메뉴 건너뛰기




Volumn 85, Issue 6, 2011, Pages 2953-2963

Subcellular localization and rearrangement of endoplasmic reticulum by brome mosaic virus capsid protein

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; DOUBLE STRANDED RNA; MOSAIC VIRUS CAPSID PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 79952365639     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02020-10     Document Type: Article
Times cited : (62)

References (57)
  • 1
    • 33646826348 scopus 로고    scopus 로고
    • Parallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses
    • Ahlquist, P. 2006. Parallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses. Nat. Rev. Microbiol. 4:371-382.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 371-382
    • Ahlquist, P.1
  • 2
    • 54749090117 scopus 로고    scopus 로고
    • Delivery and expression of functional viral RNA genomes in planta by agroinfiltration, unit 16B
    • T. Downey (ed.), John Wiley & Sons Inc., Mississauga, Ontario, Canada
    • Annamalai, P., and A. L. Rao. 2006. Delivery and expression of functional viral RNA genomes in planta by agroinfiltration, unit 16B, p. 2.1-2.15. In T. Downey (ed.), Current protocols in microbiology. John Wiley & Sons Inc., Mississauga, Ontario, Canada.
    • (2006) Current Protocols in Microbiology
    • Annamalai, P.1    Rao, A.L.2
  • 3
    • 33749490370 scopus 로고    scopus 로고
    • Packaging of brome mosaic virus subgenomic RNA is functionally coupled to replication-dependent transcription and translation of coat protein
    • Annamalai, P., and A. L. Rao. 2006. Packaging of brome mosaic virus subgenomic RNA is functionally coupled to replication-dependent transcription and translation of coat protein. J. Virol. 80:10096-10108.
    • (2006) J. Virol. , vol.80 , pp. 10096-10108
    • Annamalai, P.1    Rao, A.L.2
  • 4
    • 20544448503 scopus 로고    scopus 로고
    • Replication-independent expression of genome components and capsid protein of brome mosaic virus in planta: A functional role for viral replicase in RNA packaging
    • Annamalai, P., and A. L. Rao. 2005. Replication-independent expression of genome components and capsid protein of brome mosaic virus in planta: a functional role for viral replicase in RNA packaging. Virology 338:96-111.
    • (2005) Virology , vol.338 , pp. 96-111
    • Annamalai, P.1    Rao, A.L.2
  • 5
    • 38349115693 scopus 로고    scopus 로고
    • Replication-coupled packaging mechanism in positive-strand RNA viruses: Synchronized coexpression of functional multigenome RNA components of an animal and a plant virus in Nicotiana benthamiana cells by agroinfiltration
    • Annamalai, P., F. Rofail, D. A. Demason, and A. L. Rao. 2008. Replication-coupled packaging mechanism in positive-strand RNA viruses: synchronized coexpression of functional multigenome RNA components of an animal and a plant virus in Nicotiana benthamiana cells by agroinfiltration. J. Virol. 82:1484-1495.
    • (2008) J. Virol. , vol.82 , pp. 1484-1495
    • Annamalai, P.1    Rofail, F.2    Demason, D.A.3    Rao, A.L.4
  • 6
    • 70349835375 scopus 로고    scopus 로고
    • Analysis of potato virus X replicase and TGBp3 subcellular locations
    • Bamunusinghe, D., et al. 2009. Analysis of potato virus X replicase and TGBp3 subcellular locations. Virology 393:272-285.
    • (2009) Virology , vol.393 , pp. 272-285
    • Bamunusinghe, D.1
  • 7
    • 74549189980 scopus 로고    scopus 로고
    • A unique role for the host ESCRT proteins in replication of tomato bushy stunt virus
    • Barajas, D., Y. Jiang, and P. D. Nagy. 2009. A unique role for the host ESCRT proteins in replication of tomato bushy stunt virus. PLoS Pathog. 5:e1000705.
    • (2009) PLoS Pathog , vol.5
    • Barajas, D.1    Jiang, Y.2    Nagy, P.D.3
  • 8
    • 0031627012 scopus 로고    scopus 로고
    • Electron microscopic-silver enhancement for double labeling with antibodies raised in the same species
    • Bienz, K., and D. Egger. 1998. Electron microscopic-silver enhancement for double labeling with antibodies raised in the same species. Methods Mol. Biol. 80:313-318.
    • (1998) Methods Mol. Biol. , vol.80 , pp. 313-318
    • Bienz, K.1    Egger, D.2
  • 9
    • 84934441334 scopus 로고    scopus 로고
    • Role of capsid proteins
    • Bol, J. F. 2008. Role of capsid proteins. Methods Mol. Biol. 451:21-31.
    • (2008) Methods Mol. Biol. , vol.451 , pp. 21-31
    • Bol, J.F.1
  • 10
    • 0034001930 scopus 로고    scopus 로고
    • Brome mosaic virus polymerase-like protein 2a is directed to the endoplasmic reticulum by helicase-like viral protein 1a
    • DOI 10.1128/JVI.74.9.4310-4318.2000
    • Chen, J., and P. Ahlquist. 2000. Brome mosaic virus polymerase-like protein 2a is directed to the endoplasmic reticulum by helicase-like viral protein 1a. J. Virol. 74:4310-4318. (Pubitemid 30214439)
    • (2000) Journal of Virology , vol.74 , Issue.9 , pp. 4310-4318
    • Chen, J.1    Ahlquist, P.2
  • 11
    • 0037320030 scopus 로고    scopus 로고
    • An alternate pathway for recruiting template RNA to the brome mosaic virus RNA replication complex
    • DOI 10.1128/JVI.77.4.2568-2577.2003
    • Chen, J., A. Noueiry, and P. Ahlquist. 2003. An alternate pathway for recruiting template RNA to the brome mosaic virus RNA replication complex. J. Virol. 77:2568-2577. (Pubitemid 36222781)
    • (2003) Journal of Virology , vol.77 , Issue.4 , pp. 2568-2577
    • Chen, J.1    Noueiry, A.2    Ahlquist, P.3
  • 12
    • 0343012080 scopus 로고    scopus 로고
    • Molecular studies on bromovirus capsid protein. VI. Contributions of the N-terminal arginine-rich motif of BMV capsid protein to virion stability and RNA packaging
    • Choi, Y. G., G. L. Grantham, and A. L. Rao. 2000. Molecular studies on bromovirus capsid protein. VI. Contributions of the N-terminal arginine-rich motif of BMV capsid protein to virion stability and RNA packaging. Virology 270:377-385.
    • (2000) Virology , vol.270 , pp. 377-385
    • Choi, Y.G.1    Grantham, G.L.2    Rao, A.L.3
  • 13
    • 54949149143 scopus 로고    scopus 로고
    • Seeking membranes: Positive-strand RNA virus replication complexes
    • Denison, M. R. 2008. Seeking membranes: positive-strand RNA virus replication complexes. PLoS Biol. 6:e270.
    • (2008) PLoS Biol , vol.6
    • Denison, M.R.1
  • 14
    • 77958004276 scopus 로고    scopus 로고
    • Membrane-shaping host reticulon proteins play crucial roles in viral RNA replication compartment formation and function
    • Diaz, A., X. Wang, and P. Ahlquist. 2010. Membrane-shaping host reticulon proteins play crucial roles in viral RNA replication compartment formation and function. Proc. Natl. Acad. Sci. U. S. A. 107:16291-16296.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 16291-16296
    • Diaz, A.1    Wang, X.2    Ahlquist, P.3
  • 15
    • 0024961845 scopus 로고
    • Replication in vivo of mutant brome mosaic virus RNAs defective in aminoacylation
    • Dreher, T. W., A. L. Rao, and T. C. Hall. 1989. Replication in vivo of mutant brome mosaic virus RNAs defective in aminoacylation. J. Mol. Biol. 206:425-438.
    • (1989) J. Mol. Biol. , vol.206 , pp. 425-438
    • Dreher, T.W.1    Rao, A.L.2    Hall, T.C.3
  • 17
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • Gething, M. J. 1999. Role and regulation of the ER chaperone BiP. Semin. Cell Dev. Biol. 10:465-472.
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 465-472
    • Gething, M.J.1
  • 18
    • 50849093407 scopus 로고    scopus 로고
    • fourth ed. Academic Press, San Diego, CA
    • Hull, R. 2002. Plant virology, fourth ed. Academic Press, San Diego, CA.
    • (2002) Plant Virology
    • Hull, R.1
  • 19
    • 0035032324 scopus 로고    scopus 로고
    • Coupling between replication and packaging of flavivirus RNA: Evidence derived from the use of DNA-based full-length cDNA clones of Kunjin virus
    • Khromykh, A. A., A. N. Varnavski, P. L. Sedlak, and E. G. Westaway. 2001. Coupling between replication and packaging of flavivirus RNA: evidence derived from the use of DNA-based full-length cDNA clones of Kunjin virus. J. Virol. 75:4633-4640.
    • (2001) J. Virol. , vol.75 , pp. 4633-4640
    • Khromykh, A.A.1    Varnavski, A.N.2    Sedlak, P.L.3    Westaway, E.G.4
  • 20
    • 0017414378 scopus 로고
    • An ultrastructural study of inclusions and disease development in plant cells infected by cowpea chlorotic mottle virus
    • Kim, K. S. 1977. An ultrastructural study of inclusions and disease development in plant cells infected by cowpea chlorotic mottle virus. J. Gen. Virol. 35:535-543.
    • (1977) J. Gen. Virol. , vol.35 , pp. 535-543
    • Kim, K.S.1
  • 22
    • 77956125392 scopus 로고    scopus 로고
    • Cellular remodeling during plant virus infection
    • Laliberte, J. F., and H. Sanfacon. 2010. Cellular remodeling during plant virus infection. Annu. Rev. Phytopathol. 48:69-91.
    • (2010) Annu. Rev. Phytopathol. , vol.48 , pp. 69-91
    • Laliberte, J.F.1    Sanfacon, H.2
  • 23
    • 0028331985 scopus 로고
    • Characterization of rubella virus replication complexes using antibodies to double-stranded RNA
    • Lee, J. Y., J. A. Marshall, and D. S. Bowden. 1994. Characterization of rubella virus replication complexes using antibodies to double-stranded RNA. Virology 200:307-312.
    • (1994) Virology , vol.200 , pp. 307-312
    • Lee, J.Y.1    Marshall, J.A.2    Bowden, D.S.3
  • 24
    • 33644693303 scopus 로고    scopus 로고
    • The tobacco mosaic virus 126-kilodalton protein, a constituent of the virus replication complex, alone or within the complex aligns with and traffics along microfilaments
    • Liu, J. Z., E. B. Blancaflor, and R. S. Nelson. 2005. The tobacco mosaic virus 126-kilodalton protein, a constituent of the virus replication complex, alone or within the complex aligns with and traffics along microfilaments. Plant Physiol. 138:1853-1865.
    • (2005) Plant Physiol. , vol.138 , pp. 1853-1865
    • Liu, J.Z.1    Blancaflor, E.B.2    Nelson, R.S.3
  • 25
    • 26944495290 scopus 로고    scopus 로고
    • Wrapping things up about virus RNA replication
    • DOI 10.1111/j.1600-0854.2005.00339.x
    • Mackenzie, J. 2005. Wrapping things up about virus RNA replication. Traffic 6:967-977. (Pubitemid 41472456)
    • (2005) Traffic , vol.6 , Issue.11 , pp. 967-977
    • Mackenzie, J.1
  • 26
    • 0025809056 scopus 로고
    • Regulation of (+):(-)-Strand asymmetry in replication of brome mosaic virus RNA
    • Marsh, L. E., C. C. Huntley, G. P. Pogue, J. P. Connell, and T. C. Hall. 1991. Regulation of (+):(-)-strand asymmetry in replication of brome mosaic virus RNA. Virology 182:76-83.
    • (1991) Virology , vol.182 , pp. 76-83
    • Marsh, L.E.1    Huntley, C.C.2    Pogue, G.P.3    Connell, J.P.4    Hall, T.C.5
  • 27
    • 0036776626 scopus 로고    scopus 로고
    • Flock house virus RNA polymerase is a transmembrane protein with amino-terminal sequences sufficient for mitochondrial localization and membrane insertion
    • DOI 10.1128/JVI.76.19.9856-9867.2002
    • Miller, D. J., and P. Ahlquist. 2002. Flock house virus RNA polymerase is a transmembrane protein with amino-terminal sequences sufficient for mitochondrial localization and membrane insertion. J. Virol. 76:9856-9867. (Pubitemid 35006525)
    • (2002) Journal of Virology , vol.76 , Issue.19 , pp. 9856-9867
    • Miller, D.J.1    Ahlquist, P.2
  • 28
    • 0035169546 scopus 로고    scopus 로고
    • Flock house virus rna replicates on outer mitochondrial membranes in Drosophila cells
    • DOI 10.1128/JVI.75.23.11664-11676.2001
    • Miller, D. J., M. D. Schwartz, and P. Ahlquist. 2001. Flock house virus RNA replicates on outer mitochondrial membranes in Drosophila cells. J. Virol. 75:11664-11676. (Pubitemid 33063258)
    • (2001) Journal of Virology , vol.75 , Issue.23 , pp. 11664-11676
    • Miller, D.J.1    Schwartz, M.D.2    Ahlquist, P.3
  • 29
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • Miller, S., and J. Krijnse-Locker. 2008. Modification of intracellular membrane structures for virus replication. Nat. Rev. Microbiol. 6:363-374.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 363-374
    • Miller, S.1    Krijnse-Locker, J.2
  • 30
    • 0242406997 scopus 로고    scopus 로고
    • Brome mosaic virus RNA replication: Revealing the role of the host in RNA virus replication
    • Noueiry, A. O., and P. Ahlquist. 2003. Brome mosaic virus RNA replication: revealing the role of the host in RNA virus replication. Annu. Rev. Phytopathol. 41:77-98.
    • (2003) Annu. Rev. Phytopathol. , vol.41 , pp. 77-98
    • Noueiry, A.O.1    Ahlquist, P.2
  • 31
    • 0032889247 scopus 로고    scopus 로고
    • Functional coupling between replication and packaging of poliovirus replicon RNA
    • Nugent, C. I., K. L. Johnson, P. Sarnow, and K. Kirkegaard. 1999. Functional coupling between replication and packaging of poliovirus replicon RNA. J. Virol. 73:427-435. (Pubitemid 28565387)
    • (1999) Journal of Virology , vol.73 , Issue.1 , pp. 427-435
    • Nugent, C.I.1    Johnson, K.L.2    Sarnow, P.3    Kirkegaard, K.4
  • 32
    • 0014755474 scopus 로고
    • Electron microscopy of Bromegrass mosaic virus in infected leaves
    • Paliwal, Y. C. 1970. Electron microscopy of Bromegrass mosaic virus in infected leaves. J. Ultrastruct. Res. 30:491-502.
    • (1970) J. Ultrastruct. Res. , vol.30 , pp. 491-502
    • Paliwal, Y.C.1
  • 33
    • 0007960967 scopus 로고    scopus 로고
    • Bromoviruses
    • O. C. Maloy and T. D. Murray (ed.), John Wiley & Sons, Mississauga, Ontario, Canada
    • Rao, A. L. 2001. Bromoviruses, p. 155-158. In O. C. Maloy and T. D. Murray (ed.), Encyclopedia of plant pathology. John Wiley & Sons, Mississauga, Ontario, Canada.
    • (2001) Encyclopedia of Plant Pathology , pp. 155-158
    • Rao, A.L.1
  • 34
    • 33748940970 scopus 로고    scopus 로고
    • Genome packaging by spherical plant RNA viruses
    • Rao, A. L. 2006. Genome packaging by spherical plant RNA viruses. Annu. Rev. Phytopathol. 44:61-87.
    • (2006) Annu. Rev. Phytopathol. , vol.44 , pp. 61-87
    • Rao, A.L.1
  • 35
    • 33744726581 scopus 로고    scopus 로고
    • Capsid protein gene and the type of host plant differentially modulate cell-to-cell movement of cowpea chlorotic mottle virus
    • DOI 10.1007/s11262-005-6906-0
    • Rao, A. L., and B. Cooper. 2006. Capsid protein gene and the type of host plant differentially modulate cell-to-cell movement of cowpea chlorotic mottle virus. Virus Genes. 32:219-227. (Pubitemid 43823150)
    • (2006) Virus Genes , vol.32 , Issue.3 , pp. 219-227
    • Rao, A.L.N.1    Cooper, B.2
  • 36
    • 0030589549 scopus 로고    scopus 로고
    • Molecular studies on bromovirus capsid protein. II. Functional analysis of the amino-terminal arginine-rich motif and its role in encapsidation, movement, and pathology
    • Rao, A. L., and G. L. Grantham. 1996. Molecular studies on bromovirus capsid protein. II. Functional analysis of the amino-terminal arginine-rich motif and its role in encapsidation, movement, and pathology. Virology 226:294-305.
    • (1996) Virology , vol.226 , pp. 294-305
    • Rao, A.L.1    Grantham, G.L.2
  • 37
    • 0032708386 scopus 로고    scopus 로고
    • Brome mosaic virus RNA replication proteins 1a and 2a colocalize and 1a independently localizes on the yeast endoplasmic reticulum
    • Restrepo-Hartwig, M., and P. Ahlquist. 1999. Brome mosaic virus RNA replication proteins 1a and 2a colocalize and 1a independently localizes on the yeast endoplasmic reticulum. J. Virol. 73:10303-10309.
    • (1999) J. Virol. , vol.73 , pp. 10303-10309
    • Restrepo-Hartwig, M.1    Ahlquist, P.2
  • 38
    • 0029910198 scopus 로고    scopus 로고
    • Brome mosaic virus helicase- And polymerase-like proteins colocalize on the endoplasmic reticulum at sites of vital RNA synthesis
    • Restrepo-Hartwig, M. A., and P. Ahlquist. 1996. Brome mosaic virus helicase- and polymerase-like proteins colocalize on the endoplasmic reticulum at sites of viral RNA synthesis. J. Virol. 70:8908-8916. (Pubitemid 26378475)
    • (1996) Journal of Virology , vol.70 , Issue.12 , pp. 8908-8916
    • Restrepo-Hartwig, M.A.1    Ahlquist, P.2
  • 39
    • 0030915143 scopus 로고    scopus 로고
    • Formation of plant RNA virus replication complexes on membranes: Role of an endoplasmic reticulum-targeted viral protein
    • Schaad, M. C., P. E. Jensen, and J. C. Carrington. 1997. Formation of plant RNA virus replication complexes on membranes: role of an endoplasmic reticulum-targeted viral protein. EMBO J. 16:4049-4059.
    • (1997) EMBO J. , vol.16 , pp. 4049-4059
    • Schaad, M.C.1    Jensen, P.E.2    Carrington, J.C.3
  • 40
    • 0029794678 scopus 로고    scopus 로고
    • Cellular origin and ultrastructure of membranes induced during poliovirus infection
    • Schlegel, A., T. H. Giddings, Jr., M. S. Ladinsky, and K. Kirkegaard. 1996. Cellular origin and ultrastructure of membranes induced during poliovirus infection. J. Virol. 70:6576-6588. (Pubitemid 26307362)
    • (1996) Journal of Virology , vol.70 , Issue.10 , pp. 6576-6588
    • Schlegel, A.1    Giddings Jr., T.H.2    Ladinsky, M.S.3    Kirkegaard, K.4
  • 42
    • 0036204740 scopus 로고    scopus 로고
    • A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids
    • DOI 10.1016/S1097-2765(02)00474-4
    • Schwartz, M., et al. 2002. A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids. Mol. Cell 9:505-514. (Pubitemid 34273782)
    • (2002) Molecular Cell , vol.9 , Issue.3 , pp. 505-514
    • Schwartz, M.1    Chen, J.2    Janda, M.3    Sullivan, M.4    Den, B.J.5    Ahlquist, P.6
  • 43
    • 3843102498 scopus 로고    scopus 로고
    • Alternate, virus-induced membrane rearrangements support positive-strand RNA virus genome replication
    • Schwartz, M., J. Chen, W. M. Lee, M. Janda, and P. Ahlquist. 2004. Alternate, virus-induced membrane rearrangements support positive-strand RNA virus genome replication. Proc. Natl. Acad. Sci. U. S. A. 101:11263-11268.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11263-11268
    • Schwartz, M.1    Chen, J.2    Lee, W.M.3    Janda, M.4    Ahlquist, P.5
  • 45
    • 0031170901 scopus 로고    scopus 로고
    • The plant ER: A dynamic organelle composed of a large number of discrete functional domains
    • DOI 10.1046/j.1365-313X.1997.11061151.x
    • Staehelin, L. A. 1997. The plant ER: a dynamic organelle composed of a large number of discrete functional domains. Plant J. 11:1151-1165. (Pubitemid 27307234)
    • (1997) Plant Journal , vol.11 , Issue.6 , pp. 1151-1165
    • Staehelin, L.A.1
  • 46
    • 0029048796 scopus 로고
    • Structural variety of arginine-rich RNA-binding peptides
    • Tan, R., and A. D. Frankel. 1995. Structural variety of arginine-rich RNA-binding peptides. Proc. Natl. Acad. Sci. U. S. A. 92:5282-5286.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 5282-5286
    • Tan, R.1    Frankel, A.D.2
  • 47
    • 39749119301 scopus 로고    scopus 로고
    • Visualization of double-stranded RNA in cells supporting hepatitis C virus RNA replication
    • DOI 10.1128/JVI.01565-07
    • Targett-Adams, P., S. Boulant, and J. McLauchlan. 2008. Visualization of double-stranded RNA in cells supporting hepatitis C virus RNA replication. J. Virol. 82:2182-2195. (Pubitemid 351293519)
    • (2008) Journal of Virology , vol.82 , Issue.5 , pp. 2182-2195
    • Targett-Adams, P.1    Boulant, S.2    McLauchlan, J.3
  • 48
    • 18144391518 scopus 로고    scopus 로고
    • Capsid protein synthesis from replicating RNA directs specific packaging of the genome of a multipartite, positive-strand RNA virus
    • DOI 10.1128/JVI.79.10.6239-6248.2005
    • Venter, P. A., N. K. Krishna, and A. Schneemann. 2005. Capsid protein synthesis from replicating RNA directs specific packaging of the genome of a multipartite, positive-strand RNA virus. J. Virol. 79:6239-6248. (Pubitemid 40617228)
    • (2005) Journal of Virology , vol.79 , Issue.10 , pp. 6239-6248
    • Venter, P.A.1    Krishna, N.K.2    Schneemann, A.3
  • 49
    • 63149184752 scopus 로고    scopus 로고
    • Dual roles for an arginine-rich motif in specific genome recognition and localization of viral coat protein to RNA replication sites in flock house virus-infected cells
    • Venter, P. A., D. Marshall, and A. Schneemann. 2009. Dual roles for an arginine-rich motif in specific genome recognition and localization of viral coat protein to RNA replication sites in flock house virus-infected cells. J. Virol. 83:2872-2882.
    • (2009) J. Virol. , vol.83 , pp. 2872-2882
    • Venter, P.A.1    Marshall, D.2    Schneemann, A.3
  • 50
    • 0036776098 scopus 로고    scopus 로고
    • Structural organization of the endoplasmic reticulum
    • Voeltz, G. K., M. M. Rolls, and T. A. Rapoport. 2002. Structural organization of the endoplasmic reticulum. EMBO Rep. 3:944-950.
    • (2002) EMBO Rep. , vol.3 , pp. 944-950
    • Voeltz, G.K.1    Rolls, M.M.2    Rapoport, T.A.3
  • 51
    • 33646453915 scopus 로고    scopus 로고
    • Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses
    • Weber, F., V. Wagner, S. B. Rasmussen, R. Hartmann, and S. R. Paludan. 2006. Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses. J. Virol. 80:5059-5064.
    • (2006) J. Virol. , vol.80 , pp. 5059-5064
    • Weber, F.1    Wagner, V.2    Rasmussen, S.B.3    Hartmann, R.4    Paludan, S.R.5
  • 52
    • 73849139654 scopus 로고    scopus 로고
    • Sequential recruitment of the endoplasmic reticulum and chloroplasts for plant potyvirus replication
    • Wei, T., et al. 2010. Sequential recruitment of the endoplasmic reticulum and chloroplasts for plant potyvirus replication. J. Virol. 84:799-809.
    • (2010) J. Virol. , vol.84 , pp. 799-809
    • Wei, T.1
  • 53
    • 57349162005 scopus 로고    scopus 로고
    • Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI- And COPII-dependent manner
    • Wei, T., and A. Wang. 2008. Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI- and COPII-dependent manner. J. Virol. 82:12252-12264.
    • (2008) J. Virol. , vol.82 , pp. 12252-12264
    • Wei, T.1    Wang, A.2
  • 54
    • 64649097038 scopus 로고    scopus 로고
    • Composition and three-dimensional architecture of the dengue virus replication and assembly sites
    • Welsch, S., et al. 2009. Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell Host Microbe 5:365-375.
    • (2009) Cell Host Microbe , vol.5 , pp. 365-375
    • Welsch, S.1
  • 55
    • 0033602697 scopus 로고    scopus 로고
    • Nascent flavivirus RNA colocalized in situ with double-stranded RNA in stable replication complexes
    • Westaway, E. G., A. A. Khromykh, and J. M. Mackenzie. 1999. Nascent flavivirus RNA colocalized in situ with double-stranded RNA in stable replication complexes. Virology 258:108-117.
    • (1999) Virology , vol.258 , pp. 108-117
    • Westaway, E.G.1    Khromykh, A.A.2    Mackenzie, J.M.3
  • 56
    • 0035875665 scopus 로고    scopus 로고
    • The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum
    • DOI 10.1093/emboj/20.12.3082
    • Yamamoto, K., et al. 2001. The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum. EMBO J. 20:3082-3091. (Pubitemid 32611996)
    • (2001) EMBO Journal , vol.20 , Issue.12 , pp. 3082-3091
    • Yamamoto, K.1    Fujii, R.2    Toyofuku, Y.3    Saito, T.4    Koseki, H.5    Hsu, V.W.6    Aoe, T.7
  • 57
    • 0034715825 scopus 로고    scopus 로고
    • Mechanism of capsid assembly for an icosahedral plant virus
    • Zlotnick, A., R. Aldrich, J. M. Johnson, P. Ceres, and M. J. Young. 2000. Mechanism of capsid assembly for an icosahedral plant virus. Virology 277:450-456.
    • (2000) Virology , vol.277 , pp. 450-456
    • Zlotnick, A.1    Aldrich, R.2    Johnson, J.M.3    Ceres, P.4    Young, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.