-
1
-
-
67249119414
-
-
Jegouic, et al.: PLoS Pathog 2009, 5(5):e1000412. doi:10.1371/journal.ppat.1000412.
-
Jegouic, et al.: PLoS Pathog 2009, 5(5):e1000412. doi:10.1371/journal.ppat.1000412.
-
-
-
-
2
-
-
32344432085
-
A comparison of viral RNA-dependent RNA polymerases
-
This paper reviews the different structures available with outstanding implementations in following papers (see other references by the same authors).
-
Ferrer-Orta C., Arias A., Escarmis C., and Verdaguer N. A comparison of viral RNA-dependent RNA polymerases. Curr Opin Struct Biol 16 (2006) 1-8. This paper reviews the different structures available with outstanding implementations in following papers (see other references by the same authors).
-
(2006)
Curr Opin Struct Biol
, vol.16
, pp. 1-8
-
-
Ferrer-Orta, C.1
Arias, A.2
Escarmis, C.3
Verdaguer, N.4
-
3
-
-
33750285215
-
Structure and function of RNA replication
-
Ortin J., and Parra F. Structure and function of RNA replication. Annu Rev Microbiol 60 (2006) 305-326
-
(2006)
Annu Rev Microbiol
, vol.60
, pp. 305-326
-
-
Ortin, J.1
Parra, F.2
-
4
-
-
68649103985
-
New insights into flavivirus non structural protein 5
-
An up-to-date and rather exhaustive review.
-
Davidson A.D. New insights into flavivirus non structural protein 5. Adv Virus Res 74 (2009) 41-101. An up-to-date and rather exhaustive review.
-
(2009)
Adv Virus Res
, vol.74
, pp. 41-101
-
-
Davidson, A.D.1
-
5
-
-
33747344212
-
A 5′ RNA element promotes dengue virus RNA synthesis on a circular genome
-
A promoter element required for flavivirus RNA synthesis by the NS5 RdRp comprises a stem-loop within the 5′-nontranslated region. The authors propose that following the recognition of this RNA structure, long-range RNA-RNA interactions, mediated by cyclization motifs, shuttle the polymerase to the 3′-end of the genome to initiate minus strand RNA synthesis (see also Ref. [6]).
-
Filomatori C.V., Lodeiro M.F., Alvarez D.E., Samsa M.M., Pietrasanta L., and Gamarnik A.V. A 5′ RNA element promotes dengue virus RNA synthesis on a circular genome. Genes Dev 20 (2006) 2238-2249. A promoter element required for flavivirus RNA synthesis by the NS5 RdRp comprises a stem-loop within the 5′-nontranslated region. The authors propose that following the recognition of this RNA structure, long-range RNA-RNA interactions, mediated by cyclization motifs, shuttle the polymerase to the 3′-end of the genome to initiate minus strand RNA synthesis (see also Ref. [6]).
-
(2006)
Genes Dev
, vol.20
, pp. 2238-2249
-
-
Filomatori, C.V.1
Lodeiro, M.F.2
Alvarez, D.E.3
Samsa, M.M.4
Pietrasanta, L.5
Gamarnik, A.V.6
-
6
-
-
58149487592
-
Structural and functional studies of the promoter element for dengue virus RNA replication
-
Lodeiro M.F., Filomatori C.V., and Gamarnik A.V. Structural and functional studies of the promoter element for dengue virus RNA replication. J Virol 83 2 (2009) 993-1008
-
(2009)
J Virol
, vol.83
, Issue.2
, pp. 993-1008
-
-
Lodeiro, M.F.1
Filomatori, C.V.2
Gamarnik, A.V.3
-
7
-
-
47049089643
-
Genetic interactions among the West Nile virus methyltransferase, the RNA-dependent RNA polymerase, and the 5′ stem-loop of genomic RNA
-
Zhang B., Dong H., Zhou Y., and Shi P.Y. Genetic interactions among the West Nile virus methyltransferase, the RNA-dependent RNA polymerase, and the 5′ stem-loop of genomic RNA. J Virol 82 14 (2008) 7047-7058
-
(2008)
J Virol
, vol.82
, Issue.14
, pp. 7047-7058
-
-
Zhang, B.1
Dong, H.2
Zhou, Y.3
Shi, P.Y.4
-
8
-
-
49649102821
-
Architects of assembly: roles of Flaviviridae non-structural proteins in virion morphogenesis
-
Murray C.L., Jones C.T., and Rice C.M. Architects of assembly: roles of Flaviviridae non-structural proteins in virion morphogenesis. Nat Rev Microbiol 9 (2008) 699-708
-
(2008)
Nat Rev Microbiol
, vol.9
, pp. 699-708
-
-
Murray, C.L.1
Jones, C.T.2
Rice, C.M.3
-
9
-
-
34249845069
-
Crystal structure of the RNA polymerase domain of the West Nile virus non-structural protein 5
-
This paper reports the first structure determination of both an active as well as a truncated (and inactive) fragment of the RdRp catalytic domain from the Kunjin strain of West-Nile virus. A working model for the initiation of RNA polymerization by flaviviruses is proposed. Using a reverse genetics system, residues that contribute to the interaction between the methyltransferase and RdRp domains of NS5 are mapped, allowing the authors to propose a model for the complete NS5 protein.
-
Malet H., Egloff M.P., Selisko B., Butcher R.E., Wright P.J., Roberts M., Gruez A., Sulzenbacher G., Vonrhein C., Bricogne G., et al. Crystal structure of the RNA polymerase domain of the West Nile virus non-structural protein 5. J Biol Chem 282 14 (2007) 10678-10689. This paper reports the first structure determination of both an active as well as a truncated (and inactive) fragment of the RdRp catalytic domain from the Kunjin strain of West-Nile virus. A working model for the initiation of RNA polymerization by flaviviruses is proposed. Using a reverse genetics system, residues that contribute to the interaction between the methyltransferase and RdRp domains of NS5 are mapped, allowing the authors to propose a model for the complete NS5 protein.
-
(2007)
J Biol Chem
, vol.282
, Issue.14
, pp. 10678-10689
-
-
Malet, H.1
Egloff, M.P.2
Selisko, B.3
Butcher, R.E.4
Wright, P.J.5
Roberts, M.6
Gruez, A.7
Sulzenbacher, G.8
Vonrhein, C.9
Bricogne, G.10
-
10
-
-
34247610261
-
The crystal structure of the dengue virus RNA-dependent RNA polymerase at 1.85 Å resolution
-
This paper reports the first crystallographic structure at high resolution of an active RdRp from serotype 3 of DENV. The putative NLS regions form an integral part of the catalytic domain. A unique structural feature of flavivirus RdRp compared to the hepacivirus or pestivirus RdRps is the presence of two structural zinc ions. A complex with the chain terminator dGTP that binds to the priming loop is also described.
-
Yap T.L., Xu T., Chen Y.L., Malet H., Egloff M.-P., Canard B., Vasudevan S.G., and Lescar J. The crystal structure of the dengue virus RNA-dependent RNA polymerase at 1.85 Å resolution. J Virol 81 (2007) 4753-4765. This paper reports the first crystallographic structure at high resolution of an active RdRp from serotype 3 of DENV. The putative NLS regions form an integral part of the catalytic domain. A unique structural feature of flavivirus RdRp compared to the hepacivirus or pestivirus RdRps is the presence of two structural zinc ions. A complex with the chain terminator dGTP that binds to the priming loop is also described.
-
(2007)
J Virol
, vol.81
, pp. 4753-4765
-
-
Yap, T.L.1
Xu, T.2
Chen, Y.L.3
Malet, H.4
Egloff, M.-P.5
Canard, B.6
Vasudevan, S.G.7
Lescar, J.8
-
11
-
-
33847102726
-
A multi-step strategy to obtain crystals of the dengue virus RNA-dependent RNA polymerase that diffract to high resolution
-
The successful expression, purification, and crystallization of an active flavivirus RdRp catalytic domain is described as an initial step toward structure-based drug discovery against the dengue virus RdRp.
-
Yap T.L., Chen Y.L., Xu T., Wen D., Vasudevan S.G., and Lescar J. A multi-step strategy to obtain crystals of the dengue virus RNA-dependent RNA polymerase that diffract to high resolution. Acta Crystallogr F 63 (2007) 78-83. The successful expression, purification, and crystallization of an active flavivirus RdRp catalytic domain is described as an initial step toward structure-based drug discovery against the dengue virus RdRp.
-
(2007)
Acta Crystallogr F
, vol.63
, pp. 78-83
-
-
Yap, T.L.1
Chen, Y.L.2
Xu, T.3
Wen, D.4
Vasudevan, S.G.5
Lescar, J.6
-
12
-
-
67650106549
-
CRM1-mediated nuclear export of dengue virus RNA polymerase NS5 modulates interleukin-8 induction and virus production
-
Rawlinson S.M., Pryor M.J., Wright P.J., and Jans D.A. CRM1-mediated nuclear export of dengue virus RNA polymerase NS5 modulates interleukin-8 induction and virus production. J Biol Chem 284 23 (2009) 15589-15597
-
(2009)
J Biol Chem
, vol.284
, Issue.23
, pp. 15589-15597
-
-
Rawlinson, S.M.1
Pryor, M.J.2
Wright, P.J.3
Jans, D.A.4
-
13
-
-
34047171495
-
West Nile virus strain Kunjin NS5 polymerase is a phosphoprotein localized at the cytoplasmic site of viral RNA synthesis
-
Mackenzie J.M., Kenney M.T., and Westaway E.G. West Nile virus strain Kunjin NS5 polymerase is a phosphoprotein localized at the cytoplasmic site of viral RNA synthesis. J Gen Virol 88 Pt 4 (2007) 1163-1168
-
(2007)
J Gen Virol
, vol.88
, Issue.PART 4
, pp. 1163-1168
-
-
Mackenzie, J.M.1
Kenney, M.T.2
Westaway, E.G.3
-
14
-
-
0036120573
-
Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides
-
A seminal paper on the still elusive binding mode of nucleotide in this most wanted RdRp structure.
-
Bressanelli S., Tomei L., Rey F.A., and De Francesco R. Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides. J Virol 76 (2002) 3482-3492. A seminal paper on the still elusive binding mode of nucleotide in this most wanted RdRp structure.
-
(2002)
J Virol
, vol.76
, pp. 3482-3492
-
-
Bressanelli, S.1
Tomei, L.2
Rey, F.A.3
De Francesco, R.4
-
15
-
-
52649173300
-
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
-
This paper reports a long-known binding site of VPg, for which the clearly distinct VPg-binding site on FMDV, reported by the Verdaguer group, came as a great surprise.
-
Gruez A., Selisko B., Roberts M., Bricogne G., Bussetta C., Jabafi I., Coutard B., De Palma A.M., Neyts J., and Canard B. 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 (2008) 9577-9590. This paper reports a long-known binding site of VPg, for which the clearly distinct VPg-binding site on FMDV, reported by the Verdaguer group, came as a great surprise.
-
(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
-
16
-
-
52649143257
-
Crystal structure of coxsackievirus B3 3Dpol highlights the functional importance of residue 5 in picornavirus polymerases
-
Campagnola G., Weygandt M., Scoggin K., and Peersen O. Crystal structure of coxsackievirus B3 3Dpol highlights the functional importance of residue 5 in picornavirus polymerases. J Virol 82 (2008) 9458-9464
-
(2008)
J Virol
, vol.82
, pp. 9458-9464
-
-
Campagnola, G.1
Weygandt, M.2
Scoggin, K.3
Peersen, O.4
-
17
-
-
4644238112
-
Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase
-
This paper reports the cruelly missing data from the pioneering work on the first ever crystallized viral RdRp, in 1995. A thorough and very detailed analysis of this important enzyme.
-
Thompson A.A., and Peersen O.B. Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase. EMBO J 23 (2004) 3462-3471. This paper reports the cruelly missing data from the pioneering work on the first ever crystallized viral RdRp, in 1995. A thorough and very detailed analysis of this important enzyme.
-
(2004)
EMBO J
, vol.23
, pp. 3462-3471
-
-
Thompson, A.A.1
Peersen, O.B.2
-
18
-
-
33644519317
-
The structure of a protein primer polymerase complex in the initiation of genome replication
-
This paper reports the VPg-binding site on the front side of the FMDV polymerase, coming as a total surprise in the picornavirus community, largely opening and renewing interest in replication field.
-
Ferrer-Orta C., Arias A., Agudo R., Perez-Luque R., Escarmis C., Domingo E., and Verdaguer N. The structure of a protein primer polymerase complex in the initiation of genome replication. EMBO J 25 (2006) 880-888. This paper reports the VPg-binding site on the front side of the FMDV polymerase, coming as a total surprise in the picornavirus community, largely opening and renewing interest in replication field.
-
(2006)
EMBO J
, vol.25
, pp. 880-888
-
-
Ferrer-Orta, C.1
Arias, A.2
Agudo, R.3
Perez-Luque, R.4
Escarmis, C.5
Domingo, E.6
Verdaguer, N.7
-
19
-
-
0030732120
-
Genetic dissection of interaction between poliovirus 3D polymerase and viral protein 3AB
-
Hope D.A., Diamond S.E., and Kirkegaard K. Genetic dissection of interaction between poliovirus 3D polymerase and viral protein 3AB. J Virol 71 (1997) 9490-9498
-
(1997)
J Virol
, vol.71
, pp. 9490-9498
-
-
Hope, D.A.1
Diamond, S.E.2
Kirkegaard, K.3
-
20
-
-
0037150679
-
Visualization and functional analysis of RNA-dependent RNA polymerase lattices
-
This paper uses electron microscopy to demonstrate that purified poliovirus RNA-dependent RNA polymerase forms planar and tubular oligomeric arrays, and correlates this in vitro study to similar observations in infected cells, in which cooperative RNA binding and RNA elongation can be assayed using mutant polymerases.
-
Lyle J.M., Bullitt E., Bienz K., and Kirkegaard K. Visualization and functional analysis of RNA-dependent RNA polymerase lattices. Science 296 (2002) 2218-2222. This paper uses electron microscopy to demonstrate that purified poliovirus RNA-dependent RNA polymerase forms planar and tubular oligomeric arrays, and correlates this in vitro study to similar observations in infected cells, in which cooperative RNA binding and RNA elongation can be assayed using mutant polymerases.
-
(2002)
Science
, vol.296
, pp. 2218-2222
-
-
Lyle, J.M.1
Bullitt, E.2
Bienz, K.3
Kirkegaard, K.4
-
21
-
-
33344464455
-
Nucleotide channel of RNA-dependent RNA polymerase used for intermolecular uridylylation of protein primer
-
Tellez A.B., Crowder S., Spagnolo J.F., Thompson A.A., Peersen O.B., Brutlag D.L., and Kirkegaard K. Nucleotide channel of RNA-dependent RNA polymerase used for intermolecular uridylylation of protein primer. J Mol Biol 357 (2006) 665-675
-
(2006)
J Mol Biol
, vol.357
, pp. 665-675
-
-
Tellez, A.B.1
Crowder, S.2
Spagnolo, J.F.3
Thompson, A.A.4
Peersen, O.B.5
Brutlag, D.L.6
Kirkegaard, K.7
-
22
-
-
59649110607
-
Nucleic acid polymerases use a general acid for nucleotidyl transfer
-
A conserved basic residue from motif D (Lys or Arg) is proposed to act as an acid to assist pyrophosphate release after phosphodiester bond formation.
-
Castro C., Smidansky E.D., Arnold J.J., Maksimchuk K.R., Moustafa I., Uchida A., Götte M., Konigsberg W., and Cameron C.E. Nucleic acid polymerases use a general acid for nucleotidyl transfer. Nat Struct Mol Biol 16 (2009) 212-218. A conserved basic residue from motif D (Lys or Arg) is proposed to act as an acid to assist pyrophosphate release after phosphodiester bond formation.
-
(2009)
Nat Struct Mol Biol
, vol.16
, pp. 212-218
-
-
Castro, C.1
Smidansky, E.D.2
Arnold, J.J.3
Maksimchuk, K.R.4
Moustafa, I.5
Uchida, A.6
Götte, M.7
Konigsberg, W.8
Cameron, C.E.9
-
23
-
-
56649105365
-
2+ in the activity of phi6 RNA dependent RNA polymerase
-
This paper explains the long-standing puzzle of the Mn versus Mg role in structural flexibility of the polymerase active site to promote efficient RNA synthesis.
-
2+ in the activity of phi6 RNA dependent RNA polymerase. Nucleic Acid Res 36 (2008) 6633-6644. This paper explains the long-standing puzzle of the Mn versus Mg role in structural flexibility of the polymerase active site to promote efficient RNA synthesis.
-
(2008)
Nucleic Acid Res
, vol.36
, pp. 6633-6644
-
-
Poranen, M.N.1
Salgado, P.S.2
Koivunen, M.R.L.3
Wright, S.4
Bamford, D.H.5
Stuart, D.I.6
Grimes, J.M.7
-
24
-
-
56449126887
-
Metal ion-binding studies highlight important differences between flaviviral RNA polymerases
-
Bougie I., and Bisaillon M. Metal ion-binding studies highlight important differences between flaviviral RNA polymerases. Biochim Biophys Acta 1794 (2009) 50-60
-
(2009)
Biochim Biophys Acta
, vol.1794
, pp. 50-60
-
-
Bougie, I.1
Bisaillon, M.2
-
25
-
-
33745962422
-
Comparative mechanistic studies of de-novo RNA synthesis by flavivirus RNA-dependent RNA polymerase
-
Selisko B., Dutartre H., Guillemot J.C., Debarnot C., Benarroch D., Khromykh A., Despres P., Egloff M.-P., and Canard B. Comparative mechanistic studies of de-novo RNA synthesis by flavivirus RNA-dependent RNA polymerase. Virology 351 1 (2006) 145-158
-
(2006)
Virology
, vol.351
, Issue.1
, pp. 145-158
-
-
Selisko, B.1
Dutartre, H.2
Guillemot, J.C.3
Debarnot, C.4
Benarroch, D.5
Khromykh, A.6
Despres, P.7
Egloff, M.-P.8
Canard, B.9
-
26
-
-
50249147367
-
The flavivirus polymerase as a target for drug discovery
-
Malet H., Massé N., Selisko B., Romette J.-L., Alvarez K., Guillemot J.-C., Tolou H., Yap T.L., Vasudevan S.G., Lescar J., and Canard B. The flavivirus polymerase as a target for drug discovery. Antiviral Res 80 (2008) 23-35
-
(2008)
Antiviral Res
, vol.80
, pp. 23-35
-
-
Malet, H.1
Massé, N.2
Selisko, B.3
Romette, J.-L.4
Alvarez, K.5
Guillemot, J.-C.6
Tolou, H.7
Yap, T.L.8
Vasudevan, S.G.9
Lescar, J.10
Canard, B.11
-
27
-
-
0035826258
-
A mechanism for initiating RNA dependent RNA polymerization
-
The first crystal structure of a viral RdRp (from phi6) in complex with RNA and/or nucleotide, giving the first structure-based model about how RNA synthesis is initiated de novo.
-
Butcher S.J., Grimes J.M., Makeyev E.V., Bamford D.H., and Stuart D.I. A mechanism for initiating RNA dependent RNA polymerization. Nature 410 (2001) 235-240. The first crystal structure of a viral RdRp (from phi6) in complex with RNA and/or nucleotide, giving the first structure-based model about how RNA synthesis is initiated de novo.
-
(2001)
Nature
, vol.410
, pp. 235-240
-
-
Butcher, S.J.1
Grimes, J.M.2
Makeyev, E.V.3
Bamford, D.H.4
Stuart, D.I.5
-
28
-
-
62549117410
-
Insights into the preinitiation events of bacteriophage phi6 RNA-dependent RNA polymerase: towards the assembly of a productive binary complex
-
Sarin L.P., Poranen M.M., Lehti N.M., Ravanti J.J., Koivunen M.R., Aalto A.P., Van Dijk A.A., Stuart D.I., Grimes J.M., and Bamford D.H. Insights into the preinitiation events of bacteriophage phi6 RNA-dependent RNA polymerase: towards the assembly of a productive binary complex. Nucleic Acid Res 37 (2009) 1182-1192
-
(2009)
Nucleic Acid Res
, vol.37
, pp. 1182-1192
-
-
Sarin, L.P.1
Poranen, M.M.2
Lehti, N.M.3
Ravanti, J.J.4
Koivunen, M.R.5
Aalto, A.P.6
Van Dijk, A.A.7
Stuart, D.I.8
Grimes, J.M.9
Bamford, D.H.10
-
29
-
-
0037470586
-
Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): structural evidence for nucleotide import and de novo initiation
-
O'Farrell, Trowbridge R., Rowlands D., and Jaeger J. Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): structural evidence for nucleotide import and de novo initiation. J Mol Biol 326 (2003) 1025-1035
-
(2003)
J Mol Biol
, vol.326
, pp. 1025-1035
-
-
O'Farrell1
Trowbridge, R.2
Rowlands, D.3
Jaeger, J.4
-
30
-
-
34547178347
-
Sequential structures provide insights into the fidelity of RNA replication
-
A series of outstanding structures showing the basis of nucleotide selection in four elongation complexes, including that of ribavirin, which has been demonstrated to be mutagenic in Picornaviridae.
-
Ferrer-Orta C., Arias A., Perez-Luque R., Escarmis C., Domingo E., and Verdaguer N. Sequential structures provide insights into the fidelity of RNA replication. Proc Natl Acad Sci U S A 104 (2007) 9463-9468. A series of outstanding structures showing the basis of nucleotide selection in four elongation complexes, including that of ribavirin, which has been demonstrated to be mutagenic in Picornaviridae.
-
(2007)
Proc Natl Acad Sci U S A
, vol.104
, pp. 9463-9468
-
-
Ferrer-Orta, C.1
Arias, A.2
Perez-Luque, R.3
Escarmis, C.4
Domingo, E.5
Verdaguer, N.6
-
31
-
-
8744222695
-
Structure of foot and mouth disease virus RNA dependent RNA polymerase and its complex with a template primer RNA
-
This paper describes the crystal structure of unliganded and liganded polymerase with template/primer, giving the first image of this complex in Picornaviridae.
-
Ferrer-Orta C., Arias A., Agudo R., Perez-Luque R., Escarmis C., Domingo E., and Verdaguer N. Structure of foot and mouth disease virus RNA dependent RNA polymerase and its complex with a template primer RNA. J Biol Chem 279 (2004) 47212-47221. This paper describes the crystal structure of unliganded and liganded polymerase with template/primer, giving the first image of this complex in Picornaviridae.
-
(2004)
J Biol Chem
, vol.279
, pp. 47212-47221
-
-
Ferrer-Orta, C.1
Arias, A.2
Agudo, R.3
Perez-Luque, R.4
Escarmis, C.5
Domingo, E.6
Verdaguer, N.7
-
32
-
-
0141459560
-
Temperature requirements for initiation of RNA dependent RNA polymerization
-
Yang H., Gottlieb P., Wei H., Bamford D.H., and Makeyev E.V. Temperature requirements for initiation of RNA dependent RNA polymerization. Virology 314 (2003) 706-715
-
(2003)
Virology
, vol.314
, pp. 706-715
-
-
Yang, H.1
Gottlieb, P.2
Wei, H.3
Bamford, D.H.4
Makeyev, E.V.5
-
33
-
-
0035955628
-
De novo synthesis of RNA by the dengue vírus RNA dependent RNA polymerase exhibits temperature dependence at the initiation but not elongation phase
-
Ackermann M., and Padmanabhan R. De novo synthesis of RNA by the dengue vírus RNA dependent RNA polymerase exhibits temperature dependence at the initiation but not elongation phase. J Biol Chem 276 (2001) 39926-39937
-
(2001)
J Biol Chem
, vol.276
, pp. 39926-39937
-
-
Ackermann, M.1
Padmanabhan, R.2
-
34
-
-
50649091630
-
A locking mechanism regulates RNA synthesis and host protein interaction by the hepatitis C vírus polymerase
-
Chinnaswamy S., Yarbrough I., Palaninathan S., Kumar C.T.R., Vijayaraghavan V., Demeler B., Lemon S.M., Sachettini J.C., and Kao C.C. A locking mechanism regulates RNA synthesis and host protein interaction by the hepatitis C vírus polymerase. J Biol Chem 283 (2008) 20535-20546
-
(2008)
J Biol Chem
, vol.283
, pp. 20535-20546
-
-
Chinnaswamy, S.1
Yarbrough, I.2
Palaninathan, S.3
Kumar, C.T.R.4
Vijayaraghavan, V.5
Demeler, B.6
Lemon, S.M.7
Sachettini, J.C.8
Kao, C.C.9
-
35
-
-
34548679815
-
Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle
-
Electron tomography was used to visualize membrane vesicles that act as RNA replication sites for Flock House virus providing a model that might apply to other positive-strand RNA viruses including alphaviruses and flaviviruses.
-
Kopek B.G., Perkins G., Miller D.J., Ellisman M.H., and Ahlquist P. Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle. PLoS Biol 5 9 (2009) e220. Electron tomography was used to visualize membrane vesicles that act as RNA replication sites for Flock House virus providing a model that might apply to other positive-strand RNA viruses including alphaviruses and flaviviruses.
-
(2009)
PLoS Biol
, vol.5
, Issue.9
-
-
Kopek, B.G.1
Perkins, G.2
Miller, D.J.3
Ellisman, M.H.4
Ahlquist, P.5
-
36
-
-
57149091105
-
Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein
-
Using a set of crystallographic snapshots that include a complex with a transition state analog, this paper describes the complete ATP hydrolytic cycle as well as single-stranded RNA binding by the flavivirus NS3 protein, a key partner for viral RNA replication by the NS5 enzyme. Large conformational changes in the ATP-binding domains are induced by ssRNA binding.
-
Luo D., Xu T., Watson R.P., Scherer-Becker D., Sampath A., Jahnke W., Yeong S.S., Wang C.H., Lim S.P., Strongin A., et al. Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein. EMBO J 27 (2008) 3209-3219. Using a set of crystallographic snapshots that include a complex with a transition state analog, this paper describes the complete ATP hydrolytic cycle as well as single-stranded RNA binding by the flavivirus NS3 protein, a key partner for viral RNA replication by the NS5 enzyme. Large conformational changes in the ATP-binding domains are induced by ssRNA binding.
-
(2008)
EMBO J
, vol.27
, pp. 3209-3219
-
-
Luo, D.1
Xu, T.2
Watson, R.P.3
Scherer-Becker, D.4
Sampath, A.5
Jahnke, W.6
Yeong, S.S.7
Wang, C.H.8
Lim, S.P.9
Strongin, A.10
-
37
-
-
43149087336
-
Structural insights into mechanisms of catalysis and inhibition in Norwalk virus polymerase
-
Zamyatkin D.F., Parra F., Alonso J.M., Harki D.A., Peterson B.R., Grochulski P., and Ng K. Structural insights into mechanisms of catalysis and inhibition in Norwalk virus polymerase. J Biol Chem 283 (2008) 7705-7712
-
(2008)
J Biol Chem
, vol.283
, pp. 7705-7712
-
-
Zamyatkin, D.F.1
Parra, F.2
Alonso, J.M.3
Harki, D.A.4
Peterson, B.R.5
Grochulski, P.6
Ng, K.7
|