메뉴 건너뛰기




Volumn 8, Issue 6, 1998, Pages 453-469

Control of apoptosis by poxviruses

Author keywords

Apoptosis; Caspase; Granzyme B; Mechanism; Poxvirus; Serpin

Indexed keywords

ANKYRIN; DOUBLE STRANDED DNA; GRANZYME B; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SUPEROXIDE; TUMOR NECROSIS FACTOR RECEPTOR; VIRUS PROTEIN;

EID: 0031727385     PISSN: 10445773     EISSN: None     Source Type: Journal    
DOI: 10.1006/smvy.1998.0150     Document Type: Article
Times cited : (30)

References (122)
  • 1
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson M. D., Weil M., Raff M. C. Programmed cell death in animal development. Cell. 88:1997;347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 2
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C. B. Apoptosis in the pathogenesis and treatment of disease. Science. 267:1995;1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 3
    • 0028932731 scopus 로고
    • The CTL's kiss of death
    • Berke G. The CTL's kiss of death. Cell. 81:1995;9-12.
    • (1995) Cell , vol.81 , pp. 9-12
    • Berke, G.1
  • 4
    • 0029078587 scopus 로고
    • Cytokine receptors encoded by poxviruses: A lesson in cytokine biology
    • Alcami A., Smith G. L. Cytokine receptors encoded by poxviruses: A lesson in cytokine biology. Immunol. Today. 16:1995;474-478.
    • (1995) Immunol. Today , vol.16 , pp. 474-478
    • Alcami, A.1    Smith, G.L.2
  • 5
    • 0029812736 scopus 로고    scopus 로고
    • New strategies of immune modulation by DNA viruses
    • McFadden G., Graham K., Barry M. New strategies of immune modulation by DNA viruses. Transplant. Proc. 28:1996;2085-2088.
    • (1996) Transplant. Proc. , vol.28 , pp. 2085-2088
    • McFadden, G.1    Graham, K.2    Barry, M.3
  • 8
    • 0030218952 scopus 로고    scopus 로고
    • Virus proteins that bind cytokines, chemokines or interferons
    • Smith G. L. Virus proteins that bind cytokines, chemokines or interferons. Curr. Opin. Immunol. 8:1996;467-471.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 467-471
    • Smith, G.L.1
  • 9
    • 0031034563 scopus 로고    scopus 로고
    • Controlling cell death
    • Golstein P. Controlling cell death. Science. 275:1997;1081-1082.
    • (1997) Science , vol.275 , pp. 1081-1082
    • Golstein, P.1
  • 10
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S. Apoptosis by death factor. Cell. 88:1997;355-365.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 17
    • 0027517091 scopus 로고
    • An update on the vaccinia virus genome
    • Johnson G. P., Goebel S. J., Paoletti E. An update on the vaccinia virus genome. Virology. 196:1993;381-401.
    • (1993) Virology , vol.196 , pp. 381-401
    • Johnson, G.P.1    Goebel, S.J.2    Paoletti, E.3
  • 20
    • 2642667881 scopus 로고
    • Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases
    • Pickup D. J., Ink B. S., Hu W., Ray C. A., Joklik W. K. Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases. Proc. Natl. Acad. Sci. USA. 83:1986;7698-7702.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7698-7702
    • Pickup, D.J.1    Ink, B.S.2    Hu, W.3    Ray, C.A.4    Joklik, W.K.5
  • 21
    • 0026535483 scopus 로고
    • Acute inflammatory response to cowpox virus infection of the chorioallantoic membrane of the chick embryo
    • Fredrickson T. N., Sechler J. M., Palumbo G. J., Albert J., Khairallah L. H., Buller R. M. Acute inflammatory response to cowpox virus infection of the chorioallantoic membrane of the chick embryo. Virology. 187:1992;693-704.
    • (1992) Virology , vol.187 , pp. 693-704
    • Fredrickson, T.N.1    Sechler, J.M.2    Palumbo, G.J.3    Albert, J.4    Khairallah, L.H.5    Buller, R.M.6
  • 22
    • 0024433218 scopus 로고
    • Inhibition of an inflammatory response is mediated by a 38-kDa protein of cowpox virus
    • Palumbo G. J., Pickup D. J., Fredrickson T. N., McIntyre L. J., Buller R. M. Inhibition of an inflammatory response is mediated by a 38-kDa protein of cowpox virus. Virology. 172:1989;262-273.
    • (1989) Virology , vol.172 , pp. 262-273
    • Palumbo, G.J.1    Pickup, D.J.2    Fredrickson, T.N.3    McIntyre, L.J.4    Buller, R.M.5
  • 23
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme
    • Ray C. A., Black R. A., Kronheim S. R., Greenstreet T. A., Sleath P. R., Salvesen G. S., Pickup D. J. Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme. Cell. 69:1992;597-604.
    • (1992) Cell , vol.69 , pp. 597-604
    • Ray, C.A.1    Black, R.A.2    Kronheim, S.R.3    Greenstreet, T.A.4    Sleath, P.R.5    Salvesen, G.S.6    Pickup, D.J.7
  • 24
    • 0030338359 scopus 로고    scopus 로고
    • Inhibition of cysteine and serine proteinases by the cowpox virus serpin CRMA
    • Komiyama T., Quan L. T., Salvesen G. S. Inhibition of cysteine and serine proteinases by the cowpox virus serpin CRMA. Adv. Exp. Med. Biol. 389:1996;173-176.
    • (1996) Adv. Exp. Med. Biol. , vol.389 , pp. 173-176
    • Komiyama, T.1    Quan, L.T.2    Salvesen, G.S.3
  • 25
    • 0028168514 scopus 로고
    • Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA: An example of cross-class inhibition
    • Komiyama T., Ray C. A., Pickup D. J., Howard A. D., Thornberry N. A., Peterson E. P., Salvesen G. Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA: An example of cross-class inhibition. J. Biol. Chem. 269:1994;19331-19337.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19331-19337
    • Komiyama, T.1    Ray, C.A.2    Pickup, D.J.3    Howard, A.D.4    Thornberry, N.A.5    Peterson, E.P.6    Salvesen, G.7
  • 26
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • Yuan J., Shaham S., Ledoux S., Ellis H. M., Horvitz H. R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell. 75:1993;641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 27
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1β converting enzyme, a mammalian homolog of the C. elegans cell death gene CED-3
    • Miura M., Zhu H., Rotello R., Hartwieg E. A., Yuan J. Induction of apoptosis in fibroblasts by IL-1β converting enzyme, a mammalian homolog of the C. elegans cell death gene CED-3. Cell. 75:1993;653-660.
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartwieg, E.A.4    Yuan, J.5
  • 29
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau N., Sympson C. J., Werb Z., Bissell M. J. Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science. 267:1995;891-893.
    • (1995) Science , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.J.4
  • 30
    • 0028873964 scopus 로고
    • Fas- And tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product
    • Tewari M., Dixit V. M. Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product. J. Biol. Chem. 270:1995;3255-3260.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3255-3260
    • Tewari, M.1    Dixit, V.M.2
  • 32
    • 0029022365 scopus 로고
    • Involvement of an ICE-like protease in Fas-mediated apoptosis
    • Enari M., Hug H., Nagata S. Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature. 375:1995;78-81.
    • (1995) Nature , vol.375 , pp. 78-81
    • Enari, M.1    Hug, H.2    Nagata, S.3
  • 33
    • 0029813306 scopus 로고    scopus 로고
    • Protection against apoptosis by the vaccinia virus SPI-2 (B13R) gene product
    • Dobbelstein M., Shenk T. Protection against apoptosis by the vaccinia virus SPI-2 (B13R) gene product. J. Virol. 70:1996;6479-6485.
    • (1996) J. Virol. , vol.70 , pp. 6479-6485
    • Dobbelstein, M.1    Shenk, T.2
  • 34
    • 0029905073 scopus 로고    scopus 로고
    • Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases
    • Srinivasula S. M., Ahmad M., Fernandes Alnemri T., Litwack G., Alnemri E. S. Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases. Proc. Natl. Acad. Sci. USA. 93:1996;14486-14491.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14486-14491
    • Srinivasula, S.M.1    Ahmad, M.2    Fernandes Alnemri, T.3    Litwack, G.4    Alnemri, E.S.5
  • 36
    • 0030977847 scopus 로고    scopus 로고
    • Target protease specificity of the viral serpin CrmA - Analysis of five caspases
    • Zhou Q., Snipas S., Orth K., Muzio M., Dixit V. M., Salvesen G. S. Target protease specificity of the viral serpin CrmA - Analysis of five caspases. J. Biol. Chem. 272:1997;7797-7800.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7797-7800
    • Zhou, Q.1    Snipas, S.2    Orth, K.3    Muzio, M.4    Dixit, V.M.5    Salvesen, G.S.6
  • 38
    • 0029056059 scopus 로고
    • Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein
    • Xue D., Horvitz H. R. Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein. Nature. 377:1995;248-251.
    • (1995) Nature , vol.377 , pp. 248-251
    • Xue, D.1    Horvitz, H.R.2
  • 39
    • 0029058323 scopus 로고
    • The baculovirus p35 protein inhibits Fas- And tumor necrosis factor-induced apoptosis
    • Beidler D. R., Tewari M., Friesen P. D., Poirier G., Dixit V. M. The baculovirus p35 protein inhibits Fas- and tumor necrosis factor-induced apoptosis. J. Biol. Chem. 270:1995;16526-16528.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16526-16528
    • Beidler, D.R.1    Tewari, M.2    Friesen, P.D.3    Poirier, G.4    Dixit, V.M.5
  • 40
    • 0028955325 scopus 로고
    • Granzyme B is inhibited by the cowpox virus serpin cytokine response modifier A
    • Quan L. T., Caputo A., Bleackley R. C., Pickup D. J., Salvesen G. S. Granzyme B is inhibited by the cowpox virus serpin cytokine response modifier A. J. Biol. Chem. 270:1995;10377-10379.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10377-10379
    • Quan, L.T.1    Caputo, A.2    Bleackley, R.C.3    Pickup, D.J.4    Salvesen, G.S.5
  • 41
    • 0029099845 scopus 로고    scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell derived granzyme B
    • Darmon A. J., Nicholson D. W., Bleackley R. C. Activation of the apoptotic protease CPP32 by cytotoxic T-cell derived granzyme B. Nature. 377:1996;446-448.
    • (1996) Nature , vol.377 , pp. 446-448
    • Darmon, A.J.1    Nicholson, D.W.2    Bleackley, R.C.3
  • 42
    • 9344261615 scopus 로고    scopus 로고
    • The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism
    • Martin S. J., Amarante Mendes G. P., Shi L., Chuang T. H., Casiano C. A., O'Brien G. A., Fitzgerald P., Tan E. M., Bokoch G. M., Greenberg A. H., Green D. R. The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism. EMBO J. 15:1996;2407-2416.
    • (1996) EMBO J. , vol.15 , pp. 2407-2416
    • Martin, S.J.1    Amarante Mendes, G.P.2    Shi, L.3    Chuang, T.H.4    Casiano, C.A.5    O'Brien, G.A.6    Fitzgerald, P.7    Tan, E.M.8    Bokoch, G.M.9    Greenberg, A.H.10    Green, D.R.11
  • 43
    • 0029808217 scopus 로고    scopus 로고
    • Differential inhibition of the Fas- And granule-mediated cytolysis pathways by the orthopoxvirus cytokine response modifier A/SPI-2 and SPI-1 protein
    • Macen J. L., Garner R. S., Musy P. Y., Brooks M. A., Turner P. C., Moyer R. W., McFadden G., Bleackley R. C. Differential inhibition of the Fas- and granule-mediated cytolysis pathways by the orthopoxvirus cytokine response modifier A/SPI-2 and SPI-1 protein. Proc. Natl. Acad. Sci. USA. 93:1996;9108-9113.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9108-9113
    • MacEn, J.L.1    Garner, R.S.2    Musy, P.Y.3    Brooks, M.A.4    Turner, P.C.5    Moyer, R.W.6    McFadden, G.7    Bleackley, R.C.8
  • 44
    • 0029120118 scopus 로고
    • CrmA, a poxvirus-encoded serpin, inhibits cytotoxic T-lymphocyte-mediated apoptosis
    • Tewari M., Telford W. G., Miller R. A., Dixit V. M. CrmA, a poxvirus-encoded serpin, inhibits cytotoxic T-lymphocyte-mediated apoptosis. J. Biol. Chem. 270:1995;22705-22708.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22705-22708
    • Tewari, M.1    Telford, W.G.2    Miller, R.A.3    Dixit, V.M.4
  • 45
    • 0029914132 scopus 로고    scopus 로고
    • A cytosolic granzyme B inhibitor related to the viral apoptotic regulator cytokine response modifier A is present in cytotoxic lymphocytes
    • Sun J., Bird C. H., Sutton V., McDonald L., Coughlin P. B., De Jong T. A., Trapani J. A., Bird P. I. A cytosolic granzyme B inhibitor related to the viral apoptotic regulator cytokine response modifier A is present in cytotoxic lymphocytes. J. Biol. Chem. 271:1996;27802-27809.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27802-27809
    • Sun, J.1    Bird, C.H.2    Sutton, V.3    McDonald, L.4    Coughlin, P.B.5    De Jong, T.A.6    Trapani, J.A.7    Bird, P.I.8
  • 46
    • 0027215907 scopus 로고
    • Apoptosis reduces both the in vitro replication and the in vivo infectivity of a baculovirus
    • Clem R. J., Miller L. K. Apoptosis reduces both the in vitro replication and the in vivo infectivity of a baculovirus. J. Virol. 67:1993;3730-3738.
    • (1993) J. Virol. , vol.67 , pp. 3730-3738
    • Clem, R.J.1    Miller, L.K.2
  • 47
    • 0026344133 scopus 로고
    • Prevention of apoptosis by a baculovirus gene during infection of insect cells
    • Clem R. J., Fechheimer M., Miller L. K. Prevention of apoptosis by a baculovirus gene during infection of insect cells. Science. 254:1991;1388-1390.
    • (1991) Science , vol.254 , pp. 1388-1390
    • Clem, R.J.1    Fechheimer, M.2    Miller, L.K.3
  • 48
    • 0028896139 scopus 로고
    • Vaccinia virus serpins B13R (SPI-2) and B22R (SPI-1) encode M(r) 38.5 and 40K, intracellular polypeptides that do not affect virus virulence in a murine intranasal model
    • Kettle S., Blake N. W., Law K. M., Smith G. L. Vaccinia virus serpins B13R (SPI-2) and B22R (SPI-1) encode M(r) 38.5 and 40K, intracellular polypeptides that do not affect virus virulence in a murine intranasal model. Virology. 206:1995;136-147.
    • (1995) Virology , vol.206 , pp. 136-147
    • Kettle, S.1    Blake, N.W.2    Law, K.M.3    Smith, G.L.4
  • 49
    • 0027483720 scopus 로고
    • The effects of serpin gene mutations on the distinctive pathobiology of cowpox and rabbitpox virus following intranasal inoculation of Balb/c mice
    • Thompson J. P., Turner P. C., Ali A. N., Crenshaw B. C., Moyer R. W. The effects of serpin gene mutations on the distinctive pathobiology of cowpox and rabbitpox virus following intranasal inoculation of Balb/c mice. Virology. 197:1993;328-338.
    • (1993) Virology , vol.197 , pp. 328-338
    • Thompson, J.P.1    Turner, P.C.2    Ali, A.N.3    Crenshaw, B.C.4    Moyer, R.W.5
  • 51
    • 0026646637 scopus 로고
    • A soluble receptor for interleukin-1β encoded by vaccinia virus: A novel mechanism of virus modulation of the host response to infection
    • Alcami A., Smith G. L. A soluble receptor for interleukin-1β encoded by vaccinia virus: A novel mechanism of virus modulation of the host response to infection. Cell. 71:1992;153-167.
    • (1992) Cell , vol.71 , pp. 153-167
    • Alcami, A.1    Smith, G.L.2
  • 52
    • 0029780081 scopus 로고    scopus 로고
    • A mechanism for the inhibition of fever by a virus
    • Alcami A., Smith G. L. A mechanism for the inhibition of fever by a virus. Proc. Natl. Acad. Sci. USA. 93:1996;11029-11034.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11029-11034
    • Alcami, A.1    Smith, G.L.2
  • 53
    • 0031052956 scopus 로고    scopus 로고
    • Vaccinia virus serpin B13R (SPI-2) inhibits interleukin-1 beta-converting enzyme and protects virus-infected cells from TNF- And Fas-mediated apoptosis, but does not prevent IL-1 beta-induced fever
    • Kettle S., Alcami A., Khanna A., Ehret R., Jassoy C., Smith G. L. Vaccinia virus serpin B13R (SPI-2) inhibits interleukin-1 beta-converting enzyme and protects virus-infected cells from TNF- and Fas-mediated apoptosis, but does not prevent IL-1 beta-induced fever. J. Gen. Virol. 78:1997;677-685.
    • (1997) J. Gen. Virol. , vol.78 , pp. 677-685
    • Kettle, S.1    Alcami, A.2    Khanna, A.3    Ehret, R.4    Jassoy, C.5    Smith, G.L.6
  • 54
    • 0029976336 scopus 로고    scopus 로고
    • The mode of death of pig kidney cells infected with cowpox virus is governed by the expression of the crmA gene
    • Ray C. A., Pickup D. J. The mode of death of pig kidney cells infected with cowpox virus is governed by the expression of the crmA gene. Virology. 217:1996;384-391.
    • (1996) Virology , vol.217 , pp. 384-391
    • Ray, C.A.1    Pickup, D.J.2
  • 55
    • 0031957007 scopus 로고    scopus 로고
    • Activation of caspases in pig kidney cells infected with wild-type and CrmA/SPI-2 mutants of cowpox and rabbitpox viruses
    • Macen J., Takahashi A., Moon K. B., Nathaniel R., Turner P. C., Moyer R. W. Activation of caspases in pig kidney cells infected with wild-type and CrmA/SPI-2 mutants of cowpox and rabbitpox viruses. J. Viro. 72:1998;3524-3533.
    • (1998) J. Viro. , vol.72 , pp. 3524-3533
    • MacEn, J.1    Takahashi, A.2    Moon, K.B.3    Nathaniel, R.4    Turner, P.C.5    Moyer, R.W.6
  • 56
    • 12644256886 scopus 로고    scopus 로고
    • CrmA/SPI-2 inhibition of an endogenous ICE-related protease responsible for lamin A cleavage and apoptotic nuclear fragmentation
    • Takahashi A., Musy P. Y., Martins L. M., Poirier G. G., Moyer R. W., Earnshaw W. C. CrmA/SPI-2 inhibition of an endogenous ICE-related protease responsible for lamin A cleavage and apoptotic nuclear fragmentation. J. Biol. Chem. 271:1996;32487-32490.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32487-32490
    • Takahashi, A.1    Musy, P.Y.2    Martins, L.M.3    Poirier, G.G.4    Moyer, R.W.5    Earnshaw, W.C.6
  • 57
    • 0029839388 scopus 로고    scopus 로고
    • Characterization of a myxoma virus-encoded serpin-like protein with activity against interleukin-1β converting enzyme
    • Petit F., Bertagnoli S., Gelfi J., Fassy F., Boucraut-Baralon C., Milon A. Characterization of a myxoma virus-encoded serpin-like protein with activity against interleukin-1β converting enzyme. J. Virol. 70:1996;5860-5866.
    • (1996) J. Virol. , vol.70 , pp. 5860-5866
    • Petit, F.1    Bertagnoli, S.2    Gelfi, J.3    Fassy, F.4    Boucraut-Baralon, C.5    Milon, A.6
  • 58
    • 0027501113 scopus 로고
    • DNA sequence analysis of conserved and unique regions of swinepox virus: Identification of genetic elements supporting phenotypic observations including a novel G protein-coupled receptor homologue
    • Massung R. F., Jayarama V., Moyer R. W. DNA sequence analysis of conserved and unique regions of swinepox virus: Identification of genetic elements supporting phenotypic observations including a novel G protein-coupled receptor homologue. Virology. 197:1993;511-528.
    • (1993) Virology , vol.197 , pp. 511-528
    • Massung, R.F.1    Jayarama, V.2    Moyer, R.W.3
  • 59
    • 0013900277 scopus 로고
    • Conditional lethal mutants of rabbitpox virus. II. Mutants (p) that fail to multiply in PK-2a cells
    • Fenner F., Sambrook J. F. Conditional lethal mutants of rabbitpox virus. II. Mutants (p) that fail to multiply in PK-2a cells. Virology. 28:1966;600-609.
    • (1966) Virology , vol.28 , pp. 600-609
    • Fenner, F.1    Sambrook, J.F.2
  • 60
    • 0343843713 scopus 로고
    • Genetic studies with mammalian poxviruses. III. White (u) mutants of rabbitpox virus
    • Gemmell A., Fenner F. Genetic studies with mammalian poxviruses. III. White (u) mutants of rabbitpox virus. Virology. 11:1960;219-235.
    • (1960) Virology , vol.11 , pp. 219-235
    • Gemmell, A.1    Fenner, F.2
  • 61
    • 0028840681 scopus 로고
    • A rabbitpox virus serpin gene controls host range by inhibiting apoptosis in restrictive cells
    • Brooks M. A., Ali A. N., Turner P. C., Moyer R. W. A rabbitpox virus serpin gene controls host range by inhibiting apoptosis in restrictive cells. J. Virol. 12:1995;7688-7698.
    • (1995) J. Virol. , vol.12 , pp. 7688-7698
    • Brooks, M.A.1    Ali, A.N.2    Turner, P.C.3    Moyer, R.W.4
  • 62
    • 0027978137 scopus 로고
    • The SPI-1 gene of rabbitpox virus determines host range and is required for hemorrhagic pock formation
    • Ali A. N., Turner P. C., Brooks M. A., Moyer R. W. The SPI-1 gene of rabbitpox virus determines host range and is required for hemorrhagic pock formation. Virology. 202:1994;306-314.
    • (1994) Virology , vol.202 , pp. 306-314
    • Ali, A.N.1    Turner, P.C.2    Brooks, M.A.3    Moyer, R.W.4
  • 63
    • 0026326039 scopus 로고
    • Squamous cell carcinoma antigen is a new member of the serine protease inhibitors
    • Suminami Y., Kishi F., Sekiguchi K., Kato H. Squamous cell carcinoma antigen is a new member of the serine protease inhibitors. Biochem. Biophys. Res. Commun. 181:1991;51-58.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 51-58
    • Suminami, Y.1    Kishi, F.2    Sekiguchi, K.3    Kato, H.4
  • 65
    • 0028814981 scopus 로고
    • Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L
    • Takeda A., Yamamoto T., Nakamura Y., Takahashi T., Hibino T. Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L. FEBS Lett. 359:1995;78-80.
    • (1995) FEBS Lett. , vol.359 , pp. 78-80
    • Takeda, A.1    Yamamoto, T.2    Nakamura, Y.3    Takahashi, T.4    Hibino, T.5
  • 66
    • 0031032401 scopus 로고    scopus 로고
    • Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chymotrypsin-like proteinases cathepsin G and mast cell chymase
    • Schick C., Kamachi Y., Bartuski A. J., Cataltepe S., Schechter N. M., Pemberton P. A., Silverman G. A. Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chymotrypsin-like proteinases cathepsin G and mast cell chymase. J. Biol. Chem. 272:1997;1849-1855.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1849-1855
    • Schick, C.1    Kamachi, Y.2    Bartuski, A.J.3    Cataltepe, S.4    Schechter, N.M.5    Pemberton, P.A.6    Silverman, G.A.7
  • 67
    • 8944257378 scopus 로고    scopus 로고
    • Disruption of M-T5, a novel myxoma virus gene member of poxvirus host range superfamily, results in dramatic attenuation of myxomatosis in infected European rabbits
    • Mossman K., Lee S. F., Barry M., Boshkov L., McFadden G. Disruption of M-T5, a novel myxoma virus gene member of poxvirus host range superfamily, results in dramatic attenuation of myxomatosis in infected European rabbits. J. Virol. 70:1996;4394-4410.
    • (1996) J. Virol. , vol.70 , pp. 4394-4410
    • Mossman, K.1    Lee, S.F.2    Barry, M.3    Boshkov, L.4    McFadden, G.5
  • 69
    • 0023850595 scopus 로고
    • A cowpox virus gene required for multiplication in Chinese hamster ovary cells
    • Spehner D., Gillard S., Drillien R., Kirn A. A cowpox virus gene required for multiplication in Chinese hamster ovary cells. J. Virol. 62:1988;1297-1304.
    • (1988) J. Virol. , vol.62 , pp. 1297-1304
    • Spehner, D.1    Gillard, S.2    Drillien, R.3    Kirn, A.4
  • 72
    • 0026529480 scopus 로고
    • Restricted replication of ectromelia virus in cell culture correlates with mutations in virus-encoded host range gene
    • Chen W., Drillien R., Spehner D., Buller R. M. Restricted replication of ectromelia virus in cell culture correlates with mutations in virus-encoded host range gene. Virology. 187:1992;433-442.
    • (1992) Virology , vol.187 , pp. 433-442
    • Chen, W.1    Drillien, R.2    Spehner, D.3    Buller, R.M.4
  • 73
    • 0028800637 scopus 로고
    • Restriction of vaccinia virus replication in CHO cells occurs at the stage of viral intermediate protein synthesis
    • Ramsey-Ewing A., Moss B. Restriction of vaccinia virus replication in CHO cells occurs at the stage of viral intermediate protein synthesis. Virology. 206:1995;984-993.
    • (1995) Virology , vol.206 , pp. 984-993
    • Ramsey-Ewing, A.1    Moss, B.2
  • 74
    • 0030219781 scopus 로고    scopus 로고
    • Complementation of a vaccinia virus host-range K1L gene deletion by the nonhomologous CP77 gene
    • Ramsey-Ewing A. L., Moss B. Complementation of a vaccinia virus host-range K1L gene deletion by the nonhomologous CP77 gene. Virology. 222:1996;75-86.
    • (1996) Virology , vol.222 , pp. 75-86
    • Ramsey-Ewing, A.L.1    Moss, B.2
  • 75
    • 0028813102 scopus 로고
    • Delay of vaccinia virus-induced apoptosis in nonpermissive Chinese hamster ovary cells by the cowpox virus CHOhr and adenovirus E1B 19K genes
    • Ink B. S., Gilbert C. S., Evan G. I. Delay of vaccinia virus-induced apoptosis in nonpermissive Chinese hamster ovary cells by the cowpox virus CHOhr and adenovirus E1B 19K genes. J. Virol. 69:1995;661-668.
    • (1995) J. Virol. , vol.69 , pp. 661-668
    • Ink, B.S.1    Gilbert, C.S.2    Evan, G.I.3
  • 76
    • 0025202960 scopus 로고
    • Use of a cell-free system to identify the vaccinia virus L1R gene product as the major late myristylated virion protein M25
    • Franke C. A., Wilson E. M., Hruby D. E. Use of a cell-free system to identify the vaccinia virus L1R gene product as the major late myristylated virion protein M25. J. Virol. 64:1990;5988-5996.
    • (1990) J. Virol. , vol.64 , pp. 5988-5996
    • Franke, C.A.1    Wilson, E.M.2    Hruby, D.E.3
  • 77
    • 0029892864 scopus 로고    scopus 로고
    • Neutralizing epitope on penetration protein of vaccinia virus
    • Ichihashi Y., Oie M. Neutralizing epitope on penetration protein of vaccinia virus. Virology. 220:1996;491-494.
    • (1996) Virology , vol.220 , pp. 491-494
    • Ichihashi, Y.1    Oie, M.2
  • 78
    • 0029103360 scopus 로고
    • A myristylated membrane protein encoded by the vaccinia virus L1R open reading frame is the target of potent neutralizing monoclonal antibodies
    • Wolffe E. J., Vijaya S., Moss B. A myristylated membrane protein encoded by the vaccinia virus L1R open reading frame is the target of potent neutralizing monoclonal antibodies. Virology. 211:1995;53-63.
    • (1995) Virology , vol.211 , pp. 53-63
    • Wolffe, E.J.1    Vijaya, S.2    Moss, B.3
  • 79
    • 0030984273 scopus 로고    scopus 로고
    • A novel virus binding assay using confocal microscopy: Demonstration that the intracellular and extracellular vaccinia virions bind to different cellular receptors
    • Vanderplasschen A., Smith G. L. A novel virus binding assay using confocal microscopy: Demonstration that the intracellular and extracellular vaccinia virions bind to different cellular receptors. J. Virol. 71:1997;4032-4041.
    • (1997) J. Virol. , vol.71 , pp. 4032-4041
    • Vanderplasschen, A.1    Smith, G.L.2
  • 80
    • 0028213927 scopus 로고
    • A cellular factor is required for transcription of vaccinia viral intermediate-stage genes
    • Rosales R., Sutter G., Moss B. A cellular factor is required for transcription of vaccinia viral intermediate-stage genes. Proc. Natl. Acad. Sci. USA. 91:1994;3794-3798.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3794-3798
    • Rosales, R.1    Sutter, G.2    Moss, B.3
  • 81
    • 0023408021 scopus 로고
    • Tumorigenic poxviruses: Genomic organization and DNA sequence of the telomeric region of the Shope fibroma virus genome
    • Upton C., Delange A. M., McFadden G. Tumorigenic poxviruses: Genomic organization and DNA sequence of the telomeric region of the Shope fibroma virus genome. Virology. 160:1987;20-30.
    • (1987) Virology , vol.160 , pp. 20-30
    • Upton, C.1    Delange, A.M.2    McFadden, G.3
  • 82
    • 0025880218 scopus 로고
    • Myxoma virus expresses a secreted protein with homology to the tumor necrosis factor receptor gene family that contributes to viral virulence
    • Upton C., Macen J. L., Schreiber M., McFadden G. Myxoma virus expresses a secreted protein with homology to the tumor necrosis factor receptor gene family that contributes to viral virulence. Virology. 184:1991;370-382.
    • (1991) Virology , vol.184 , pp. 370-382
    • Upton, C.1    MacEn, J.L.2    Schreiber, M.3    McFadden, G.4
  • 84
    • 0003148434 scopus 로고
    • Tumor necrosis factor receptors in the poxvirus family: Biological and Genetic implications
    • G. McFadden. Galveston: R. G. Landes
    • Smith C. A., Goodwin R. G. Tumor necrosis factor receptors in the poxvirus family: Biological and Genetic implications. McFadden G. Viroceptors, Virokines and Related Immune Modulators Encoded by DNA Viruses. 1995;29-40 R. G. Landes, Galveston.
    • (1995) Viroceptors, Virokines and Related Immune Modulators Encoded by DNA Viruses , pp. 29-40
    • Smith, C.A.1    Goodwin, R.G.2
  • 85
    • 0028063820 scopus 로고
    • The myxoma virus TNF-receptor homologue (T2) inhibits tumor necrosis factor-alpha in a species-specific fashion
    • Schreiber M., McFadden G. The myxoma virus TNF-receptor homologue (T2) inhibits tumor necrosis factor-alpha in a species-specific fashion. Virology. 204:1994;692-705.
    • (1994) Virology , vol.204 , pp. 692-705
    • Schreiber, M.1    McFadden, G.2
  • 86
    • 0030588633 scopus 로고    scopus 로고
    • Mutational analysis of the ligand-binding domain of M-T2 protein, the tumor necrosis factor receptor homologue of myxoma virus
    • Schreiber M., McFadden G. Mutational analysis of the ligand-binding domain of M-T2 protein, the tumor necrosis factor receptor homologue of myxoma virus. J. Immunol. 157:1996;4486-4495.
    • (1996) J. Immunol. , vol.157 , pp. 4486-4495
    • Schreiber, M.1    McFadden, G.2
  • 87
    • 0029934430 scopus 로고    scopus 로고
    • Myxoma virus T2 protein, a tumor necrosis factor (TNF) receptor homolog, is secreted as a monomer and dimer that each bind rabbit TNFalpha, but the dimer is a more potent TNF inhibitor
    • Schreiber M., Rajarathnam K., McFadden G. Myxoma virus T2 protein, a tumor necrosis factor (TNF) receptor homolog, is secreted as a monomer and dimer that each bind rabbit TNFalpha, but the dimer is a more potent TNF inhibitor. J. Biol. Chem. 271:1996;13333-13341.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13333-13341
    • Schreiber, M.1    Rajarathnam, K.2    McFadden, G.3
  • 88
    • 0030248239 scopus 로고    scopus 로고
    • Cowpox virus genome encodes a second soluble homologue of cellular TNF receptors, distinct from CrmB, that binds TNF but not LT alpha
    • Smith C. A., Hu F. Q., Smith T. D., Richards C. L., Smolak P., Goodwin R. G., Pickup D. J. Cowpox virus genome encodes a second soluble homologue of cellular TNF receptors, distinct from CrmB, that binds TNF but not LT alpha. Virology. 223:1996;132-147.
    • (1996) Virology , vol.223 , pp. 132-147
    • Smith, C.A.1    Hu, F.Q.2    Smith, T.D.3    Richards, C.L.4    Smolak, P.5    Goodwin, R.G.6    Pickup, D.J.7
  • 89
    • 0029772017 scopus 로고    scopus 로고
    • M-T2: A poxvirus TNF receptor homologue with dual activities
    • Sedger L., McFadden G. M-T2: A poxvirus TNF receptor homologue with dual activities. Immun. Cell Biol. 74:1996;538-545.
    • (1996) Immun. Cell Biol. , vol.74 , pp. 538-545
    • Sedger, L.1    McFadden, G.2
  • 90
    • 0031041650 scopus 로고    scopus 로고
    • Distinct domains of M-T2, the myxoma virus tumor necrosis factor (TNF) receptor homolog, mediate extracellular TNF binding and intracellular apoptosis inhibition
    • Schreiber M., Sedger L., McFadden G. Distinct domains of M-T2, the myxoma virus tumor necrosis factor (TNF) receptor homolog, mediate extracellular TNF binding and intracellular apoptosis inhibition. J. Virol. 71:1997;2171-2181.
    • (1997) J. Virol. , vol.71 , pp. 2171-2181
    • Schreiber, M.1    Sedger, L.2    McFadden, G.3
  • 91
    • 0026563754 scopus 로고
    • Cytoplasmic truncation of the p55 tumour necrosis factor (TNF) receptor abolishes signalling, but not induced shedding of the receptor
    • Brakebusch C., Nophar Y., Kemper O., Engelmann H., Wallach D. Cytoplasmic truncation of the p55 tumour necrosis factor (TNF) receptor abolishes signalling, but not induced shedding of the receptor. EMBO J. 11:1992;943-950.
    • (1992) EMBO J. , vol.11 , pp. 943-950
    • Brakebusch, C.1    Nophar, Y.2    Kemper, O.3    Engelmann, H.4    Wallach, D.5
  • 92
    • 0026744103 scopus 로고
    • Tumor necrosis factor receptor signaling. A dominant negative mutation suppresses the activation of the 55-kDa tumor necrosis factor receptor
    • Tartaglia L. A., Goeddel D. V. Tumor necrosis factor receptor signaling. A dominant negative mutation suppresses the activation of the 55-kDa tumor necrosis factor receptor. J. Biol. Chem. 267:1992;4304-4307.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4304-4307
    • Tartaglia, L.A.1    Goeddel, D.V.2
  • 94
    • 0030560808 scopus 로고    scopus 로고
    • Growth of molluscum contagiosum virus in a human foreskin xenograft model
    • Fife K. H., Whitfeld M., Faust H., Goheen M. P., Bryan J., Brown D. R. Growth of molluscum contagiosum virus in a human foreskin xenograft model. Virology. 226:1996;95-101.
    • (1996) Virology , vol.226 , pp. 95-101
    • Fife, K.H.1    Whitfeld, M.2    Faust, H.3    Goheen, M.P.4    Bryan, J.5    Brown, D.R.6
  • 95
    • 0028971467 scopus 로고
    • Replication of molluscum contagiosum virus
    • Buller R. M., Burnett J., Chen W., Kreider J. Replication of molluscum contagiosum virus. Virology. 213:1995;655-659.
    • (1995) Virology , vol.213 , pp. 655-659
    • Buller, R.M.1    Burnett, J.2    Chen, W.3    Kreider, J.4
  • 96
    • 0029764593 scopus 로고    scopus 로고
    • Genome sequence of a human tumorigenic poxvirus: Prediction of specific host response-evasion genes
    • Senkevich T. G., Bugert J. J., Sisler J. R., Koonin E. V., Darai G., Moss B. Genome sequence of a human tumorigenic poxvirus: Prediction of specific host response-evasion genes. Science. 273:1996;813-816.
    • (1996) Science , vol.273 , pp. 813-816
    • Senkevich, T.G.1    Bugert, J.J.2    Sisler, J.R.3    Koonin, E.V.4    Darai, G.5    Moss, B.6
  • 97
    • 0030851338 scopus 로고    scopus 로고
    • The genome of molluscum contagiosum virus: Analysis and comparison with other poxviruses
    • Senkevich T. G., Koonin E. V., Bugert J. J., Darai G., Moss B. The genome of molluscum contagiosum virus: Analysis and comparison with other poxviruses. Virology. 233:1997;19-42.
    • (1997) Virology , vol.233 , pp. 19-42
    • Senkevich, T.G.1    Koonin, E.V.2    Bugert, J.J.3    Darai, G.4    Moss, B.5
  • 99
    • 0030950228 scopus 로고    scopus 로고
    • A novel family of viral death effector domain-containing molecules that inhibit both CD-95- And tumor necrosis factor receptor-1-induced apoptosis
    • Hu S., Vincenz C., Buller M., Dixit V. M. A novel family of viral death effector domain-containing molecules that inhibit both CD-95- and tumor necrosis factor receptor-1-induced apoptosis. J. Biol. Chem. 272:1997;9621-9624.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9621-9624
    • Hu, S.1    Vincenz, C.2    Buller, M.3    Dixit, V.M.4
  • 102
    • 0026787799 scopus 로고
    • Myxoma virus M11L ORF encodes a protein for which cell surface localization is critical in manifestation of viral virulence
    • Graham K. A., Opgenorth A., Upton C., McFadden G. Myxoma virus M11L ORF encodes a protein for which cell surface localization is critical in manifestation of viral virulence. Virology. 191:1992;112-124.
    • (1992) Virology , vol.191 , pp. 112-124
    • Graham, K.A.1    Opgenorth, A.2    Upton, C.3    McFadden, G.4
  • 103
    • 0026765460 scopus 로고
    • Deletion analysis of two tandemly arranged virulence genes in myxoma virus, M11L and myxoma growth factor
    • Opgenorth A., Graham K., Nation N., Strayer D., McFadden G. Deletion analysis of two tandemly arranged virulence genes in myxoma virus, M11L and myxoma growth factor. J. Virol. 66:1992;4720-4731.
    • (1992) J. Virol. , vol.66 , pp. 4720-4731
    • Opgenorth, A.1    Graham, K.2    Nation, N.3    Strayer, D.4    McFadden, G.5
  • 104
    • 0029971614 scopus 로고    scopus 로고
    • Expression of the myxoma virus tumor necrosis factor receptor homologue and M11L genes is required to prevent virus-induced apoptosis in infected rabbit T lymphocytes
    • Macen J. L., Graham K. A., Lee S. F., Schreiber M., Boshkov L. K., McFadden G. Expression of the myxoma virus tumor necrosis factor receptor homologue and M11L genes is required to prevent virus-induced apoptosis in infected rabbit T lymphocytes. Virology. 218:1996;232-237.
    • (1996) Virology , vol.218 , pp. 232-237
    • MacEn, J.L.1    Graham, K.A.2    Lee, S.F.3    Schreiber, M.4    Boshkov, L.K.5    McFadden, G.6
  • 105
    • 0032472279 scopus 로고    scopus 로고
    • Ultraviolet-induced cell death blocked by a selenoprotein from a human dermatotropic poxvirus
    • Shisler J. L., Senkevich T. G., Berry M. J., Moss B. Ultraviolet-induced cell death blocked by a selenoprotein from a human dermatotropic poxvirus. Science. 279:1998;102-105.
    • (1998) Science , vol.279 , pp. 102-105
    • Shisler, J.L.1    Senkevich, T.G.2    Berry, M.J.3    Moss, B.4
  • 106
    • 0029894345 scopus 로고    scopus 로고
    • Knowing when not to stop: Selenocysteine incorporation in eukaryotes
    • Low S. C., Berry M. J. Knowing when not to stop: Selenocysteine incorporation in eukaryotes. Trends Biochem. Sci. 21:1996;203-208.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 203-208
    • Low, S.C.1    Berry, M.J.2
  • 107
    • 0031027794 scopus 로고    scopus 로고
    • Role of peroxide and superoxide anion during tumour cell apoptosis
    • Gorman A., McGowan A., Cotter T. G. Role of peroxide and superoxide anion during tumour cell apoptosis. FEBS Lett. 404:1997;27-33.
    • (1997) FEBS Lett. , vol.404 , pp. 27-33
    • Gorman, A.1    McGowan, A.2    Cotter, T.G.3
  • 108
    • 0027281682 scopus 로고
    • Cell death by apoptosis in epidermal biology
    • Haake A. R., Polakowska R. R. Cell death by apoptosis in epidermal biology. J. Invest. Dermatol. 101:1993;107-112.
    • (1993) J. Invest. Dermatol. , vol.101 , pp. 107-112
    • Haake, A.R.1    Polakowska, R.R.2
  • 109
    • 0025947970 scopus 로고
    • Characterization of a vaccinia virus-encoded double-stranded RNA-binding protein that may be involved in inhibition of the double-stranded RNA-dependent protein kinase
    • Watson J. C., Chang H. W., Jacobs B. L. Characterization of a vaccinia virus-encoded double-stranded RNA-binding protein that may be involved in inhibition of the double-stranded RNA-dependent protein kinase. Virology. 185:1991;206-216.
    • (1991) Virology , vol.185 , pp. 206-216
    • Watson, J.C.1    Chang, H.W.2    Jacobs, B.L.3
  • 110
    • 0025184763 scopus 로고
    • Identification of rpo30, a vaccinia virus RNA polymerase gene with structural similarity to a eucaryotic transcription elongation factor
    • Ahn B. Y., Gershon P. D., Jones E. V., Moss B. Identification of rpo30, a vaccinia virus RNA polymerase gene with structural similarity to a eucaryotic transcription elongation factor. Mol. Cell Biol. 10:1990;5433-5441.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 5433-5441
    • Ahn, B.Y.1    Gershon, P.D.2    Jones, E.V.3    Moss, B.4
  • 111
    • 0021140522 scopus 로고
    • Characterization of a specific kinase inhibitory factor produced by vaccinia virus which inhibits the interferon-induced protein kinase
    • Whitaker Dowling P., Youngner J. S. Characterization of a specific kinase inhibitory factor produced by vaccinia virus which inhibits the interferon-induced protein kinase. Virology. 137:1984;171-181.
    • (1984) Virology , vol.137 , pp. 171-181
    • Whitaker Dowling, P.1    Youngner, J.S.2
  • 112
    • 0021332001 scopus 로고
    • Interferon-mediated, double-stranded RNA-dependent protein kinase is inhibited in extracts from vaccinia virus-infected cells
    • Rice A. P., Kerr I. M. Interferon-mediated, double-stranded RNA-dependent protein kinase is inhibited in extracts from vaccinia virus-infected cells. J. Virol. 50:1984;229-236.
    • (1984) J. Virol. , vol.50 , pp. 229-236
    • Rice, A.P.1    Kerr, I.M.2
  • 113
    • 0026751682 scopus 로고
    • The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase
    • Chang H.-W., Watson J. C., Jacobs B. L. The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase. Proc. Natl. Acad. Sci. USA. 89:1992;4825-4829.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4825-4829
    • Chang, H.-W.1    Watson, J.C.2    Jacobs, B.L.3
  • 114
    • 0028936838 scopus 로고
    • Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene
    • Beattie E., Denzler K. L., Tartaglia J., Perkus M. E., Paoletti E., Jacobs B. L. Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene. J. Virol. 69:1995;499-505.
    • (1995) J. Virol. , vol.69 , pp. 499-505
    • Beattie, E.1    Denzler, K.L.2    Tartaglia, J.3    Perkus, M.E.4    Paoletti, E.5    Jacobs, B.L.6
  • 115
    • 0029133407 scopus 로고
    • Rescue of vaccinia virus lacking the E3L gene by mutants of E3L
    • Chang H. W., Uribe L. H., Jacobs B. L. Rescue of vaccinia virus lacking the E3L gene by mutants of E3L. J. Virol. 69:1995;6605-6608.
    • (1995) J. Virol. , vol.69 , pp. 6605-6608
    • Chang, H.W.1    Uribe, L.H.2    Jacobs, B.L.3
  • 116
    • 0027407080 scopus 로고
    • The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms
    • Davies M. V., Chang H. W., Jacobs B. L., Kaufman R. J. The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms. J. Virol. 67:1993;1688-1692.
    • (1993) J. Virol. , vol.67 , pp. 1688-1692
    • Davies, M.V.1    Chang, H.W.2    Jacobs, B.L.3    Kaufman, R.J.4
  • 119
    • 0028362126 scopus 로고
    • Products of the porcine group C rotavirus NSP3 gene bind specifically to double-stranded RNA and inhibit activation of the interferon-induced protein kinase PKR
    • Langland J. O., Pettiford S., Jiang B., Jacobs B. L. Products of the porcine group C rotavirus NSP3 gene bind specifically to double-stranded RNA and inhibit activation of the interferon-induced protein kinase PKR. J. Virol. 68:1994;3821-3829.
    • (1994) J. Virol. , vol.68 , pp. 3821-3829
    • Langland, J.O.1    Pettiford, S.2    Jiang, B.3    Jacobs, B.L.4
  • 120
    • 0028290902 scopus 로고
    • The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis
    • Lee S. B., Esteban M. The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis. Virology. 199:1994;491-496.
    • (1994) Virology , vol.199 , pp. 491-496
    • Lee, S.B.1    Esteban, M.2
  • 122
    • 0343812093 scopus 로고    scopus 로고
    • The apoptosis pathway triggered by the interferon-induced protein kinase PKR requires the third basic domain, initiates upstream of Bcl-2, and involves ICE-like proteases
    • Lee S. B., Rodriguez D., Rodriguez J. R., Esteban M. The apoptosis pathway triggered by the interferon-induced protein kinase PKR requires the third basic domain, initiates upstream of Bcl-2, and involves ICE-like proteases. Virology. 231:1997;81-88.
    • (1997) Virology , vol.231 , pp. 81-88
    • Lee, S.B.1    Rodriguez, D.2    Rodriguez, J.R.3    Esteban, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.