메뉴 건너뛰기




Volumn 81, Issue 16, 2007, Pages 8477-8487

Processing of capsid protein by cathepsin L plays a crucial role in replication of Japanese encephalitis virus in neural and macrophage cells

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CAPSID PROTEIN; CATHEPSIN L; COMPLEMENTARY DNA; CYSTEINE PROTEINASE;

EID: 34547745385     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00477-07     Document Type: Article
Times cited : (24)

References (54)
  • 3
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • Barrett, A. J., and H. Kirschke. 1981. Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol. 80:535-661.
    • (1981) Methods Enzymol , vol.80 , pp. 535-661
    • Barrett, A.J.1    Kirschke, H.2
  • 4
    • 0026438869 scopus 로고
    • Nuclear localization of dengue 2 virus core protein detected with monoclonal antibodies
    • Bulich, R., and J. G. Aaskov. 1992. Nuclear localization of dengue 2 virus core protein detected with monoclonal antibodies. J. Gen. Virol. 73:2999-3003.
    • (1992) J. Gen. Virol , vol.73 , pp. 2999-3003
    • Bulich, R.1    Aaskov, J.G.2
  • 5
    • 34547807515 scopus 로고    scopus 로고
    • Burke, D. S., and T. P. Monath. 2001. Flaviviruses, p. 1043-1125. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 4th ed., 1. Lippincott Williams & Wilkins, Philadelphia, PA.
    • Burke, D. S., and T. P. Monath. 2001. Flaviviruses, p. 1043-1125. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 4th ed., vol. 1. Lippincott Williams & Wilkins, Philadelphia, PA.
  • 6
  • 7
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran, K., N. J. Sullivan, U. Felbor, S. P. Whelan, and J. M. Cunningham. 2005. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308:1643-1645.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 8
    • 0034761111 scopus 로고    scopus 로고
    • The heterogeneous nuclear ribonucleoprotein K (hnRNP K) interacts with dengue virus core protein
    • Chang, C. J., H. W. Luh, S. H. Wang, H. J. Lin, S. C. Lee, and S. T. Hu. 2001. The heterogeneous nuclear ribonucleoprotein K (hnRNP K) interacts with dengue virus core protein. DNA Cell Biol. 20:569-577.
    • (2001) DNA Cell Biol , vol.20 , pp. 569-577
    • Chang, C.J.1    Luh, H.W.2    Wang, S.H.3    Lin, H.J.4    Lee, S.C.5    Hu, S.T.6
  • 9
    • 33144458778 scopus 로고    scopus 로고
    • RNA secondary structure in the coding region of dengue virus type 2 directs translation start codon selection and is required for viral replication
    • Clyde, K., and E. Harris. 2006. RNA secondary structure in the coding region of dengue virus type 2 directs translation start codon selection and is required for viral replication. J. Virol. 80:2170-2182.
    • (2006) J. Virol , vol.80 , pp. 2170-2182
    • Clyde, K.1    Harris, E.2
  • 10
    • 0037303672 scopus 로고    scopus 로고
    • Fine mapping of a cis-acting sequence element in yellow fever virus RNA that is required for RNA replication and cyclization
    • Corver, J., E. Lenches, K. Smith, R. A. Robison, T. Sando, E. G. Strauss, and J. H. Strauss. 2003. Fine mapping of a cis-acting sequence element in yellow fever virus RNA that is required for RNA replication and cyclization. J. Virol. 77:2265-2270.
    • (2003) J. Virol , vol.77 , pp. 2265-2270
    • Corver, J.1    Lenches, E.2    Smith, K.3    Robison, R.A.4    Sando, T.5    Strauss, E.G.6    Strauss, J.H.7
  • 11
    • 3142611054 scopus 로고    scopus 로고
    • West nile virus core protein; tetramer structure and ribbon formation
    • Dokland, T., M. Walsh, J. M. Mackenzie, A. A. Khromykh, K. H. Ee, and S. Wang. 2004. West nile virus core protein; tetramer structure and ribbon formation. Structure 12:1157-1163.
    • (2004) Structure , vol.12 , pp. 1157-1163
    • Dokland, T.1    Walsh, M.2    Mackenzie, J.M.3    Khromykh, A.A.4    Ee, K.H.5    Wang, S.6
  • 12
    • 0025787737 scopus 로고
    • Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by cathepsins B, D, and L
    • Dunn, A. D., H. E. Crutchfield, and J. T. Dunn. 1991. Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by cathepsins B, D, and L. J. Biol. Chem. 266:20198-20204.
    • (1991) J. Biol. Chem , vol.266 , pp. 20198-20204
    • Dunn, A.D.1    Crutchfield, H.E.2    Dunn, J.T.3
  • 13
    • 0037025342 scopus 로고    scopus 로고
    • Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells
    • Ebert, D. H., J. Deussing, C. Peters, and T. S. Dermody. 2002. Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells. J. Biol. Chem. 277:24609-24617.
    • (2002) J. Biol. Chem , vol.277 , pp. 24609-24617
    • Ebert, D.H.1    Deussing, J.2    Peters, C.3    Dermody, T.S.4
  • 15
    • 0032472245 scopus 로고    scopus 로고
    • Fu, Y. H., T. Nishinaka, K. Yokoyama, and R. Chiu. 1998. A retinoblastoma susceptibility gene product, RB, targeting protease is regulated through the cell cycle. FEBS Lett. 421:89-93.
    • Fu, Y. H., T. Nishinaka, K. Yokoyama, and R. Chiu. 1998. A retinoblastoma susceptibility gene product, RB, targeting protease is regulated through the cell cycle. FEBS Lett. 421:89-93.
  • 16
    • 1942470581 scopus 로고    scopus 로고
    • A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor
    • Goulet, B., A. Baruch, N. S. Moon, M. Poirier, L. L. Sansregret, A. Erickson, M. Bogyo, and A. Nepveu. 2004. A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Mol. Cell 14:207-219.
    • (2004) Mol. Cell , vol.14 , pp. 207-219
    • Goulet, B.1    Baruch, A.2    Moon, N.S.3    Poirier, M.4    Sansregret, L.L.5    Erickson, A.6    Bogyo, M.7    Nepveu, A.8
  • 17
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., B. Krummel, and R. K. Saiki. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16:7351-7367.
    • (1988) Nucleic Acids Res , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 19
    • 0034984219 scopus 로고    scopus 로고
    • Essential role of cyclization sequences in flavivirus RNA replication
    • Khromykh, A. A., H. Meka, K. J. Guyatt, and E. G. Westaway. 2001. Essential role of cyclization sequences in flavivirus RNA replication. J. Virol. 75:6719-6728.
    • (2001) J. Virol , vol.75 , pp. 6719-6728
    • Khromykh, A.A.1    Meka, H.2    Guyatt, K.J.3    Westaway, E.G.4
  • 20
    • 0029684652 scopus 로고    scopus 로고
    • RNA binding properties of core protein of the flavivirus
    • Khromykh, A. A., and E. G. Westaway. 1996. RNA binding properties of core protein of the flavivirus Kunjin. Arch. Virol. 141:685-699.
    • (1996) Kunjin. Arch. Virol , vol.141 , pp. 685-699
    • Khromykh, A.A.1    Westaway, E.G.2
  • 21
    • 3242656261 scopus 로고    scopus 로고
    • Isolation of capsid protein dimers from the tick-borne encephalitis flavivirus and in vitro assembly of capsid-like particles
    • Kiermayr, S., R. M. Kofler, C. W. Mandl, P. Messner, and F. X. Heinz. 2004. Isolation of capsid protein dimers from the tick-borne encephalitis flavivirus and in vitro assembly of capsid-like particles. J. Virol. 78:8078-8084.
    • (2004) J. Virol , vol.78 , pp. 8078-8084
    • Kiermayr, S.1    Kofler, R.M.2    Mandl, C.W.3    Messner, P.4    Heinz, F.X.5
  • 22
    • 0027352732 scopus 로고
    • Specific tropism of Japanese encephalitis virus for developing neurons in primary rat brain culture
    • Kimura-Kuroda, J., M. Ichikawa, A. Ogata, K. Nagashima, and K. Yasui. 1993. Specific tropism of Japanese encephalitis virus for developing neurons in primary rat brain culture. Arch. Virol. 130:477-484.
    • (1993) Arch. Virol , vol.130 , pp. 477-484
    • Kimura-Kuroda, J.1    Ichikawa, M.2    Ogata, A.3    Nagashima, K.4    Yasui, K.5
  • 23
    • 0036118270 scopus 로고    scopus 로고
    • Capsid protein C of tick-borne encephalitis virus tolerates large internal deletions and is a favorable target for attenuation of virulence
    • Kofler, R. M., F. X. Heinz, and C. W. Mandl. 2002. Capsid protein C of tick-borne encephalitis virus tolerates large internal deletions and is a favorable target for attenuation of virulence. J. Virol. 76:3534-3543.
    • (2002) J. Virol , vol.76 , pp. 3534-3543
    • Kofler, R.M.1    Heinz, F.X.2    Mandl, C.W.3
  • 24
    • 34547803070 scopus 로고    scopus 로고
    • Lindenbach, B. D., and C. M. Rice. 2001. Flaviviridae: the viruses and their replication, p. 991-1041. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.). Fields virology, 4th ed., 1. Lippincott Williams & Wilkins, Philadelphia, PA.
    • Lindenbach, B. D., and C. M. Rice. 2001. Flaviviridae: the viruses and their replication, p. 991-1041. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.). Fields virology, 4th ed., vol. 1. Lippincott Williams & Wilkins, Philadelphia, PA.
  • 25
    • 0141570502 scopus 로고    scopus 로고
    • Functional analysis of mosquito-borne flavivirus conserved sequence elements within 3′ untranslated region of West Nile virus by use of a reporting replicon that differentiates between viral translation and RNA replication
    • Lo, M. K., M. Tilgner, K. A. Bernard, and P. Y. Shi. 2003. Functional analysis of mosquito-borne flavivirus conserved sequence elements within 3′ untranslated region of West Nile virus by use of a reporting replicon that differentiates between viral translation and RNA replication. J. Virol. 77:10004-10014.
    • (2003) J. Virol , vol.77 , pp. 10004-10014
    • Lo, M.K.1    Tilgner, M.2    Bernard, K.A.3    Shi, P.Y.4
  • 26
    • 0345734203 scopus 로고    scopus 로고
    • Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes
    • Lobigs, M., and E. Lee. 2004. Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes. J. Virol. 78: 178-186.
    • (2004) J. Virol , vol.78 , pp. 178-186
    • Lobigs, M.1    Lee, E.2
  • 27
  • 28
    • 0024335590 scopus 로고
    • Detection of dengue 4 virus core protein in the nucleus. II. Antibody against dengue 4 core protein produced by a recombinant baculovirus reacts with the antigen in the nucleus
    • Makino, Y., M. Tadano, T. Anzai, S. P. Ma, S. Yasuda, and T. Fukunaga. 1989. Detection of dengue 4 virus core protein in the nucleus. II. Antibody against dengue 4 core protein produced by a recombinant baculovirus reacts with the antigen in the nucleus. J. Gen. Virol. 70:1417-1425.
    • (1989) J. Gen. Virol , vol.70 , pp. 1417-1425
    • Makino, Y.1    Tadano, M.2    Anzai, T.3    Ma, S.P.4    Yasuda, S.5    Fukunaga, T.6
  • 29
    • 0030838369 scopus 로고    scopus 로고
    • A conserved internal hydrophobic domain mediates the stable membrane integration of the dengue virus capsid protein
    • Markoff, L., B. Falgout, and A. Chang. 1997. A conserved internal hydrophobic domain mediates the stable membrane integration of the dengue virus capsid protein. Virology 233:105-117.
    • (1997) Virology , vol.233 , pp. 105-117
    • Markoff, L.1    Falgout, B.2    Chang, A.3
  • 33
    • 0030990586 scopus 로고    scopus 로고
    • Nishinaka, T., Y. H. Fu, L. I. Chen, K. Yokoyama, and R. Chiu. 1997. A unique cathepsin-like protease isolated from CV-1 cells is involved in rapid degradation of retinoblastoma susceptibility gene product, RB, and transcription factor SP1. Biochim. Biophys. Acta 1351:274-286.
    • Nishinaka, T., Y. H. Fu, L. I. Chen, K. Yokoyama, and R. Chiu. 1997. A unique cathepsin-like protease isolated from CV-1 cells is involved in rapid degradation of retinoblastoma susceptibility gene product, RB, and transcription factor SP1. Biochim. Biophys. Acta 1351:274-286.
  • 34
    • 33749559162 scopus 로고    scopus 로고
    • Jab1 mediates cytoplasmic localization and degradation of West Nile virus capsid protein
    • Oh, W., M. R. Yang, E. W. Lee, K. M. Park, S. Pyo, J. S. Yang, H. W. Lee, and J. Song. 2006. Jab1 mediates cytoplasmic localization and degradation of West Nile virus capsid protein. J. Biol. Chem. 281:30166-30174.
    • (2006) J. Biol. Chem , vol.281 , pp. 30166-30174
    • Oh, W.1    Yang, M.R.2    Lee, E.W.3    Park, K.M.4    Pyo, S.5    Yang, J.S.6    Lee, H.W.7    Song, J.8
  • 35
    • 33746336657 scopus 로고    scopus 로고
    • Hsp70 functions as a negative regulator of West Nile virus capsid protein through direct interaction
    • Oh, W. K., and J. Song. 2006. Hsp70 functions as a negative regulator of West Nile virus capsid protein through direct interaction. Biochem. Biophys. Res. Commun. 347:994-1000.
    • (2006) Biochem. Biophys. Res. Commun , vol.347 , pp. 994-1000
    • Oh, W.K.1    Song, J.2
  • 36
    • 2642539953 scopus 로고    scopus 로고
    • Intramembrane proteolysis and endoplasmic reticulum retention of hepatitis C virus core protein
    • Okamoto, K., K. Moriishi, T. Miyamura, and Y. Matsuura. 2004. Intramembrane proteolysis and endoplasmic reticulum retention of hepatitis C virus core protein. J. Virol. 78:6370-6380.
    • (2004) J. Virol , vol.78 , pp. 6370-6380
    • Okamoto, K.1    Moriishi, K.2    Miyamura, T.3    Matsuura, Y.4
  • 37
    • 0034176273 scopus 로고    scopus 로고
    • Probing the specificity of cysteine proteinases at subsites remote from the active site: Analysis of P4, P3, P2′ and P3′ variations in extended substrates
    • Portaro, F. C., A. B. Santos, M. H. Cezari, M. A. Juliano, L. Juliano, and E. Carmona. 2000. Probing the specificity of cysteine proteinases at subsites remote from the active site: analysis of P4, P3, P2′ and P3′ variations in extended substrates. Biochem. J. 347:123-129.
    • (2000) Biochem. J , vol.347 , pp. 123-129
    • Portaro, F.C.1    Santos, A.B.2    Cezari, M.H.3    Juliano, M.A.4    Juliano, L.5    Carmona, E.6
  • 39
    • 33745158157 scopus 로고
    • A simple method of estimationg fifty per cent endpoints
    • Reed, L. J., and H. Müench. 1938. A simple method of estimationg fifty per cent endpoints. Am. J. Hyg. 27:493.
    • (1938) Am. J. Hyg , vol.27 , pp. 493
    • Reed, L.J.1    Müench, H.2
  • 40
    • 0027433869 scopus 로고
    • The affinity-labelling of cathepsin S with peptidyl diazomethyl ketones. Comparison with the inhibition of cathepsin L and calpain
    • Shaw, E., S. Mohanty, A. Colic, V. Stoka, and V. Turk. 1993. The affinity-labelling of cathepsin S with peptidyl diazomethyl ketones. Comparison with the inhibition of cathepsin L and calpain. FEBS Lett. 334:340-342.
    • (1993) FEBS Lett , vol.334 , pp. 340-342
    • Shaw, E.1    Mohanty, S.2    Colic, A.3    Stoka, V.4    Turk, V.5
  • 43
    • 0031935890 scopus 로고    scopus 로고
    • Signal peptidase cleavage at the flavivirus C-prM junction: Dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM
    • Stocks, C. E., and M. Lobigs. 1998. Signal peptidase cleavage at the flavivirus C-prM junction: dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM. J. Virol. 72:2141-2149.
    • (1998) J. Virol , vol.72 , pp. 2141-2149
    • Stocks, C.E.1    Lobigs, M.2
  • 44
    • 0024318343 scopus 로고
    • Detection of dengue 4 virus core protein in the nucleus. I. A monoclonal antibody to dengue 4 virus reacts with the antigen in the nucleus and cytoplasm
    • Tadano, M., Y. Makino, T. Fukunaga, Y. Okuno, and K. Fukai. 1989. Detection of dengue 4 virus core protein in the nucleus. I. A monoclonal antibody to dengue 4 virus reacts with the antigen in the nucleus and cytoplasm. J. Gen. Virol. 70:1409-1415.
    • (1989) J. Gen. Virol , vol.70 , pp. 1409-1415
    • Tadano, M.1    Makino, Y.2    Fukunaga, T.3    Okuno, Y.4    Fukai, K.5
  • 45
    • 0034724144 scopus 로고    scopus 로고
    • New initiatives for the control of Japanese encephalitis by vaccination: Minutes of a WHO/CVI meeting, Bangkok, Thailand, 13-15 October 1998
    • Tsai, T. F. 2000. New initiatives for the control of Japanese encephalitis by vaccination: minutes of a WHO/CVI meeting, Bangkok, Thailand, 13-15 October 1998. Vaccine 18:1-25.
    • (2000) Vaccine , vol.18 , pp. 1-25
    • Tsai, T.F.1
  • 46
    • 33645046901 scopus 로고    scopus 로고
    • Nucleolar protein b23 interacts with Japanese encephalitis virus core protein and participates in viral replication
    • Tsuda, Y., Y. Mori, T. Abe, T. Yamashita, T. Okamoto, T. Ichimura, K. Moriishi, and Y. Matsuura. 2006. Nucleolar protein b23 interacts with Japanese encephalitis virus core protein and participates in viral replication. Microbiol. Immunol. 50:225-234.
    • (2006) Microbiol. Immunol , vol.50 , pp. 225-234
    • Tsuda, Y.1    Mori, Y.2    Abe, T.3    Yamashita, T.4    Okamoto, T.5    Ichimura, T.6    Moriishi, K.7    Matsuura, Y.8
  • 47
    • 0036932907 scopus 로고    scopus 로고
    • Intracellular localization and determination of a nuclear localization signal of the core protein of dengue virus
    • Wang, S. H., W. J. Syu, K. J. Huang, H. Y. Lei, C. W. Yao, C. C. King, and S. T. Hu. 2002. Intracellular localization and determination of a nuclear localization signal of the core protein of dengue virus. J. Gen. Virol. 83: 3093-3102.
    • (2002) J. Gen. Virol , vol.83 , pp. 3093-3102
    • Wang, S.H.1    Syu, W.J.2    Huang, K.J.3    Lei, H.Y.4    Yao, C.W.5    King, C.C.6    Hu, S.T.7
  • 48
    • 0031582633 scopus 로고    scopus 로고
    • Proteins C and NS4B of the flavivirus Kunjin translocate independently into the nucleus
    • Westaway, E. G., A. A. Khromykh, M. T. Kenney, J. M. Mackenzie, and M. K. Jones. 1997. Proteins C and NS4B of the flavivirus Kunjin translocate independently into the nucleus. Virology 234:31-41.
    • (1997) Virology , vol.234 , pp. 31-41
    • Westaway, E.G.1    Khromykh, A.A.2    Kenney, M.T.3    Mackenzie, J.M.4    Jones, M.K.5
  • 49
    • 0028146784 scopus 로고
    • Processing of the intracellular form of the west Nile virus capsid protein by the viral NS2B-NS3 protease: An in vitro study
    • Yamshchikov, V. F., and R. W. Compans. 1994. Processing of the intracellular form of the west Nile virus capsid protein by the viral NS2B-NS3 protease: an in vitro study. J. Virol. 68:5765-5771.
    • (1994) J. Virol , vol.68 , pp. 5765-5771
    • Yamshchikov, V.F.1    Compans, R.W.2
  • 50
    • 1642344616 scopus 로고    scopus 로고
    • A model to study neurotropism and persistency of Japanese encephalitis virus infection in human neuroblastoma cells and leukocytes
    • Yang, K. D., W. T. Yeh, R. F. Chen, H. L. Chuon, H. P. Tsai, C. W. Yao, and M. F. Shaio. 2004. A model to study neurotropism and persistency of Japanese encephalitis virus infection in human neuroblastoma cells and leukocytes. J. Gen. Virol. 85:635-642.
    • (2004) J. Gen. Virol , vol.85 , pp. 635-642
    • Yang, K.D.1    Yeh, W.T.2    Chen, R.F.3    Chuon, H.L.4    Tsai, H.P.5    Yao, C.W.6    Shaio, M.F.7
  • 52
    • 0035844132 scopus 로고    scopus 로고
    • In vitro RNA synthesis from exogenous dengue viral RNA templates requires long range interactions between 5′- and 3′-terminal regions that influence RNA structure
    • You, S., B. Falgout, L. Markoff, and R. Padmanabhan. 2001. In vitro RNA synthesis from exogenous dengue viral RNA templates requires long range interactions between 5′- and 3′-terminal regions that influence RNA structure. J. Biol. Chem. 276:15581-15591.
    • (2001) J. Biol. Chem , vol.276 , pp. 15581-15591
    • You, S.1    Falgout, B.2    Markoff, L.3    Padmanabhan, R.4
  • 53
    • 0033585015 scopus 로고    scopus 로고
    • A novel in vitro replication system for dengue virus. Initiation of RNA synthesis at the 3′-end of exogenous viral RNA templates requires 5′- and 3′-terminal complementary sequence motifs of the viral RNA
    • You, S., and R. Padmanabhan. 1999. A novel in vitro replication system for dengue virus. Initiation of RNA synthesis at the 3′-end of exogenous viral RNA templates requires 5′- and 3′-terminal complementary sequence motifs of the viral RNA. J. Biol. Chem. 274:33714-33722.
    • (1999) J. Biol. Chem , vol.274 , pp. 33714-33722
    • You, S.1    Padmanabhan, R.2
  • 54
    • 23044470828 scopus 로고    scopus 로고
    • Characterization of the E-138 (Glu/Lys) mutation in Japanese encephalitis virus by using a stable, full-length, infectious cDNA clone
    • Zhao, Z., T. Date, Y. Li, T. Kato, M. Miyamoto, K. Yasui, and T. Wakita. 2005. Characterization of the E-138 (Glu/Lys) mutation in Japanese encephalitis virus by using a stable, full-length, infectious cDNA clone. J. Gen. Virol. 86:2209-2220.
    • (2005) J. Gen. Virol , vol.86 , pp. 2209-2220
    • Zhao, Z.1    Date, T.2    Li, Y.3    Kato, T.4    Miyamoto, M.5    Yasui, K.6    Wakita, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.