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Volumn 79, Issue 24, 2005, Pages 15189-15198

The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ASPARTIC ACID; COUMARIN DERIVATIVE; CYSTEINE; DIUBIQUITIN; HISTIDINE; PAPAIN LIKE PROTEASE; POLYPROTEIN; PROTEINASE; RNA DIRECTED RNA POLYMERASE; UBIQUITIN; UBIQUITIN 7 AMINO 4 METHYLCOUMARIN; UNCLASSIFIED DRUG; VIRUS RNA; ZINC;

EID: 29744455503     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.24.15189-15198.2005     Document Type: Article
Times cited : (457)

References (63)
  • 1
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik, A. Y., and M. Hochstrasser. 2004. Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta 1695:189-207.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 2
    • 2142713046 scopus 로고    scopus 로고
    • Identification of novel inhibitors of the SARS coronavirus main protease 3CLpro
    • Bacha, U., J. Barrila, A. Velazquez-Campoy, S. A. Leavitt, and E. Freire. 2004. Identification of novel inhibitors of the SARS coronavirus main protease 3CLpro. Biochemistry 43:4906-4912.
    • (2004) Biochemistry , vol.43 , pp. 4906-4912
    • Bacha, U.1    Barrila, J.2    Velazquez-Campoy, A.3    Leavitt, S.A.4    Freire, E.5
  • 3
    • 0024405242 scopus 로고
    • Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene a polyprotein
    • Baker, S. C., C. K. Shieh, L. H. Soe, M. F. Chang, D. M. Vannier, and M. M. Lai. 1989. Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein. J. Virol. 63:3693-3699.
    • (1989) J. Virol. , vol.63 , pp. 3693-3699
    • Baker, S.C.1    Shieh, C.K.2    Soe, L.H.3    Chang, M.F.4    Vannier, D.M.5    Lai, M.M.6
  • 4
    • 0027170410 scopus 로고
    • Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus
    • Baker, S. C., K. Yokomori, S. Dong, R. Carlisle, A. E. Gorbalenya, E. V. Koonin, and M. M. Lai, 1993. Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus. J. Virol. 67:6056-6063.
    • (1993) J. Virol. , vol.67 , pp. 6056-6063
    • Baker, S.C.1    Yokomori, K.2    Dong, S.3    Carlisle, R.4    Gorbalenya, A.E.5    Koonin, E.V.6    Lai, M.M.7
  • 5
  • 6
    • 0028923541 scopus 로고
    • Alignment/phylogeny of the papain superfamily of cysteine proteases
    • Berti, P. J., and A. C. Storer. 1995. Alignment/phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 246:273-283.
    • (1995) J. Mol. Biol. , vol.246 , pp. 273-283
    • Berti, P.J.1    Storer, A.C.2
  • 8
    • 0031028291 scopus 로고    scopus 로고
    • Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59
    • Bonilla, P. J., S. A. Hughes, and S. R. Weiss. 1997. Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59. J. Virol. 71:900-909.
    • (1997) J. Virol. , vol.71 , pp. 900-909
    • Bonilla, P.J.1    Hughes, S.A.2    Weiss, S.R.3
  • 10
    • 0032539582 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes
    • Dang, L. C., F. D. Melandri, and R. L. Stein. 1998. Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes. Biochemistry 37:1868-1879.
    • (1998) Biochemistry , vol.37 , pp. 1868-1879
    • Dang, L.C.1    Melandri, F.D.2    Stein, R.L.3
  • 14
    • 0036196634 scopus 로고    scopus 로고
    • RNA replication of mouse hepatitis virus takes place at double-membrane vesicles
    • Gosert, R., A. Kanjanahaluethai, D. Egger, K. Bienz, and S. C. Baker. 2002. RNA replication of mouse hepatitis virus takes place at double-membrane vesicles. J. Virol. 76:3697-3708.
    • (2002) J. Virol. , vol.76 , pp. 3697-3708
    • Gosert, R.1    Kanjanahaluethai, A.2    Egger, D.3    Bienz, K.4    Baker, S.C.5
  • 16
    • 23044490251 scopus 로고    scopus 로고
    • Papain-like protease 2 (PLP2) from severe acute respiratory syndrome coronavirus (SARS-CoV): Expression, purification, characterization, and inhibition
    • Han, Y. S., G. G. Chang, C. G. Juo, H. J. Lee, S. H. Yeh, J. T. Hsu, and X. Chen. 2005. Papain-like protease 2 (PLP2) from severe acute respiratory syndrome coronavirus (SARS-CoV): expression, purification, characterization, and inhibition. Biochemistry 44:10349-10359.
    • (2005) Biochemistry , vol.44 , pp. 10349-10359
    • Han, Y.S.1    Chang, G.G.2    Juo, C.G.3    Lee, H.J.4    Yeh, S.H.5    Hsu, J.T.6    Chen, X.7
  • 17
    • 10044268025 scopus 로고    scopus 로고
    • Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity
    • Harcourt, B. H., D. Jukneliene, A. Kanjanahaluethai, J. Bechill, K. M. Severson, C. M. Smith, P. A. Rota, and S. C. Baker. 2004. Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity. J. Virol. 78:13600-13612.
    • (2004) J. Virol. , vol.78 , pp. 13600-13612
    • Harcourt, B.H.1    Jukneliene, D.2    Kanjanahaluethai, A.3    Bechill, J.4    Severson, K.M.5    Smith, C.M.6    Rota, P.A.7    Baker, S.C.8
  • 18
    • 0031907557 scopus 로고    scopus 로고
    • Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: Identification of a papain-like proteinase and its substrate
    • Herold, J., A. E. Gorbalenya, V. Thiel, B. Schelle, and S. G. Siddell. 1998. Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: identification of a papain-like proteinase and its substrate. J. Virol. 72:910-918.
    • (1998) J. Virol. , vol.72 , pp. 910-918
    • Herold, J.1    Gorbalenya, A.E.2    Thiel, V.3    Schelle, B.4    Siddell, S.G.5
  • 19
    • 0033591345 scopus 로고    scopus 로고
    • A human RNA viral cysteine proteinase that depends upon a unique Zn2+-binding finger connecting the two domains of a papain-like fold
    • Herold, J., S. G. Siddell, and A. E. Gorbalenya. 1999. A human RNA viral cysteine proteinase that depends upon a unique Zn2+-binding finger connecting the two domains of a papain-like fold. J. Biol. Chem. 274:14918-14925.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14918-14925
    • Herold, J.1    Siddell, S.G.2    Gorbalenya, A.E.3
  • 20
    • 0002257116 scopus 로고    scopus 로고
    • Coronaviruses
    • D. M. Knipe, P. M. Howley, D. E. Griffin. R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Holmes, K. V. 2001. Coronaviruses, p. 1187-1203. 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. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology, 4th Ed. , pp. 1187-1203
    • Holmes, K.V.1
  • 21
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu, M., P. Li, M. Li, W. Li, T. Yao, J. W. Wu, W. Gu, R. E. Cohen, and Y. Shi. 2002. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 111:1041-1054.
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 23
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinatine enzyme (human UCH-L3) at 1.8 Å resolution
    • Johnston, S. C., C. N. Larsen, W. J. Cook, K. D. Wilkinson, and C. P. Hill. 1997. Crystal structure of a deubiquitinatine enzyme (human UCH-L3) at 1.8 Å resolution. EMBO J. 16:3787-3796.
    • (1997) EMBO J , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 24
    • 0033565867 scopus 로고    scopus 로고
    • Structural basis for the specificity of ubiquitin C-terminal hydrolases
    • Johnston, S. C., S. M. Riddle, R. E. Cohen, and C. P. Hill. 1999. Structural basis for the specificity of ubiquitin C-terminal hydrolases. EMBO J. 18:3877-3887.
    • (1999) EMBO J , vol.18 , pp. 3877-3887
    • Johnston, S.C.1    Riddle, S.M.2    Cohen, R.E.3    Hill, C.P.4
  • 25
    • 0033882187 scopus 로고    scopus 로고
    • Identification of mouse hepatitis virus papain-like proteinase 2 activity
    • Kanjanahaluethai, A., and S. C. Baker. 2000. Identification of mouse hepatitis virus papain-like proteinase 2 activity. J. Virol. 74:7911-7921.
    • (2000) J. Virol. , vol.74 , pp. 7911-7921
    • Kanjanahaluethai, A.1    Baker, S.C.2
  • 26
    • 0037791748 scopus 로고    scopus 로고
    • Identification of the murine coronavirus MP1 cleavage site recognized by papain-like proteinase 2
    • Kanjanahaluethai, A., Jukneliene, D., and S. C. Baker. 2003. Identification of the murine coronavirus MP1 cleavage site recognized by papain-like proteinase 2. J. Virol. 77:7376-7382.
    • (2003) J. Virol. , vol.77 , pp. 7376-7382
    • Kanjanahaluethai, A.1    Jukneliene, D.2    Baker, S.C.3
  • 27
    • 0028907271 scopus 로고
    • Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor E64d
    • Kim, J. C., R. A. Spence, P. F. Currier, X. Lu, and M. R. Denison. 1995. Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor E64d. Virology 208:1-8.
    • (1995) Virology , vol.208 , pp. 1-8
    • Kim, J.C.1    Spence, R.A.2    Currier, P.F.3    Lu, X.4    Denison, M.R.5
  • 28
    • 2142752480 scopus 로고    scopus 로고
    • Cellular autophagy; surrender, avoidance and subversion by microorganisms
    • Kirkegaard, K., M. P. Taylor, and W. T. Jackson. 2004. Cellular autophagy; surrender, avoidance and subversion by microorganisms. Nat. Rev. Microbiol. 2:301-314.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 301-314
    • Kirkegaard, K.1    Taylor, M.P.2    Jackson, W.T.3
  • 29
    • 0003208239 scopus 로고    scopus 로고
    • Coronaviridae: The viruses and their replication
    • D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Lai, M. M. C., and K. V. Holmes. 2001. Coronaviridae: the viruses and their replication, p. 1163-1185. 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. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology, 4th Ed. , pp. 1163-1185
    • Lai, M.M.C.1    Holmes, K.V.2
  • 30
    • 0030699383 scopus 로고    scopus 로고
    • Specificity of the ubiquitin isopeptidase in the PA700 regulatory complex of 26 S proteasomes
    • Lam, Y. A., G. N. DeMartino, C. M. Pickart, and R. E. Cohen. 1997. Specificity of the ubiquitin isopeptidase in the PA700 regulatory complex of 26 S proteasomes. J. Biol. Chem. 272:28438-28446.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28438-28446
    • Lam, Y.A.1    Demartino, G.N.2    Pickart, C.M.3    Cohen, R.E.4
  • 31
    • 0032502276 scopus 로고    scopus 로고
    • Substrate specificity of deubiquitinating enzymes: Ubiquitin C-terminal hydrolases
    • Larsen, C. N., B. A. Krantz, and K. D. Wilkinson. 1998. Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases. Biochemistry 37:3358-3368.
    • (1998) Biochemistry , vol.37 , pp. 3358-3368
    • Larsen, C.N.1    Krantz, B.A.2    Wilkinson, K.D.3
  • 32
    • 0029999683 scopus 로고    scopus 로고
    • Substrate binding and catalysis by ubiquitin C-terminal hydrolases: Identification of two active site residues
    • Larsen, C. N., J. S. Price, and K. D. Wilkinson. 1996. Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues. Biochemistry 35:6735-6744.
    • (1996) Biochemistry , vol.35 , pp. 6735-6744
    • Larsen, C.N.1    Price, J.S.2    Wilkinson, K.D.3
  • 33
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • Li, M., C. L. Brooks, N. Kon, and W. Gu. 2004. A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol. Cell 13:879-886.
    • (2004) Mol. Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 34
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li, M., D. Chen, A. Shiloh, J. Luo, A. Y. Nikolaev, J. Qin, and W. Gu. 2002. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 416:648-653.
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 35
    • 0033947165 scopus 로고    scopus 로고
    • Identification of a novel cleavage activity of the first papain-like proteinase domain encoded by open reading frame 1a of the coronavirus avian infectious bronchitis virus and characterization of the cleavage products
    • Lim, K. P., L. F. Ng, and D. X. Liu. 2000. Identification of a novel cleavage activity of the first papain-like proteinase domain encoded by open reading frame 1a of the coronavirus avian infectious bronchitis virus and characterization of the cleavage products. J. Virol. 74:1674-1685.
    • (2000) J. Virol. , vol.74 , pp. 1674-1685
    • Lim, K.P.1    Ng, L.F.2    Liu, D.X.3
  • 39
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Ohsumi, Y. 2001. Molecular dissection of autophagy: two ubiquitin-like systems. Nat. Rev. Mol. Cell Biol. 2:211-216.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 40
    • 0033017866 scopus 로고    scopus 로고
    • Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex
    • Pedersen, K. W., Y. van der Meer, N. Roos, and E. J. Snijder. 1999. Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex. J. Virol. 73:2016-2026.
    • (1999) J. Virol. , vol.73 , pp. 2016-2026
    • Pedersen, K.W.1    Van Der Meer, Y.2    Roos, N.3    Snijder, E.J.4
  • 41
    • 10944238037 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome
    • Peiris, J. S., Y. Guan, and K. Y. Yuen. 2004. Severe acute respiratory syndrome. Nat. Med. 10:588-97.
    • (2004) Nat. Med. , vol.10 , pp. 588-597
    • Peiris, J.S.1    Guan, Y.2    Yuen, K.Y.3
  • 43
    • 1642280930 scopus 로고    scopus 로고
    • Coronavirus replication complex formation utilizes components of cellular autophagy
    • Prentice, E., W. G. Jerome, T. Yoshimori, N. Mizushima, and M. R. Denison. 2004. Coronavirus replication complex formation utilizes components of cellular autophagy. J. Biol. Chem. 279:10136-10141.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10136-10141
    • Prentice, E.1    Jerome, W.G.2    Yoshimori, T.3    Mizushima, N.4    Denison, M.R.5
  • 45
    • 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.
    • (1996) J. Virol. , vol.70 , pp. 6576-6588
    • Schlegel, A.1    Giddings Jr., T.H.2    Ladinsky, M.S.3    Kirkegaard, K.4
  • 46
    • 0038434056 scopus 로고    scopus 로고
    • A superfamily of protein tags: Ubiquitin, SUMO and related modifiers
    • Schwartz, D. C., and M. Hochstrasser. 2003. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem. Sci. 28:321-328.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 321-328
    • Schwartz, D.C.1    Hochstrasser, M.2
  • 47
    • 0037961585 scopus 로고    scopus 로고
    • Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS)
    • Seto, W. H., D. Tsang, R. W. Yung, T. Y. Ching, T. K. Ng, M. Ho, L. M. Ho, and J. S. Peiris. 2003. Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS). Lancet 361:1519-1520.
    • (2003) Lancet , vol.361 , pp. 1519-1520
    • Seto, W.H.1    Tsang, D.2    Yung, R.W.3    Ching, T.Y.4    Ng, T.K.5    Ho, M.6    Ho, L.M.7    Peiris, J.S.8
  • 48
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • Shintani, T., and D. J. Klionsky. 2004. Autophagy in health and disease: a double-edged sword. Science 306:990-995.
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 49
    • 13444260839 scopus 로고    scopus 로고
    • Inhibition of beta interferon induction by severe acute respiratory syndrome coronavirus suggests a two-step model for activation of interferon regulatory factor 3
    • Spiegel, M., A. Pichlmair, L. Martinez-Sobrido, J. Cros, A. Garcia-Sastre, O. Haller, and F. Weber. 2005. Inhibition of beta interferon induction by severe acute respiratory syndrome coronavirus suggests a two-step model for activation of interferon regulatory factor 3. J. Virol. 79:2079-2086.
    • (2005) J. Virol. , vol.79 , pp. 2079-2086
    • Spiegel, M.1    Pichlmair, A.2    Martinez-Sobrido, L.3    Cros, J.4    Garcia-Sastre, A.5    Haller, O.6    Weber, F.7
  • 51
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer, A. C., and R. Menard. 1994. Catalytic mechanism in papain family of cysteine peptidases. Methods Enzymol. 244:486-500.
    • (1994) Methods Enzymol , vol.244 , pp. 486-500
    • Storer, A.C.1    Menard, R.2
  • 52
    • 0033798416 scopus 로고    scopus 로고
    • Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: An autophagy-like origin for virus-induced vesicles
    • Suhy, D. A., T. H. Giddings, Jr., and K. Kirkegaard. 2000. Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles. J. Virol. 74:8953-8965.
    • (2000) J. Virol. , vol.74 , pp. 8953-8965
    • Suhy, D.A.1    Giddings Jr., T.H.2    Kirkegaard, K.3
  • 53
    • 15244348284 scopus 로고    scopus 로고
    • Deubiquitination, a new function of the severe acute respiratory syndrome coronavirus papain-like protease?
    • Sulea, T., H. A. Lindner, E. O. Purisima, and R. Menard. 2005. Deubiquitination, a new function of the severe acute respiratory syndrome coronavirus papain-like protease? J. Virol. 79:4550-4551.
    • (2005) J. Virol. , vol.79 , pp. 4550-4551
    • Sulea, T.1    Lindner, H.A.2    Purisima, E.O.3    Menard, R.4
  • 56
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson, K. D. 2000. Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. Semin. Cell Dev. Biol. 11:141-148.
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 61
    • 1942467995 scopus 로고    scopus 로고
    • Evidence of airborne transmission of the severe acute respiratory syndrome virus
    • Yu, I. T., Y. Li, T. W. Wong, W. Tam, A. T. Chan, J. H. Lee, D. Y. Leung, and T. Ho. 2004. Evidence of airborne transmission of the severe acute respiratory syndrome virus. N. Engl. J. Med. 350:1731-1739.
    • (2004) N. Engl. J. Med. , vol.350 , pp. 1731-1739
    • Yu, I.T.1    Li, Y.2    Wong, T.W.3    Tam, W.4    Chan, A.T.5    Lee, J.H.6    Leung, D.Y.7    Ho, T.8
  • 62
    • 0035253852 scopus 로고    scopus 로고
    • Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
    • Yuan, W., and R. M. Krug. 2001. Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. EMBO J. 20:362-371.
    • (2001) EMBO J , vol.20 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2


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