메뉴 건너뛰기
Journal of Virology
Volumn 90, Issue 6, 2016, Pages 3229-3242
Involvement of the N-terminal deubiquitinating protease domain of human cytomegalovirus UL48 tegument protein in autoubiquitination, virion stability, and virus entry
Author keywords

[No Author keywords available]
Indexed keywords

PROTEINASE; DEUBIQUITINASE; MUTANT PROTEIN; UL48 PROTEIN, HUMAN CYTOMEGALOVIRUS; VIRAL PROTEIN;
EID: 84961173162     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02766-15     Document Type: Article
Times cited : (24)
References (50)
  • 1
    • 84965169693 scopus 로고    scopus 로고
    • Cytomegaloviruses
    • Knipe DM, Howley PM, Cohen JI, Griffin DE, Lamb RA, Martin MA, Racaniello VR, Roizman B (ed), Lippincott Williams & Wilkins, Philadelphia, PA, 6th ed
    • Mocarski ES, Shenk T, Griffiths PD, Pass RF. 2013. Cytomegaloviruses, p 1960-2014. In Knipe DM, Howley PM, Cohen JI, Griffin DE, Lamb RA, Martin MA, Racaniello VR, Roizman B (ed), Fields virology, 6th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2013) Fields virology , pp. 1960-2014
    • Mocarski, E.S.1    Shenk, T.2    Griffiths, P.D.3    Pass, R.F.4
  • 2
    • 43949104594 scopus 로고    scopus 로고
    • Structure and formation of the cytomegalovirus virion
    • Gibson W. 2008. Structure and formation of the cytomegalovirus virion. Curr Top Microbiol Immunol 325:187-204.
    • (2008) Curr Top Microbiol Immunol , vol.325 , pp. 187-204
    • Gibson, W.1
  • 3
    • 44949216259 scopus 로고    scopus 로고
    • Functions of human cytomegalovirus tegument proteins prior to immediate early gene expression
    • Kalejta RF. 2008. Functions of human cytomegalovirus tegument proteins prior to immediate early gene expression. Curr Top Microbiol Immunol 325:101-115.
    • (2008) Curr Top Microbiol Immunol , vol.325 , pp. 101-115
    • Kalejta, R.F.1
  • 4
    • 44949213015 scopus 로고    scopus 로고
    • Tegument proteins of human cytomegalovirus
    • Kalejta RF. 2008. Tegument proteins of human cytomegalovirus. Microbiol Mol Biol Rev 72:249-265. http://dx.doi.org/10.1128/MMBR.00040-07.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 249-265
    • Kalejta, R.F.1
  • 5
    • 84864293794 scopus 로고    scopus 로고
    • Viral and host control of cytomegalovirus maturation
    • Tandon R, Mocarski ES. 2012. Viral and host control of cytomegalovirus maturation. Trends Microbiol 20:392-401. http://dx.doi.org/10.1016/j.tim.2012.04.008.
    • (2012) Trends Microbiol , vol.20 , pp. 392-401
    • Tandon, R.1    Mocarski, E.S.2
  • 7
    • 79955648479 scopus 로고    scopus 로고
    • Biochemical and structural characterization of the capsid-bound tegument proteins of human cytomegalovirus
    • Yu X, Shah S, Lee M, Dai W, Lo P, Britt W, Zhu H, Liu F, Zhou ZH. 2011. Biochemical and structural characterization of the capsid-bound tegument proteins of human cytomegalovirus. J Struct Biol 174:451-460. http://dx.doi.org/10.1016/j.jsb.2011.03.006.
    • (2011) J Struct Biol , vol.174 , pp. 451-460
    • Yu, X.1    Shah, S.2    Lee, M.3    Dai, W.4    Lo, P.5    Britt, W.6    Zhu, H.7    Liu, F.8    Zhou, Z.H.9
  • 9
    • 0142091343 scopus 로고    scopus 로고
    • Functional map of human cytomegalovirus AD169 defined by global mutational analysis
    • Yu D, Silva MC, Shenk T. 2003. Functional map of human cytomegalovirus AD169 defined by global mutational analysis. Proc Natl Acad Sci U S A 100: 12396-12401. http://dx.doi.org/10.1073/pnas.1635160100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 12396-12401
    • Yu, D.1    Silva, M.C.2    Shenk, T.3
  • 10
    • 33744917811 scopus 로고    scopus 로고
    • High-molecular-weight protein (pUL48) of human cytomegalovirus is a competent deubiquitinating protease: mutant viruses altered in its activesite cysteine or histidine are viable
    • Wang J, Loveland AN, Kattenhorn LM, Ploegh HL, Gibson W. 2006. High-molecular-weight protein (pUL48) of human cytomegalovirus is a competent deubiquitinating protease: mutant viruses altered in its activesite cysteine or histidine are viable. J Virol 80:6003-6012. http://dx.doi.org/10.1128/JVI.00401-06.
    • (2006) J Virol , vol.80 , pp. 6003-6012
    • Wang, J.1    Loveland, A.N.2    Kattenhorn, L.M.3    Ploegh, H.L.4    Gibson, W.5
  • 11
    • 70450176023 scopus 로고    scopus 로고
    • Cleavage specificity of the UL48 deubiquitinating protease activity of human cytomegalovirus and the growth of an active-site mutant virus in cultured cells
    • Kim ET, Oh SE, Lee YO, Gibson W, Ahn JH. 2009. Cleavage specificity of the UL48 deubiquitinating protease activity of human cytomegalovirus and the growth of an active-site mutant virus in cultured cells. J Virol 83:12046-12056. http://dx.doi.org/10.1128/JVI.00411-09.
    • (2009) J Virol , vol.83 , pp. 12046-12056
    • Kim, E.T.1    Oh, S.E.2    Lee, Y.O.3    Gibson, W.4    Ahn, J.H.5
  • 12
    • 84903880250 scopus 로고    scopus 로고
    • Recovery of an HMWP/hmwBP (pUL48/pUL47) complex from virions of human cytomegalovirus: subunit interactions, oligomer composition, and deubiquitylase activity
    • Tullman JA, Harmon ME, Delannoy M, Gibson W. 2014. Recovery of an HMWP/hmwBP (pUL48/pUL47) complex from virions of human cytomegalovirus: subunit interactions, oligomer composition, and deubiquitylase activity. J Virol 88:8256-8267. http://dx.doi.org/10.1128/JVI.00971-14.
    • (2014) J Virol , vol.88 , pp. 8256-8267
    • Tullman, J.A.1    Harmon, M.E.2    Delannoy, M.3    Gibson, W.4
  • 13
    • 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. http://dx.doi.org/10.1016/j.molcel.2005.07.003.
    • (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
  • 14
    • 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. http://dx.doi.org/10.1128/JVI.79.24.15582-15585.2005.
    • (2005) J Virol , vol.79 , pp. 15582-15585
    • Schlieker, C.1    Korbel, G.A.2    Kattenhorn, L.M.3    Ploegh, H.L.4
  • 15
    • 32944480977 scopus 로고    scopus 로고
    • The pseudorabies virus VP1/2 tegument protein is required for intracellular capsid transport
    • Luxton GW, Lee JI, Haverlock-Moyns S, Schober JM, Smith GA. 2006. The pseudorabies virus VP1/2 tegument protein is required for intracellular capsid transport. J Virol 80:201-209. http://dx.doi.org/10.1128/JVI.80.1.201-209.2006.
    • (2006) J Virol , vol.80 , pp. 201-209
    • Luxton, G.W.1    Lee, J.I.2    Haverlock-Moyns, S.3    Schober, J.M.4    Smith, G.A.5
  • 16
    • 77957652501 scopus 로고    scopus 로고
    • Plus-and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures
    • Radtke K, Kieneke D, Wolfstein A, Michael K, Steffen W, Scholz T, Karger A, Sodeik B. 2010. Plus-and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures. PLoS Pathog 6:e1000991. http://dx.doi.org/10.1371/journal.ppat.1000991.
    • (2010) PLoS Pathog , vol.6
    • Radtke, K.1    Kieneke, D.2    Wolfstein, A.3    Michael, K.4    Steffen, W.5    Scholz, T.6    Karger, A.7    Sodeik, B.8
  • 17
    • 47749138960 scopus 로고    scopus 로고
    • UL36p is required for efficient transport of membrane-associated herpes simplex virus type 1 along microtubules
    • Shanda SK, Wilson DW. 2008. UL36p is required for efficient transport of membrane-associated herpes simplex virus type 1 along microtubules. J Virol 82:7388-7394. http://dx.doi.org/10.1128/JVI.00225-08.
    • (2008) J Virol , vol.82 , pp. 7388-7394
    • Shanda, S.K.1    Wilson, D.W.2
  • 18
    • 84873933638 scopus 로고    scopus 로고
    • The herpesvirus VP1/2 protein is an effector of dyneinmediated capsid transport and neuroinvasion
    • Zaichick SV, Bohannon KP, Hughes A, Sollars PJ, Pickard GE, Smith GA. 2013. The herpesvirus VP1/2 protein is an effector of dyneinmediated capsid transport and neuroinvasion. Cell Host Microbe 13:193-203. http://dx.doi.org/10.1016/j.chom.2013.01.009.
    • (2013) Cell Host Microbe , vol.13 , pp. 193-203
    • Zaichick, S.V.1    Bohannon, K.P.2    Hughes, A.3    Sollars, P.J.4    Pickard, G.E.5    Smith, G.A.6
  • 19
    • 43949107502 scopus 로고    scopus 로고
    • Identification of a highly conserved, functional nuclear localization signal within the N-terminal region of herpes simplex virus type 1 VP1-2 tegument protein
    • Abaitua F, O'Hare P. 2008. Identification of a highly conserved, functional nuclear localization signal within the N-terminal region of herpes simplex virus type 1 VP1-2 tegument protein. J Virol 82:5234-5244. http://dx.doi.org/10.1128/JVI.02497-07.
    • (2008) J Virol , vol.82 , pp. 5234-5244
    • Abaitua, F.1    O'Hare, P.2
  • 20
    • 84866184239 scopus 로고    scopus 로고
    • A nuclear localization signal in herpesvirus protein VP1-2 is essential for infection via capsid routing to the nuclear pore
    • Abaitua F, Hollinshead M, Bolstad M, Crump CM, O'Hare P. 2012. A nuclear localization signal in herpesvirus protein VP1-2 is essential for infection via capsid routing to the nuclear pore. J Virol 86:8998-9014. http://dx.doi.org/10.1128/JVI.01209-12.
    • (2012) J Virol , vol.86 , pp. 8998-9014
    • Abaitua, F.1    Hollinshead, M.2    Bolstad, M.3    Crump, C.M.4    O'Hare, P.5
  • 21
    • 41149126620 scopus 로고    scopus 로고
    • Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1DNAinto the nucleus
    • Jovasevic V, Liang L, Roizman B. 2008. Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1DNAinto the nucleus. J Virol 82:3311-3319. http://dx.doi.org/10.1128/JVI.01919-07.
    • (2008) J Virol , vol.82 , pp. 3311-3319
    • Jovasevic, V.1    Liang, L.2    Roizman, B.3
  • 22
    • 84877346042 scopus 로고    scopus 로고
    • Nuclear targeting of human cytomegalovirus large tegument protein pUL48 is essential for viral growth
    • Brock I, Kruger M, Mertens T, von Einem J. 2013. Nuclear targeting of human cytomegalovirus large tegument protein pUL48 is essential for viral growth. J Virol 87:6005-6019. http://dx.doi.org/10.1128/JVI.03558-12.
    • (2013) J Virol , vol.87 , pp. 6005-6019
    • Brock, I.1    Kruger, M.2    Mertens, T.3    von Einem, J.4
  • 23
    • 84899126061 scopus 로고    scopus 로고
    • Functional analysis of nuclear localization signals in VP1-2 homologues from all herpesvirus subfamilies
    • Hennig T, Abaitua F, O'Hare P. 2014. Functional analysis of nuclear localization signals in VP1-2 homologues from all herpesvirus subfamilies. J Virol 88:5391-5405. http://dx.doi.org/10.1128/JVI.03797-13.
    • (2014) J Virol , vol.88 , pp. 5391-5405
    • Hennig, T.1    Abaitua, F.2    O'Hare, P.3
  • 24
    • 34147100237 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids
    • Bucks MA, O'Regan KJ, Murphy MA, Wills JW, Courtney RJ. 2007. Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids. Virology 361:316-324. http://dx.doi.org/10.1016/j.virol.2006.11.031.
    • (2007) Virology , vol.361 , pp. 316-324
    • Bucks, M.A.1    O'Regan, K.J.2    Murphy, M.A.3    Wills, J.W.4    Courtney, R.J.5
  • 25
    • 84863606066 scopus 로고    scopus 로고
    • Nuclear egress of pseudorabies virus capsids is enhanced by a subspecies of the large tegument protein that is lost upon cytoplasmic maturation
    • Leelawong M, Lee JI, Smith GA. 2012. Nuclear egress of pseudorabies virus capsids is enhanced by a subspecies of the large tegument protein that is lost upon cytoplasmic maturation. J Virol 86:6303-6314. http://dx.doi.org/10.1128/JVI.07051-11.
    • (2012) J Virol , vol.86 , pp. 6303-6314
    • Leelawong, M.1    Lee, J.I.2    Smith, G.A.3
  • 26
    • 0034466764 scopus 로고    scopus 로고
    • A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells
    • Desai PJ. 2000. A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells. J Virol 74:11608-11618. http://dx.doi.org/10.1128/JVI.74.24.11608-11618.2000.
    • (2000) J Virol , vol.74 , pp. 11608-11618
    • Desai, P.J.1
  • 27
    • 6344219960 scopus 로고    scopus 로고
    • Essential function of the pseudorabies virus UL36 gene product is independent of its interaction with the UL37 protein
    • Fuchs W, Klupp BG, Granzow H, Mettenleiter TC. 2004. Essential function of the pseudorabies virus UL36 gene product is independent of its interaction with the UL37 protein. J Virol 78:11879-11889. http://dx.doi.org/10.1128/JVI.78.21.11879-11889.2004.
    • (2004) J Virol , vol.78 , pp. 11879-11889
    • Fuchs, W.1    Klupp, B.G.2    Granzow, H.3    Mettenleiter, T.C.4
  • 28
    • 84861303783 scopus 로고    scopus 로고
    • The C terminus of the large tegument protein pUL36 contains multiple capsid binding sites that function differently during assembly and cell entry of herpes simplex virus
    • Schipke J, Pohlmann A, Diestel R, Binz A, Rudolph K, Nagel CH, Bauerfeind R, Sodeik B. 2012. The C terminus of the large tegument protein pUL36 contains multiple capsid binding sites that function differently during assembly and cell entry of herpes simplex virus. J Virol 86: 3682-3700. http://dx.doi.org/10.1128/JVI.06432-11.
    • (2012) J Virol , vol.86 , pp. 3682-3700
    • Schipke, J.1    Pohlmann, A.2    Diestel, R.3    Binz, A.4    Rudolph, K.5    Nagel, C.H.6    Bauerfeind, R.7    Sodeik, B.8
  • 29
    • 84904906427 scopus 로고    scopus 로고
    • Identification of human cytomegalovirus genes important for biogenesis of the cytoplasmic virion assembly complex
    • Das S, Ortiz DA, Gurczynski SJ, Khan F, Pellett PE. 2014. Identification of human cytomegalovirus genes important for biogenesis of the cytoplasmic virion assembly complex. J Virol 88:9086-9099. http://dx.doi.org/10.1128/JVI.01141-14.
    • (2014) J Virol , vol.88 , pp. 9086-9099
    • Das, S.1    Ortiz, D.A.2    Gurczynski, S.J.3    Khan, F.4    Pellett, P.E.5
  • 30
    • 2642574870 scopus 로고    scopus 로고
    • Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells
    • Lee HR, Kim DJ, Lee JM, Choi CY, Ahn BY, Hayward GS, Ahn JH. 2004. Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells. J Virol 78: 6527-6542. http://dx.doi.org/10.1128/JVI.78.12.6527-6542.2004.
    • (2004) J Virol , vol.78 , pp. 6527-6542
    • Lee, H.R.1    Kim, D.J.2    Lee, J.M.3    Choi, C.Y.4    Ahn, B.Y.5    Hayward, G.S.6    Ahn, J.H.7
  • 31
    • 55249109587 scopus 로고    scopus 로고
    • Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO
    • Huh YH, Kim YE, Kim ET, Park JJ, Song MJ, Zhu H, Hayward GS, Ahn JH. 2008. Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO. J Virol 82:10444-10454. http://dx.doi.org/10.1128/JVI.00833-08.
    • (2008) J Virol , vol.82 , pp. 10444-10454
    • Huh, Y.H.1    Kim, Y.E.2    Kim, E.T.3    Park, J.J.4    Song, M.J.5    Zhu, H.6    Hayward, G.S.7    Ahn, J.H.8
  • 32
    • 0024283936 scopus 로고
    • A versatile in vivo and in vitro eukaryotic expression vector for protein engineering
    • Green S, Issemann I, Sheer E. 1988. A versatile in vivo and in vitro eukaryotic expression vector for protein engineering. Nucleic Acids Res 16:369. http://dx.doi.org/10.1093/nar/16.1.369.
    • (1988) Nucleic Acids Res , vol.16 , pp. 369
    • Green, S.1    Issemann, I.2    Sheer, E.3
  • 33
    • 0025931225 scopus 로고
    • A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription
    • Roth MB, Zahler AM, Stolk JA. 1991. A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription. J Cell Biol 115:587-596. http://dx.doi.org/10.1083/jcb.115.3.587.
    • (1991) J Cell Biol , vol.115 , pp. 587-596
    • Roth, M.B.1    Zahler, A.M.2    Stolk, J.A.3
  • 34
    • 84904596068 scopus 로고    scopus 로고
    • Analysis of human cytomegalovirus-encoded SUMO targets and temporal regulation of SUMOylation of the immediate-early proteins IE1 and IE2 during infection
    • Kim ET, Kim YE, Kim YJ, Lee MK, Hayward GS, Ahn JH. 2014. Analysis of human cytomegalovirus-encoded SUMO targets and temporal regulation of SUMOylation of the immediate-early proteins IE1 and IE2 during infection. PLoS One 9:e103308. http://dx.doi.org/10.1371/journal.pone.0103308.
    • (2014) PLoS One , vol.9
    • Kim, E.T.1    Kim, Y.E.2    Kim, Y.J.3    Lee, M.K.4    Hayward, G.S.5    Ahn, J.H.6
  • 35
    • 0035082279 scopus 로고    scopus 로고
    • Evaluation of interactions of human cytomegalovirus immediate-early IE2 regulatory protein with small ubiquitin-like modifiers and their conjuga-tion enzyme Ubc9
    • Ahn JH, Xu Y, Jang WJ, Matunis MJ, Hayward GS. 2001. Evaluation of interactions of human cytomegalovirus immediate-early IE2 regulatory protein with small ubiquitin-like modifiers and their conjuga-tion enzyme Ubc9. J Virol 75:3859-3872. http://dx.doi.org/10.1128/JVI.75.8.3859-3872.2001.
    • (2001) J Virol , vol.75 , pp. 3859-3872
    • Ahn, J.H.1    Xu, Y.2    Jang, W.J.3    Matunis, M.J.4    Hayward, G.S.5
  • 36
    • 0035132107 scopus 로고    scopus 로고
    • Human cytomegalovirus with IE-2 (UL122) deleted fails to express early lytic genes
    • Marchini A, Liu H, Zhu H. 2001. Human cytomegalovirus with IE-2 (UL122) deleted fails to express early lytic genes. J Virol 75:1870-1878. http://dx.doi.org/10.1128/JVI.75.4.1870-1878.2001.
    • (2001) J Virol , vol.75 , pp. 1870-1878
    • Marchini, A.1    Liu, H.2    Zhu, H.3
  • 37
    • 0032728379 scopus 로고    scopus 로고
    • The human cytomegalovirus IE2 and UL112-113 proteins accumulate in viral DNA replication compartments that initiate from the periphery of promyelocytic leukemia proteinassociated nuclear bodies (PODs or ND10)
    • Ahn JH, Jang WJ, Hayward GS. 1999. The human cytomegalovirus IE2 and UL112-113 proteins accumulate in viral DNA replication compartments that initiate from the periphery of promyelocytic leukemia proteinassociated nuclear bodies (PODs or ND10). J Virol 73:10458-10471.
    • (1999) J Virol , vol.73 , pp. 10458-10471
    • Ahn, J.H.1    Jang, W.J.2    Hayward, G.S.3
  • 38
    • 0033256559 scopus 로고    scopus 로고
    • Analysis of transcripts expressed from the UL47 gene of human cytomegalovirus
    • Hyun JJ, Park HS, Kim KH, Kim HJ. 1999. Analysis of transcripts expressed from the UL47 gene of human cytomegalovirus. Arch Pharm Res 22:542-548. http://dx.doi.org/10.1007/BF02975323.
    • (1999) Arch Pharm Res , vol.22 , pp. 542-548
    • Hyun, J.J.1    Park, H.S.2    Kim, K.H.3    Kim, H.J.4
  • 39
    • 0022458651 scopus 로고
    • Characterization of phosphoproteins and protein kinase activity of virions, noninfectious enveloped particles, and dense bodies of human cytomegalovirus
    • Roby C, Gibson W. 1986. Characterization of phosphoproteins and protein kinase activity of virions, noninfectious enveloped particles, and dense bodies of human cytomegalovirus. J Virol 59:714-727.
    • (1986) J Virol , vol.59 , pp. 714-727
    • Roby, C.1    Gibson, W.2
  • 40
    • 79953661477 scopus 로고    scopus 로고
    • Yeast two hybrid analyses reveal novel binary interactions between human cytomegalovirus-encoded virion proteins
    • To A, Bai Y, Shen A, Gong H, Umamoto S, Lu S, Liu F. 2011. Yeast two hybrid analyses reveal novel binary interactions between human cytomegalovirus-encoded virion proteins. PLoS One 6:e17796. http://dx.doi.org/10.1371/journal.pone.0017796.
    • (2011) PLoS One , vol.6
    • To, A.1    Bai, Y.2    Shen, A.3    Gong, H.4    Umamoto, S.5    Lu, S.6    Liu, F.7
  • 41
    • 78650066595 scopus 로고    scopus 로고
    • Identification of binary interactions between human cytomegalovirus virion proteins
    • Phillips SL, Bresnahan WA. 2011. Identification of binary interactions between human cytomegalovirus virion proteins. J Virol 85:440-447. http://dx.doi.org/10.1128/JVI.01551-10.
    • (2011) J Virol , vol.85 , pp. 440-447
    • Phillips, S.L.1    Bresnahan, W.A.2
  • 42
    • 58149384474 scopus 로고    scopus 로고
    • Role of the UL25 protein in herpes simplex virus DNA encapsidation
    • Cockrell SK, Sanchez ME, Erazo A, Homa FL. 2009. Role of the UL25 protein in herpes simplex virus DNA encapsidation. J Virol 83:47-57. http://dx.doi.org/10.1128/JVI.01889-08.
    • (2009) J Virol , vol.83 , pp. 47-57
    • Cockrell, S.K.1    Sanchez, M.E.2    Erazo, A.3    Homa, F.L.4
  • 43
    • 35448946916 scopus 로고    scopus 로고
    • The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins
    • Coller KE, Lee JI, Ueda A, Smith GA. 2007. The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins. J Virol 81:11790-11797. http://dx.doi.org/10.1128/JVI.01113-07.
    • (2007) J Virol , vol.81 , pp. 11790-11797
    • Coller, K.E.1    Lee, J.I.2    Ueda, A.3    Smith, G.A.4
  • 44
    • 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. http://dx.doi.org/10.1038/nri2337.
    • (2008) Nat Rev Immunol , vol.8 , pp. 501-511
    • Sun, S.C.1
  • 45
    • 84940301972 scopus 로고    scopus 로고
    • Herpesvirus-encoded deubiquitinating proteases and their roles in regulating immune signaling pathways
    • Kwon KM, Ahn JH. 2013. Herpesvirus-encoded deubiquitinating proteases and their roles in regulating immune signaling pathways. J Bacteriol Virol 43:244-252. http://dx.doi.org/10.4167/jbv.2013.43.4.244.
    • (2013) J Bacteriol Virol , vol.43 , pp. 244-252
    • Kwon, K.M.1    Ahn, J.H.2
  • 46
    • 84886877704 scopus 로고    scopus 로고
    • Herpes simplex virus 1 ubiquitinspecific protease UL36 inhibits beta interferon production by deubiquitinating TRAF3
    • Wang S, Wang K, Li J, Zheng C. 2013. Herpes simplex virus 1 ubiquitinspecific protease UL36 inhibits beta interferon production by deubiquitinating TRAF3. J Virol 87:11851-11860. http://dx.doi.org/10.1128/JVI.01211-13.
    • (2013) J Virol , vol.87 , pp. 11851-11860
    • Wang, S.1    Wang, K.2    Li, J.3    Zheng, C.4
  • 47
    • 84875514442 scopus 로고    scopus 로고
    • Epstein-Barr virus deubiquitinase downregulates TRAF6-mediated NF-kappaB signaling during productive replication
    • Saito S, Murata T, Kanda T, Isomura H, Narita Y, Sugimoto A, Kawashima D, Tsurumi T. 2013. Epstein-Barr virus deubiquitinase downregulates TRAF6-mediated NF-kappaB signaling during productive replication. J Virol 87:4060-4070. http://dx.doi.org/10.1128/JVI.02020-12.
    • (2013) J Virol , vol.87 , pp. 4060-4070
    • Saito, S.1    Murata, T.2    Kanda, T.3    Isomura, H.4    Narita, Y.5    Sugimoto, A.6    Kawashima, D.7    Tsurumi, T.8
  • 48
    • 80055007460 scopus 로고    scopus 로고
    • Inhibition of RIG-I-mediated signaling by Kaposi's sarcoma-associated herpesvirus-encoded deubiquitinase ORF64
    • Inn KS, Lee SH, Rathbun JY, Wong LY, Toth Z, Machida K, Ou JH, Jung JU. 2011. Inhibition of RIG-I-mediated signaling by Kaposi's sarcoma-associated herpesvirus-encoded deubiquitinase ORF64. J Virol 85: 10899-10904. http://dx.doi.org/10.1128/JVI.00690-11.
    • (2011) J Virol , vol.85 , pp. 10899-10904
    • Inn, K.S.1    Lee, S.H.2    Rathbun, J.Y.3    Wong, L.Y.4    Toth, Z.5    Machida, K.6    Ou, J.H.7    Jung, J.U.8
  • 49
    • 80052289989 scopus 로고    scopus 로고
    • Autocatalytic activity of the ubiquitin-specific protease domain of herpes simplex virus 1 VP1-2
    • Bolstad M, Abaitua F, Crump CM, O'Hare P. 2011. Autocatalytic activity of the ubiquitin-specific protease domain of herpes simplex virus 1 VP1-2. J Virol 85:8738-8751. http://dx.doi.org/10.1128/JVI.00798-11.
    • (2011) J Virol , vol.85 , pp. 8738-8751
    • Bolstad, M.1    Abaitua, F.2    Crump, C.M.3    O'Hare, P.4

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.