6
  • 49
    • 68949187846 scopus 로고    scopus 로고
    • mRNA nuclear export at a glance
    • Carmody, S.R. and Wente, S.R. (2009) mRNA nuclear export at a glance. J. Cell Sci., 122, 1933-1937.
    • (2009) J. Cell Sci. , vol.122 , pp. 1933-1937
    • Carmody, S.R.1    Wente, S.R.2
  • 50
    • 2142826777 scopus 로고    scopus 로고
    • Nuclear export of mRNA: From the site of transcription to the cytoplasm
    • Erkmann, J.A. and Kutay, U. (2004) Nuclear export of mRNA: from the site of transcription to the cytoplasm. Exp. Cell Res., 296, 12-20.
    • (2004) Exp. Cell Res. , vol.296 , pp. 12-20
    • Erkmann, J.A.1    Kutay, U.2
  • 51
    • 0033636895 scopus 로고    scopus 로고
    • The yeast nuclear cap binding complex can interact with translation factor eIF4G and mediate translation initiation
    • Fortes, P., Inada, T., Preiss, T., Hentze, M.W., Mattaj, I.W. and Sachs, A.B. (2000) The yeast nuclear cap binding complex can interact with translation factor eIF4G and mediate translation initiation. Mol. Cell, 6, 191-196.
    • (2000) Mol. Cell , vol.6 , pp. 191-196
    • Fortes, P.1    Inada, T.2    Preiss, T.3    Hentze, M.W.4    Mattaj, I.W.5    Sachs, A.B.6
  • 52
    • 1842682946 scopus 로고    scopus 로고
    • The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex
    • Chiu, S.-Y., Lejeune, F., Ranganathan, A.C. and Maquat, L.E. (2004) The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex. Genes Dev., 18, 745-754.
    • (2004) Genes Dev. , vol.18 , pp. 745-754
    • Chiu, S.-Y.1    Lejeune, F.2    Ranganathan, A.C.3    Maquat, L.E.4
  • 53
    • 84925268892 scopus 로고    scopus 로고
    • An RNA biosensor for imaging the first round of translation from single cells to living animals
    • Halstead, J.M., Lionnet, T., Wilbertz, J.H., Wippich, F., Ephrussi, A., Singer, R.H. and Chao, J.A. (2015) An RNA biosensor for imaging the first round of translation from single cells to living animals. Science, 347, 1367-1671.
    • (2015) Science , vol.347 , pp. 1367-1671
    • Halstead, J.M.1    Lionnet, T.2    Wilbertz, J.H.3    Wippich, F.4    Ephrussi, A.5    Singer, R.H.6    Chao, J.A.7
  • 54
    • 84908565789 scopus 로고    scopus 로고
    • EIF4AIII enhances translation of nuclear cap-binding complex-bound mRNAs by promoting disruption of secondary structures in 5′UTR
    • Choe, J., Ryu, I., Park, O.H., Park, J., Cho, H., Yoo, J.S., Chi, S.W., Kim, M.K., Song, H.K. and Kim, Y.K. (2014) eIF4AIII enhances translation of nuclear cap-binding complex-bound mRNAs by promoting disruption of secondary structures in 5′UTR. Proc. Natl. Acad. Sci. U.S.A., 111, E4577-E4586.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. E4577-E4586
    • Choe, J.1    Ryu, I.2    Park, O.H.3    Park, J.4    Cho, H.5    Yoo, J.S.6    Chi, S.W.7    Kim, M.K.8    Song, H.K.9    Kim, Y.K.10
  • 55
    • 80052411929 scopus 로고    scopus 로고
    • CBP80-promoted mRNP rearrangements during the pioneer round of translation, nonsense-mediated mRNA decay, and thereafter
    • Maquat, L.E., Hwang, J., Sato, H. and Tang, Y. (2010) CBP80-promoted mRNP rearrangements during the pioneer round of translation, nonsense-mediated mRNA decay, and thereafter. Cold Spring Harb. Symp. Quant. Biol., 75, 127-134.
    • (2010) Cold Spring Harb. Symp. Quant. Biol. , vol.75 , pp. 127-134
    • Maquat, L.E.1    Hwang, J.2    Sato, H.3    Tang, Y.4
  • 56
    • 84861534940 scopus 로고    scopus 로고
    • Translation initiation on mRNAs bound by nuclear cap-binding protein complex CBP80/20 requires interaction between CBP80/20-dependent translation initiation factor and eukaryotic translation initiation factor 3g
    • Choe, J., Oh, N., Park, S., Lee, Y.K., Song, O.-K., Locker, N., Chi, S.-G. and Kim, Y.K. (2012) Translation initiation on mRNAs bound by nuclear cap-binding protein complex CBP80/20 requires interaction between CBP80/20-dependent translation initiation factor and eukaryotic translation initiation factor 3g. J. Biol. Chem., 287, 18500-18509.
    • (2012) J. Biol. Chem. , vol.287 , pp. 18500-18509
    • Choe, J.1    Oh, N.2    Park, S.3    Lee, Y.K.4    Song, O.-K.5    Locker, N.6    Chi, S.-G.7    Kim, Y.K.8
  • 57
    • 77955326776 scopus 로고    scopus 로고
    • The pioneer round of translation: Features and functions
    • Maquat, L.E., Tarn, W.-Y. and Isken, O. (2010) The pioneer round of translation: features and functions. Cell, 142, 368-374.
    • (2010) Cell , vol.142 , pp. 368-374
    • Maquat, L.E.1    Tarn, W.-Y.2    Isken, O.3
  • 59
    • 0032473954 scopus 로고    scopus 로고
    • Dual function of the messenger RNA cap structure in poly(A)-tail-promoted translation in yeast
    • Preiss, T. and Hentze, M.W. (1998) Dual function of the messenger RNA cap structure in poly(A)-tail-promoted translation in yeast. Nature, 392, 516-520.
    • (1998) Nature , vol.392 , pp. 516-520
    • Preiss, T.1    Hentze, M.W.2
  • 60
    • 0031759964 scopus 로고    scopus 로고
    • Poly(A)-tail-promoted translation in yeast: Implications for translational control
    • Preiss, T., Muckenthaler, M. and Hentze, M.W. (1998) Poly(A)-tail-promoted translation in yeast: implications for translational control. RNA, 4, 1321-1331.
    • (1998) RNA , vol.4 , pp. 1321-1331
    • Preiss, T.1    Muckenthaler, M.2    Hentze, M.W.3
  • 61
    • 0032858414 scopus 로고    scopus 로고
    • From factors to mechanisms: Translation and translational control in eukaryotes
    • Preiss, T. and Hentze, M.W. (1999) From factors to mechanisms: translation and translational control in eukaryotes. Curr. Opin. Genet. Dev., 9, 515-521.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 515-521
    • Preiss, T.1    Hentze, M.W.2
  • 62
    • 84905870497 scopus 로고    scopus 로고
    • Poly(A)-binding proteins are required for diverse biological processes in metazoans
    • Smith, R.W.P., Blee, T.K.P. and Gray, N.K. (2014) Poly(A)-binding proteins are required for diverse biological processes in metazoans. Biochem. Soc. Trans., 42, 1229-1237.
    • (2014) Biochem. Soc. Trans. , vol.42 , pp. 1229-1237
    • Smith, R.W.P.1    Blee, T.K.P.2    Gray, N.K.3
  • 63
    • 0017806321 scopus 로고
    • Influence of 5′-terminal cap structure on the initiation of translation of vaccinia virus mRNA
    • Muthukrishnan, S., Moss, B., Cooper, J.A. and Maxwell, E.S. (1978) Influence of 5′-terminal cap structure on the initiation of translation of vaccinia virus mRNA. J. Biol. Chem., 253, 1710-1715.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1710-1715
    • Muthukrishnan, S.1    Moss, B.2    Cooper, J.A.3    Maxwell, E.S.4
  • 64
    • 0032126521 scopus 로고    scopus 로고
    • Cap ribose methylation of c-mos mRNA stimulates translation and oocyte maturation in Xenopus laevis
    • Kuge, H. (1998) Cap ribose methylation of c-mos mRNA stimulates translation and oocyte maturation in Xenopus laevis. Nucleic Acids Res., 26, 3208-3214.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3208-3214
    • Kuge, H.1
  • 66
    • 84883759334 scopus 로고    scopus 로고
    • RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner
    • Peisley, A., Wu, B., Yao, H., Walz, T. and Hur, S. (2013) RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner. Mol. Cell, 51, 573-583.
    • (2013) Mol. Cell , vol.51 , pp. 573-583
    • Peisley, A.1    Wu, B.2    Yao, H.3    Walz, T.4    Hur, S.5
  • 69
    • 84926104091 scopus 로고    scopus 로고
    • The innate immune sensor LGP2 activates antiviral signaling by regulating MDA5-RNA interaction and filament assembly
    • Bruns, A.M., Leser, G.P., Lamb, R.A. and Horvath, C.M. (2014) The innate immune sensor LGP2 activates antiviral signaling by regulating MDA5-RNA interaction and filament assembly. Mol. Cell, 55, 771-781.
    • (2014) Mol. Cell , vol.55 , pp. 771-781
    • Bruns, A.M.1    Leser, G.P.2    Lamb, R.A.3    Horvath, C.M.4
  • 71
    • 84869845792 scopus 로고    scopus 로고
    • A structure-based model of RIG-I activation
    • Kolakofsky, D., Kowalinski, E. and Cusack, S. (2012) A structure-based model of RIG-I activation. RNA, 18, 2118-2127.
    • (2012) RNA , vol.18 , pp. 2118-2127
    • Kolakofsky, D.1    Kowalinski, E.2    Cusack, S.3
  • 78
    • 84874671928 scopus 로고    scopus 로고
    • Structural basis for viral 5′-PPP-RNA recognition by human IFIT proteins
    • Abbas, Y.M., Pichlmair, A., Gorna, M.W., Superti-Furga, G. and Nagar, B. (2013) Structural basis for viral 5′-PPP-RNA recognition by human IFIT proteins. Nature, 494, 60-64.
    • (2013) Nature , vol.494 , pp. 60-64
    • Abbas, Y.M.1    Pichlmair, A.2    Gorna, M.W.3    Superti-Furga, G.4    Nagar, B.5
  • 79
    • 84929374105 scopus 로고    scopus 로고
    • Innate immune restriction and antagonism of viral RNA lacking 2′-O methylation
    • Hyde, J.L. and Diamond, M.S. (2015) Innate immune restriction and antagonism of viral RNA lacking 2′-O methylation. Virology, 479-480, 66-74.
    • (2015) Virology , vol.479-480 , pp. 66-74
    • Hyde, J.L.1    Diamond, M.S.2
  • 80
    • 84908309281 scopus 로고    scopus 로고
    • IFIT1: A dual sensor and effector molecule that detects non-2′-O methylated viral RNA and inhibits its translation
    • Diamond, M.S. (2014) IFIT1: A dual sensor and effector molecule that detects non-2′-O methylated viral RNA and inhibits its translation. Cytokine Growth Factor Rev., 25, 543-550.
    • (2014) Cytokine Growth Factor Rev. , vol.25 , pp. 543-550
    • Diamond, M.S.1
  • 81
    • 84897952004 scopus 로고    scopus 로고
    • Inhibition of translation by IFIT family members is determined by their ability to interact selectively with the 5′-terminal regions of cap0-, cap1- and 5′pppmRNAs
    • Kumar, P., Sweeney, T.R., Skabkin, M.A., Skabkina, O. V, Hellen, C.U.T. and Pestova, T. V (2014) Inhibition of translation by IFIT family members is determined by their ability to interact selectively with the 5′-terminal regions of cap0-, cap1- and 5′pppmRNAs. Nucleic Acids Res., 42, 3228-3245.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 3228-3245
    • Kumar, P.1    Sweeney, T.R.2    Skabkin, M.A.3    Skabkina, O.V.4    Hellen, C.U.T.5    Pestova, T.V.6
  • 82
    • 84884157315 scopus 로고    scopus 로고
    • Master sensors of pathogenic RNA - RIG-I like receptors
    • Schlee, M. (2013) Master sensors of pathogenic RNA - RIG-I like receptors. Immunobiology, 218, 1322-1335.
    • (2013) Immunobiology , vol.218 , pp. 1322-1335
    • Schlee, M.1
  • 83
    • 0035873620 scopus 로고    scopus 로고
    • Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme
    • Changela, A., Ho, C.K., Martins, A., Shuman, S. and Mondragon, A. (2001) Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme. EMBO J., 20, 2575-2586.
    • (2001) EMBO J. , vol.20 , pp. 2575-2586
    • Changela, A.1    Ho, C.K.2    Martins, A.3    Shuman, S.4    Mondragon, A.5
  • 84
    • 0035907366 scopus 로고    scopus 로고
    • Structure-function analysis of the active site tunnel of yeast RNA triphosphatase
    • Bisaillon, M. and Shuman, S. (2001) Structure-function analysis of the active site tunnel of yeast RNA triphosphatase. J. Biol. Chem., 276, 17261-17266.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17261-17266
    • Bisaillon, M.1    Shuman, S.2
  • 85
    • 0037013218 scopus 로고    scopus 로고
    • Chlorella virus RNA triphosphatase. Mutational analysis and mechanism of inhibition by tripolyphosphate
    • Gong, C. and Shuman, S. (2002) Chlorella virus RNA triphosphatase. Mutational analysis and mechanism of inhibition by tripolyphosphate. J. Biol. Chem., 277, 15317-15324.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15317-15324
    • Gong, C.1    Shuman, S.2
  • 86
    • 44849109378 scopus 로고    scopus 로고
    • Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase
    • Song, J., Bettendorff, L., Tonelli, M. and Markley, J.L. (2008) Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase. J. Biol. Chem., 283, 10939-10948.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10939-10948
    • Song, J.1    Bettendorff, L.2    Tonelli, M.3    Markley, J.L.4
  • 88
    • 57649155902 scopus 로고    scopus 로고
    • Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme
    • Jain, R. and Shuman, S. (2008) Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme. J. Biol. Chem., 283, 31047-31057.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31047-31057
    • Jain, R.1    Shuman, S.2
  • 89
    • 84886798108 scopus 로고    scopus 로고
    • Crystal structure and biochemical analyses reveal that the Arabidopsis triphosphate tunnel metalloenzyme AtTTM3 is a tripolyphosphatase involved in root development
    • Moeder, W., Garcia-Petit, C., Ung, H., Fucile, G., Samuel, M.A., Christendat, D. and Yoshioka, K. (2013) Crystal structure and biochemical analyses reveal that the Arabidopsis triphosphate tunnel metalloenzyme AtTTM3 is a tripolyphosphatase involved in root development. Plant J., 76, 615-626.
    • (2013) Plant J. , vol.76 , pp. 615-626
    • Moeder, W.1    Garcia-Petit, C.2    Ung, H.3    Fucile, G.4    Samuel, M.A.5    Christendat, D.6    Yoshioka, K.7
  • 91
    • 84942890966 scopus 로고    scopus 로고
    • Structural determinants for substrate binding and catalysis in triphosphate tunnel metalloenzymes
    • Martinez, J., Truffault, V. and Hothorn, M. (2015) Structural determinants for substrate binding and catalysis in triphosphate tunnel metalloenzymes. J. Biol. Chem., 290, 23348-23360.
    • (2015) J. Biol. Chem. , vol.290 , pp. 23348-23360
    • Martinez, J.1    Truffault, V.2    Hothorn, M.3
  • 92
    • 0033601125 scopus 로고    scopus 로고
    • Structure and mechanism of yeast RNA triphosphatase: An essential component of the mRNA capping apparatus
    • Lima, C.D., Wang, L.K. and Shuman, S. (1999) Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus. Cell, 99, 533-543.
    • (1999) Cell , vol.99 , pp. 533-543
    • Lima, C.D.1    Wang, L.K.2    Shuman, S.3
  • 93
    • 9944230069 scopus 로고    scopus 로고
    • The polynucleotide ligase and RNA capping enzyme superfamily of covalent nucleotidyltransferases
    • Shuman, S. and Lima, C.D. (2004) The polynucleotide ligase and RNA capping enzyme superfamily of covalent nucleotidyltransferases. Curr. Opin. Struct. Biol., 14, 757-764.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 757-764
    • Shuman, S.1    Lima, C.D.2
  • 94
    • 0028172876 scopus 로고
    • Covalent catalysis in nucleotidyl transfer reactions: Essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligases
    • Shuman, S., Liu, Y. and Schwer, B. (1994) Covalent catalysis in nucleotidyl transfer reactions: essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligases. Proc. Natl. Acad. Sci. U.S.A., 91, 12046-12050.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12046-12050
    • Shuman, S.1    Liu, Y.2    Schwer, B.3
  • 95
    • 0000262312 scopus 로고
    • Mechanism of mRNA capping by vaccinia virus guanylyltransferase: Characterization of an enzyme-guanylate intermediate
    • Shuman, S. and Hurwitz, J. (1981) Mechanism of mRNA capping by vaccinia virus guanylyltransferase: characterization of an enzyme-guanylate intermediate. Proc. Natl. Acad. Sci. U.S.A., 78, 187-191.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 187-191
    • Shuman, S.1    Hurwitz, J.2
  • 96
    • 41149117977 scopus 로고    scopus 로고
    • Kinetic and thermodynamic characterization of the RNA guanylyltransferase reaction
    • Souliere, M.F., Perreault, J.-P. and Bisaillon, M. (2008) Kinetic and thermodynamic characterization of the RNA guanylyltransferase reaction. Biochemistry, 47, 3863-3874.
    • (2008) Biochemistry , vol.47 , pp. 3863-3874
    • Souliere, M.F.1    Perreault, J.-P.2    Bisaillon, M.3
  • 98
    • 0036913982 scopus 로고    scopus 로고
    • OB-fold domains: A snapshot of the evolution of sequence, structure and function
    • Arcus, V. (2002) OB-fold domains: a snapshot of the evolution of sequence, structure and function. Curr. Opin. Struct. Biol., 12, 794-801.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 794-801
    • Arcus, V.1
  • 99
    • 77954589779 scopus 로고    scopus 로고
    • Oligonucleotide/oligosaccharide-binding fold proteins: A growing family of genome guardians
    • Flynn, R.L. and Zou, L. (2010) Oligonucleotide/oligosaccharide-binding fold proteins: a growing family of genome guardians. Crit. Rev. Biochem. Mol. Biol., 45, 266-275.
    • (2010) Crit. Rev. Biochem. Mol. Biol. , vol.45 , pp. 266-275
    • Flynn, R.L.1    Zou, L.2
  • 100
    • 0038228666 scopus 로고    scopus 로고
    • X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes
    • Hakansson, K., Doherty, A.J., Shuman, S. and Wigley, D.B. (1997) X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes. Cell, 89, 545-553.
    • (1997) Cell , vol.89 , pp. 545-553
    • Hakansson, K.1    Doherty, A.J.2    Shuman, S.3    Wigley, D.B.4
  • 101
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • Schubert, H.L., Blumenthal, R.M. and Cheng, X. (2003) Many paths to methyltransfer: a chronicle of convergence. Trends Biochem. Sci., 28, 329-335.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 102
    • 84924917866 scopus 로고    scopus 로고
    • RNA methyltransferases involved in 5′ cap biosynthesis
    • Byszewska, M., Smietanski, M., Purta, E. and Bujnicki, J.M. (2014) RNA methyltransferases involved in 5′ cap biosynthesis. RNA Biol., 11, 1597-1607.
    • (2014) RNA Biol. , vol.11 , pp. 1597-1607
    • Byszewska, M.1    Smietanski, M.2    Purta, E.3    Bujnicki, J.M.4
  • 103
    • 33749985758 scopus 로고    scopus 로고
    • Structure, function and mechanism of exocyclic DNA methyltransferases
    • Bheemanaik, S., Reddy, Y.V.R. and Rao, D.N. (2006) Structure, function and mechanism of exocyclic DNA methyltransferases. Biochem. J., 399, 177-190.
    • (2006) Biochem. J. , vol.399 , pp. 177-190
    • Bheemanaik, S.1    Reddy, Y.V.R.2    Rao, D.N.3
  • 104
    • 1642482865 scopus 로고    scopus 로고
    • Structure and mechanism of mRNA cap (guanine-N7) methyltransferase
    • Fabrega, C., Hausmann, S., Shen, V., Shuman, S. and Lima, C.D. (2004) Structure and mechanism of mRNA cap (guanine-N7) methyltransferase. Mol. Cell, 13, 77-89.
    • (2004) Mol. Cell , vol.13 , pp. 77-89
    • Fabrega, C.1    Hausmann, S.2    Shen, V.3    Shuman, S.4    Lima, C.D.5
  • 106
    • 71949113286 scopus 로고    scopus 로고
    • S-adenosyl homocysteine hydrolase is required for Myc-induced mRNA cap methylation, protein synthesis and cell proliferation
    • Fernandez-Sanchez, M.E., Gonatopoulos-Pournatzis, T., Preston, G., Lawlor, M.A. and Cowling, V.H. (2009) S-adenosyl homocysteine hydrolase is required for Myc-induced mRNA cap methylation, protein synthesis, and cell proliferation. Mol. Cell. Biol., 29, 6182-6191.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 6182-6191
    • Fernandez-Sanchez, M.E.1    Gonatopoulos-Pournatzis, T.2    Preston, G.3    Lawlor, M.A.4    Cowling, V.H.5
  • 107
    • 62049085499 scopus 로고    scopus 로고
    • Specific regulation of mRNA cap methylation by the c-Myc and E2F1 transcription factors
    • Cole, M.D. and Cowling, V.H. (2009) Specific regulation of mRNA cap methylation by the c-Myc and E2F1 transcription factors. Oncogene, 28, 1169-1175.
    • (2009) Oncogene , vol.28 , pp. 1169-1175
    • Cole, M.D.1    Cowling, V.H.2
  • 109
    • 84884242540 scopus 로고    scopus 로고
    • Human cap methyltransferase (RNMT) N-terminal non-catalytic domain mediates recruitment to transcription initiation sites
    • Aregger, M. and Cowling, V.H. (2013) Human cap methyltransferase (RNMT) N-terminal non-catalytic domain mediates recruitment to transcription initiation sites. Biochem. J., 455, 67-73.
    • (2013) Biochem. J. , vol.455 , pp. 67-73
    • Aregger, M.1    Cowling, V.H.2
  • 111
    • 0028833053 scopus 로고
    • Reaction in alphavirus mRNA capping: Formation of a covalent complex of nonstructural protein nsP1 with 7-methyl-GMP
    • Ahola, T. and Kaariainen, L. (1995) Reaction in alphavirus mRNA capping: formation of a covalent complex of nonstructural protein nsP1 with 7-methyl-GMP. Proc. Natl. Acad. Sci. U.S.A., 92, 507-511.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 507-511
    • Ahola, T.1    Kaariainen, L.2
  • 112
    • 0034625437 scopus 로고    scopus 로고
    • Identification of a novel function of the alphavirus capping apparatus. RNA 5′-triphosphatase activity of Nsp2
    • Vasiljeva, L., Merits, A., Auvinen, P. and Kaariainen, L. (2000) Identification of a novel function of the alphavirus capping apparatus. RNA 5′-triphosphatase activity of Nsp2. J. Biol. Chem., 275, 17281-17287.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17281-17287
    • Vasiljeva, L.1    Merits, A.2    Auvinen, P.3    Kaariainen, L.4
  • 113
    • 0034633849 scopus 로고    scopus 로고
    • Suppressor mutations that allow sindbis virus RNA polymerase to function with nonaromatic amino acids at the N-terminus: Evidence for interaction between nsP1 and nsP4 in minus-strand RNA synthesis
    • Shirako, Y., Strauss, E.G. and Strauss, J.H. (2000) Suppressor mutations that allow sindbis virus RNA polymerase to function with nonaromatic amino acids at the N-terminus: evidence for interaction between nsP1 and nsP4 in minus-strand RNA synthesis. Virology, 276, 148-160.
    • (2000) Virology , vol.276 , pp. 148-160
    • Shirako, Y.1    Strauss, E.G.2    Strauss, J.H.3
  • 114
    • 0036333797 scopus 로고    scopus 로고
    • Modification of Asn374 of nsP1 suppresses a Sindbis virus nsP4 minus-strand polymerase mutant
    • Fata, C.L., Sawicki, S.G. and Sawicki, D.L. (2002) Modification of Asn374 of nsP1 suppresses a Sindbis virus nsP4 minus-strand polymerase mutant. J. Virol., 76, 8641-8649.
    • (2002) J. Virol. , vol.76 , pp. 8641-8649
    • Fata, C.L.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 115
    • 33744795205 scopus 로고    scopus 로고
    • A unique strategy for mRNA cap methylation used by vesicular stomatitis virus
    • Li, J., Wang, J.T. and Whelan, S.P.J. (2006) A unique strategy for mRNA cap methylation used by vesicular stomatitis virus. Proc. Natl. Acad. Sci. U.S.A., 103, 8493-8498.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 8493-8498
    • Li, J.1    Wang, J.T.2    Whelan, S.P.J.3
  • 116
    • 33845992557 scopus 로고    scopus 로고
    • Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus
    • Ogino, T. and Banerjee, A.K. (2007) Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus. Mol. Cell, 25, 85-97.
    • (2007) Mol. Cell , vol.25 , pp. 85-97
    • Ogino, T.1    Banerjee, A.K.2
  • 117
    • 77649260792 scopus 로고    scopus 로고
    • Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase
    • Ogino, T., Yadav, S.P. and Banerjee, A.K. (2010) Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase. Proc. Natl. Acad. Sci. U.S.A., 107, 3463-3468.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 3463-3468
    • Ogino, T.1    Yadav, S.P.2    Banerjee, A.K.3
  • 118
    • 84875258948 scopus 로고    scopus 로고
    • In vitro capping and transcription of rhabdoviruses
    • Ogino, T. (2013) In vitro capping and transcription of rhabdoviruses. Methods, 59, 188-198.
    • (2013) Methods , vol.59 , pp. 188-198
    • Ogino, T.1
  • 120
    • 42449160175 scopus 로고    scopus 로고
    • West Nile virus methyltransferase catalyzes two methylations of the viral RNA cap through a substrate-repositioning mechanism
    • Dong, H., Ren, S., Zhang, B., Zhou, Y., Puig-Basagoiti, F., Li, H. and Shi, P.-Y. (2008) West Nile virus methyltransferase catalyzes two methylations of the viral RNA cap through a substrate-repositioning mechanism. J. Virol., 82, 4295-4307.
    • (2008) J. Virol. , vol.82 , pp. 4295-4307
    • Dong, H.1    Ren, S.2    Zhang, B.3    Zhou, Y.4    Puig-Basagoiti, F.5    Li, H.6    Shi, P.-Y.7
  • 121
    • 0028239360 scopus 로고
    • The mRNA (guanine-7-)methyltransferase domain of the vaccinia virus mRNA capping enzyme. Expression in Escherichia coli and structural and kinetic comparison to the intact capping enzyme
    • Higman, M.A., Christen, L.A. and Niles, E.G. (1994) The mRNA (guanine-7-)methyltransferase domain of the vaccinia virus mRNA capping enzyme. Expression in Escherichia coli and structural and kinetic comparison to the intact capping enzyme. J. Biol. Chem., 269, 14974-14981.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14974-14981
    • Higman, M.A.1    Christen, L.A.2    Niles, E.G.3
  • 122
    • 0028088458 scopus 로고
    • Intrinsic RNA (guanine-7) methyltransferase activity of the vaccinia virus capping enzyme D1 subunit is stimulated by the D12 subunit. Identification of amino acid residues in the D1 protein required for subunit association and methyl group transfer
    • Mao, X. and Shuman, S. (1994) Intrinsic RNA (guanine-7) methyltransferase activity of the vaccinia virus capping enzyme D1 subunit is stimulated by the D12 subunit. Identification of amino acid residues in the D1 protein required for subunit association and methyl group transfer. J. Biol. Chem., 269, 24472-24479.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24472-24479
    • Mao, X.1    Shuman, S.2
  • 123
    • 33746518147 scopus 로고    scopus 로고
    • Genetic analysis of poxvirus mRNA cap methyltransferase: Suppression of conditional mutations in the stimulatory D12 subunit by second-site mutations in the catalytic D1 subunit
    • Schwer, B. and Shuman, S. (2006) Genetic analysis of poxvirus mRNA cap methyltransferase: Suppression of conditional mutations in the stimulatory D12 subunit by second-site mutations in the catalytic D1 subunit. Virology, 352, 145-156.
    • (2006) Virology , vol.352 , pp. 145-156
    • Schwer, B.1    Shuman, S.2
  • 124
    • 36549088581 scopus 로고    scopus 로고
    • Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferase
    • De La Pea, M., Kyrieleis, O.J.P. and Cusack, S. (2007) Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferase. EMBO J., 26, 4913-4925.
    • (2007) EMBO J. , vol.26 , pp. 4913-4925
    • De La Pea, M.1    Kyrieleis, O.J.P.2    Cusack, S.3
  • 125
    • 84895774578 scopus 로고    scopus 로고
    • Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus
    • Kyrieleis, O.J., Chang, J., de la Pena, M., Shuman, S. and Cusack, S. (2014) Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus. Structure, 22, 452-465.
    • (2014) Structure , vol.22 , pp. 452-465
    • Kyrieleis, O.J.1    Chang, J.2    De La Pena, M.3    Shuman, S.4    Cusack, S.5
  • 126
    • 0026778224 scopus 로고
    • The expressed VP4 protein of bluetongue virus binds GTP and is the candidate guanylyl transferase of the virus
    • Le Blois, H., French, T., Mertens, P.P., Burroughs, J.N. and Roy, P. (1992) The expressed VP4 protein of bluetongue virus binds GTP and is the candidate guanylyl transferase of the virus. Virology, 189, 757-761.
    • (1992) Virology , vol.189 , pp. 757-761
    • Le Blois, H.1    French, T.2    Mertens, P.P.3    Burroughs, J.N.4    Roy, P.5
  • 127
    • 0032584782 scopus 로고    scopus 로고
    • Guanylyltransferase and RNA 5′-triphosphatase activities of the purified expressed VP4 protein of bluetongue virus
    • Martinez-Costas, J., Sutton, G., Ramadevi, N. and Roy, P. (1998) Guanylyltransferase and RNA 5′-triphosphatase activities of the purified expressed VP4 protein of bluetongue virus. J. Mol. Biol., 280, 859-866.
    • (1998) J. Mol. Biol. , vol.280 , pp. 859-866
    • Martinez-Costas, J.1    Sutton, G.2    Ramadevi, N.3    Roy, P.4
  • 128
    • 0032506128 scopus 로고    scopus 로고
    • Capping and methylation of mRNA by purified recombinant VP4 protein of bluetongue virus
    • Ramadevi, N., Burroughs, N.J., Mertens, P.P., Jones, I.M. and Roy, P. (1998) Capping and methylation of mRNA by purified recombinant VP4 protein of bluetongue virus. Proc. Natl. Acad. Sci. U.S.A., 95, 13537-13542.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13537-13542
    • Ramadevi, N.1    Burroughs, N.J.2    Mertens, P.P.3    Jones, I.M.4    Roy, P.5
  • 129
    • 0031901745 scopus 로고    scopus 로고
    • A leucine zipper-like domain is essential for dimerization and encapsidation of bluetongue virus nucleocapsid protein VP4
    • Ramadevi, N., Rodriguez, J. and Roy, P. (1998) A leucine zipper-like domain is essential for dimerization and encapsidation of bluetongue virus nucleocapsid protein VP4. J. Virol., 72, 2983-2990.
    • (1998) J. Virol. , vol.72 , pp. 2983-2990
    • Ramadevi, N.1    Rodriguez, J.2    Roy, P.3
  • 130
    • 67649552964 scopus 로고    scopus 로고
    • Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase
    • Sugiyama, K., Obayashi, E., Kawaguchi, A., Suzuki, Y., Tame, J.R.H., Nagata, K. and Park, S.-Y. (2009) Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase. EMBO J., 28, 1803-1811.
    • (2009) EMBO J. , vol.28 , pp. 1803-1811
    • Sugiyama, K.1    Obayashi, E.2    Kawaguchi, A.3    Suzuki, Y.4    Tame, J.R.H.5    Nagata, K.6    Park, S.-Y.7
  • 132
    • 73949092407 scopus 로고    scopus 로고
    • Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy
    • Huet, S., Avilov, S. V, Ferbitz, L., Daigle, N., Cusack, S. and Ellenberg, J. (2010) Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy. J. Virol., 84, 1254-1264.
    • (2010) J. Virol. , vol.84 , pp. 1254-1264
    • Huet, S.1    Avilov, S.V.2    Ferbitz, L.3    Daigle, N.4    Cusack, S.5    Ellenberg, J.6
  • 134
    • 0018459347 scopus 로고
    • Transfer of 5′-terminal cap of globin mRNA to influenza viral complementary RNA during transcription in vitro
    • Plotch, S.J., Bouloy, M. and Krug, R.M. (1979) Transfer of 5′-terminal cap of globin mRNA to influenza viral complementary RNA during transcription in vitro. Proc. Natl. Acad. Sci. U.S.A., 76, 1618-1622.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 1618-1622
    • Plotch, S.J.1    Bouloy, M.2    Krug, R.M.3
  • 135
    • 0019394947 scopus 로고
    • A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription
    • Plotch, S.J., Bouloy, M., Ulmanen, I. and Krug, R.M. (1981) A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription. Cell, 23, 847-858.
    • (1981) Cell , vol.23 , pp. 847-858
    • Plotch, S.J.1    Bouloy, M.2    Ulmanen, I.3    Krug, R.M.4
  • 136
    • 77749322610 scopus 로고    scopus 로고
    • Towards an atomic resolution understanding of the influenza virus replication machinery
    • Ruigrok, R.W., Crepin, T., Hart, D.J. and Cusack, S. (2010) Towards an atomic resolution understanding of the influenza virus replication machinery. Curr. Opin. Struct. Biol., 20, 104-113.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 104-113
    • Ruigrok, R.W.1    Crepin, T.2    Hart, D.J.3    Cusack, S.4
  • 137
    • 0018703697 scopus 로고
    • Are the 5′ ends of influenza viral mRNAs synthesized in vivo donated by host mRNAs?
    • Krug, R.M., Broni, B.A. and Bouloy, M. (1979) Are the 5′ ends of influenza viral mRNAs synthesized in vivo donated by host mRNAs? Cell, 18, 329-334.
    • (1979) Cell , vol.18 , pp. 329-334
    • Krug, R.M.1    Broni, B.A.2    Bouloy, M.3
  • 139
    • 84859741035 scopus 로고    scopus 로고
    • Cap snatching of yeast L-A double-stranded RNA virus can operate in trans and requires viral polymerase actively engaging in transcription
    • Fujimura, T. and Esteban, R. (2012) Cap snatching of yeast L-A double-stranded RNA virus can operate in trans and requires viral polymerase actively engaging in transcription. J. Biol. Chem., 287, 12797-12804.
    • (2012) J. Biol. Chem. , vol.287 , pp. 12797-12804
    • Fujimura, T.1    Esteban, R.2
  • 140
    • 80055082823 scopus 로고    scopus 로고
    • Cap-snatching mechanism in yeast L-A double-stranded RNA virus
    • Fujimura, T. and Esteban, R. (2011) Cap-snatching mechanism in yeast L-A double-stranded RNA virus. Proc. Natl. Acad. Sci. U.S.A., 108, 17667-17671.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 17667-17671
    • Fujimura, T.1    Esteban, R.2
  • 141
    • 84882367190 scopus 로고    scopus 로고
    • Cap snatching in yeast L-BC double-stranded RNA totivirus
    • Fujimura, T. and Esteban, R. (2013) Cap snatching in yeast L-BC double-stranded RNA totivirus. J. Biol. Chem., 288, 23716-23724.
    • (2013) J. Biol. Chem. , vol.288 , pp. 23716-23724
    • Fujimura, T.1    Esteban, R.2
  • 142
    • 0026668288 scopus 로고
    • The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA
    • Blanc, A., Goyer, C. and Sonenberg, N. (1992) The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA. Mol. Cell. Biol., 12, 3390-3398.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3390-3398
    • Blanc, A.1    Goyer, C.2    Sonenberg, N.3
  • 143
    • 0028231420 scopus 로고
    • His-154 is involved in the linkage of the Saccharomyces cerevisiae L-A double-stranded RNA virus Gag protein to the cap structure of mRNAs and is essential for M1 satellite virus expression
    • Blanc, A., Ribas, J.C., Wickner, R.B. and Sonenberg, N. (1994) His-154 is involved in the linkage of the Saccharomyces cerevisiae L-A double-stranded RNA virus Gag protein to the cap structure of mRNAs and is essential for M1 satellite virus expression. Mol. Cell. Biol., 14, 2664-2674.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2664-2674
    • Blanc, A.1    Ribas, J.C.2    Wickner, R.B.3    Sonenberg, N.4
  • 144
    • 84990248408 scopus 로고    scopus 로고
    • Efficient preparation and properties of mRNAs containing a fluorescent cap analog: Anthraniloyl-m(7)GpppG
    • Gunawardana, D., Domashevskiy, A. V, Gayler, K.R. and Goss, D.J. (2015) Efficient preparation and properties of mRNAs containing a fluorescent cap analog: Anthraniloyl-m(7)GpppG. Transl. (Austin, Tex.), 3, e988538.
    • (2015) Transl. (Austin, Tex. , vol.3 , pp. e988538
    • Gunawardana, D.1    Domashevskiy, A.V.2    Gayler, K.R.3    Goss, D.J.4
  • 145
    • 85007602707 scopus 로고    scopus 로고
    • A novel enrichment strategy reveals unprecedented number of novel transcription start sites at single base resolution in a model prokaryote and the gut microbiome
    • Ettwiller, L., Buswell, J., Yigit, E. and Schildkraut, I. (2016) A novel enrichment strategy reveals unprecedented number of novel transcription start sites at single base resolution in a model prokaryote and the gut microbiome. BMC Genomics, 17, 199.
    • (2016) BMC Genomics , vol.17 , pp. 199
    • Ettwiller, L.1    Buswell, J.2    Yigit, E.3    Schildkraut, I.4
  • 146
    • 84912080017 scopus 로고    scopus 로고
    • Synthetic mRNAs for manipulating cellular phenotypes: An overview
    • Quabius, E.S. and Krupp, G. (2015) Synthetic mRNAs for manipulating cellular phenotypes: an overview. N. Biotechnol., 32, 229-235.
    • (2015) N. Biotechnol. , vol.32 , pp. 229-235
    • Quabius, E.S.1    Krupp, G.2
  • 147
    • 84923775885 scopus 로고    scopus 로고
    • Efficient delivery and functional expression of transfected modified mRNA in human embryonic stem cell-derived retinal pigmented epithelial cells
    • Hansson, M.L., Albert, S., Gonzalez Somermeyer, L., Peco, R., Mejia-Ramirez, E., Montserrat, N. and Izpisua Belmonte, J.C. (2015) Efficient delivery and functional expression of transfected modified mRNA in human embryonic stem cell-derived retinal pigmented epithelial cells. J. Biol. Chem., 290, 5661-5672.
    • (2015) J. Biol. Chem. , vol.290 , pp. 5661-5672
    • Hansson, M.L.1    Albert, S.2    Gonzalez Somermeyer, L.3    Peco, R.4    Mejia-Ramirez, E.5    Montserrat, N.6    Izpisua Belmonte, J.C.7
  • 148
    • 77958536106 scopus 로고    scopus 로고
    • Highly efficient reprogramming to pluripotency and directed differentiation of human cells with synthetic modified mRNA
    • Warren, L., Manos, P.D., Ahfeldt, T., Loh, Y.-H., Li, H., Lau, F., Ebina, W., Mandal, P.K., Smith, Z.D., Meissner, A., et al. (2010) Highly efficient reprogramming to pluripotency and directed differentiation of human cells with synthetic modified mRNA. Cell Stem Cell, 7, 618-630.
    • (2010) Cell Stem Cell , vol.7 , pp. 618-630
    • Warren, L.1    Manos, P.D.2    Ahfeldt, T.3    Loh, Y.-H.4    Li, H.5    Lau, F.6    Ebina, W.7    Mandal, P.K.8    Smith, Z.D.9    Meissner, A.10
  • 149
    • 84897571877 scopus 로고    scopus 로고
    • Optimized conditions for successful transfection of human endothelial cells with in vitro synthesized and modified mRNA for induction of protein expression
    • Avci-Adali, M., Behring, A., Keller, T., Krajewski, S., Schlensak, C. and Wendel, H.P. (2014) Optimized conditions for successful transfection of human endothelial cells with in vitro synthesized and modified mRNA for induction of protein expression. J. Biol. Eng., 8, 8.
    • (2014) J. Biol. Eng. , vol.8 , pp. 8
    • Avci-Adali, M.1    Behring, A.2    Keller, T.3    Krajewski, S.4    Schlensak, C.5    Wendel, H.P.6
  • 152
    • 84875202495 scopus 로고    scopus 로고
    • RNA-based vaccination: Sending a strong message
    • Weiner, D.B. (2013) RNA-based vaccination: sending a strong message. Mol. Ther., 21, 506-508.
    • (2013) Mol. Ther. , vol.21 , pp. 506-508
    • Weiner, D.B.1
  • 154
    • 84874724470 scopus 로고    scopus 로고
    • mRNA: From a chemical blueprint for protein production to an off-the-shelf therapeutic
    • Van Lint, S., Heirman, C., Thielemans, K. and Breckpot, K. (2013) mRNA: From a chemical blueprint for protein production to an off-the-shelf therapeutic. Hum. Vaccin. Immunother., 9, 265-274.
    • (2013) Hum. Vaccin. Immunother. , vol.9 , pp. 265-274
    • Van Lint, S.1    Heirman, C.2    Thielemans, K.3    Breckpot, K.4
  • 155
    • 34447633941 scopus 로고    scopus 로고
    • Spontaneous cellular uptake of exogenous messenger RNA in vivo is nucleic acid-specific, saturable and ion dependent
    • Probst, J., Weide, B., Scheel, B., Pichler, B.J., Hoerr, I., Rammensee, H.-G. and Pascolo, S. (2007) Spontaneous cellular uptake of exogenous messenger RNA in vivo is nucleic acid-specific, saturable and ion dependent. Gene Ther., 14, 1175-1180.
    • (2007) Gene Ther. , vol.14 , pp. 1175-1180
    • Probst, J.1    Weide, B.2    Scheel, B.3    Pichler, B.J.4    Hoerr, I.5    Rammensee, H.-G.6    Pascolo, S.7
  • 156
    • 84902097227 scopus 로고    scopus 로고
    • Intranasal mRNA nanoparticle vaccination induces prophylactic and therapeutic anti-tumor immunity
    • Phua, K.K.L., Staats, H.F., Leong, K.W. and Nair, S.K. (2014) Intranasal mRNA nanoparticle vaccination induces prophylactic and therapeutic anti-tumor immunity. Sci. Rep., 4, 5128.
    • (2014) Sci. Rep. , vol.4 , pp. 5128
    • Phua, K.K.L.1    Staats, H.F.2    Leong, K.W.3    Nair, S.K.4
  • 158
    • 0034984898 scopus 로고    scopus 로고
    • Nonviral gene delivery to the lateral ventricles in rat brain: Initial evidence for widespread distribution and expression in the central nervous system
    • Hecker, J.G., Hall, L.L. and Irion, V.R. (2001) Nonviral gene delivery to the lateral ventricles in rat brain: initial evidence for widespread distribution and expression in the central nervous system. Mol. Ther., 3, 375-384.
    • (2001) Mol. Ther. , vol.3 , pp. 375-384
    • Hecker, J.G.1    Hall, L.L.2    Irion, V.R.3
  • 159
    • 0037429077 scopus 로고    scopus 로고
    • Stability of mRNA/cationic lipid lipoplexes in human and rat cerebrospinal fluid: Methods and evidence for nonviral mRNA gene delivery to the central nervous system
    • Anderson, D.M., Hall, L.L., Ayyalapu, A.R., Irion, V.R., Nantz, M.H. and Hecker, J.G. (2003) Stability of mRNA/cationic lipid lipoplexes in human and rat cerebrospinal fluid: methods and evidence for nonviral mRNA gene delivery to the central nervous system. Hum. Gene Ther., 14, 191-202.
    • (2003) Hum. Gene Ther. , vol.14 , pp. 191-202
    • Anderson, D.M.1    Hall, L.L.2    Ayyalapu, A.R.3    Irion, V.R.4    Nantz, M.H.5    Hecker, J.G.6
  • 161
    • 84860539841 scopus 로고    scopus 로고
    • Increased erythropoiesis in mice injected with submicrogram quantities of pseudouridine-containing mRNA encoding erythropoietin
    • Kariko, K., Muramatsu, H., Keller, J.M. and Weissman, D. (2012) Increased erythropoiesis in mice injected with submicrogram quantities of pseudouridine-containing mRNA encoding erythropoietin. Mol. Ther., 20, 948-953.
    • (2012) Mol. Ther. , vol.20 , pp. 948-953
    • Kariko, K.1    Muramatsu, H.2    Keller, J.M.3    Weissman, D.4
  • 162
    • 23844464444 scopus 로고    scopus 로고
    • Suppression of RNA recognition by Toll-like receptors: The impact of nucleoside modification and the evolutionary origin of RNA
    • Kariko, K., Buckstein, M., Ni, H. and Weissman, D. (2005) Suppression of RNA recognition by Toll-like receptors: the impact of nucleoside modification and the evolutionary origin of RNA. Immunity, 23, 165-175.
    • (2005) Immunity , vol.23 , pp. 165-175
    • Kariko, K.1    Buckstein, M.2    Ni, H.3    Weissman, D.4
  • 164
    • 84921345772 scopus 로고    scopus 로고
    • Introduction to RNA-based vaccines and therapeutics
    • Geall, A.J. and Ulmer, J.B. (2015) Introduction to RNA-based vaccines and therapeutics. Expert Rev. Vaccines, 14, 151-152.
    • (2015) Expert Rev. Vaccines , vol.14 , pp. 151-152
    • Geall, A.J.1    Ulmer, J.B.2
  • 170
    • 84862891254 scopus 로고    scopus 로고
    • Highly potent mRNA based cancer vaccines represent an attractive platform for combination therapies supporting an improved therapeutic effect
    • Fotin-Mleczek, M., Zanzinger, K., Heidenreich, R., Lorenz, C., Thess, A., Duchardt, K.M. and Kallen, K.-J. (2012) Highly potent mRNA based cancer vaccines represent an attractive platform for combination therapies supporting an improved therapeutic effect. J. Gene Med., 14, 428-439.
    • (2012) J. Gene Med. , vol.14 , pp. 428-439
    • Fotin-Mleczek, M.1    Zanzinger, K.2    Heidenreich, R.3    Lorenz, C.4    Thess, A.5    Duchardt, K.M.6    Kallen, K.-J.7
  • 172
    • 0029045376 scopus 로고
    • A Sindbis virus mRNA polynucleotide vector achieves prolonged and high level heterologous gene expression in vivo
    • Johanning, F.W., Conry, R.M., LoBuglio, A.F., Wright, M., Sumerel, L.A., Pike, M.J. and Curiel, D.T. (1995) A Sindbis virus mRNA polynucleotide vector achieves prolonged and high level heterologous gene expression in vivo. Nucleic Acids Res., 23, 1495-1501.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1495-1501
    • Johanning, F.W.1    Conry, R.M.2    LoBuglio, A.F.3    Wright, M.4    Sumerel, L.A.5    Pike, M.J.6    Curiel, D.T.7
  • 176
    • 80051832804 scopus 로고    scopus 로고
    • An essential role for trimethylguanosine RNA caps in Saccharomyces cerevisiae meiosis and their requirement for splicing of SAE3 and PCH2 meiotic pre-mRNAs
    • Qiu, Z.R., Shuman, S. and Schwer, B. (2011) An essential role for trimethylguanosine RNA caps in Saccharomyces cerevisiae meiosis and their requirement for splicing of SAE3 and PCH2 meiotic pre-mRNAs. Nucleic Acids Res., 39, 5633-5646.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 5633-5646
    • Qiu, Z.R.1    Shuman, S.2    Schwer, B.3
  • 177
    • 77951154264 scopus 로고    scopus 로고
    • Mutational analyses of trimethylguanosine synthase (Tgs1) and Mud2: Proteins implicated in pre-mRNA splicing
    • Chang, J., Schwer, B. and Shuman, S. (2010) Mutational analyses of trimethylguanosine synthase (Tgs1) and Mud2: proteins implicated in pre-mRNA splicing. RNA, 16, 1018-1031.
    • (2010) RNA , vol.16 , pp. 1018-1031
    • Chang, J.1    Schwer, B.2    Shuman, S.3
  • 178
    • 84867595496 scopus 로고    scopus 로고
    • The Bin3 RNA methyltransferase targets 7SK RNA to control transcription and translation
    • Cosgrove, M.S., Ding, Y., Rennie, W.A., Lane, M.J. and Hanes, S.D. (2012) The Bin3 RNA methyltransferase targets 7SK RNA to control transcription and translation. Wiley Interdiscip. Rev. RNA, 3, 633-647.
    • (2012) Wiley Interdiscip. Rev. RNA , vol.3 , pp. 633-647
    • Cosgrove, M.S.1    Ding, Y.2    Rennie, W.A.3    Lane, M.J.4    Hanes, S.D.5
  • 179
    • 84867553154 scopus 로고    scopus 로고
    • Human RNA methyltransferase BCDIN3D regulates microRNA processing
    • Xhemalce, B., Robson, S.C. and Kouzarides, T. (2012) Human RNA methyltransferase BCDIN3D regulates microRNA processing. Cell, 151, 278-288.
    • (2012) Cell , vol.151 , pp. 278-288
    • Xhemalce, B.1    Robson, S.C.2    Kouzarides, T.3
  • 182
    • 66049158949 scopus 로고    scopus 로고
    • A chemical screen for biological small molecule-RNA conjugates reveals CoA-linked RNA
    • Kowtoniuk, W.E., Shen, Y., Heemstra, J.M., Agarwal, I. and Liu, D.R. (2009) A chemical screen for biological small molecule-RNA conjugates reveals CoA-linked RNA. Proc. Natl. Acad. Sci. U.S.A., 106, 7768-7773.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 7768-7773
    • Kowtoniuk, W.E.1    Shen, Y.2    Heemstra, J.M.3    Agarwal, I.4    Liu, D.R.5
  • 183
    • 84925490079 scopus 로고    scopus 로고
    • NAD captureSeq indicates NAD as a bacterial cap for a subset of regulatory RNAs
    • Cahova, H., Winz, M.-L., Hofer, K., Nubel, G. and Jaschke, A. (2015) NAD captureSeq indicates NAD as a bacterial cap for a subset of regulatory RNAs. Nature, 519, 374-377.
    • (2015) Nature , vol.519 , pp. 374-377
    • Cahova, H.1    Winz, M.-L.2    Hofer, K.3    Nubel, G.4    Jaschke, A.5


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