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Volumn 42, Issue 4, 2014, Pages 2538-2554

A cypovirus VP5 displays the RNA chaperone-like activity that destabilizes RNA helices and accelerates strand annealing

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CAPSID PROTEIN; CHAPERONE; DOUBLE STRANDED RNA; MAGNESIUM ION; MANGANESE; PROTEIN VP5; UNCLASSIFIED DRUG; VIRUS RNA; ZINC ION;

EID: 84895813112     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt1256     Document Type: Article
Times cited : (20)

References (54)
  • 1
    • 1542328804 scopus 로고    scopus 로고
    • The dsRNA viruses
    • Mertens, P. (2004) The dsRNA viruses. Virus Res., 101, 3-13.
    • (2004) Virus Res. , vol.101 , pp. 3-13
    • Mertens, P.1
  • 2
    • 0036784877 scopus 로고    scopus 로고
    • The dsRNA Viridae and their catalytic capsids
    • Reinisch, K.M. (2002) The dsRNA Viridae and their catalytic capsids. Nat. Struct. Biol., 9, 714-716.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 714-716
    • Reinisch, K.M.1
  • 3
    • 0037428437 scopus 로고    scopus 로고
    • Structural comparisons of empty and full cytoplasmic polyhedrosis virus. Protein-RNA interactions and implications for endogenous RNA transcription mechanism
    • Xia, Q., Jakana, J., Zhang, J.Q. and Zhou, Z.H. (2003) Structural comparisons of empty and full cytoplasmic polyhedrosis virus. Protein-RNA interactions and implications for endogenous RNA transcription mechanism. J. Biol. Chem., 278, 1094-1100.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1094-1100
    • Xia, Q.1    Jakana, J.2    Zhang, J.Q.3    Zhou, Z.H.4
  • 4
    • 84858221251 scopus 로고    scopus 로고
    • Rossmann, M.G. and Rao, V.B. (eds), Science, Springer, New York, NY, USA
    • Poranen, M.M. and Bamford, D.H. (2012) In: Rossmann, M.G. and Rao, V.B. (eds), Viral Molecular Machines. Science, Springer, New York, NY, USA, pp. 379-402.
    • (2012) Viral Molecular Machines , pp. 379-402
    • Poranen, M.M.1    Bamford, D.H.2
  • 10
    • 0141960927 scopus 로고    scopus 로고
    • Cytoplasmic polyhedrosis virus structure at 8 A by electron cryomicroscopy: Structural basis of capsid stability and mRNA processing regulation
    • Zhou, Z.H., Zhang, H., Jakana, J., Lu, X.-Y. and Zhang, J.-Q. (2003) Cytoplasmic polyhedrosis virus structure at 8 A by electron cryomicroscopy: structural basis of capsid stability and mRNA processing regulation. Structure, 11, 651-663.
    • (2003) Structure , vol.11 , pp. 651-663
    • Zhou, Z.H.1    Zhang, H.2    Jakana, J.3    Lu, X.-Y.4    Zhang, J.-Q.5
  • 11
    • 43749092377 scopus 로고    scopus 로고
    • 3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
    • Yu, X., Jin, L. and Zhou, Z.H. (2008) 3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy. Nature, 453, 415-419.
    • (2008) Nature , vol.453 , pp. 415-419
    • Yu, X.1    Jin, L.2    Zhou, Z.H.3
  • 12
    • 79952178436 scopus 로고    scopus 로고
    • Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping
    • Cheng, L., Sun, J., Zhang, K., Mou, Z., Huang, X., Ji, G., Sun, F., Zhang, J. and Zhu, P. (2011) Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping. Proc. Natl Acad. Sci. USA, 108, 1373-1378.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 1373-1378
    • Cheng, L.1    Sun, J.2    Zhang, K.3    Mou, Z.4    Huang, X.5    Ji, G.6    Sun, F.7    Zhang, J.8    Zhu, P.9
  • 14
    • 59749097987 scopus 로고    scopus 로고
    • Role of RNA chaperones in virus replication
    • Zuniga, S., Sola, I., Cruz, J.L. and Enjuanes, L. (2009) Role of RNA chaperones in virus replication. Virus Res., 139, 253-266.
    • (2009) Virus Res. , vol.139 , pp. 253-266
    • Zuniga, S.1    Sola, I.2    Cruz, J.L.3    Enjuanes, L.4
  • 15
    • 78751661207 scopus 로고    scopus 로고
    • RNA remodeling by chaperones and helicases
    • Musier-Forsyth, K. (2010) RNA remodeling by chaperones and helicases. RNA Biol., 7, 632-633.
    • (2010) RNA Biol. , vol.7 , pp. 632-633
    • Musier-Forsyth, K.1
  • 16
    • 0023645817 scopus 로고
    • Conserved elements in the 3' untranslated region of flavivirus RNAs and potential cyclization sequences
    • Hahn, C.S., Hahn, Y.S., Rice, C.M., Lee, E., Dalgarno, L., Strauss, E.G. and Strauss, J.H. (1987) Conserved elements in the 3' untranslated region of flavivirus RNAs and potential cyclization sequences. J. Mol. Biol., 198, 33-41.
    • (1987) J. Mol. Biol. , vol.198 , pp. 33-41
    • Hahn, C.S.1    Hahn, Y.S.2    Rice, C.M.3    Lee, E.4    Dalgarno, L.5    Strauss, E.G.6    Strauss, J.H.7
  • 17
    • 0024497177 scopus 로고
    • The ends of la Crosse virus genome and antigenome RNAs within nucleocapsids are base paired
    • Raju, R. and Kolakofsky, D. (1989) The ends of La Crosse virus genome and antigenome RNAs within nucleocapsids are base paired. J. Virol., 63, 122-128.
    • (1989) J. Virol. , vol.63 , pp. 122-128
    • Raju, R.1    Kolakofsky, D.2
  • 18
    • 29844450783 scopus 로고    scopus 로고
    • A base-specific recognition signal in the 5' consensus sequence of rotavirus plus-strand RNAs promotes replication of the double-stranded RNA genome segments
    • Tortorici, M.A., Shapiro, B.A. and Patton, J.T. (2006) A base-specific recognition signal in the 5' consensus sequence of rotavirus plus-strand RNAs promotes replication of the double-stranded RNA genome segments. RNA, 12, 133-146.
    • (2006) RNA , vol.12 , pp. 133-146
    • Tortorici, M.A.1    Shapiro, B.A.2    Patton, J.T.3
  • 19
    • 0031870250 scopus 로고    scopus 로고
    • Rotavirus RNA replication requires a single-stranded 3' end for efficient minus-strand synthesis
    • Chen, D. and Patton, J.T. (1998) Rotavirus RNA replication requires a single-stranded 3' end for efficient minus-strand synthesis. J. Virol., 72, 7387-7396.
    • (1998) J. Virol. , vol.72 , pp. 7387-7396
    • Chen, D.1    Patton, J.T.2
  • 20
    • 29844447905 scopus 로고    scopus 로고
    • RNA structure and the replication of the rotavirus segmented double-stranded RNA genome
    • Patton, J.T. and Spencer, E. (2001) RNA structure and the replication of the rotavirus segmented double-stranded RNA genome. Recent Res. Devel. Virol., 3, 529-539.
    • (2001) Recent Res. Devel. Virol. , vol.3 , pp. 529-539
    • Patton, J.T.1    Spencer, E.2
  • 21
    • 33745257290 scopus 로고    scopus 로고
    • Characterization of the RNA chaperone activity of hantavirus nucleocapsid protein
    • Mir, M.A. and Panganiban, A.T. (2006) Characterization of the RNA chaperone activity of hantavirus nucleocapsid protein. J. Virol., 80, 6276-6285.
    • (2006) J. Virol. , vol.80 , pp. 6276-6285
    • Mir, M.A.1    Panganiban, A.T.2
  • 22
    • 78751677070 scopus 로고    scopus 로고
    • Taming free energy landscapes with RNA chaperones
    • Woodson, S.A. (2010) Taming free energy landscapes with RNA chaperones. RNA Biol., 7, 677-686.
    • (2010) RNA Biol. , vol.7 , pp. 677-686
    • Woodson, S.A.1
  • 23
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton, M.R., Dillingham, M.S. and Wigley, D.B. (2007) Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem., 76, 23-50.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 24
    • 31644432213 scopus 로고    scopus 로고
    • Identification and genome characterization of Heliothis armigera cypovirus types 5 and 14 and Heliothis assulta cypovirus type 14
    • Li, Y., Tan, L., Chen, W., Zhang, J. and Hu, Y. (2006) Identification and genome characterization of Heliothis armigera cypovirus types 5 and 14 and Heliothis assulta cypovirus type 14. J. Gen. Virol., 87, 387-394.
    • (2006) J. Gen. Virol. , vol.87 , pp. 387-394
    • Li, Y.1    Tan, L.2    Chen, W.3    Zhang, J.4    Hu, Y.5
  • 25
    • 43049130283 scopus 로고    scopus 로고
    • The complete nucleotide sequence of the type 5 Helicoverpa armigera cytoplasmic polyhedrosis virus genome
    • Tan, L., Zhang, J., Li, Y., Li, Y., Jiang, H., Cao, X. and Hu, Y. (2008) The complete nucleotide sequence of the type 5 Helicoverpa armigera cytoplasmic polyhedrosis virus genome. Virus Genes, 36, 587-593.
    • (2008) Virus Genes , vol.36 , pp. 587-593
    • Tan, L.1    Zhang, J.2    Li, Y.3    Li, Y.4    Jiang, H.5    Cao, X.6    Hu, Y.7
  • 26
    • 0043222570 scopus 로고    scopus 로고
    • Fully automated ab initio protein structure prediction using I-SITES, HMMSTR and ROSETTA
    • Bystroff, C. and Shao, Y. (2002) Fully automated ab initio protein structure prediction using I-SITES, HMMSTR and ROSETTA. Bioinformatics, 18(Suppl. 1), S54-S61.
    • (2002) Bioinformatics , vol.18 , Issue.SUPPL. 1
    • Bystroff, C.1    Shao, Y.2
  • 27
    • 84863710481 scopus 로고    scopus 로고
    • Genetic modification of baculovirus expression vectors
    • Li, S.F., Wang, H.L., Hu, Z.H. and Deng, F. (2012) Genetic modification of baculovirus expression vectors. Virol. Sin., 27, 71-82.
    • (2012) Virol. Sin. , vol.27 , pp. 71-82
    • Li, S.F.1    Wang, H.L.2    Hu, Z.H.3    Deng, F.4
  • 28
    • 84867204423 scopus 로고    scopus 로고
    • Identification and characterization of RNA duplex unwinding and ATPase activities of an alphatetravirus superfamily 1 helicase
    • Wang, Q., Han, Y., Qiu, Y., Zhang, S., Tang, F., Wang, Y., Zhang, J., Hu, Y. and Zhou, X. (2012) Identification and characterization of RNA duplex unwinding and ATPase activities of an alphatetravirus superfamily 1 helicase. Virology, 433, 440-448.
    • (2012) Virology , vol.433 , pp. 440-448
    • Wang, Q.1    Han, Y.2    Qiu, Y.3    Zhang, S.4    Tang, F.5    Wang, Y.6    Zhang, J.7    Hu, Y.8    Zhou, X.9
  • 29
    • 80052481402 scopus 로고    scopus 로고
    • RNA binding by a novel helical fold of B2 protein from wuhan nodavirus mediates the suppression of RNA interference and promotes B2 dimerization
    • Qi, N., Cai, D., Qiu, Y., Xie, J., Wang, Z., Si, J., Zhang, J., Zhou, X. and Hu, Y. (2011) RNA binding by a novel helical fold of B2 protein from wuhan nodavirus mediates the suppression of RNA interference and promotes B2 dimerization. J. Virol., 85, 9543-9554.
    • (2011) J. Virol. , vol.85 , pp. 9543-9554
    • Qi, N.1    Cai, D.2    Qiu, Y.3    Xie, J.4    Wang, Z.5    Si, J.6    Zhang, J.7    Zhou, X.8    Hu, Y.9
  • 30
    • 84860840233 scopus 로고    scopus 로고
    • Targeting of Dicer-2 and RNA by a viral RNA silencing suppressor in Drosophila cells
    • Qi, N., Zhang, L., Qiu, Y., Wang, Z., Si, J., Liu, Y., Xiang, X., Xie, J., Qin, C.F., Zhou, X. et al. (2012) Targeting of Dicer-2 and RNA by a viral RNA silencing suppressor in Drosophila cells. J. Virol., 86, 5763-5773.
    • (2012) J. Virol. , vol.86 , pp. 5763-5773
    • Qi, N.1    Zhang, L.2    Qiu, Y.3    Wang, Z.4    Si, J.5    Liu, Y.6    Xiang, X.7    Xie, J.8    Qin, C.F.9    Zhou, X.10
  • 31
    • 84875809495 scopus 로고    scopus 로고
    • Membrane association of Wuhan nodavirus protein A is required for its ability to accumulate genomic RNA1 template
    • Qiu, Y., Wang, Z., Liu, Y., Qi, N., Miao, M., Si, J., Xiang, X., Cai, D., Hu, Y. and Zhou, X. (2013) Membrane association of Wuhan nodavirus protein A is required for its ability to accumulate genomic RNA1 template. Virology, 439, 140-151.
    • (2013) Virology , vol.439 , pp. 140-151
    • Qiu, Y.1    Wang, Z.2    Liu, Y.3    Qi, N.4    Miao, M.5    Si, J.6    Xiang, X.7    Cai, D.8    Hu, Y.9    Zhou, X.10
  • 32
    • 84876338726 scopus 로고    scopus 로고
    • The nonstructural protein 2C of a picorna-like virus displays nucleic acid helix destabilizing activity that can be functionally separated from its ATPase activity
    • Cheng, Z., Yang, J., Xia, H., Qiu, Y., Wang, Z., Han, Y., Xia, X., Qin, C.-F., Hu, Y. and Zhou, X. (2013) The nonstructural protein 2C of a picorna-like virus displays nucleic acid helix destabilizing activity that can be functionally separated from its ATPase activity. J. Virol., 87, 5205-5218.
    • (2013) J. Virol. , vol.87 , pp. 5205-5218
    • Cheng, Z.1    Yang, J.2    Xia, H.3    Qiu, Y.4    Wang, Z.5    Han, Y.6    Xia, X.7    Qin, C.-F.8    Hu, Y.9    Zhou, X.10
  • 33
    • 79955867558 scopus 로고    scopus 로고
    • Atomic model of CPV reveals the mechanism used by this single-shelled virus to economically carry out functions conserved in multishelled reoviruses
    • Yu, X., Ge, P., Jiang, J., Atanasov, I. and Zhou, Z.H. (2011) Atomic model of CPV reveals the mechanism used by this single-shelled virus to economically carry out functions conserved in multishelled reoviruses. Structure, 19, 652-661.
    • (2011) Structure , vol.19 , pp. 652-661
    • Yu, X.1    Ge, P.2    Jiang, J.3    Atanasov, I.4    Zhou, Z.H.5
  • 34
    • 0036307597 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein as a nucleic acid chaperone: Spectroscopic study of its helix-destabilizing properties structural binding specificity, and annealing activity
    • Urbaneja, M.A., Wu, M., Casas-Finet, J.R. and Karpel, R.L. (2002) HIV-1 nucleocapsid protein as a nucleic acid chaperone: spectroscopic study of its helix-destabilizing properties, structural binding specificity, and annealing activity. J. Mol. Biol., 318, 749-764.
    • (2002) J. Mol. Biol. , vol.318 , pp. 749-764
    • Urbaneja, M.A.1    Wu, M.2    Casas-Finet, J.R.3    Karpel, R.L.4
  • 35
    • 84859343415 scopus 로고    scopus 로고
    • Analysis of the RNA chaperoning activity of the hepatitis C virus core protein on the conserved 3'X region of the viral genome
    • Sharma, K.K., de Rocquigny, H., Darlix, J.L., Lavergne, J.P., Penin, F., Lessinger, J.M. and Mely, Y. (2011) Analysis of the RNA chaperoning activity of the hepatitis C virus core protein on the conserved 3'X region of the viral genome. Nucleic Acids Res., 40, 2540-2553.
    • (2011) Nucleic Acids Res. , vol.40 , pp. 2540-2553
    • Sharma, K.K.1    De Rocquigny, H.2    Darlix, J.L.3    Lavergne, J.P.4    Penin, F.5    Lessinger, J.M.6    Mely, Y.7
  • 36
    • 0033558752 scopus 로고    scopus 로고
    • In vivo detection, RNA-binding properties and characterization of the rna-binding domain of the p7 putative movement protein from carnation mottle carmovirus (CarMV)
    • Marcos, J.F., Vilar, M., Perez-Paya, E. and Pallas, V. (1999) In vivo detection, RNA-binding properties and characterization of the rna-binding domain of the p7 putative movement protein from carnation mottle carmovirus (CarMV). Virology, 255, 354-365.
    • (1999) Virology , vol.255 , pp. 354-365
    • Marcos, J.F.1    Vilar, M.2    Perez-Paya, E.3    Pallas, V.4
  • 37
    • 0042389654 scopus 로고    scopus 로고
    • Characterization of the RNA-binding domains in the replicase proteins of tomato bushy stunt virus
    • Rajendran, K.S. and Nagy, P.D. (2003) Characterization of the RNA-binding domains in the replicase proteins of tomato bushy stunt virus. J. Virol., 77, 9244-9258.
    • (2003) J. Virol. , vol.77 , pp. 9244-9258
    • Rajendran, K.S.1    Nagy, P.D.2
  • 38
    • 0041732006 scopus 로고    scopus 로고
    • Differing roles of the N-and C-terminal zinc fingers in human immunodeficiency virus nucleocapsid protein-enhanced nucleic acid annealing
    • Heath, M.J., Derebail, S.S., Gorelick, R.J. and DeStefano, J.J. (2003) Differing roles of the N-and C-terminal zinc fingers in human immunodeficiency virus nucleocapsid protein-enhanced nucleic acid annealing. J. Biol. Chem., 278, 30755-30763.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30755-30763
    • Heath, M.J.1    Derebail, S.S.2    Gorelick, R.J.3    Destefano, J.J.4
  • 39
    • 32444439218 scopus 로고    scopus 로고
    • Poliovirus protein 3AB displays nucleic acid chaperone and helix-destabilizing activities
    • DeStefano, J.J. and Titilope, O. (2006) Poliovirus protein 3AB displays nucleic acid chaperone and helix-destabilizing activities. J. Virol., 80, 1662-1671.
    • (2006) J. Virol. , vol.80 , pp. 1662-1671
    • Destefano, J.J.1    Titilope, O.2
  • 40
    • 78751674527 scopus 로고    scopus 로고
    • The twenty-nine amino acid C-terminal cytoplasmic domain of poliovirus 3AB is critical for nucleic acid chaperone activity
    • Gangaramani, D.R., Eden, E.L., Shah, M. and DeStefano, J.J. (2010) The twenty-nine amino acid C-terminal cytoplasmic domain of poliovirus 3AB is critical for nucleic acid chaperone activity. RNA Biol., 7, 820-829.
    • (2010) RNA Biol. , vol.7 , pp. 820-829
    • Gangaramani, D.R.1    Eden, E.L.2    Shah, M.3    Destefano, J.J.4
  • 41
    • 0026011591 scopus 로고
    • Chelation of divalent cations by ATP studied by titration calorimetry
    • Wilson, J.E. and Chin, A. (1991) Chelation of divalent cations by ATP, studied by titration calorimetry. Anal. Biochem., 193, 16-19.
    • (1991) Anal. Biochem. , vol.193 , pp. 16-19
    • Wilson, J.E.1    Chin, A.2
  • 42
    • 49349112116 scopus 로고    scopus 로고
    • Subnanometer-resolution structures of the grass carp reovirus core and virion
    • Cheng, L., Fang, Q., Shah, S., Atanasov, I.C. and Zhou, Z.H. (2008) Subnanometer-resolution structures of the grass carp reovirus core and virion. J. Mol. Biol., 382, 213-222.
    • (2008) J. Mol. Biol. , vol.382 , pp. 213-222
    • Cheng, L.1    Fang, Q.2    Shah, S.3    Atanasov, I.C.4    Zhou, Z.H.5
  • 45
    • 0035034563 scopus 로고    scopus 로고
    • Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2
    • Taraporewala, Z.F. and Patton, J.T. (2001) Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2. J. Virol., 75, 4519-4527.
    • (2001) J. Virol. , vol.75 , pp. 4519-4527
    • Taraporewala, Z.F.1    Patton, J.T.2
  • 46
    • 0032759060 scopus 로고    scopus 로고
    • Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity
    • Taraporewala, Z., Chen, D. and Patton, J.T. (1999) Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity. J. Virol., 73, 9934-9943.
    • (1999) J. Virol. , vol.73 , pp. 9934-9943
    • Taraporewala, Z.1    Chen, D.2    Patton, J.T.3
  • 47
    • 0027932436 scopus 로고
    • The rotavirus RNA-binding protein NS35 (NSP2) forms 10S multimers and interacts with the viral RNA polymerase
    • Kattoura, M.D., Chen, X. and Patton, J.T. (1994) The rotavirus RNA-binding protein NS35 (NSP2) forms 10S multimers and interacts with the viral RNA polymerase. Virology, 202, 803-813.
    • (1994) Virology , vol.202 , pp. 803-813
    • Kattoura, M.D.1    Chen, X.2    Patton, J.T.3
  • 49
    • 0034715823 scopus 로고    scopus 로고
    • Genome replication and packaging of segmented double-stranded RNA viruses
    • Patton, J.T. and Spencer, E. (2000) Genome replication and packaging of segmented double-stranded RNA viruses. Virology, 277, 217-225.
    • (2000) Virology , vol.277 , pp. 217-225
    • Patton, J.T.1    Spencer, E.2
  • 50
    • 31044439245 scopus 로고    scopus 로고
    • The bunyavirus nucleocapsid protein is an RNA chaperone: Possible roles in viral RNA panhandle formation and genome replication
    • Mir, M.A. and Panganiban, A.T. (2006) The bunyavirus nucleocapsid protein is an RNA chaperone: possible roles in viral RNA panhandle formation and genome replication. RNA, 12, 272-282.
    • (2006) RNA , vol.12 , pp. 272-282
    • Mir, M.A.1    Panganiban, A.T.2
  • 51
    • 84855497590 scopus 로고    scopus 로고
    • Identification of a region of hantavirus nucleocapsid protein required for RNA chaperone activity
    • Brown, B.A. and Panganiban, A.T. (2010) Identification of a region of hantavirus nucleocapsid protein required for RNA chaperone activity. RNA Biol., 7, 830-837.
    • (2010) RNA Biol. , vol.7 , pp. 830-837
    • Brown, B.A.1    Panganiban, A.T.2
  • 52
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa, P. and Csermely, P. (2004) The role of structural disorder in the function of RNA and protein chaperones. FASEB J., 18, 1169-1175.
    • (2004) FASEB J. , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 53
    • 78650294691 scopus 로고    scopus 로고
    • RNA chaperone activity of the tombusviral p33 replication protein facilitates initiation of RNA synthesis by the viral RdRp in vitro
    • Stork, J., Kovalev, N., Sasvari, Z. and Nagy, P.D. (2011) RNA chaperone activity of the tombusviral p33 replication protein facilitates initiation of RNA synthesis by the viral RdRp in vitro. Virology, 409, 338-347.
    • (2011) Virology , vol.409 , pp. 338-347
    • Stork, J.1    Kovalev, N.2    Sasvari, Z.3    Nagy, P.D.4
  • 54
    • 4744349987 scopus 로고    scopus 로고
    • Combining prediction computation and experiment for the characterization of protein disorder
    • Bracken, C., Iakoucheva, L.M., Romero, P.R. and Dunker, A.K. (2004) Combining prediction, computation and experiment for the characterization of protein disorder. Curr. Opin. Struct. Biol., 14, 570-576.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 570-576
    • Bracken, C.1    Iakoucheva, L.M.2    Romero, P.R.3    Dunker, A.K.4


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