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Volumn 24, Issue 4, 2009, Pages 227-242

The long road to understanding the baculovirus P10 protein

Author keywords

Baculovirus; Fibrous body fibrillar structure; Microtubule; P10; Polyhedral occlusion body

Indexed keywords

POLYHEDRIN; PROTEIN P10; VIRUS PROTEIN;

EID: 68349144386     PISSN: 16740769     EISSN: 1995820X     Source Type: Journal    
DOI: 10.1007/s12250-009-3045-0     Document Type: Article
Times cited : (6)

References (66)
  • 1
    • 0020429554 scopus 로고
    • Molecular cloning of DNA complementary to mRNA of the baculovirus Autographa californica nuclear polyhedrosis virus: Location and gene products of RNA transcripts found late in infection
    • Adang M J, Miller L K. 1982. Molecular cloning of DNA complementary to mRNA of the baculovirus Autographa californica nuclear polyhedrosis virus: Location and gene products of RNA transcripts found late in infection. J Virol, 44(3): 782-793.
    • (1982) J Virol , vol.44 , Issue.3 , pp. 782-793
    • Adang, M.J.1    Miller, L.K.2
  • 2
    • 0029998883 scopus 로고    scopus 로고
    • Identification and characterization of a filament-associated protein encoded by Amsacta moorei entomopoxvirus
    • Alaoui-Ismaili M H, Richardson C D. 1996. Identification and characterization of a filament-associated protein encoded by Amsacta moorei entomopoxvirus. J Virol, 70(5): 2697-2705.
    • (1996) J Virol , vol.70 , Issue.5 , pp. 2697-2705
    • Alaoui-Ismaili, M.H.1    Richardson, C.D.2
  • 3
    • 0031935588 scopus 로고    scopus 로고
    • Insect virus proteins (FALPE and p10) self-associate to form filaments in infected cells
    • Alaoui-Ismaili M H, Richardson C D. 1998. Insect virus proteins (FALPE and p10) self-associate to form filaments in infected cells. J Virol, 72(3): 2213-2223.
    • (1998) J Virol , vol.72 , Issue.3 , pp. 2213-2223
    • Alaoui-Ismaili, M.H.1    Richardson, C.D.2
  • 4
    • 0016442221 scopus 로고
    • Protein migration into nuclei. I. Frog oocyte nuclei in vivo accumulate microinjected histones, allow entry to small proteins, and exclude large proteins
    • Bonner W M. 1975. Protein migration into nuclei. I. Frog oocyte nuclei in vivo accumulate microinjected histones, allow entry to small proteins, and exclude large proteins. J Cell Biol, 64(2): 421-430.
    • (1975) J Cell Biol , vol.64 , Issue.2 , pp. 421-430
    • Bonner, W.M.1
  • 5
    • 0029957901 scopus 로고    scopus 로고
    • Heptad breaks in alpha-helical coiled coils: Stutters and stammers
    • Brown J H, Cohen C, Parry D A. 1996. Heptad breaks in alpha-helical coiled coils: Stutters and stammers. Proteins, 26(2): 134-145.
    • (1996) Proteins , vol.26 , Issue.2 , pp. 134-145
    • Brown, J.H.1    Cohen, C.2    Parry, D.A.3
  • 6
    • 38649130497 scopus 로고    scopus 로고
    • The baculovirus P10 protein of Autographa californica nucleopolyhedrovirus forms two distinct cytoskeletal-like structures and associates with polyhedral occlusion bodies during infection
    • Carpentier D C, Griffiths C M, King L A. 2008. The baculovirus P10 protein of Autographa californica nucleopolyhedrovirus forms two distinct cytoskeletal-like structures and associates with polyhedral occlusion bodies during infection. Virology, 371(2): 278-291.
    • (2008) Virology , vol.371 , Issue.2 , pp. 278-291
    • Carpentier, D.C.1    Griffiths, C.M.2    King, L.A.3
  • 7
    • 0027412448 scopus 로고
    • Competition between baculovirus polyhedrin and p10 gene expression during infection of insect cells
    • Chaabihi H, Ogliastro M H, Martin M, et al. 1993. Competition between baculovirus polyhedrin and p10 gene expression during infection of insect cells. J Virol, 67(5): 2664-2671.
    • (1993) J Virol , vol.67 , Issue.5 , pp. 2664-2671
    • Chaabihi, H.1    Ogliastro, M.H.2    Martin, M.3
  • 8
    • 0033619917 scopus 로고    scopus 로고
    • Proline affects oligomerization of a coiled coil by inducing a kink in a long helix
    • Chang D K, Cheng S F, Trivedi V D, et al. 1999. Proline affects oligomerization of a coiled coil by inducing a kink in a long helix. J Struct Biol, 128(3): 270-279.
    • (1999) J Struct Biol , vol.128 , Issue.3 , pp. 270-279
    • Chang, D.K.1    Cheng, S.F.2    Trivedi, V.D.3
  • 9
    • 0026663076 scopus 로고
    • Phosphorylated baculovirus p10 is a heat-stable microtubuleassociated protein associated with process formation in Sf9 cells
    • Cheley S, Kosik K S, Paskevich P, et al. 1992. Phosphorylated baculovirus p10 is a heat-stable microtubuleassociated protein associated with process formation in Sf9 cells. J Cell Sci, 102(Pt 4): 739-752.
    • (1992) J Cell Sci , vol.102 , Issue.PART 4 , pp. 739-752
    • Cheley, S.1    Kosik, K.S.2    Paskevich, P.3
  • 10
    • 0019872825 scopus 로고
    • Helix to helix packing in proteins
    • Chothia C, Levitt M, Richardson D. 1981. Helix to helix packing in proteins. J Mol Biol, 145(1): 215-250.
    • (1981) J Mol Biol , vol.145 , Issue.1 , pp. 215-250
    • Chothia, C.1    Levitt, M.2    Richardson, D.3
  • 11
    • 0018898562 scopus 로고
    • Studies on the morphogenesis of polyhedral inclusion bodies of a baculovirus autographa californica NPV
    • Chung K L, Brown M, Faulkner P. 1980. Studies on the morphogenesis of polyhedral inclusion bodies of a baculovirus autographa californica NPV. J Gen Virol, 46: 335-347.
    • (1980) J Gen Virol , vol.46 , pp. 335-347
    • Chung, K.L.1    Brown, M.2    Faulkner, P.3
  • 12
    • 0028293441 scopus 로고
    • Alpha-helical coiled coils: More facts and better predictions
    • Cohen C, Parry D A. 1994. Alpha-helical coiled coils: More facts and better predictions. Science, 263(5146): 488-489.
    • (1994) Science , vol.263 , Issue.5146 , pp. 488-489
    • Cohen, C.1    Parry, D.A.2
  • 13
    • 0001105482 scopus 로고
    • Is alpha-keratin a coiled coil?
    • Crick F H C. 1952. Is alpha-keratin a coiled coil? Nature, 170(4334): 882-883.
    • (1952) Nature , vol.170 , Issue.4334 , pp. 882-883
    • Crick, F.H.C.1
  • 14
    • 0000920828 scopus 로고
    • The packing of alpha-helices: Simple coiled-coils
    • Crick F H C. 1953. The packing of alpha-helices: Simple coiled-coils. Acta Crystallogr, 6: 689-697.
    • (1953) Acta Crystallogr , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 15
    • 0039695872 scopus 로고
    • Localisation cytologique de la proteine non structurale p10 du baculovirus de la polyedrose nucleaire do Lepidoptere Galleria mellonella
    • Croizier G, Gonnet P, Devauchelle G. 1987. Localisation cytologique de la proteine non structurale p10 du baculovirus de la polyedrose nucleaire do Lepidoptere Galleria mellonella. L CR Acad Sci Paris, 305: 677-681.
    • (1987) L CR Acad Sci Paris , vol.305 , pp. 677-681
    • Croizier, G.1    Gonnet, P.2    Devauchelle, G.3
  • 16
    • 0003237132 scopus 로고
    • Baculoviridae: Subgroup B: Comparative aspects of granulosis viruses
    • In: (Kurstak E, ed.), New York: Marcel Dekker
    • Crook N. 1991. Baculoviridae: Subgroup B: Comparative aspects of granulosis viruses. In: Viruses of Invertebrates (Kurstak E, ed.), New York: Marcel Dekker. p73-110.
    • (1991) Viruses of Invertebrates , pp. 73-110
    • Crook, N.1
  • 17
    • 34547667210 scopus 로고    scopus 로고
    • The heptad repeats region is essential for AcMNPV P10 filament formation and not the proline-rich or the C-terminus basic regions
    • Dong C, Deng F, Li D, et al. 2007. The heptad repeats region is essential for AcMNPV P10 filament formation and not the proline-rich or the C-terminus basic regions. Virology, 365(2): 390-397
    • (2007) Virology , vol.365 , Issue.2 , pp. 390-397
    • Dong, C.1    Deng, F.2    Li, D.3
  • 18
    • 20644466221 scopus 로고    scopus 로고
    • Identification of functional domains required for HearNPV P10 filament formation
    • Dong C, Li D, Long G, et al. 2005. Identification of functional domains required for HearNPV P10 filament formation. Virology, 338(1): 112-120.
    • (2005) Virology , vol.338 , Issue.1 , pp. 112-120
    • Dong, C.1    Li, D.2    Long, G.3
  • 19
    • 4143058720 scopus 로고    scopus 로고
    • Predicting specificity in bZIP coiled-coil protein interactions
    • Fong J H, Keating A E, Singh M. 2004. Predicting specificity in bZIP coiled-coil protein interactions. Genome Biol, 5(2): R11.
    • (2004) Genome Biol , vol.5 , Issue.2
    • Fong, J.H.1    Keating, A.E.2    Singh, M.3
  • 20
    • 0034974426 scopus 로고    scopus 로고
    • Persistence and Distribution of Wild-Type and Recombinant Nucleopolyhedroviruses in Soil
    • Fuxa J R, Matter M M, Abdel-Rahman A, et al. 2001. Persistence and Distribution of Wild-Type and Recombinant Nucleopolyhedroviruses in Soil. Microb Ecol, 41(3): 222-231.
    • (2001) Microb Ecol , vol.41 , Issue.3 , pp. 222-231
    • Fuxa, J.R.1    Matter, M.M.2    Abdel-Rahman, A.3
  • 21
    • 0035140975 scopus 로고    scopus 로고
    • Going new places using an old MAP: Tau, microtubules and human neurodegenerative disease
    • Garcia M L, Cleveland D W. 2001. Going new places using an old MAP: Tau, microtubules and human neurodegenerative disease. Curr Opin Cell Biol, 13(1): 41-48.
    • (2001) Curr Opin Cell Biol , vol.13 , Issue.1 , pp. 41-48
    • Garcia, M.L.1    Cleveland, D.W.2
  • 22
    • 0034753803 scopus 로고    scopus 로고
    • A novel, specific interaction involving the Csk SH3 domain and its natural ligand
    • Ghose R, Shekhtman A, Goger M J, et al. 2001. A novel, specific interaction involving the Csk SH3 domain and its natural ligand. Nat Struct Biol, 8(11): 998-1004.
    • (2001) Nat Struct Biol , vol.8 , Issue.11 , pp. 998-1004
    • Ghose, R.1    Shekhtman, A.2    Goger, M.J.3
  • 23
    • 38649099698 scopus 로고    scopus 로고
    • The p26 gene of the Autographa californica nucleopolyhedrovirus: Timing of transcription, and cellular localization and dimerization of product
    • Feb
    • Goenka S, Weaver R F. The p26 gene of the Autographa californica nucleopolyhedrovirus: Timing of transcription, and cellular localization and dimerization of product. Virus Res. 2008 Feb;131(2): 136-44.
    • (2008) Virus Res , vol.131 , Issue.2 , pp. 136-144
    • Goenka, S.1    Weaver, R.F.2
  • 24
    • 33747788700 scopus 로고    scopus 로고
    • Comparative analysis of coiled-coil prediction methods
    • Gruber M, Soding J, Lupas A N. 2006. Comparative analysis of coiled-coil prediction methods. J Struct Biol, 155(2): 140-145.
    • (2006) J Struct Biol , vol.155 , Issue.2 , pp. 140-145
    • Gruber, M.1    Soding, J.2    Lupas, A.N.3
  • 25
    • 1842457815 scopus 로고    scopus 로고
    • Ancient coevolution of baculoviruses and their insect hosts
    • Herniou E A, Olszewski J A, O'Reilly D R, et al. 2004. Ancient coevolution of baculoviruses and their insect hosts. J Virol, 78(7): 3244-3251.
    • (2004) J Virol , vol.78 , Issue.7 , pp. 3244-3251
    • Herniou, E.A.1    Olszewski, J.A.2    O'Reilly, D.R.3
  • 26
    • 0017890069 scopus 로고
    • Electron microscope observations of the membrane surrounding polyhedral inclusion bodies of insects
    • Hess R T, Falcon L A. 1978. Electron microscope observations of the membrane surrounding polyhedral inclusion bodies of insects. Arch Virol, 56(1-2): 169-176.
    • (1978) Arch Virol , vol.56 , Issue.1-2 , pp. 169-176
    • Hess, R.T.1    Falcon, L.A.2
  • 27
    • 0035185978 scopus 로고    scopus 로고
    • Cell motility: Proline-rich proteins promote protrusions
    • Holt M R, Koffer A. 2001. Cell motility: Proline-rich proteins promote protrusions. Trends Cell Biol, 11(1): 38-46.
    • (2001) Trends Cell Biol , vol.11 , Issue.1 , pp. 38-46
    • Holt, M.R.1    Koffer, A.2
  • 28
    • 0026356042 scopus 로고
    • Requirements for nuclear localization and supramolecular assembly of a baculovirus polyhedrin protein
    • Jarvis D L, Bohlmeyer D A, Jr. Garcia A. 1991. Requirements for nuclear localization and supramolecular assembly of a baculovirus polyhedrin protein. Virology, 185(2): 795-810.
    • (1991) Virology , vol.185 , Issue.2 , pp. 795-810
    • Jarvis, D.L.1    Bohlmeyer Jr., D.A.2    Garcia, A.3
  • 29
    • 32844463672 scopus 로고    scopus 로고
    • Molecular identification and phylogenetic analysis of baculoviruses from Lepidoptera
    • Jehle J A, Lange M, Wang H, et al. 2006. Molecular identification and phylogenetic analysis of baculoviruses from Lepidoptera. Virology, 346(1): 180-193.
    • (2006) Virology , vol.346 , Issue.1 , pp. 180-193
    • Jehle, J.A.1    Lange, M.2    Wang, H.3
  • 30
    • 0032712646 scopus 로고    scopus 로고
    • Functional analysis of microtubule-binding domain of bovine MAP4
    • Katsuki M, Tokuraku K, Murofushi H, et al. 1999. Functional analysis of microtubule-binding domain of bovine MAP4. Cell Struct Funct, 24(5): 337-344.
    • (1999) Cell Struct Funct , vol.24 , Issue.5 , pp. 337-344
    • Katsuki, M.1    Tokuraku, K.2    Murofushi, H.3
  • 31
    • 33947520367 scopus 로고    scopus 로고
    • Ever-expanding network of dynamininteracting proteins
    • Kim Y, Chang S. 2006. Ever-expanding network of dynamininteracting proteins. Mol Neurobiol, 34(2): 129-136.
    • (2006) Mol Neurobiol , vol.34 , Issue.2 , pp. 129-136
    • Kim, Y.1    Chang, S.2
  • 32
    • 0016872066 scopus 로고
    • Replication of nuclear polyhedrosis virus in a continuous cell culture of Spodoptera frugiperda: Microscopy study of the sequence of events of the virus infection
    • Knudson D L, Harrap K A. 1975. Replication of nuclear polyhedrosis virus in a continuous cell culture of Spodoptera frugiperda: Microscopy study of the sequence of events of the virus infection. J Virol, 17(1): 254-268.
    • (1975) J Virol , vol.17 , Issue.1 , pp. 254-268
    • Knudson, D.L.1    Harrap, K.A.2
  • 33
    • 0021682191 scopus 로고
    • Nucleotide sequence of the p10 polypeptide gene of Autographa californica nuclear polyhedrosis virus
    • Kuzio J, Rohel D Z, Curry C J, et al. 1984. Nucleotide sequence of the p10 polypeptide gene of Autographa californica nuclear polyhedrosis virus. Virology, 139: 414-418.
    • (1984) Virology , vol.139 , pp. 414-418
    • Kuzio, J.1    Rohel, D.Z.2    Curry, C.J.3
  • 34
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of tau protein from mouse brain
    • Lee G, Cowan N, Kirschner M. 1988. The primary structure and heterogeneity of tau protein from mouse brain. Science, 239(4837): 285-288.
    • (1988) Science , vol.239 , Issue.4837 , pp. 285-288
    • Lee, G.1    Cowan, N.2    Kirschner, M.3
  • 35
    • 0029789893 scopus 로고    scopus 로고
    • A common pathway for p10 and calyx proteins in progressive stages of polyhedron envelope assembly in AcMNPV-infected Spodoptera frugiperda larvae
    • Lee S Y, Poloumienko A, Belfry S, et al. 1996. A common pathway for p10 and calyx proteins in progressive stages of polyhedron envelope assembly in AcMNPV-infected Spodoptera frugiperda larvae. Arch Virol, 141(7): 1247-1258.
    • (1996) Arch Virol , vol.141 , Issue.7 , pp. 1247-1258
    • Lee, S.Y.1    Poloumienko, A.2    Belfry, S.3
  • 36
    • 0024268202 scopus 로고
    • Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein
    • Lewis S A, Wang D H, Cowan N J. 1988. Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein. Science, 242(4880): 936-939.
    • (1988) Science , vol.242 , Issue.4880 , pp. 936-939
    • Lewis, S.A.1    Wang, D.H.2    Cowan, N.J.3
  • 37
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains: Structural basis and implications for cellular signal transduction
    • Li S S. 2005. Specificity and versatility of SH3 and other proline-recognition domains: Structural basis and implications for cellular signal transduction. Biochem J, 390(Pt 3): 641-653.
    • (2005) Biochem J , vol.390 , Issue.PART 3 , pp. 641-653
    • Li, S.S.1
  • 38
    • 0029029529 scopus 로고
    • Properties of a baculovirus mutant defective in the protein phosphatase gene
    • Li Y, Miller L K. 1995. Properties of a baculovirus mutant defective in the protein phosphatase gene. J Virol, 69(7): 4533-4537.
    • (1995) J Virol , vol.69 , Issue.7 , pp. 4533-4537
    • Li, Y.1    Miller, L.K.2
  • 39
    • 17444424974 scopus 로고    scopus 로고
    • The structure of alphahelical coiled coils
    • Lupas A N, Gruber M. 2005. The structure of alphahelical coiled coils. Adv Protein Chem, 70: 37-78.
    • (2005) Adv Protein Chem , vol.70 , pp. 37-78
    • Lupas, A.N.1    Gruber, M.2
  • 40
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, Van Dyke M, Stock J. 1991. Predicting coiled coils from protein sequences. Science, 252(5010): 1162-1164.
    • (1991) Science , vol.252 , Issue.5010 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 41
    • 0016316088 scopus 로고
    • Morphogenesis of nuclear polyhedrosis virus under conditions of prolonged passage in vitro
    • MacKinnon E A, Henderson J F, Stoltz D B, et al. 1974. Morphogenesis of nuclear polyhedrosis virus under conditions of prolonged passage in vitro. J Ultrastruct Res, 49(3): 419-435.
    • (1974) J Ultrastruct Res , vol.49 , Issue.3 , pp. 419-435
    • MacKinnon, E.A.1    Henderson, J.F.2    Stoltz, D.B.3
  • 42
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio F, Pinna L A. 2003. One-thousand-and-one substrates of protein kinase CK2? Faseb J, 17(3): 349-368.
    • (2003) Faseb J , vol.17 , Issue.3 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 43
    • 0026325311 scopus 로고
    • Interaction of microtubule-associated proteins with microtubules: Yeast lysyl-and valyl-tRNA synthetases and tau 218-235 synthetic peptide as model systems
    • Melki R, Kerjan P, Waller J P, et al. 1991. Interaction of microtubule-associated proteins with microtubules: Yeast lysyl-and valyl-tRNA synthetases and tau 218-235 synthetic peptide as model systems. Biochemistry, 30(49): 11536-11545.
    • (1991) Biochemistry , vol.30 , Issue.49 , pp. 11536-11545
    • Melki, R.1    Kerjan, P.2    Waller, J.P.3
  • 44
    • 0026000615 scopus 로고
    • A strongly basic protein of the MAP2 family copolymerizes with tubulin and induces polymerization
    • Nguyen M, Fasold H. 1991. A strongly basic protein of the MAP2 family copolymerizes with tubulin and induces polymerization. J Protein Chem, 10(5): 511-516.
    • (1991) J Protein Chem , vol.10 , Issue.5 , pp. 511-516
    • Nguyen, M.1    Fasold, H.2
  • 45
    • 0036444017 scopus 로고    scopus 로고
    • Generalized Crick equations for modeling noncanonical coiled coils
    • Offer G, Hicks M R, Woolfson D N. 2002. Generalized Crick equations for modeling noncanonical coiled coils. J Struct Biol, 137(1-2): 41-53.
    • (2002) J Struct Biol , vol.137 , Issue.1-2 , pp. 41-53
    • Offer, G.1    Hicks, M.R.2    Woolfson, D.N.3
  • 46
    • 0347416790 scopus 로고    scopus 로고
    • Formation of P10 tubular structures during AcMNPV infection depends on the integrity of host-cell microtubules
    • Patmanidi A L, Possee R D, King L A. 2003. Formation of P10 tubular structures during AcMNPV infection depends on the integrity of host-cell microtubules. Virology, 317(2): 308-320.
    • (2003) Virology , vol.317 , Issue.2 , pp. 308-320
    • Patmanidi, A.L.1    Possee, R.D.2    King, L.A.3
  • 47
    • 0030913980 scopus 로고    scopus 로고
    • The 'jaws' model of tau-microtubule interaction examined in CHO cells
    • Preuss U, Biernat J, Mandelkow E M, et al. 1997. The 'jaws' model of tau-microtubule interaction examined in CHO cells. J Cell Sci, 110(Pt 6): 789-800.
    • (1997) J Cell Sci , vol.110 , Issue.PART 6 , pp. 789-800
    • Preuss, U.1    Biernat, J.2    Mandelkow, E.M.3
  • 48
    • 0023407319 scopus 로고
    • Characterization of baculovirus p10 synthesis using monoclonal antibodies
    • Quant-Russell R L, Pearson M N, Rohrmann G F, et al. 1987. Characterization of baculovirus p10 synthesis using monoclonal antibodies. Virology, 160(1): 9-19.
    • (1987) Virology , vol.160 , Issue.1 , pp. 9-19
    • Quant-Russell, R.L.1    Pearson, M.N.2    Rohrmann, G.F.3
  • 49
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S, Wells R, Rechsteiner M. 1986. Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis. Science, 234(4774): 364-368.
    • (1986) Science , vol.234 , Issue.4774 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 50
    • 0020660956 scopus 로고
    • Characterization of two abundant mRNAs of Autographa californica nuclear polyhedrosis virus present late in infection
    • Rohel D Z, Cochran M A, Faulkner P. 1983. Characterization of two abundant mRNAs of Autographa californica nuclear polyhedrosis virus present late in infection. Virology, 124(2): 357-365.
    • (1983) Virology , vol.124 , Issue.2 , pp. 357-365
    • Rohel, D.Z.1    Cochran, M.A.2    Faulkner, P.3
  • 51
    • 0021263451 scopus 로고
    • Time Course Analysis and Mapping of Autographa californica Nuclear Polyhedrosis Virus Transcripts
    • Rohel D Z, Faulkner P. 1984. Time Course Analysis and Mapping of Autographa californica Nuclear Polyhedrosis Virus Transcripts. J Virol, 50(3): 739-747.
    • (1984) J Virol , vol.50 , Issue.3 , pp. 739-747
    • Rohel, D.Z.1    Faulkner, P.2
  • 52
    • 0020532148 scopus 로고
    • Molecular Engineering of the Autographa californica Nuclear Polyhedrosis Virus Genome: Deletion Mutations Within the Polyhedrin Gene
    • Smith G E, Fraser M J, Summers M D. 1983. Molecular Engineering of the Autographa californica Nuclear Polyhedrosis Virus Genome: Deletion Mutations Within the Polyhedrin Gene. J Virol, 46(2):584-593.
    • (1983) J Virol , vol.46 , Issue.2 , pp. 584-593
    • Smith, G.E.1    Fraser, M.J.2    Summers, M.D.3
  • 53
    • 0031603694 scopus 로고    scopus 로고
    • Mapping the specificity of SH3 domains with phage-displayed randompeptide libraries
    • Sparks A B, Rider J E, Kay B K. 1998. Mapping the specificity of SH3 domains with phage-displayed randompeptide libraries. Methods Mol Biol, 84: 87-103.
    • (1998) Methods Mol Biol , vol.84 , pp. 87-103
    • Sparks, A.B.1    Rider, J.E.2    Kay, B.K.3
  • 54
    • 0014577540 scopus 로고
    • Ultrastructural studies on inclusion formation and virus occlusion in nuclear polyhedrosis and granulosis virus-infected cells of Trichoplusia ni (Hubner)
    • Summers M D, Arnott H J. 1969. Ultrastructural studies on inclusion formation and virus occlusion in nuclear polyhedrosis and granulosis virus-infected cells of Trichoplusia ni (Hubner). J Ultrastruct Res, 28(5): 462-480.
    • (1969) J Ultrastruct Res , vol.28 , Issue.5 , pp. 462-480
    • Summers, M.D.1    Arnott, H.J.2
  • 55
    • 0000791282 scopus 로고
    • Immunogold detection of polyhedrin, p10 and virion antigens in Autographa californica nuclear polyhedrosis virus-infected Spodoptera frugiperda cells
    • Van der Wilk F, Van Lent J W M, Vlak J M. 1987. Immunogold detection of polyhedrin, p10 and virion antigens in Autographa californica nuclear polyhedrosis virus-infected Spodoptera frugiperda cells. J Gen Virol, 68: 2615-2623.
    • (1987) J Gen Virol , vol.68 , pp. 2615-2623
    • Van der Wilk, F.1    Van Lent, J.W.M.2    Vlak, J.M.3
  • 56
    • 0027410097 scopus 로고
    • Functional domains of the p10 protein of Autographa californica nuclear polyhedrosis virus
    • Van Oers M M, Flipsen J T, Reusken C B, et al. 1993. Functional domains of the p10 protein of Autographa californica nuclear polyhedrosis virus. J Gen Virol, 74(Pt 4): 563-574.
    • (1993) J Gen Virol , vol.74 , Issue.PART 4 , pp. 563-574
    • Van Oers, M.M.1    Flipsen, J.T.2    Reusken, C.B.3
  • 57
    • 0028211960 scopus 로고
    • Specificity of baculovirus p10 functions
    • Van Oers M M, Flipsen J T, Reusken CB, et al. 1994. Specificity of baculovirus p10 functions. Virology, 200(2): 513-23.
    • (1994) Virology , vol.200 , Issue.2 , pp. 513-523
    • Van Oers, M.M.1    Flipsen, J.T.2    Reusken, C.B.3
  • 58
    • 0031182592 scopus 로고    scopus 로고
    • The baculovirus 10-kDa protein
    • Van Oers M M, Vlak J M. 1997. The baculovirus 10-kDa protein. J Invertebr Pathol, 70(1): 1-17.
    • (1997) J Invertebr Pathol , vol.70 , Issue.1 , pp. 1-17
    • Van Oers, M.M.1    Vlak, J.M.2
  • 59
    • 0023986560 scopus 로고
    • Functional studies on the p10 gene of Autographa californica nuclear polyhedrosis virus using a recombinant expressing a p10-beta-galactosidase fusion gene
    • Vlak J M, Klinkenberg F A, Zaal K J, et al. 1988. Functional studies on the p10 gene of Autographa californica nuclear polyhedrosis virus using a recombinant expressing a p10-beta-galactosidase fusion gene. J Gen Virol, 69(Pt 4): 765-776.
    • (1988) J Gen Virol , vol.69 , Issue.PART 4 , pp. 765-776
    • Vlak, J.M.1    Klinkenberg, F.A.2    Zaal, K.J.3
  • 60
    • 0019802383 scopus 로고
    • Hybridization Selection and In Vitro Translation of Autographa californica Nuclear Polyhedrosis Virus mRNA
    • Vlak J M, Smith G E, Summers M D. 1981. Hybridization Selection and In Vitro Translation of Autographa californica Nuclear Polyhedrosis Virus mRNA. J Virol, 40(3): 762-771.
    • (1981) J Virol , vol.40 , Issue.3 , pp. 762-771
    • Vlak, J.M.1    Smith, G.E.2    Summers, M.D.3
  • 61
    • 0025272020 scopus 로고
    • Autographa californica M nuclear polyhedrosis virus: Microtubules and replication
    • Volkman L E, Zaal K J. 1990. Autographa californica M nuclear polyhedrosis virus: Microtubules and replication. Virology, 175(1): 292-302.
    • (1990) Virology , vol.175 , Issue.1 , pp. 292-302
    • Volkman, L.E.1    Zaal, K.J.2
  • 62
    • 0035100279 scopus 로고    scopus 로고
    • Open-and-shut cases in coiled-coil assembly: Alpha-sheets and alpha-cylinders
    • Walshaw J, Woolfson D N. 2001. Open-and-shut cases in coiled-coil assembly: Alpha-sheets and alpha-cylinders. Protein Sci, 10(3): 668-673.
    • (2001) Protein Sci , vol.10 , Issue.3 , pp. 668-673
    • Walshaw, J.1    Woolfson, D.N.2
  • 63
    • 0024490166 scopus 로고
    • A cytopathological investigation of Autographa californica nuclear polyhedrosis virus p10 gene function using insertion/deletion mutants
    • Williams G V, Rohel D Z, Kuzio J, et al. 1989. A cytopathological investigation of Autographa californica nuclear polyhedrosis virus p10 gene function using insertion/deletion mutants. J Gen Virol, 70(Pt 1): 187-202.
    • (1989) J Gen Virol , vol.70 , Issue.PART 1 , pp. 187-202
    • Williams, G.V.1    Rohel, D.Z.2    Kuzio, J.3
  • 64
    • 0029559066 scopus 로고
    • Characterization of the baculovirus Choristoneura fumiferana multicapsid nuclear polyhedrosis virus p10 gene indicates that the polypeptide contains a coiled-coil domain
    • Wilson J A, Hill J E, Kuzio J, et al. 1995. Characterization of the baculovirus Choristoneura fumiferana multicapsid nuclear polyhedrosis virus p10 gene indicates that the polypeptide contains a coiled-coil domain. J Gen Virol, 76(Pt 12): 2923-2932.
    • (1995) J Gen Virol , vol.76 , Issue.PART 12 , pp. 2923-2932
    • Wilson, J.A.1    Hill, J.E.2    Kuzio, J.3
  • 65
    • 0027665269 scopus 로고
    • Phylogenetic interrelationships among baculoviruses: Evolutionary rates and host associations
    • Zanotto P M, Kessing B D, Maruniak J E. 1993. Phylogenetic interrelationships among baculoviruses: Evolutionary rates and host associations. J Invertebr Pathol, 62(2): 147-164.
    • (1993) J Invertebr Pathol , vol.62 , Issue.2 , pp. 147-164
    • Zanotto, P.M.1    Kessing, B.D.2    Maruniak, J.E.3
  • 66
    • 0035451226 scopus 로고    scopus 로고
    • A conserved helix-unfolding motif in the naturally unfolded proteins
    • Zetina C R. 2001. A conserved helix-unfolding motif in the naturally unfolded proteins. Proteins, 44(4): 479-483.
    • (2001) Proteins , vol.44 , Issue.4 , pp. 479-483
    • Zetina, C.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.