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Volumn 87, Issue 10, 2013, Pages 5629-5644

Structural features of a picornavirus polymerase involved in the polyadenylation of viral RNA

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; COMPLEMENTARY DNA; DOUBLE STRANDED RNA; LYSINE; PHOSPHATE; RNA POLYMERASE; VIRUS RNA;

EID: 84877358918     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02590-12     Document Type: Article
Times cited : (15)

References (57)
  • 1
    • 0018740432 scopus 로고
    • Determination of the length distribution of poly(A) at the 3′ terminus of the virion RNAs of EMC virus, poliovirus, rhinovirus, RAV-61 and CPMV and of mouse globin mRNA
    • Ahlquist P, Kaesberg P. 1979. Determination of the length distribution of poly(A) at the 3′ terminus of the virion RNAs of EMC virus, poliovirus, rhinovirus, RAV-61 and CPMV and of mouse globin mRNA. Nucleic Acids Res. 7:1195-1204.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1195-1204
    • Ahlquist, P.1    Kaesberg, P.2
  • 2
    • 0024585229 scopus 로고
    • Role of 3′-end sequences in infectivity of poliovirus transcripts made in vitro
    • Sarnow P. 1989. Role of 3′-end sequences in infectivity of poliovirus transcripts made in vitro. J. Virol. 63:467-470.
    • (1989) J. Virol. , vol.63 , pp. 467-470
    • Sarnow, P.1
  • 3
    • 31944452620 scopus 로고    scopus 로고
    • Relationship between poliovirus negative-strand RNA synthesis and the length of the 3′ poly(A) tail
    • Silvestri LS, Parilla JM, Morasco BJ, Ogram SA, Flanegan JB. 2006. Relationship between poliovirus negative-strand RNA synthesis and the length of the 3′ poly(A) tail. Virology 345:509-519.
    • (2006) Virology , vol.345 , pp. 509-519
    • Silvestri, L.S.1    Parilla, J.M.2    Morasco, B.J.3    Ogram, S.A.4    Flanegan, J.B.5
  • 4
    • 0034543678 scopus 로고    scopus 로고
    • Picornavirus IRESes and the poly(A) tail jointly promote cap-independent translation in a mammalian cell-free system
    • Bergamini G, Preiss T, Hentze MW. 2000. Picornavirus IRESes and the poly(A) tail jointly promote cap-independent translation in a mammalian cell-free system. RNA 6:1781-1790.
    • (2000) RNA , vol.6 , pp. 1781-1790
    • Bergamini, G.1    Preiss, T.2    Hentze, M.W.3
  • 6
    • 0030802760 scopus 로고    scopus 로고
    • Replicationcompetent picornaviruses with complete genomic RNA 3′ noncoding region deletions
    • Todd S, Towner JS, Brown DM, Semler BL. 1997. Replicationcompetent picornaviruses with complete genomic RNA 3′ noncoding region deletions. J. Virol. 71:8868-8874.
    • (1997) J. Virol. , vol.71 , pp. 8868-8874
    • Todd, S.1    Towner, J.S.2    Brown, D.M.3    Semler, B.L.4
  • 7
    • 24644461482 scopus 로고    scopus 로고
    • An authentic 3′ noncoding region is necessary for efficient poliovirus replication
    • Brown DM, Cornell CT, Tran GP, Nguyen JH, Semler BL. 2005. An authentic 3′ noncoding region is necessary for efficient poliovirus replication. J. Virol. 79:11962-11973.
    • (2005) J. Virol. , vol.79 , pp. 11962-11973
    • Brown, D.M.1    Cornell, C.T.2    Tran, G.P.3    Nguyen, J.H.4    Semler, B.L.5
  • 8
    • 77649143165 scopus 로고    scopus 로고
    • Poly(A) at the 3′ end of positivestrand RNA and VPg-linked poly(U) at the 5′ end of negative-strand RNA are reciprocal templates during replication of poliovirus RNA
    • Steil BP, Kempf BJ, Barton DJ. 2010. Poly(A) at the 3′ end of positivestrand RNA and VPg-linked poly(U) at the 5′ end of negative-strand RNA are reciprocal templates during replication of poliovirus RNA. J. Virol. 84:2843-2858.
    • (2010) J. Virol. , vol.84 , pp. 2843-2858
    • Steil, B.P.1    Kempf, B.J.2    Barton, D.J.3
  • 9
    • 0034948006 scopus 로고    scopus 로고
    • Polymerase slippage at vesicular stomatitis virus gene junctions to generate poly(A) is regulated by the upstream 3′-AUAC-5′ tetranucleotide: implications for the mechanism of transcription termination
    • Barr JN, Wertz GW. 2001. Polymerase slippage at vesicular stomatitis virus gene junctions to generate poly(A) is regulated by the upstream 3′-AUAC-5′ tetranucleotide: implications for the mechanism of transcription termination. J. Virol. 75:6901-6913.
    • (2001) J. Virol. , vol.75 , pp. 6901-6913
    • Barr, J.N.1    Wertz, G.W.2
  • 11
    • 70549097351 scopus 로고    scopus 로고
    • RNA-dependent RNA polymerases from flaviviruses and Picornaviridae
    • Lescar J, Canard B. 2009. RNA-dependent RNA polymerases from flaviviruses and Picornaviridae. Curr. Opin. Struct. Biol. 19:759-767.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 759-767
    • Lescar, J.1    Canard, B.2
  • 12
    • 40649100793 scopus 로고    scopus 로고
    • Structure-function relationships among RNA-dependent RNA polymerases
    • Ng KK, Arnold JJ, Cameron CE. 2008. Structure-function relationships among RNA-dependent RNA polymerases. Curr. Top. Microbiol. Immunol. 320:137-156.
    • (2008) Curr. Top. Microbiol. Immunol. , vol.320 , pp. 137-156
    • Ng, K.K.1    Arnold, J.J.2    Cameron, C.E.3
  • 13
    • 4644238112 scopus 로고    scopus 로고
    • Structural basis for proteolysisdependent activation of the poliovirus RNA-dependent RNA polymerase
    • Thompson AA, Peersen OB. 2004. Structural basis for proteolysisdependent activation of the poliovirus RNA-dependent RNA polymerase. EMBO J. 23:3462-3471.
    • (2004) EMBO J. , vol.23 , pp. 3462-3471
    • Thompson, A.A.1    Peersen, O.B.2
  • 14
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen JL, Long AM, Schultz SC. 1997. Structure of the RNA-dependent RNA polymerase of poliovirus. Structure 5:1109-1122.
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 15
    • 33846833843 scopus 로고    scopus 로고
    • Stabilization of poliovirus polymerase by NTP binding and fingers-thumb interactions
    • Thompson AA, Albertini RA, Peersen OB. 2007. Stabilization of poliovirus polymerase by NTP binding and fingers-thumb interactions. J. Mol. Biol. 366:1459-1474.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1459-1474
    • Thompson, A.A.1    Albertini, R.A.2    Peersen, O.B.3
  • 16
    • 78651097570 scopus 로고    scopus 로고
    • Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase
    • Gong P, Peersen OB. 2010. Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase. Proc. Natl. Acad. Sci. U. S. A. 107:22505-22510.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 22505-22510
    • Gong, P.1    Peersen, O.B.2
  • 17
    • 0028904540 scopus 로고
    • Encephalomyocarditis viruses with short poly(C) tracts are more virulent than their mengovirus counterparts
    • Hahn H, Palmenberg AC. 1995. Encephalomyocarditis viruses with short poly(C) tracts are more virulent than their mengovirus counterparts. J. Virol. 69:2697-2699.
    • (1995) J. Virol. , vol.69 , pp. 2697-2699
    • Hahn, H.1    Palmenberg, A.C.2
  • 18
    • 0029155434 scopus 로고
    • Complete replication of poliovirus in vitro: preinitiation RNA replication complexes require soluble cellular factors for the synthesis of VPg-linked RNA
    • Barton DJ, Black EP, Flanegan JB. 1995. Complete replication of poliovirus in vitro: preinitiation RNA replication complexes require soluble cellular factors for the synthesis of VPg-linked RNA. J. Virol. 69:5516-5527.
    • (1995) J. Virol. , vol.69 , pp. 5516-5527
    • Barton, D.J.1    Black, E.P.2    Flanegan, J.B.3
  • 19
    • 0037383425 scopus 로고    scopus 로고
    • Poliovirus CRE-dependent VPg uridylylation is required for positive-strand RNA synthesis but not for negativestrand RNA synthesis
    • Murray KE, Barton DJ. 2003. Poliovirus CRE-dependent VPg uridylylation is required for positive-strand RNA synthesis but not for negativestrand RNA synthesis. J. Virol. 77:4739-4750.
    • (2003) J. Virol. , vol.77 , pp. 4739-4750
    • Murray, K.E.1    Barton, D.J.2
  • 20
    • 52649121446 scopus 로고    scopus 로고
    • Poliovirus cis-acting replication elementdependent VPg uridylylation lowers the Km of the initiating nucleoside triphosphate for viral RNA replication
    • Steil BP, Barton DJ. 2008. Poliovirus cis-acting replication elementdependent VPg uridylylation lowers the Km of the initiating nucleoside triphosphate for viral RNA replication. J. Virol. 82:9400-9408.
    • (2008) J. Virol. , vol.82 , pp. 9400-9408
    • Steil, B.P.1    Barton, D.J.2
  • 21
    • 0030820126 scopus 로고    scopus 로고
    • Synchronous replication of poliovirus RNA: initiation of negative-strand RNA synthesis requires the guanidineinhibited activity of protein 2C
    • Barton DJ, Flanegan JB. 1997. Synchronous replication of poliovirus RNA: initiation of negative-strand RNA synthesis requires the guanidineinhibited activity of protein 2C. J. Virol. 71:8482-8489.
    • (1997) J. Virol. , vol.71 , pp. 8482-8489
    • Barton, D.J.1    Flanegan, J.B.2
  • 22
    • 84857997971 scopus 로고    scopus 로고
    • A template RNA entry channel in the fingers domain of the poliovirus polymerase
    • Kortus MG, Kempf BJ, Haworth KG, Barton DJ, Peersen OB. 2012. A template RNA entry channel in the fingers domain of the poliovirus polymerase. J. Mol. Biol. 417:263-278.
    • (2012) J. Mol. Biol. , vol.417 , pp. 263-278
    • Kortus, M.G.1    Kempf, B.J.2    Haworth, K.G.3    Barton, D.J.4    Peersen, O.B.5
  • 23
    • 77954979735 scopus 로고    scopus 로고
    • Poliovirus polymerase residue 5 plays a critical role in elongation complex stability
    • Hobdey SE, Kempf BJ, Steil BP, Barton DJ, Peersen OB. 2010. Poliovirus polymerase residue 5 plays a critical role in elongation complex stability. J. Virol. 84:8072-8084.
    • (2010) J. Virol. , vol.84 , pp. 8072-8084
    • Hobdey, S.E.1    Kempf, B.J.2    Steil, B.P.3    Barton, D.J.4    Peersen, O.B.5
  • 24
    • 0035868852 scopus 로고    scopus 로고
    • 5′ cloverleaf in poliovirus RNA is a cis-acting replication element required for negative-strand synthesis
    • Barton DJ, O'Donnell BJ, Flanegan JB. 2001. 5′ cloverleaf in poliovirus RNA is a cis-acting replication element required for negative-strand synthesis. EMBO J. 20:1439-1448.
    • (2001) EMBO J. , vol.20 , pp. 1439-1448
    • Barton, D.J.1    O'Donnell, B.J.2    Flanegan, J.B.3
  • 25
    • 0038809107 scopus 로고    scopus 로고
    • A single mutation in poliovirus RNAdependent RNA polymerase confers resistance to mutagenic nucleotide analogs via increased fidelity
    • Pfeiffer JK, Kirkegaard K. 2003. A single mutation in poliovirus RNAdependent RNA polymerase confers resistance to mutagenic nucleotide analogs via increased fidelity. Proc. Natl. Acad. Sci. U. S. A. 100:7289-7294.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7289-7294
    • Pfeiffer, J.K.1    Kirkegaard, K.2
  • 26
    • 33745490138 scopus 로고    scopus 로고
    • Increased fidelity reduces poliovirus fitness and virulence under selective pressure in mice
    • doi:10.1371/journal.ppat.0010011
    • Pfeiffer JK, Kirkegaard K. 2005. Increased fidelity reduces poliovirus fitness and virulence under selective pressure in mice. PLoS Pathog. 1:e11. doi:10.1371/journal.ppat.0010011.
    • (2005) PLoS Pathog. , vol.1
    • Pfeiffer, J.K.1    Kirkegaard, K.2
  • 27
    • 31144465690 scopus 로고    scopus 로고
    • Quasispecies diversity determines pathogenesis through cooperative interactions in a viral population
    • Vignuzzi M, Stone JK, Arnold JJ, Cameron CE, Andino R. 2006. Quasispecies diversity determines pathogenesis through cooperative interactions in a viral population. Nature 439:344-348.
    • (2006) Nature , vol.439 , pp. 344-348
    • Vignuzzi, M.1    Stone, J.K.2    Arnold, J.J.3    Cameron, C.E.4    Andino, R.5
  • 28
    • 21844431621 scopus 로고    scopus 로고
    • Remote site control of an active site fidelity checkpoint in a viral RNA-dependent RNA polymerase
    • Arnold JJ, Vignuzzi M, Stone JK, Andino R, Cameron CE. 2005. Remote site control of an active site fidelity checkpoint in a viral RNA-dependent RNA polymerase. J. Biol. Chem. 280:25706-25716.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25706-25716
    • Arnold, J.J.1    Vignuzzi, M.2    Stone, J.K.3    Andino, R.4    Cameron, C.E.5
  • 29
    • 11844292013 scopus 로고    scopus 로고
    • Ribavirin and lethal mutagenesis of poliovirus: molecular mechanisms, resistance and biological implications
    • Vignuzzi M, Stone JK, Andino R. 2005. Ribavirin and lethal mutagenesis of poliovirus: molecular mechanisms, resistance and biological implications. Virus Res. 107:173-181.
    • (2005) Virus Res. , vol.107 , pp. 173-181
    • Vignuzzi, M.1    Stone, J.K.2    Andino, R.3
  • 30
    • 0028044755 scopus 로고
    • Clustered charged-to-alanine mutagenesis of poliovirus RNA-dependent RNA polymerase yields multiple temperature-sensitive mutants defective in RNA synthesis
    • Diamond SE, Kirkegaard K. 1994. Clustered charged-to-alanine mutagenesis of poliovirus RNA-dependent RNA polymerase yields multiple temperature-sensitive mutants defective in RNA synthesis. J. Virol. 68: 863-876.
    • (1994) J. Virol. , vol.68 , pp. 863-876
    • Diamond, S.E.1    Kirkegaard, K.2
  • 31
    • 38949184924 scopus 로고    scopus 로고
    • Engineering attenuated virus vaccines by controlling replication fidelity
    • Vignuzzi M, Wendt E, Andino R. 2008. Engineering attenuated virus vaccines by controlling replication fidelity. Nat. Med. 14:154-161.
    • (2008) Nat. Med. , vol.14 , pp. 154-161
    • Vignuzzi, M.1    Wendt, E.2    Andino, R.3
  • 32
    • 78649881479 scopus 로고    scopus 로고
    • To polyadenylate or to deadenylate: that is the question
    • Zhang XK, Virtanen A, Kleiman FE. 2010. To polyadenylate or to deadenylate: that is the question. Cell Cycle 9:4437-4449.
    • (2010) Cell Cycle , vol.9 , pp. 4437-4449
    • Zhang, X.K.1    Virtanen, A.2    Kleiman, F.E.3
  • 35
    • 79952537148 scopus 로고    scopus 로고
    • Structures of EV71 RNA-dependent RNA polymerase in complex with substrate and analogue provide a drug target against the hand-footand-mouth disease pandemic in China
    • Wu Y, Lou Z, Miao Y, Yu Y, Dong H, Peng W, Bartlam M, Li X, Rao Z. 2010. Structures of EV71 RNA-dependent RNA polymerase in complex with substrate and analogue provide a drug target against the hand-footand-mouth disease pandemic in China. Protein Cell 1:491-500.
    • (2010) Protein Cell , vol.1 , pp. 491-500
    • Wu, Y.1    Lou, Z.2    Miao, Y.3    Yu, Y.4    Dong, H.5    Peng, W.6    Bartlam, M.7    Li, X.8    Rao, Z.9
  • 36
    • 52649143257 scopus 로고    scopus 로고
    • Crystal structure of coxsackievirus B3 3Dpol highlights the functional importance of residue 5 in picornavirus polymerases
    • Campagnola G, Weygandt M, Scoggin K, Peersen O. 2008. Crystal structure of coxsackievirus B3 3Dpol highlights the functional importance of residue 5 in picornavirus polymerases. J. Virol. 82:9458-9464.
    • (2008) J. Virol. , vol.82 , pp. 9458-9464
    • Campagnola, G.1    Weygandt, M.2    Scoggin, K.3    Peersen, O.4
  • 37
    • 52649173300 scopus 로고    scopus 로고
    • The crystal structure of coxsackievirus B3 RNA-dependent RNA polymerase in complex with its protein primer VPg confirms the existence of a second VPg binding site on Picornaviridae polymerases
    • Gruez A, Selisko B, Roberts M, Bricogne G, Bussetta C, Jabafi I, Coutard B, De Palma AM, Neyts J, Canard B. 2008. The crystal structure of coxsackievirus B3 RNA-dependent RNA polymerase in complex with its protein primer VPg confirms the existence of a second VPg binding site on Picornaviridae polymerases. J. Virol. 82:9577-9590.
    • (2008) J. Virol. , vol.82 , pp. 9577-9590
    • Gruez, A.1    Selisko, B.2    Roberts, M.3    Bricogne, G.4    Bussetta, C.5    Jabafi, I.6    Coutard, B.7    De Palma, A.M.8    Neyts, J.9    Canard, B.10
  • 39
    • 4143147318 scopus 로고    scopus 로고
    • The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy
    • Love RA, Maegley KA, Yu X, Ferre RA, Lingardo LK, Diehl W, Parge HE, Dragovich PS, Fuhrman SA. 2004. The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy. Structure 12:1533-1544.
    • (2004) Structure , vol.12 , pp. 1533-1544
    • Love, R.A.1    Maegley, K.A.2    Yu, X.3    Ferre, R.A.4    Lingardo, L.K.5    Diehl, W.6    Parge, H.E.7    Dragovich, P.S.8    Fuhrman, S.A.9
  • 40
    • 8744222695 scopus 로고    scopus 로고
    • Structure of foot-and-mouth disease virus RNAdependent RNA polymerase and its complex with a template-primer RNA
    • Ferrer-Orta C, Arias A, Perez-Luque R, Escarmis C, Domingo E, Verdaguer N. 2004. Structure of foot-and-mouth disease virus RNAdependent RNA polymerase and its complex with a template-primer RNA. J. Biol. Chem. 279:47212-47221.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47212-47221
    • Ferrer-Orta, C.1    Arias, A.2    Perez-Luque, R.3    Escarmis, C.4    Domingo, E.5    Verdaguer, N.6
  • 42
    • 0033613849 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3D(pol)) is sufficient for template switching in vitro
    • Arnold JJ, Cameron CE. 1999. Poliovirus RNA-dependent RNA polymerase (3D(pol)) is sufficient for template switching in vitro. J. Biol. Chem. 274:2706-2716.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2706-2716
    • Arnold, J.J.1    Cameron, C.E.2
  • 43
    • 0023017765 scopus 로고
    • The mechanism of RNA recombination in poliovirus
    • Kirkegaard K, Baltimore D. 1986. The mechanism of RNA recombination in poliovirus. Cell 47:433-443.
    • (1986) Cell , vol.47 , pp. 433-443
    • Kirkegaard, K.1    Baltimore, D.2
  • 45
    • 0033600752 scopus 로고    scopus 로고
    • Replication slippage of different DNA polymerases is inversely related to their strand displacement efficiency
    • Canceill D, Viguera E, Ehrlich SD. 1999. Replication slippage of different DNA polymerases is inversely related to their strand displacement efficiency. J. Biol. Chem. 274:27481-27490.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27481-27490
    • Canceill, D.1    Viguera, E.2    Ehrlich, S.D.3
  • 46
    • 0242415195 scopus 로고    scopus 로고
    • A "slide-back" mechanism for the initiation of protein-primedRNAsynthesis by the RNA polymerase of poliovirus
    • Paul AV, Yin J, Mugavero J, Rieder E, Liu Y, Wimmer E. 2003. A "slide-back" mechanism for the initiation of protein-primedRNAsynthesis by the RNA polymerase of poliovirus. J. Biol. Chem. 278:43951-43960.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43951-43960
    • Paul, A.V.1    Yin, J.2    Mugavero, J.3    Rieder, E.4    Liu, Y.5    Wimmer, E.6
  • 49
    • 57349131683 scopus 로고    scopus 로고
    • Determinants of RNA-dependent RNA polymerase (in)fidelity revealed by kinetic analysis of the polymerase encoded by a foot-and-mouth disease virus mutant with reduced sensitivity to ribavirin
    • Arias A, Arnold JJ, Sierra M, Smidansky ED, Domingo E, Cameron CE. 2008. Determinants of RNA-dependent RNA polymerase (in)fidelity revealed by kinetic analysis of the polymerase encoded by a foot-and-mouth disease virus mutant with reduced sensitivity to ribavirin. J. Virol. 82: 12346-12355.
    • (2008) J. Virol. , vol.82 , pp. 12346-12355
    • Arias, A.1    Arnold, J.J.2    Sierra, M.3    Smidansky, E.D.4    Domingo, E.5    Cameron, C.E.6
  • 50
    • 0035265836 scopus 로고    scopus 로고
    • Poliovirus RNA replication requires genome circularization through a protein-protein bridge
    • Herold J, Andino R. 2001. Poliovirus RNA replication requires genome circularization through a protein-protein bridge. Mol. Cell 7:581-591.
    • (2001) Mol. Cell , vol.7 , pp. 581-591
    • Herold, J.1    Andino, R.2
  • 51
    • 56349152646 scopus 로고    scopus 로고
    • The Big Bang of picorna-like virus evolution antedates the radiation of eukaryotic supergroups
    • Koonin EV, Wolf YI, Nagasaki K, Dolja VV. 2008. The Big Bang of picorna-like virus evolution antedates the radiation of eukaryotic supergroups. Nat. Rev. Microbiol. 6:925-939.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 925-939
    • Koonin, E.V.1    Wolf, Y.I.2    Nagasaki, K.3    Dolja, V.V.4
  • 53
    • 53349161932 scopus 로고    scopus 로고
    • Structure of the Tribolium castaneum telomerase catalytic subunit TERT
    • Gillis AJ, Schuller AP, Skordalakes E. 2008. Structure of the Tribolium castaneum telomerase catalytic subunit TERT. Nature 455:633-637.
    • (2008) Nature , vol.455 , pp. 633-637
    • Gillis, A.J.1    Schuller, A.P.2    Skordalakes, E.3
  • 54
    • 77950471767 scopus 로고    scopus 로고
    • Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA
    • Mitchell M, Gillis A, Futahashi M, Fujiwara H, Skordalakes E. 2010. Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA. Nat. Struct. Mol. Biol. 17:513-518.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 513-518
    • Mitchell, M.1    Gillis, A.2    Futahashi, M.3    Fujiwara, H.4    Skordalakes, E.5
  • 56
    • 0002974648 scopus 로고    scopus 로고
    • Telomerase
    • world:the nature of modern RNA suggests a prebiotic RNA. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Blackburn EH. 1999. Telomerase, p 609-635. In Gesteland RF, Cech TR, Atkins JF (ed), The RNA world: the nature of modern RNA suggests a prebiotic RNA. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1999) In Gesteland RF, Cech TR, Atkins JF (ed), The RNA , pp. 609-635
    • Blackburn, E.H.1
  • 57
    • 0029837263 scopus 로고    scopus 로고
    • Assays for poliovirus polymerase, 3D(Pol), and authentic RNA replication in HeLa S10 extracts
    • Barton DJ, Morasco BJ, Flanegan JB. 1996. Assays for poliovirus polymerase, 3D(Pol), and authentic RNA replication in HeLa S10 extracts. Methods Enzymol. 275:35-57.
    • (1996) Methods Enzymol. , vol.275 , pp. 35-57
    • Barton, D.J.1    Morasco, B.J.2    Flanegan, J.B.3


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