메뉴 건너뛰기




Volumn 41, Issue 2, 2007, Pages 227-239

RNA editing

Author keywords

ADAR; ADAT; Apobec; Deaminase; Editosome; Guide RNA; Mitochondria; RNA editing; RNA modifications

Indexed keywords

EUKARYOTA;

EID: 34247517803     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893307020057     Document Type: Article
Times cited : (7)

References (124)
  • 1
    • 0022552305 scopus 로고
    • Major transcript of the frame-shifted coxII gene from trypanosome mitochondria contains four nucleotides that are not encoded in the DNA
    • Benne R., van den Burg J., Brakenhoff J., Sloof P., van Boom J., Tromp M. 1986. Major transcript of the frame-shifted coxII gene from trypanosome mitochondria contains four nucleotides that are not encoded in the DNA. Cell. 46, 819-826.
    • (1986) Cell , vol.46 , pp. 819-826
    • Benne, R.1    van den Burg, J.2    Brakenhoff, J.3    Sloof, P.4    van Boom, J.5    Tromp, M.6
  • 2
    • 0024279854 scopus 로고
    • Extensive editing of the cytochrome c oxidase III transcript in Trypanosoma brucei
    • Feagin J.E., Abraham J., Stuart K. 1988. Extensive editing of the cytochrome c oxidase III transcript in Trypanosoma brucei. Cell. 53, 413-422.
    • (1988) Cell , vol.53 , pp. 413-422
    • Feagin, J.E.1    Abraham, J.2    Stuart, K.3
  • 3
    • 0024279904 scopus 로고
    • Editing of mitochondrial mRNAs by undine addition and deletion generates conserved amino acid sequences and AUG initiation codons
    • Shaw J., Feagin J.E., Stuart K., Simpson L. 1988. Editing of mitochondrial mRNAs by undine addition and deletion generates conserved amino acid sequences and AUG initiation codons. Cell. 53, 401-411.
    • (1988) Cell , vol.53 , pp. 401-411
    • Shaw, J.1    Feagin, J.E.2    Stuart, K.3    Simpson, L.4
  • 4
    • 0025189769 scopus 로고
    • A model for RNA editing in kinetoplastid mitochondria: "Guide" RNA molecules transcribed from maxicircle DNA provide the edited information
    • Blum B., Bakalara N., Simpson L. 1990. A model for RNA editing in kinetoplastid mitochondria: "Guide" RNA molecules transcribed from maxicircle DNA provide the edited information. Cell. 60, 189-198.
    • (1990) Cell , vol.60 , pp. 189-198
    • Blum, B.1    Bakalara, N.2    Simpson, L.3
  • 6
    • 0023651359 scopus 로고
    • A novel form of tissue-specific RNA processing produces apolipoprotein-B48 in intestine
    • Powell L.M., Wallis S.C., Pease R.J., Edwards Y.H., Knott T.J., Scott J. 1987. A novel form of tissue-specific RNA processing produces apolipoprotein-B48 in intestine. Cell. 50, 831-840.
    • (1987) Cell , vol.50 , pp. 831-840
    • Powell, L.M.1    Wallis, S.C.2    Pease, R.J.3    Edwards, Y.H.4    Knott, T.J.5    Scott, J.6
  • 7
    • 0025995296 scopus 로고
    • RNA editing in brain controls a determinant of ion flow in glutamate-gated channels
    • Sommer B., Kohler M., Sprengel R., Seeburg P.H. 1991. RNA editing in brain controls a determinant of ion flow in glutamate-gated channels. Cell. 67, 11-19.
    • (1991) Cell , vol.67 , pp. 11-19
    • Sommer, B.1    Kohler, M.2    Sprengel, R.3    Seeburg, P.H.4
  • 8
    • 0024419064 scopus 로고
    • RNA editing in plant mitochondria
    • Covello P.S., Gray M.W. 1989. RNA editing in plant mitochondria. Nature. 341, 662-666.
    • (1989) Nature , vol.341 , pp. 662-666
    • Covello, P.S.1    Gray, M.W.2
  • 9
    • 0024414676 scopus 로고
    • RNA editing in wheat mitochondria results in the conservation of protein sequences
    • Gualberto J.M., Lamattina L., Bonnard G., Weil J.H., Greinenberger J.M. 1989. RNA editing in wheat mitochondria results in the conservation of protein sequences. Nature. 341, 660-666.
    • (1989) Nature , vol.341 , pp. 660-666
    • Gualberto, J.M.1    Lamattina, L.2    Bonnard, G.3    Weil, J.H.4    Greinenberger, J.M.5
  • 11
    • 0025910413 scopus 로고
    • Editing of a chloroplast mRNA by creation of an initiation codon
    • Hoch B., Maier R.M., Appel K., Igloi G.L., Kossel H. 1991. Editing of a chloroplast mRNA by creation of an initiation codon. Nature. 353, 178-180.
    • (1991) Nature , vol.353 , pp. 178-180
    • Hoch, B.1    Maier, R.M.2    Appel, K.3    Igloi, G.L.4    Kossel, H.5
  • 13
  • 14
    • 0033762432 scopus 로고    scopus 로고
    • Uridylate addition and RNA ligation contribute to the specificity of kinetoplastid insertion RNA editing
    • Igo R.P., Palazzo S.S., Burgess M.L., Panigrahi A.K., Stuart K. 2000. Uridylate addition and RNA ligation contribute to the specificity of kinetoplastid insertion RNA editing. Mol. Cell Biol. 20, 8447-8457.
    • (2000) Mol. Cell Biol , vol.20 , pp. 8447-8457
    • Igo, R.P.1    Palazzo, S.S.2    Burgess, M.L.3    Panigrahi, A.K.4    Stuart, K.5
  • 15
    • 0036173906 scopus 로고    scopus 로고
    • RNA sequence and base pairing effects on insertion editing in Trypanosoma brucei
    • Igo R.P., Jr., Lawson S.D., Stuart K. 2002. RNA sequence and base pairing effects on insertion editing in Trypanosoma brucei. Mol. Cell Biol. 22, 1567-1576.
    • (2002) Mol. Cell Biol , vol.22 , pp. 1567-1576
    • Igo Jr., R.P.1    Lawson, S.D.2    Stuart, K.3
  • 16
    • 0029788229 scopus 로고    scopus 로고
    • RNA editing: A mechanism for gRNA-specified uridylate insertion into precursor mRNA [see comments]
    • Kable M.L., Seiwert S.D., Heidmann S., Stuart K. 1996. RNA editing: A mechanism for gRNA-specified uridylate insertion into precursor mRNA [see comments]. Science. 273, 1189-1195.
    • (1996) Science , vol.273 , pp. 1189-1195
    • Kable, M.L.1    Seiwert, S.D.2    Heidmann, S.3    Stuart, K.4
  • 17
    • 0029942430 scopus 로고    scopus 로고
    • Direct visualization of uridylate deletion in vitro suggests a mechanism for kinetoplastid RNA editing
    • Seiwert S.D., Heidmann S., Stuart K. 1996. Direct visualization of uridylate deletion in vitro suggests a mechanism for kinetoplastid RNA editing. Cell. 84, 831-841.
    • (1996) Cell , vol.84 , pp. 831-841
    • Seiwert, S.D.1    Heidmann, S.2    Stuart, K.3
  • 20
    • 0038488182 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the edi tosome and other multiprotein complexes in Trypanosoma brucei
    • Panigrahi A.K., Allen T.E., Stuart K., Haynes P.A., Gygi S.P. 2003. Mass spectrometric analysis of the edi tosome and other multiprotein complexes in Trypanosoma brucei. J. Am. Soc. Mass Spectrom. 14, 728-735.
    • (2003) J. Am. Soc. Mass Spectrom , vol.14 , pp. 728-735
    • Panigrahi, A.K.1    Allen, T.E.2    Stuart, K.3    Haynes, P.A.4    Gygi, S.P.5
  • 21
    • 0030928201 scopus 로고    scopus 로고
    • Purification of a functional enzymatic editing complex from Trypanosoma brucei mitochondria
    • Rusche L.N., Cruz-Reyes J., Piller K.J., Sollner-Webb B. 1997. Purification of a functional enzymatic editing complex from Trypanosoma brucei mitochondria. EMBO J. 16, 4069-4081.
    • (1997) EMBO J , vol.16 , pp. 4069-4081
    • Rusche, L.N.1    Cruz-Reyes, J.2    Piller, K.J.3    Sollner-Webb, B.4
  • 22
    • 0037040412 scopus 로고    scopus 로고
    • Trypanosome Mitochondrial 3' Terminal Uridylyl Transferase (TUTase): The key enzyme in U-insertion/deletion RNA editing
    • Aphasizhev R., Sbicego S., Peris M., Jang S.H., Aphasizheva I., Simpson A.M., Rivlin A., Simpson L. 2002. Trypanosome Mitochondrial 3' Terminal Uridylyl Transferase (TUTase): The key enzyme in U-insertion/deletion RNA editing. Cell. 108, 637-648.
    • (2002) Cell , vol.108 , pp. 637-648
    • Aphasizhev, R.1    Sbicego, S.2    Peris, M.3    Jang, S.H.4    Aphasizheva, I.5    Simpson, A.M.6    Rivlin, A.7    Simpson, L.8
  • 23
    • 0037276124 scopus 로고    scopus 로고
    • A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentotae catalyzes RNA annealing and interacts with several RNA editing components
    • Aphasizhev R., Aphasizheva I., Nelson R.E., Simpson L. 2003. A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentotae catalyzes RNA annealing and interacts with several RNA editing components. RNA. 9, 62-76.
    • (2003) RNA , vol.9 , pp. 62-76
    • Aphasizhev, R.1    Aphasizheva, I.2    Nelson, R.E.3    Simpson, L.4
  • 24
    • 0035878980 scopus 로고    scopus 로고
    • Cloning and characterization of two guide RNA-binding proteins from mitochondria of Crithidia fasciculata: GBP27, a novel protein, and gBP29, the orthologue of Trypanosoma brucei gBP21
    • Blom D., Burg J., Breek C.K., Speijer D., Muijsers A.O., Benne R. 2001. Cloning and characterization of two guide RNA-binding proteins from mitochondria of Crithidia fasciculata: gBP27, a novel protein, and gBP29, the orthologue of Trypanosoma brucei gBP21. Nucleic Acids Res. 29, 2950-2962.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2950-2962
    • Blom, D.1    Burg, J.2    Breek, C.K.3    Speijer, D.4    Muijsers, A.O.5    Benne, R.6
  • 25
    • 0033597222 scopus 로고    scopus 로고
    • Trypanosoma brucei RBP16 is a mitochondrial Y-box family protein with guide RNA binding activity
    • Hayman M.L., Read L.K. 1999. Trypanosoma brucei RBP16 is a mitochondrial Y-box family protein with guide RNA binding activity. J. Biol. Chem. 274, 12067-12074.
    • (1999) J. Biol. Chem , vol.274 , pp. 12067-12074
    • Hayman, M.L.1    Read, L.K.2
  • 26
    • 0031013396 scopus 로고    scopus 로고
    • Trypanosoma brucei gBP21. An arginine-rich mitochondrial protein that binds to guide RNA with high affinity
    • Koller J., Muller U.F., Schmid B., Missel A., Kruft V., Stuart K., Goringer H.U. 1997. Trypanosoma brucei gBP21. An arginine-rich mitochondrial protein that binds to guide RNA with high affinity. J. Biol. Chem. 272, 3749-3757.
    • (1997) J. Biol. Chem , vol.272 , pp. 3749-3757
    • Koller, J.1    Muller, U.F.2    Schmid, B.3    Missel, A.4    Kruft, V.5    Stuart, K.6    Goringer, H.U.7
  • 27
    • 1642580825 scopus 로고    scopus 로고
    • Mitochondrial proteins and complexes in Leishmania and Trypanosoma involved in U-insertion/deletion RNA editing
    • Simpson L., Aphasizhev R., Gao G., Kang X. 2004. Mitochondrial proteins and complexes in Leishmania and Trypanosoma involved in U-insertion/deletion RNA editing. RNA. 10, 159-170.
    • (2004) RNA , vol.10 , pp. 159-170
    • Simpson, L.1    Aphasizhev, R.2    Gao, G.3    Kang, X.4
  • 29
    • 1542350036 scopus 로고    scopus 로고
    • The effect of RNA interference down-regulation of RNA editing 3'-terminal uridylyl transferase (TUT-ase) 1 on mitochondrial de novo protein synthesis and stability of respiratory complexes in Trypanosoma brucei
    • Nebohacova M., Maslov D.A., Falick A.M., Simpson L. 2004. The effect of RNA interference down-regulation of RNA editing 3'-terminal uridylyl transferase (TUT-ase) 1 on mitochondrial de novo protein synthesis and stability of respiratory complexes in Trypanosoma brucei. J. Biol. Chem. 279, 7819-7825.
    • (2004) J. Biol. Chem , vol.279 , pp. 7819-7825
    • Nebohacova, M.1    Maslov, D.A.2    Falick, A.M.3    Simpson, L.4
  • 31
    • 0035896357 scopus 로고    scopus 로고
    • An RNA ligase essential for RNA editing and survival of the bloodstream form of Trypanosoma brucei
    • Schnaufer A., Panigrahi A.K., Panicucci B., Igo R.P., Salavati R., Stuart K. 2001. An RNA ligase essential for RNA editing and survival of the bloodstream form of Trypanosoma brucei. Science. 291, 2159-2161.
    • (2001) Science , vol.291 , pp. 2159-2161
    • Schnaufer, A.1    Panigrahi, A.K.2    Panicucci, B.3    Igo, R.P.4    Salavati, R.5    Stuart, K.6
  • 32
    • 0037371743 scopus 로고    scopus 로고
    • Uridine insertion/deletion RNA editing in trypanosome mitochondria: A complex business
    • Simpson L., Sbicego S., Aphasizhev R. 2003. Uridine insertion/deletion RNA editing in trypanosome mitochondria: A complex business. RNA. 9, 265-276.
    • (2003) RNA , vol.9 , pp. 265-276
    • Simpson, L.1    Sbicego, S.2    Aphasizhev, R.3
  • 33
    • 0035868965 scopus 로고    scopus 로고
    • Annealing of RNA editing substrates facilitated by guide RNA-binding protein gBP21
    • Muller U.F., Lambert L., Goringer H.U. 2001. Annealing of RNA editing substrates facilitated by guide RNA-binding protein gBP21. EMBO J. 20, 1394-1404.
    • (2001) EMBO J , vol.20 , pp. 1394-1404
    • Muller, U.F.1    Lambert, L.2    Goringer, H.U.3
  • 34
    • 33747478692 scopus 로고    scopus 로고
    • Crystal structures of T. brucei MRP1/MRP2 guide-RNA binding complex reveal RNA matchmaking mechanism
    • Schumacher M.A., Karamooz E., Zikova A., Trantirek L., Lukes J. 2006. Crystal structures of T. brucei MRP1/MRP2 guide-RNA binding complex reveal RNA matchmaking mechanism. Cell. 126, 701-711.
    • (2006) Cell , vol.126 , pp. 701-711
    • Schumacher, M.A.1    Karamooz, E.2    Zikova, A.3    Trantirek, L.4    Lukes, J.5
  • 38
    • 33749023006 scopus 로고    scopus 로고
    • Reconstitution of full-round uridine-deletion RNA editing with three recombinant proteins
    • Kang X., Gao G., Rogers K., Falick A.M., Zhou S., Simpson L. 2006. Reconstitution of full-round uridine-deletion RNA editing with three recombinant proteins. Proc. Natl. Acad. Sci. USA. 103, 13944-13949.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13944-13949
    • Kang, X.1    Gao, G.2    Rogers, K.3    Falick, A.M.4    Zhou, S.5    Simpson, L.6
  • 39
    • 12844285613 scopus 로고    scopus 로고
    • Reconstitution of undine-deletion precleaved RNA editing with two recombinant enzymes
    • Kang X., Rogers K., Gao G., Falick A.M., Zhou S., Simpson L. 2005. Reconstitution of undine-deletion precleaved RNA editing with two recombinant enzymes. Proc. Natl. Acad. Sci. USA. 102, 1017-1022.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1017-1022
    • Kang, X.1    Rogers, K.2    Gao, G.3    Falick, A.M.4    Zhou, S.5    Simpson, L.6
  • 40
    • 0038433297 scopus 로고    scopus 로고
    • TbMP57 is a 3' terminal uridylyl transferase (TUTase) of the Trypanosoma brucei editosome
    • Ernst N.L., Panicucci B., Igo R.P., Jr., Panigrahi A.K., Salavati R., Stuart K. 2003. TbMP57 is a 3' terminal uridylyl transferase (TUTase) of the Trypanosoma brucei editosome. Mol. Cell. 11, 1525-1536.
    • (2003) Mol. Cell , vol.11 , pp. 1525-1536
    • Ernst, N.L.1    Panicucci, B.2    Igo Jr., R.P.3    Panigrahi, A.K.4    Salavati, R.5    Stuart, K.6
  • 41
    • 0035877839 scopus 로고    scopus 로고
    • Isolation and characterization of a U-specific 3'-5' exonuclease from mitochondria of Leishmania tarentolae
    • Aphasizhev R., Simpson L. 2001. Isolation and characterization of a U-specific 3'-5' exonuclease from mitochondria of Leishmania tarentolae. J. Biol. Chem. 276, 21280-21284.
    • (2001) J. Biol. Chem , vol.276 , pp. 21280-21284
    • Aphasizhev, R.1    Simpson, L.2
  • 42
    • 28644431836 scopus 로고    scopus 로고
    • Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei
    • Deng J., Ernst N.L., Turley S., Stuart K.D., Hol W.G. 2005. Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei. EMBO J. 24, 4007-4017.
    • (2005) EMBO J , vol.24 , pp. 4007-4017
    • Deng, J.1    Ernst, N.L.2    Turley, S.3    Stuart, K.D.4    Hol, W.G.5
  • 43
    • 0033588338 scopus 로고    scopus 로고
    • The mitochondrial RNA ligase from Leishmania tarentolae can join RNA molecules bridged by a complementary RNA
    • Blanc V., Aphasizhev R., Alfonzo J.D., Simpson L. 1999. The mitochondrial RNA ligase from Leishmania tarentolae can join RNA molecules bridged by a complementary RNA. J. Biol. Chem. 274, 24289-24296.
    • (1999) J. Biol. Chem , vol.274 , pp. 24289-24296
    • Blanc, V.1    Aphasizhev, R.2    Alfonzo, J.D.3    Simpson, L.4
  • 44
    • 0031993321 scopus 로고    scopus 로고
    • Cruz-Reyes J., Rusche L., Piller K.J., Sollner-Webb B. 1998. T. brucei RNA editing: Adenosine nucleotides inversely affect U-deletion and U-insertion reactions at mRNA cleavage. Mol. Cell. 1, 401-409.
    • Cruz-Reyes J., Rusche L., Piller K.J., Sollner-Webb B. 1998. T. brucei RNA editing: Adenosine nucleotides inversely affect U-deletion and U-insertion reactions at mRNA cleavage. Mol. Cell. 1, 401-409.
  • 45
    • 0035801635 scopus 로고    scopus 로고
    • Roles for ligases in the RNA editing complex of Trypanosoma brucei: Band IV is needed for U-deletion and RNA repair
    • Huang C.E., Cruz-Reyes J., Zhelonkina A.G., O'Hearn S., Wirtz E., Sollner-Webb B. 2001. Roles for ligases in the RNA editing complex of Trypanosoma brucei: Band IV is needed for U-deletion and RNA repair. EMBO J. 20, 4694-4703.
    • (2001) EMBO J , vol.20 , pp. 4694-4703
    • Huang, C.E.1    Cruz-Reyes, J.2    Zhelonkina, A.G.3    O'Hearn, S.4    Wirtz, E.5    Sollner-Webb, B.6
  • 46
    • 0036235406 scopus 로고    scopus 로고
    • Assembly and function of the RNA editing complex in Trypanosoma brucei requires band III protein
    • Huang C.E., O'Hearn S.F., Sollner-Webb B. 2002. Assembly and function of the RNA editing complex in Trypanosoma brucei requires band III protein. Mol. Cell Biol. 22, 3194-3203.
    • (2002) Mol. Cell Biol , vol.22 , pp. 3194-3203
    • Huang, C.E.1    O'Hearn, S.F.2    Sollner-Webb, B.3
  • 47
    • 15044358727 scopus 로고    scopus 로고
    • In Trypanosoma brucei RNA editing, band II enables recognition specifically at each step of the U insertion cycle
    • Law J.A., Huang C.E., O'Hearn S.F., Sollner-Webb B. 2005. In Trypanosoma brucei RNA editing, band II enables recognition specifically at each step of the U insertion cycle. Mol. Cell Biol. 25, 2785-2794.
    • (2005) Mol. Cell Biol , vol.25 , pp. 2785-2794
    • Law, J.A.1    Huang, C.E.2    O'Hearn, S.F.3    Sollner-Webb, B.4
  • 48
    • 0141922994 scopus 로고    scopus 로고
    • Separate insertion and deletion subcomplexes of the Trypanosoma brucei RNA editing complex
    • Schnaufer A., Ernst N.L., Palazzo S.S., O'Rear J., Salavati R., Stuart K. 2003. Separate insertion and deletion subcomplexes of the Trypanosoma brucei RNA editing complex. Mol Cell. 12, 307-319.
    • (2003) Mol Cell , vol.12 , pp. 307-319
    • Schnaufer, A.1    Ernst, N.L.2    Palazzo, S.S.3    O'Rear, J.4    Salavati, R.5    Stuart, K.6
  • 49
    • 1042278183 scopus 로고    scopus 로고
    • Disruption of the zinc finger motifs in the Leishmania tarentolae LC-4 (= TbMP63) L-complex editing protein affects the stability of the L-complex
    • Kang X., Falick A.M., Nelson R.E., Gao G., Rogers K., Aphasizhev R., Simpson L. 2004. Disruption of the zinc finger motifs in the Leishmania tarentolae LC-4 (= TbMP63) L-complex editing protein affects the stability of the L-complex. J. Biol Chem. 279, 3893-3899.
    • (2004) J. Biol Chem , vol.279 , pp. 3893-3899
    • Kang, X.1    Falick, A.M.2    Nelson, R.E.3    Gao, G.4    Rogers, K.5    Aphasizhev, R.6    Simpson, L.7
  • 51
    • 0042346420 scopus 로고    scopus 로고
    • Is the Trypanosoma brucei REL1 RNA ligase specific for U-deletion RNA editing, and is the REL2 RNA ligase specific for U-insertion editing?
    • Gao G., Simpson L. 2003. Is the Trypanosoma brucei REL1 RNA ligase specific for U-deletion RNA editing, and is the REL2 RNA ligase specific for U-insertion editing? J. Biol. Chem. 278, 27570-27574.
    • (2003) J. Biol. Chem , vol.278 , pp. 27570-27574
    • Gao, G.1    Simpson, L.2
  • 52
    • 33244498173 scopus 로고    scopus 로고
    • Zhelonkina A.G., O'Hearn S.F., Law J.A., Cruz-Reyes J., Huang C.E., Alatortsev V.S., Sollner-Webb B. 2006. T. brucei RNA editing: Action of the U-insertional TUTase within a U-deletion cycle. RNA. 12, 476-487.
    • Zhelonkina A.G., O'Hearn S.F., Law J.A., Cruz-Reyes J., Huang C.E., Alatortsev V.S., Sollner-Webb B. 2006. T. brucei RNA editing: Action of the U-insertional TUTase within a U-deletion cycle. RNA. 12, 476-487.
  • 53
    • 33646870148 scopus 로고    scopus 로고
    • Compositionally and functionally distinct editosomes in Trypanosoma brucei
    • Panigrahi A.K., Ernst N.L., Domingo G.J., Fleck M., Salavati R., Stuart K.D. 2006. Compositionally and functionally distinct editosomes in Trypanosoma brucei. RNA. 12, 1038-1049.
    • (2006) RNA , vol.12 , pp. 1038-1049
    • Panigrahi, A.K.1    Ernst, N.L.2    Domingo, G.J.3    Fleck, M.4    Salavati, R.5    Stuart, K.D.6
  • 55
    • 0025290631 scopus 로고
    • An extensively edited mitochondrial transcript in kinetoplastids encodes a protein homologous to ATPase subunit 6
    • Bhat G.J., Koslowsky D.J., Feagin J.E., Smiley B.L., Stuart K. 1990. An extensively edited mitochondrial transcript in kinetoplastids encodes a protein homologous to ATPase subunit 6. Cell. 61, 885-894.
    • (1990) Cell , vol.61 , pp. 885-894
    • Bhat, G.J.1    Koslowsky, D.J.2    Feagin, J.E.3    Smiley, B.L.4    Stuart, K.5
  • 56
    • 0025108122 scopus 로고
    • The MURF3 gene of T. brucei contains multiple domains of extensive editing and is homologous to a subunit of NADH dehydrogenase
    • Koslowsky D.J., Bhat G.J., Perrollaz A.L., Feagin J.E., Stuart K. 1990. The MURF3 gene of T. brucei contains multiple domains of extensive editing and is homologous to a subunit of NADH dehydrogenase. Cell. 62, 901-911.
    • (1990) Cell , vol.62 , pp. 901-911
    • Koslowsky, D.J.1    Bhat, G.J.2    Perrollaz, A.L.3    Feagin, J.E.4    Stuart, K.5
  • 57
    • 0037815082 scopus 로고    scopus 로고
    • Diversity and evolution of mitochondrial RNA editing systems
    • Gray M.W. 2003. Diversity and evolution of mitochondrial RNA editing systems. IUBMB Life. 55, 227-233.
    • (2003) IUBMB Life , vol.55 , pp. 227-233
    • Gray, M.W.1
  • 58
    • 33646251852 scopus 로고    scopus 로고
    • Is kinetoplastid pan-editing the result of an evolutionary balancing act?
    • Speijer D. 2006. Is kinetoplastid pan-editing the result of an evolutionary balancing act? IUBMB Life. 58, 91-96.
    • (2006) IUBMB Life , vol.58 , pp. 91-96
    • Speijer, D.1
  • 59
    • 0037449753 scopus 로고    scopus 로고
    • C-to-U RNA editing: Mechanisms leading to genetic diversity
    • Blanc V., Davidson N.O. 2003. C-to-U RNA editing: Mechanisms leading to genetic diversity J. Biol. Chem. 278, 1395-1398.
    • (2003) J. Biol. Chem , vol.278 , pp. 1395-1398
    • Blanc, V.1    Davidson, N.O.2
  • 60
    • 0035083798 scopus 로고    scopus 로고
    • Molecular mechanisms of apolipoprotein B mRNA editing
    • Anant S., Davidson N.O. 2001. Molecular mechanisms of apolipoprotein B mRNA editing. Curr. Opin. Lipidol. 12, 159-165.
    • (2001) Curr. Opin. Lipidol , vol.12 , pp. 159-165
    • Anant, S.1    Davidson, N.O.2
  • 61
    • 0027200620 scopus 로고
    • Molecular cloning of an apolipoprotein B messenger RNA editing protein
    • Teng B., Burant C.F., Davidson N.O. 1993. Molecular cloning of an apolipoprotein B messenger RNA editing protein. Science. 260, 1816-1819.
    • (1993) Science , vol.260 , pp. 1816-1819
    • Teng, B.1    Burant, C.F.2    Davidson, N.O.3
  • 62
    • 0034733528 scopus 로고    scopus 로고
    • Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme complex
    • Lellek H., Kirsten R., Diehl I., Apostel F., Buck F., Greeve J. 2000. Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme complex. J. Biol. Chem. 275, 19848-19856.
    • (2000) J. Biol. Chem , vol.275 , pp. 19848-19856
    • Lellek, H.1    Kirsten, R.2    Diehl, I.3    Apostel, F.4    Buck, F.5    Greeve, J.6
  • 63
    • 0033970066 scopus 로고    scopus 로고
    • Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA
    • Mehta A., Kinter M.T., Sherman N.B., Driscoll D.M. 2000. Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA. Mol. Cell Biol. 20, 1846-1854.
    • (2000) Mol. Cell Biol , vol.20 , pp. 1846-1854
    • Mehta, A.1    Kinter, M.T.2    Sherman, N.B.3    Driscoll, D.M.4
  • 64
    • 0036811663 scopus 로고    scopus 로고
    • Identification and regulation of protein components of the apolipoprotein B mRNA editing enzyme. A complex event
    • Anant S., Davidson N.O. 2002. Identification and regulation of protein components of the apolipoprotein B mRNA editing enzyme. A complex event. Trends Cardiovasc. Med. 12, 311-317.
    • (2002) Trends Cardiovasc. Med , vol.12 , pp. 311-317
    • Anant, S.1    Davidson, N.O.2
  • 65
    • 0037189521 scopus 로고    scopus 로고
    • Reconstitution of mRNA editing in yeast using a Gal4-apoB-Gal80 fusion transcript as the selectable marker
    • Lellek H., Welker S., Diehl I., Kirsten R., Greeve J. 2002. Reconstitution of mRNA editing in yeast using a Gal4-apoB-Gal80 fusion transcript as the selectable marker. J. Biol. Chem. 277, 23638-23644.
    • (2002) J. Biol. Chem , vol.277 , pp. 23638-23644
    • Lellek, H.1    Welker, S.2    Diehl, I.3    Kirsten, R.4    Greeve, J.5
  • 66
    • 0026441405 scopus 로고
    • Three distinct RNA sequence elements are required for efficient apolipopro tein B (apoB) RNA editing in vitro
    • Backus J.W., Smith H.C. 1992. Three distinct RNA sequence elements are required for efficient apolipopro tein B (apoB) RNA editing in vitro. Nucleic Acids Res. 20, 6007-6014.
    • (1992) Nucleic Acids Res , vol.20 , pp. 6007-6014
    • Backus, J.W.1    Smith, H.C.2
  • 68
    • 0032540348 scopus 로고    scopus 로고
    • Two efficiency elements flanking the editing site of cytidine 6666 in the apolipoprotein B mRNA support mooring-dependent editing
    • Hersberger M., Innerarity T.L. 1998. Two efficiency elements flanking the editing site of cytidine 6666 in the apolipoprotein B mRNA support mooring-dependent editing. J. Biol. Chem. 273, 9435-9442.
    • (1998) J. Biol. Chem , vol.273 , pp. 9435-9442
    • Hersberger, M.1    Innerarity, T.L.2
  • 69
    • 0033610859 scopus 로고    scopus 로고
    • Secondary structure for the apolipoprotein B mRNA editing site: AU-binding proteins interact with a stem loop
    • Richardson N., Navaratnam N., Scott J. 1998. Secondary structure for the apolipoprotein B mRNA editing site: AU-binding proteins interact with a stem loop. J. Biol. Chem. 273, 31707-31717.
    • (1998) J. Biol. Chem , vol.273 , pp. 31707-31717
    • Richardson, N.1    Navaratnam, N.2    Scott, J.3
  • 70
    • 0033998026 scopus 로고    scopus 로고
    • An AU-rich sequence element (UUUN[A/U]U) downstream of the edited C in apolipoprotein B mRNA is a high-affinity binding site for Apobec-1: Binding of Apobec-1 to this motif in the 3' untranslated region of c-myc increases mRNA stability
    • Anant S., Davidson N.O. 2000. An AU-rich sequence element (UUUN[A/U]U) downstream of the edited C in apolipoprotein B mRNA is a high-affinity binding site for Apobec-1: Binding of Apobec-1 to this motif in the 3' untranslated region of c-myc increases mRNA stability. Mol. Cell Biol. 20, 1982-1992.
    • (2000) Mol. Cell Biol , vol.20 , pp. 1982-1992
    • Anant, S.1    Davidson, N.O.2
  • 71
    • 22744444873 scopus 로고    scopus 로고
    • Messenger RNA surveillance: Neutralizing natural nonsense
    • Weischenfeldt J., Lykke-Andersen J., Porse B. 2005. Messenger RNA surveillance: Neutralizing natural nonsense. Curr. Biol. 15, R559-R562.
    • (2005) Curr. Biol , vol.15
    • Weischenfeldt, J.1    Lykke-Andersen, J.2    Porse, B.3
  • 72
    • 0041524056 scopus 로고    scopus 로고
    • The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay
    • Chester A., Somasekaram A., Tzimina M., Jarmuz A., Gisbourne J., O'Keefe R., Scott J., Navaratnam N. 2003. The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay. EMBO J. 22, 3971-3982.
    • (2003) EMBO J , vol.22 , pp. 3971-3982
    • Chester, A.1    Somasekaram, A.2    Tzimina, M.3    Jarmuz, A.4    Gisbourne, J.5    O'Keefe, R.6    Scott, J.7    Navaratnam, N.8
  • 73
    • 0037471698 scopus 로고    scopus 로고
    • Gene expression in plant mitochondria: Transcriptional and post-transcriptional control
    • Binder S., Brennicke A. 2003. Gene expression in plant mitochondria: Transcriptional and post-transcriptional control. Philos. Trans. R. Soc. Lond. B: Biol. Sci. 358, 181-188.
    • (2003) Philos. Trans. R. Soc. Lond. B: Biol. Sci , vol.358 , pp. 181-188
    • Binder, S.1    Brennicke, A.2
  • 74
    • 12744253474 scopus 로고    scopus 로고
    • A pentatri-copeptide repeat protein is essential for RNA editing in chloroplasts
    • Kotera E., Tasaka M., Shikanai T. 2005. A pentatri-copeptide repeat protein is essential for RNA editing in chloroplasts. Nature. 433, 326-330.
    • (2005) Nature , vol.433 , pp. 326-330
    • Kotera, E.1    Tasaka, M.2    Shikanai, T.3
  • 75
    • 33645074681 scopus 로고    scopus 로고
    • RNA editing in plant organelles: Machinery, physiological function and evolution
    • Shikanai T. 2006. RNA editing in plant organelles: machinery, physiological function and evolution. Cell Mol. Life Sci. 63, 698-708.
    • (2006) Cell Mol. Life Sci , vol.63 , pp. 698-708
    • Shikanai, T.1
  • 76
    • 0029989864 scopus 로고    scopus 로고
    • Sequences directing C to U editing of the plastid psbL mRNA are located within a 22 nucleotide segment spanning the editing site
    • Chaudhuri S., Maliga P. 1996. Sequences directing C to U editing of the plastid psbL mRNA are located within a 22 nucleotide segment spanning the editing site. EMBO J. 15, 5958-5964.
    • (1996) EMBO J , vol.15 , pp. 5958-5964
    • Chaudhuri, S.1    Maliga, P.2
  • 77
    • 0029075116 scopus 로고
    • In vivo testing of a tobacco plastid DNA segment for guide RNA function in psbL editing
    • Bock R., Maliga P. 1995. In vivo testing of a tobacco plastid DNA segment for guide RNA function in psbL editing. Mol. Gen. Genet. 247, 439-443.
    • (1995) Mol. Gen. Genet , vol.247 , pp. 439-443
    • Bock, R.1    Maliga, P.2
  • 78
    • 0034802513 scopus 로고    scopus 로고
    • cis Recognition elements in plant mitochondrion RNA editing
    • Farre J.C., Leon G., Jordana X., Araya A. 2001. cis Recognition elements in plant mitochondrion RNA editing. Mol. Cell Biol. 21, 6731-6737.
    • (2001) Mol. Cell Biol , vol.21 , pp. 6731-6737
    • Farre, J.C.1    Leon, G.2    Jordana, X.3    Araya, A.4
  • 79
    • 0036892814 scopus 로고    scopus 로고
    • Cross-competition in transgenic chloroplasts expressing single editing sites reveals shared cis elements
    • Chateigner-Boutin A.L., Hanson M.R. 2002. Cross-competition in transgenic chloroplasts expressing single editing sites reveals shared cis elements. Mol. Cell Biol. 22, 8448-8456.
    • (2002) Mol. Cell Biol , vol.22 , pp. 8448-8456
    • Chateigner-Boutin, A.L.1    Hanson, M.R.2
  • 80
    • 4744347763 scopus 로고    scopus 로고
    • Control of human potassium channel inactivation by editing of a small mRNA hairpin
    • Bhalla T., Rosenthal J.J., Holmgren M., Reenan R. 2004. Control of human potassium channel inactivation by editing of a small mRNA hairpin. Nature Struct. Mol. Biol. 11, 950-956.
    • (2004) Nature Struct. Mol. Biol , vol.11 , pp. 950-956
    • Bhalla, T.1    Rosenthal, J.J.2    Holmgren, M.3    Reenan, R.4
  • 82
    • 19344368678 scopus 로고    scopus 로고
    • Retention and repression: Fates of hyperedited RNAs in the nucleus
    • DeCerbo J., Carmichael G.G. 2005. Retention and repression: Fates of hyperedited RNAs in the nucleus. Curr. Opin. Cell Biol. 17, 302-308.
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 302-308
    • DeCerbo, J.1    Carmichael, G.G.2
  • 83
    • 0035369742 scopus 로고    scopus 로고
    • RNA editing by base deamination: More enzymes, more targets, new mysteries
    • Gerber A.P., Keller W. 2001. RNA editing by base deamination: More enzymes, more targets, new mysteries. Trends Biochem. Sci. 26, 376-384.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 376-384
    • Gerber, A.P.1    Keller, W.2
  • 84
    • 0034682706 scopus 로고    scopus 로고
    • A-to-I pre-mRNA editing in Drosophila is primarily involved in adult nervous system function and integrity
    • Palladino M.J., Keegan L.P., O'Connell M.A., Reenan R.A. 2000. A-to-I pre-mRNA editing in Drosophila is primarily involved in adult nervous system function and integrity. Cell. 102, 437-449.
    • (2000) Cell , vol.102 , pp. 437-449
    • Palladino, M.J.1    Keegan, L.P.2    O'Connell, M.A.3    Reenan, R.A.4
  • 85
    • 0036703330 scopus 로고    scopus 로고
    • RNA editing by adenosine deaminases generates RNA and protein diversity
    • Schaub M., Keller W. 2002. RNA editing by adenosine deaminases generates RNA and protein diversity. Biochimie. 84, 791-803.
    • (2002) Biochimie , vol.84 , pp. 791-803
    • Schaub, M.1    Keller, W.2
  • 86
    • 0033603359 scopus 로고    scopus 로고
    • Serotonin-2C receptor pre-mRNA editing in rat brain and in vitro by splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase ADAR1
    • Liu Y., Emeson R.B., Samuel C.E. 1999. Serotonin-2C receptor pre-mRNA editing in rat brain and in vitro by splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase ADAR1. J. Biol. Chem. 274, 18351-18358.
    • (1999) J. Biol. Chem , vol.274 , pp. 18351-18358
    • Liu, Y.1    Emeson, R.B.2    Samuel, C.E.3
  • 87
    • 0031047968 scopus 로고    scopus 로고
    • Functionally distinct double-stranded RNA-binding domains associated with alternative splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase
    • Liu Y., George C.X., Patterson J.B., Samuel C.E. 1997. Functionally distinct double-stranded RNA-binding domains associated with alternative splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase. J. Biol. Chem. 272, 4419-4428.
    • (1997) J. Biol. Chem , vol.272 , pp. 4419-4428
    • Liu, Y.1    George, C.X.2    Patterson, J.B.3    Samuel, C.E.4
  • 88
    • 33748607688 scopus 로고    scopus 로고
    • Maydanovych O., Beal P.A. 2006. Breaking the central dogma by RNA editing. Chem. Rev. 106, 3397-3411.
    • Maydanovych O., Beal P.A. 2006. Breaking the central dogma by RNA editing. Chem. Rev. 106, 3397-3411.
  • 90
    • 0035997389 scopus 로고    scopus 로고
    • RNA editing by adenosine deaminases that act on RNA
    • Bass B.L. 2002. RNA editing by adenosine deaminases that act on RNA. Annu. Rev. Biochem. 71, 817-846.
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 817-846
    • Bass, B.L.1
  • 91
    • 0024233053 scopus 로고
    • An unwinding activity that covalently modifies its double-stranded RNA substrate
    • Bass B., Weintraub H. 1988. An unwinding activity that covalently modifies its double-stranded RNA substrate. Cell. 55, 1089-1098.
    • (1988) Cell , vol.55 , pp. 1089-1098
    • Bass, B.1    Weintraub, H.2
  • 92
    • 0036966283 scopus 로고    scopus 로고
    • New and old roles of the double-stranded RNA-binding domain
    • Doyle M., Jantsch M.F. 2002. New and old roles of the double-stranded RNA-binding domain. J. Struct. Biol. 140, 147-153.
    • (2002) J. Struct. Biol , vol.140 , pp. 147-153
    • Doyle, M.1    Jantsch, M.F.2
  • 93
    • 0021176227 scopus 로고
    • Vesicular stomatitis virus defective interfering particles can contain extensive genomic sequence rearrangements and base substitutions
    • O'Hara P.J., Nichol S.T., Horodyski P.M., Holland J.J. 1984. Vesicular stomatitis virus defective interfering particles can contain extensive genomic sequence rearrangements and base substitutions. Cell. 36, 915-924.
    • (1984) Cell , vol.36 , pp. 915-924
    • O'Hara, P.J.1    Nichol, S.T.2    Horodyski, P.M.3    Holland, J.J.4
  • 94
    • 0023763122 scopus 로고
    • Biased hypermutation and other genetic changes in defective measles viruses in human brain infections
    • Cattaneo R., Schmid A., Eschle D., Baczko K., Meulen V., Billeter M. 1988. Biased hypermutation and other genetic changes in defective measles viruses in human brain infections. Cell. 55, 255-265.
    • (1988) Cell , vol.55 , pp. 255-265
    • Cattaneo, R.1    Schmid, A.2    Eschle, D.3    Baczko, K.4    Meulen, V.5    Billeter, M.6
  • 95
    • 0024966063 scopus 로고
    • Biased hypermutation of viral RNA genomes could be due to unwinding/modification of double-stranded RNA
    • Bass B., Weintraub H., Cattaneo R., Billeter M. 1989. Biased hypermutation of viral RNA genomes could be due to unwinding/modification of double-stranded RNA. Cell. 56, 331.
    • (1989) Cell , vol.56 , pp. 331
    • Bass, B.1    Weintraub, H.2    Cattaneo, R.3    Billeter, M.4
  • 96
    • 0344035669 scopus 로고    scopus 로고
    • The importance of internal loops within RNA substrates of ADAR1
    • Lehmann K.A., Bass B.L. 1999. The importance of internal loops within RNA substrates of ADAR1. J. Mol. Biol. 291, 1-13.
    • (1999) J. Mol. Biol , vol.291 , pp. 1-13
    • Lehmann, K.A.1    Bass, B.L.2
  • 97
    • 0034711082 scopus 로고    scopus 로고
    • Double-stranded RNA adenosine deaminases ADAR1 and ADAR2 have overlapping specificities
    • Lehmann K.A., Bass B.L. 2000. Double-stranded RNA adenosine deaminases ADAR1 and ADAR2 have overlapping specificities. Biochemistry. 39, 12875-12884.
    • (2000) Biochemistry , vol.39 , pp. 12875-12884
    • Lehmann, K.A.1    Bass, B.L.2
  • 98
    • 0033911001 scopus 로고    scopus 로고
    • RNA editing of the Drosophila para Na(+) channel transcript. Evolutionary conservation and developmental regulation
    • Hanrahan C.J., Palladino M.J., Ganetzky B., Reenan R.A. 2000. RNA editing of the Drosophila para Na(+) channel transcript. Evolutionary conservation and developmental regulation. Genetics. 155, 1149-1160.
    • (2000) Genetics , vol.155 , pp. 1149-1160
    • Hanrahan, C.J.1    Palladino, M.J.2    Ganetzky, B.3    Reenan, R.A.4
  • 99
    • 0034535312 scopus 로고    scopus 로고
    • Requirement of the RNA editing deaminase ADAR1 gene for embryonic erythropoiesis
    • Wang Q., Khillan J., Gadue P., Nishikura K. 2000. Requirement of the RNA editing deaminase ADAR1 gene for embryonic erythropoiesis. Science. 290, 1765-1768.
    • (2000) Science , vol.290 , pp. 1765-1768
    • Wang, Q.1    Khillan, J.2    Gadue, P.3    Nishikura, K.4
  • 101
    • 0001580215 scopus 로고
    • Nucleotide sequences in yeast alanine transfer ribonucleic acid
    • Holley R.W., Everett G.A., Madison J.T., Zamir A. 1965. Nucleotide sequences in yeast alanine transfer ribonucleic acid. J. Biol. Chem. 240, 2122-2128.
    • (1965) J. Biol. Chem , vol.240 , pp. 2122-2128
    • Holley, R.W.1    Everett, G.A.2    Madison, J.T.3    Zamir, A.4
  • 102
    • 0028069147 scopus 로고
    • Analysis of action of wobble nucleoside modifications on codon-anticodon pairing within the ribosome
    • Lim V.I. 1994. Analysis of action of wobble nucleoside modifications on codon-anticodon pairing within the ribosome. J. Mol. Biol. 240, 8-19.
    • (1994) J. Mol. Biol , vol.240 , pp. 8-19
    • Lim, V.I.1
  • 103
    • 0030816674 scopus 로고    scopus 로고
    • The modified wobble base inosine in yeast tRNAIle is a positive determinant for aminoacylation by isoleucyl-tRNA synthetase
    • Senger B., Auxilien S., Englisch U., Cramer F., Fasiolo F. 1997. The modified wobble base inosine in yeast tRNAIle is a positive determinant for aminoacylation by isoleucyl-tRNA synthetase. Biochemistry. 36, 8269-8275.
    • (1997) Biochemistry , vol.36 , pp. 8269-8275
    • Senger, B.1    Auxilien, S.2    Englisch, U.3    Cramer, F.4    Fasiolo, F.5
  • 104
    • 0032541331 scopus 로고    scopus 로고
    • Tad1p, a yeast tRNA-specific adenosine deaminase, is related to the mammalian pre-mRNA editing enzymes ADAR1 and ADAR2
    • Gerber A., Grosjean H., Melcher T., Keller W. 1998. Tad1p, a yeast tRNA-specific adenosine deaminase, is related to the mammalian pre-mRNA editing enzymes ADAR1 and ADAR2. EMBO J. 17, 4780-4789.
    • (1998) EMBO J , vol.17 , pp. 4780-4789
    • Gerber, A.1    Grosjean, H.2    Melcher, T.3    Keller, W.4
  • 105
    • 0033527628 scopus 로고    scopus 로고
    • An adenosine deaminase that generates inosine at the wobble position of tRNAs
    • Gerber A.P., Keller W. 1999. An adenosine deaminase that generates inosine at the wobble position of tRNAs. Science. 286, 1146-1149.
    • (1999) Science , vol.286 , pp. 1146-1149
    • Gerber, A.P.1    Keller, W.2
  • 106
    • 0035851115 scopus 로고    scopus 로고
    • Conformational changes that occur during an RNA-editing adenosine deamination reaction
    • Yi-Brunozzi H.Y., Stephens O.M., Beal P.A. 2001. Conformational changes that occur during an RNA-editing adenosine deamination reaction. J. Biol. Chem. 276, 37827-37833.
    • (2001) J. Biol. Chem , vol.276 , pp. 37827-37833
    • Yi-Brunozzi, H.Y.1    Stephens, O.M.2    Beal, P.A.3
  • 107
    • 0011895723 scopus 로고    scopus 로고
    • Mechanism, specificity and general properties of the yeast enzyme catalysing the formation of inosine 34 in the anticodon of transfer RNA
    • Auxilien S., Crain P.P., Trewyn R.W., Grosjean H. 1996. Mechanism, specificity and general properties of the yeast enzyme catalysing the formation of inosine 34 in the anticodon of transfer RNA. J. Mol Biol. 262, 437-458.
    • (1996) J. Mol Biol , vol.262 , pp. 437-458
    • Auxilien, S.1    Crain, P.P.2    Trewyn, R.W.3    Grosjean, H.4
  • 108
    • 0029857254 scopus 로고    scopus 로고
    • RNA editing changes the identity of a mitochondrial tRNA in marsupials
    • Borner G.V., Morl M., Janke A., Paabo S. 1996. RNA editing changes the identity of a mitochondrial tRNA in marsupials. EMBO J. 15, 5949-5957.
    • (1996) EMBO J , vol.15 , pp. 5949-5957
    • Borner, G.V.1    Morl, M.2    Janke, A.3    Paabo, S.4
  • 109
    • 0141621017 scopus 로고    scopus 로고
    • RNA editing of larch mitochondrial tRNA(His) precursors is a prerequisite for processing
    • Marechal-Drouard L., Kumar R., Remacle C., Small I. 1996. RNA editing of larch mitochondrial tRNA(His) precursors is a prerequisite for processing. Nucleic Acids Res. 24, 3229-3234.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3229-3234
    • Marechal-Drouard, L.1    Kumar, R.2    Remacle, C.3    Small, I.4
  • 110
    • 0033572678 scopus 로고    scopus 로고
    • C to U editing of the anticodon of imported mitochondrial tRNATrp allows decoding of the UGA stop codon in Leishmania tarentolae
    • Alfonzo J.D., Blanc V., Estevez A.M., Rubio M.A., Simpson L. 1999. C to U editing of the anticodon of imported mitochondrial tRNATrp allows decoding of the UGA stop codon in Leishmania tarentolae. EMBO J. 18, 7056-7062.
    • (1999) EMBO J , vol.18 , pp. 7056-7062
    • Alfonzo, J.D.1    Blanc, V.2    Estevez, A.M.3    Rubio, M.A.4    Simpson, L.5
  • 111
    • 33646469995 scopus 로고    scopus 로고
    • Dual targeting of a single tRNA(Trp) requires two different tryptophanyl-tRNA synthetases in Trypanosoma brucei
    • Charriere F., Helgadottir S., Horn E.K., Soll D., Schneider A. 2006. Dual targeting of a single tRNA(Trp) requires two different tryptophanyl-tRNA synthetases in Trypanosoma brucei. Proc. Natl. Acad. Sci. USA. 103, 6847-6852.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6847-6852
    • Charriere, F.1    Helgadottir, S.2    Horn, E.K.3    Soll, D.4    Schneider, A.5
  • 112
    • 0027500536 scopus 로고
    • Editing of transfer RNAs in Acanthamoeba castellanii mitochondria
    • Lonergan K.M., Gray M.W. 1993. Editing of transfer RNAs in Acanthamoeba castellanii mitochondria. Science. 259, 812-816.
    • (1993) Science , vol.259 , pp. 812-816
    • Lonergan, K.M.1    Gray, M.W.2
  • 113
    • 13244296941 scopus 로고    scopus 로고
    • In vitro characterization of a tRNA editing activity in the mitochondria of Spizellomyces punctatus, a Chytridiomycete fungus
    • Bullerwell C.E., Gray M.W. 2005. In vitro characterization of a tRNA editing activity in the mitochondria of Spizellomyces punctatus, a Chytridiomycete fungus. J. Biol. Chem. 280, 2463-2470.
    • (2005) J. Biol. Chem , vol.280 , pp. 2463-2470
    • Bullerwell, C.E.1    Gray, M.W.2
  • 114
    • 0034507456 scopus 로고    scopus 로고
    • Functions and mechanisms of RNA editing. Annu
    • 499-NIL34
    • Gott J.M., Emeson R.B. 2000. Functions and mechanisms of RNA editing. Annu. Rev. Genet. 34, 499-NIL34.
    • (2000) Rev. Genet , vol.34
    • Gott, J.M.1    Emeson, R.B.2
  • 115
    • 0027373196 scopus 로고
    • Substitutional and insertional RNA editing of the cytochrome c oxidase subunit 1 mRNA of Physarum polycephatum
    • Gott J.M., Visomirski L.M., Hunter J.L. 1993. Substitutional and insertional RNA editing of the cytochrome c oxidase subunit 1 mRNA of Physarum polycephatum. J. Biol. Chem. 268, 25483-25486.
    • (1993) J. Biol. Chem , vol.268 , pp. 25483-25486
    • Gott, J.M.1    Visomirski, L.M.2    Hunter, J.L.3
  • 116
    • 4444336611 scopus 로고    scopus 로고
    • Unexpectedly complex editing patterns at dinucleotide insertion sites in Physarum mitochondria
    • Byrne E.M., Gott J.M. 2004. Unexpectedly complex editing patterns at dinucleotide insertion sites in Physarum mitochondria. Mol. Cell Biol. 24, 7821-7828.
    • (2004) Mol. Cell Biol , vol.24 , pp. 7821-7828
    • Byrne, E.M.1    Gott, J.M.2
  • 117
    • 0030940116 scopus 로고    scopus 로고
    • Insertional editing of nascent mitochondrial RNAs in Physarum
    • Visomirski-Robic L.M., Gott J.M. 1997. Insertional editing of nascent mitochondrial RNAs in Physarum. Proc. Natl. Acad. Sci. USA. 94, 4324-4329.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4324-4329
    • Visomirski-Robic, L.M.1    Gott, J.M.2
  • 118
    • 0024282829 scopus 로고
    • Two mRNAs that differ by two nontemplated nucleotides encode the amino coterminal proteins P and V of the Paramyxovirus SV5
    • Thomas S.M., Lamb R.A., Paterson R.G. 1988. Two mRNAs that differ by two nontemplated nucleotides encode the amino coterminal proteins P and V of the Paramyxovirus SV5. Cell. 54, 891-903.
    • (1988) Cell , vol.54 , pp. 891-903
    • Thomas, S.M.1    Lamb, R.A.2    Paterson, R.G.3
  • 119
    • 21444456320 scopus 로고    scopus 로고
    • Paramyxovirus mRNA editing, the "rule of six" and error catastrophe: A hypothesis
    • Kolakofsky D., Roux L., Garcin D., Ruigrok R.W. 2005. Paramyxovirus mRNA editing, the "rule of six" and error catastrophe: A hypothesis. J. Gen. Virol. 86, 1869-1877.
    • (2005) J. Gen. Virol , vol.86 , pp. 1869-1877
    • Kolakofsky, D.1    Roux, L.2    Garcin, D.3    Ruigrok, R.W.4
  • 120
    • 0029589329 scopus 로고    scopus 로고
    • Volchkov V.E., Becker S., Volchkova V.A., Ternovoj V.A., Kotov A.N., Netesov S.V., Klenk H.D. 1995. GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases. Virology. 214, 421-430.
    • Volchkov V.E., Becker S., Volchkova V.A., Ternovoj V.A., Kotov A.N., Netesov S.V., Klenk H.D. 1995. GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases. Virology. 214, 421-430.
  • 121
    • 0025359331 scopus 로고
    • A stuttering model for paramyxovirus P mRNA editing
    • Vidal S., Curran J., Kolakofsky D. 1990. A stuttering model for paramyxovirus P mRNA editing. EMBO J. 9, 2017-2022.
    • (1990) EMBO J , vol.9 , pp. 2017-2022
    • Vidal, S.1    Curran, J.2    Kolakofsky, D.3
  • 122
    • 0036675180 scopus 로고    scopus 로고
    • Chemical modification of nucleotide bases and mRNA editing depend on hexamer or nucleoprotein phase in Sendai virus nucleocapsids
    • Iseni F., Baudin F., Garcin D., Marq J.B., Ruigrok R.W., Kolakofsky D. 2002. Chemical modification of nucleotide bases and mRNA editing depend on hexamer or nucleoprotein phase in Sendai virus nucleocapsids. RNA. 8, 1056-1067.
    • (2002) RNA , vol.8 , pp. 1056-1067
    • Iseni, F.1    Baudin, F.2    Garcin, D.3    Marq, J.B.4    Ruigrok, R.W.5    Kolakofsky, D.6
  • 123
    • 0027201750 scopus 로고
    • On the evolution of RNA editing
    • Covello P.S., Gray M.W. 1993. On the evolution of RNA editing. Trends Genet. 9, 265-268.
    • (1993) Trends Genet , vol.9 , pp. 265-268
    • Covello, P.S.1    Gray, M.W.2
  • 124
    • 0030739912 scopus 로고    scopus 로고
    • A three-dimensional working model for a guide RNA from Trypanosoma brucei
    • Hermann T., Schmid B., Heumann H., Geringer H.U. 1997. A three-dimensional working model for a guide RNA from Trypanosoma brucei. Nucleic Acids Res. 25, 2311-2318.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2311-2318
    • Hermann, T.1    Schmid, B.2    Heumann, H.3    Geringer, H.U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.