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Volumn 10, Issue 5, 2014, Pages

Structural Basis for the Ubiquitin-Linkage Specificity and deISGylating Activity of SARS-CoV Papain-Like Protease

Author keywords

[No Author keywords available]

Indexed keywords

3C-LIKE PROTEASE, SARS CORONAVIRUS; CYSTEINE PROTEINASE; CYTOKINE; ISG15 PROTEIN, HUMAN; UBIQUITIN; VIRUS PROTEIN;

EID: 84901670584     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004113     Document Type: Article
Times cited : (169)

References (66)
  • 1
    • 84655176306 scopus 로고    scopus 로고
    • The role of ubiquitylation in immune defence and pathogen evasion
    • Jiang X, Chen ZJ, (2011) The role of ubiquitylation in immune defence and pathogen evasion. Nature reviewsImmunology 12: 35-48.
    • (2011) Nature ReviewsImmunology , vol.12 , pp. 35-48
    • Jiang, X.1    Chen, Z.J.2
  • 4
    • 62549155321 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation
    • Rahighi S, Ikeda F, Kawasaki M, Akutsu M, Suzuki N, et al. (2009) Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation. Cell 136: 1098-1109.
    • (2009) Cell , vol.136 , pp. 1098-1109
    • Rahighi, S.1    Ikeda, F.2    Kawasaki, M.3    Akutsu, M.4    Suzuki, N.5
  • 5
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • Welchman RL, Gordon C, Mayer RJ, (2005) Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat Rev Mol Cell Biol 6: 599-609.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 6
    • 0023160888 scopus 로고
    • Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin
    • Haas AL, Ahrens P, Bright PM, Ankel H, (1987) Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin. J Biol Chem 262: 11315-11323.
    • (1987) J Biol Chem , vol.262 , pp. 11315-11323
    • Haas, A.L.1    Ahrens, P.2    Bright, P.M.3    Ankel, H.4
  • 7
    • 84861783400 scopus 로고    scopus 로고
    • Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions
    • Husnjak K, Dikic I, (2012) Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions. Annu Rev Biochem 81: 291-322.
    • (2012) Annu Rev Biochem , vol.81 , pp. 291-322
    • Husnjak, K.1    Dikic, I.2
  • 8
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbe S, (2009) Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 10: 550-563.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 9
    • 77950873763 scopus 로고    scopus 로고
    • Species specificity of the NS1 protein of influenza B virus: NS1 binds only human and non-human primate ubiquitin-like ISG15 proteins
    • Sridharan H, Zhao C, Krug RM, (2010) Species specificity of the NS1 protein of influenza B virus: NS1 binds only human and non-human primate ubiquitin-like ISG15 proteins. J Biol Chem 285: 7852-7856.
    • (2010) J Biol Chem , vol.285 , pp. 7852-7856
    • Sridharan, H.1    Zhao, C.2    Krug, R.M.3
  • 11
    • 23744434659 scopus 로고    scopus 로고
    • A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae
    • Kattenhorn LM, Korbel GA, Kessler BM, Spooner E, Ploegh HL, (2005) A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae. Mol Cell 19: 547-557.
    • (2005) Mol Cell , vol.19 , pp. 547-557
    • Kattenhorn, L.M.1    Korbel, G.A.2    Kessler, B.M.3    Spooner, E.4    Ploegh, H.L.5
  • 12
    • 29744463885 scopus 로고    scopus 로고
    • A deubiquitinating activity is conserved in the large tegument protein of the herpesviridae
    • Schlieker C, Korbel GA, Kattenhorn LM, Ploegh HL, (2005) A deubiquitinating activity is conserved in the large tegument protein of the herpesviridae. J Virol 79: 15582-15585.
    • (2005) J Virol , vol.79 , pp. 15582-15585
    • Schlieker, C.1    Korbel, G.A.2    Kattenhorn, L.M.3    Ploegh, H.L.4
  • 13
    • 77649338569 scopus 로고    scopus 로고
    • A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses
    • Lilley CE, Chaurushiya MS, Boutell C, Landry S, Suh J, et al. A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses. Embo J 29: 943-955.
    • Embo J , vol.29 , pp. 943-955
    • Lilley, C.E.1    Chaurushiya, M.S.2    Boutell, C.3    Landry, S.4    Suh, J.5
  • 14
    • 79953314427 scopus 로고    scopus 로고
    • Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21
    • Ye Y, Akutsu M, Reyes-Turcu F, Enchev RI, Wilkinson KD, et al. (2011) Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21. EMBO reports 12: 350-357.
    • (2011) EMBO Reports , vol.12 , pp. 350-357
    • Ye, Y.1    Akutsu, M.2    Reyes-Turcu, F.3    Enchev, R.I.4    Wilkinson, K.D.5
  • 18
    • 67349158649 scopus 로고    scopus 로고
    • Coronaviruses post-SARS: update on replication and pathogenesis
    • Perlman S, Netland J, (2009) Coronaviruses post-SARS: update on replication and pathogenesis. Nature reviewsMicrobiology 7: 439-450.
    • (2009) Nature ReviewsMicrobiology , vol.7 , pp. 439-450
    • Perlman, S.1    Netland, J.2
  • 19
    • 0042377358 scopus 로고    scopus 로고
    • Mechanisms and enzymes involved in SARS coronavirus genome expression
    • Thiel V, Ivanov KA, Putics A, Hertzig T, Schelle B, et al. (2003) Mechanisms and enzymes involved in SARS coronavirus genome expression. J Gen Virol 84: 2305-2315.
    • (2003) J Gen Virol , vol.84 , pp. 2305-2315
    • Thiel, V.1    Ivanov, K.A.2    Putics, A.3    Hertzig, T.4    Schelle, B.5
  • 20
    • 10044268025 scopus 로고    scopus 로고
    • Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity
    • Harcourt BH, Jukneliene D, Kanjanahaluethai A, Bechill J, Severson KM, et al. (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
  • 21
    • 33645822092 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme
    • Ratia K, Saikatendu KS, Santarsiero BD, Barretto N, Baker SC, et al. (2006) Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme. Proc Natl Acad Sci U S A 103: 5717-5722.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 5717-5722
    • Ratia, K.1    Saikatendu, K.S.2    Santarsiero, B.D.3    Barretto, N.4    Baker, S.C.5
  • 22
    • 15244348284 scopus 로고    scopus 로고
    • Deubiquitination, a new function of the severe acute respiratory syndrome coronavirus papain-like protease?
    • Sulea T, Lindner HA, Purisima EO, Menard R, (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
  • 23
    • 29744463886 scopus 로고    scopus 로고
    • The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme
    • Lindner HA, Fotouhi-Ardakani N, Lytvyn V, Lachance P, Sulea T, et al. (2005) The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme. J Virol 79: 15199-15208.
    • (2005) J Virol , vol.79 , pp. 15199-15208
    • Lindner, H.A.1    Fotouhi-Ardakani, N.2    Lytvyn, V.3    Lachance, P.4    Sulea, T.5
  • 24
    • 34548651826 scopus 로고    scopus 로고
    • Selectivity in ISG15 and ubiquitin recognition by the SARS coronavirus papain-like protease
    • Lindner HA, Lytvyn V, Qi H, Lachance P, Ziomek E, et al. (2007) Selectivity in ISG15 and ubiquitin recognition by the SARS coronavirus papain-like protease. Arch Biochem Biophys 466: 8-14.
    • (2007) Arch Biochem Biophys , vol.466 , pp. 8-14
    • Lindner, H.A.1    Lytvyn, V.2    Qi, H.3    Lachance, P.4    Ziomek, E.5
  • 25
    • 29744455503 scopus 로고    scopus 로고
    • The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity
    • Barretto N, Jukneliene D, Ratia K, Chen Z, Mesecar AD, et al. (2005) The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity. J Virol 79: 15189-15198.
    • (2005) J Virol , vol.79 , pp. 15189-15198
    • Barretto, N.1    Jukneliene, D.2    Ratia, K.3    Chen, Z.4    Mesecar, A.D.5
  • 26
    • 36148979683 scopus 로고    scopus 로고
    • Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus
    • Devaraj SG, Wang N, Chen Z, Chen Z, Tseng M, et al. (2007) Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus. J Biol Chem 282: 32208-32221.
    • (2007) J Biol Chem , vol.282 , pp. 32208-32221
    • Devaraj, S.G.1    Wang, N.2    Chen, Z.3    Chen, Z.4    Tseng, M.5
  • 27
    • 67449088510 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling
    • Frieman M, Ratia K, Johnston RE, Mesecar AD, Baric RS, (2009) Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling. J Virol 83: 6689-6705.
    • (2009) J Virol , vol.83 , pp. 6689-6705
    • Frieman, M.1    Ratia, K.2    Johnston, R.E.3    Mesecar, A.D.4    Baric, R.S.5
  • 28
    • 77950806384 scopus 로고    scopus 로고
    • Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases
    • Clementz MA, Chen Z, Banach BS, Wang Y, Sun L, et al. Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases. J Virol 84: 4619-4629.
    • J Virol , vol.84 , pp. 4619-4629
    • Clementz, M.A.1    Chen, Z.2    Banach, B.S.3    Wang, Y.4    Sun, L.5
  • 29
    • 28544435897 scopus 로고    scopus 로고
    • Immunity by ubiquitylation: a reversible process of modification
    • Liu YC, Penninger J, Karin M, (2005) Immunity by ubiquitylation: a reversible process of modification. Nat Rev Immunol 5: 941-952.
    • (2005) Nat Rev Immunol , vol.5 , pp. 941-952
    • Liu, Y.C.1    Penninger, J.2    Karin, M.3
  • 30
    • 0029794580 scopus 로고    scopus 로고
    • Kinetic studies on the inhibition of isopeptidase T by ubiquitin aldehyde
    • Melandri F, Grenier L, Plamondon L, Huskey WP, Stein RL, (1996) Kinetic studies on the inhibition of isopeptidase T by ubiquitin aldehyde. Biochemistry 35: 12893-12900.
    • (1996) Biochemistry , vol.35 , pp. 12893-12900
    • Melandri, F.1    Grenier, L.2    Plamondon, L.3    Huskey, W.P.4    Stein, R.L.5
  • 31
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu M, Li P, Li M, Li W, Yao T, et al. (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
  • 32
    • 33746827805 scopus 로고    scopus 로고
    • Structural basis of ubiquitin recognition by the deubiquitinating protease USP2
    • Renatus M, Parrado SG, D'Arcy A, Eidhoff U, Gerhartz B, et al. (2006) Structural basis of ubiquitin recognition by the deubiquitinating protease USP2. Structure 14: 1293-1302.
    • (2006) Structure , vol.14 , pp. 1293-1302
    • Renatus, M.1    Parrado, S.G.2    D'Arcy, A.3    Eidhoff, U.4    Gerhartz, B.5
  • 34
    • 0028316184 scopus 로고
    • Structure of tetraubiquitin shows how multiubiquitin chains can be formed
    • Cook WJ, Jeffrey LC, Kasperek E, Pickart CM, (1994) Structure of tetraubiquitin shows how multiubiquitin chains can be formed. J Mol Biol 236: 601-609.
    • (1994) J Mol Biol , vol.236 , pp. 601-609
    • Cook, W.J.1    Jeffrey, L.C.2    Kasperek, E.3    Pickart, C.M.4
  • 35
    • 33847056330 scopus 로고    scopus 로고
    • Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH
    • Eddins MJ, Varadan R, Fushman D, Pickart CM, Wolberger C, (2007) Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH. J Mol Biol 367: 204-211.
    • (2007) J Mol Biol , vol.367 , pp. 204-211
    • Eddins, M.J.1    Varadan, R.2    Fushman, D.3    Pickart, C.M.4    Wolberger, C.5
  • 36
    • 70149104456 scopus 로고    scopus 로고
    • The structure and conformation of Lys63-linked tetraubiquitin
    • Datta AB, Hura GL, Wolberger C, (2009) The structure and conformation of Lys63-linked tetraubiquitin. J Mol Biol 392: 1117-1124.
    • (2009) J Mol Biol , vol.392 , pp. 1117-1124
    • Datta, A.B.1    Hura, G.L.2    Wolberger, C.3
  • 37
    • 67349231313 scopus 로고    scopus 로고
    • Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains
    • Komander D, Reyes-Turcu F, Licchesi JD, Odenwaelder P, Wilkinson KD, et al. (2009) Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains. EMBO Rep 10: 466-473.
    • (2009) EMBO Rep , vol.10 , pp. 466-473
    • Komander, D.1    Reyes-Turcu, F.2    Licchesi, J.D.3    Odenwaelder, P.4    Wilkinson, K.D.5
  • 38
    • 22844450969 scopus 로고    scopus 로고
    • Crystal structure of the interferon-induced ubiquitin-like protein ISG15
    • Narasimhan J, Wang M, Fu Z, Klein JM, Haas AL, et al. (2005) Crystal structure of the interferon-induced ubiquitin-like protein ISG15. J Biol Chem 280: 27356-27365.
    • (2005) J Biol Chem , vol.280 , pp. 27356-27365
    • Narasimhan, J.1    Wang, M.2    Fu, Z.3    Klein, J.M.4    Haas, A.L.5
  • 39
    • 84871031152 scopus 로고    scopus 로고
    • Ubiquitin chain conformation regulates recognition and activity of interacting proteins
    • Ye Y, Blaser G, Horrocks MH, Ruedas-Rama MJ, Ibrahim S, et al. (2012) Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Nature 492: 266-270.
    • (2012) Nature , vol.492 , pp. 266-270
    • Ye, Y.1    Blaser, G.2    Horrocks, M.H.3    Ruedas-Rama, M.J.4    Ibrahim, S.5
  • 41
    • 77950806384 scopus 로고    scopus 로고
    • Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases
    • Clementz MA, Chen Z, Banach BS, Wang Y, Sun L, et al. (2010) Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases. Journal of virology 84: 4619-4629.
    • (2010) Journal of Virology , vol.84 , pp. 4619-4629
    • Clementz, M.A.1    Chen, Z.2    Banach, B.S.3    Wang, Y.4    Sun, L.5
  • 42
    • 0030026562 scopus 로고    scopus 로고
    • Both amino- and carboxyl-terminal sequences within I kappa B alpha regulate its inducible degradation
    • Sun S, Elwood J, Greene WC, (1996) Both amino- and carboxyl-terminal sequences within I kappa B alpha regulate its inducible degradation. Molecular and cellular biology 16: 1058-1065.
    • (1996) Molecular and Cellular Biology , vol.16 , pp. 1058-1065
    • Sun, S.1    Elwood, J.2    Greene, W.C.3
  • 43
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
    • Borodovsky A, Kessler BM, Casagrande R, Overkleeft HS, Wilkinson KD, et al. (2001) A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. Embo J 20: 5187-5196.
    • (2001) Embo J , vol.20 , pp. 5187-5196
    • Borodovsky, A.1    Kessler, B.M.2    Casagrande, R.3    Overkleeft, H.S.4    Wilkinson, K.D.5
  • 44
    • 27744516748 scopus 로고    scopus 로고
    • Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14
    • Hu M, Li P, Song L, Jeffrey PD, Chenova TA, et al. (2005) Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. Embo J 24: 3747-3756.
    • (2005) Embo J , vol.24 , pp. 3747-3756
    • Hu, M.1    Li, P.2    Song, L.3    Jeffrey, P.D.4    Chenova, T.A.5
  • 45
    • 39549106692 scopus 로고    scopus 로고
    • The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module
    • Komander D, Lord CJ, Scheel H, Swift S, Hofmann K, et al. (2008) The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module. Mol Cell 29: 451-464.
    • (2008) Mol Cell , vol.29 , pp. 451-464
    • Komander, D.1    Lord, C.J.2    Scheel, H.3    Swift, S.4    Hofmann, K.5
  • 46
    • 52149103164 scopus 로고    scopus 로고
    • Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains
    • Sato Y, Yoshikawa A, Yamagata A, Mimura H, Yamashita M, et al. (2008) Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains. Nature 455: 358-362.
    • (2008) Nature , vol.455 , pp. 358-362
    • Sato, Y.1    Yoshikawa, A.2    Yamagata, A.3    Mimura, H.4    Yamashita, M.5
  • 47
    • 0032539582 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes
    • Dang LC, Melandri FD, Stein RL, (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
  • 48
    • 33846021632 scopus 로고    scopus 로고
    • Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)
    • Avvakumov GV, Walker JR, Xue S, Finerty PJ Jr, Mackenzie F, et al. (2006) Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J Biol Chem 281: 38061-38070.
    • (2006) J Biol Chem , vol.281 , pp. 38061-38070
    • Avvakumov, G.V.1    Walker, J.R.2    Xue, S.3    Finerty Jr., P.J.4    Mackenzie, F.5
  • 49
    • 84875540102 scopus 로고    scopus 로고
    • Diversity of ubiquitin and ISG15 specificity among nairoviruses' viral ovarian tumor domain proteases
    • Capodagli GC, Deaton MK, Baker EA, Lumpkin RJ, Pegan SD, (2013) Diversity of ubiquitin and ISG15 specificity among nairoviruses' viral ovarian tumor domain proteases. Journal of virology 87: 3815-3827.
    • (2013) Journal of Virology , vol.87 , pp. 3815-3827
    • Capodagli, G.C.1    Deaton, M.K.2    Baker, E.A.3    Lumpkin, R.J.4    Pegan, S.D.5
  • 50
    • 79952613536 scopus 로고    scopus 로고
    • Structural analysis of a viral ovarian tumor domain protease from the Crimean-Congo hemorrhagic fever virus in complex with covalently bonded ubiquitin
    • Capodagli GC, McKercher MA, Baker EA, Masters EM, Brunzelle JS, et al. (2011) Structural analysis of a viral ovarian tumor domain protease from the Crimean-Congo hemorrhagic fever virus in complex with covalently bonded ubiquitin. Journal of virology 85: 3621-3630.
    • (2011) Journal of Virology , vol.85 , pp. 3621-3630
    • Capodagli, G.C.1    McKercher, M.A.2    Baker, E.A.3    Masters, E.M.4    Brunzelle, J.S.5
  • 51
    • 77953114765 scopus 로고    scopus 로고
    • The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15
    • Durfee LA, Lyon N, Seo K, Huibregtse JM, (2010) The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15. Mol Cell 38: 722-732.
    • (2010) Mol Cell , vol.38 , pp. 722-732
    • Durfee, L.A.1    Lyon, N.2    Seo, K.3    Huibregtse, J.M.4
  • 52
    • 36749007273 scopus 로고    scopus 로고
    • Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses
    • Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, et al. (2007) Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe 2: 404-416.
    • (2007) Cell Host Microbe , vol.2 , pp. 404-416
    • Frias-Staheli, N.1    Giannakopoulos, N.V.2    Kikkert, M.3    Taylor, S.L.4    Bridgen, A.5
  • 53
    • 77951991690 scopus 로고    scopus 로고
    • Positive regulation of interferon regulatory factor 3 activation by Herc5 via ISG15 modification
    • Shi HX, Yang K, Liu X, Liu XY, Wei B, et al. (2010) Positive regulation of interferon regulatory factor 3 activation by Herc5 via ISG15 modification. Mol Cell Biol 30: 2424-2436.
    • (2010) Mol Cell Biol , vol.30 , pp. 2424-2436
    • Shi, H.X.1    Yang, K.2    Liu, X.3    Liu, X.Y.4    Wei, B.5
  • 54
    • 84858725584 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by deubiquitinases
    • Harhaj EW, Dixit VM, (2012) Regulation of NF-kappaB by deubiquitinases. Immunol Rev 246: 107-124.
    • (2012) Immunol Rev , vol.246 , pp. 107-124
    • Harhaj, E.W.1    Dixit, V.M.2
  • 55
    • 46249124976 scopus 로고    scopus 로고
    • Deubiquitylation and regulation of the immune response
    • Sun SC, (2008) Deubiquitylation and regulation of the immune response. Nat Rev Immunol 8: 501-511.
    • (2008) Nat Rev Immunol , vol.8 , pp. 501-511
    • Sun, S.C.1
  • 56
    • 36448943427 scopus 로고    scopus 로고
    • DUBA: a deubiquitinase that regulates type I interferon production
    • Kayagaki N, Phung Q, Chan S, Chaudhari R, Quan C, et al. (2007) DUBA: a deubiquitinase that regulates type I interferon production. Science 318: 1628-1632.
    • (2007) Science , vol.318 , pp. 1628-1632
    • Kayagaki, N.1    Phung, Q.2    Chan, S.3    Chaudhari, R.4    Quan, C.5
  • 57
    • 33947606938 scopus 로고    scopus 로고
    • CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha
    • Schweitzer K, Bozko PM, Dubiel W, Naumann M, (2007) CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha. Embo J 26: 1532-1541.
    • (2007) Embo J , vol.26 , pp. 1532-1541
    • Schweitzer, K.1    Bozko, P.M.2    Dubiel, W.3    Naumann, M.4
  • 59
    • 81255200507 scopus 로고    scopus 로고
    • A double-inactivated severe acute respiratory syndrome coronavirus vaccine provides incomplete protection in mice and induces increased eosinophilic proinflammatory pulmonary response upon challenge
    • Bolles M, Deming D, Long K, Agnihothram S, Whitmore A, et al. (2011) A double-inactivated severe acute respiratory syndrome coronavirus vaccine provides incomplete protection in mice and induces increased eosinophilic proinflammatory pulmonary response upon challenge. Journal of virology 85: 12201-12215.
    • (2011) Journal of Virology , vol.85 , pp. 12201-12215
    • Bolles, M.1    Deming, D.2    Long, K.3    Agnihothram, S.4    Whitmore, A.5
  • 60
    • 84873085753 scopus 로고    scopus 로고
    • A Strategy for Modulation of Enzymes in the Ubiquitin System
    • Ernst A, Avvakumov G, Tong J, Fan Y, Zhao Y, et al. (2013) A Strategy for Modulation of Enzymes in the Ubiquitin System. Science 339 (6119) (): 590-5.
    • (2013) Science , vol.339 , Issue.6119 , pp. 590-595
    • Ernst, A.1    Avvakumov, G.2    Tong, J.3    Fan, Y.4    Zhao, Y.5
  • 61
    • 28844440079 scopus 로고    scopus 로고
    • Derivitization of the C-terminus of ubiquitin and ubiquitin-like proteins using intein chemistry: methods and uses
    • Wilkinson KD, Gan-Erdene T, Kolli N, (2005) Derivitization of the C-terminus of ubiquitin and ubiquitin-like proteins using intein chemistry: methods and uses. Methods Enzymol 399: 37-51.
    • (2005) Methods Enzymol , vol.399 , pp. 37-51
    • Wilkinson, K.D.1    Gan-Erdene, T.2    Kolli, N.3
  • 62
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW, (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41: 207-234.
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.