메뉴 건너뛰기




Volumn 10, Issue 1, 1999, Pages 21-28

An antiviral mechanism of nitric oxide: Inhibition of a viral protease

Author keywords

[No Author keywords available]

Indexed keywords

NITRIC OXIDE;

EID: 0033026199     PISSN: 10747613     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-7613(00)80003-5     Document Type: Article
Times cited : (225)

References (70)
  • 2
    • 0028805193 scopus 로고
    • Inhibitory effect of nitric oxide on the replication of a murine retrovirus in vitro and in vivo
    • Akarid, K., Sinet, M., Desforges, B., and Gougerot-Pocidalo, M.A. (1995). Inhibitory effect of nitric oxide on the replication of a murine retrovirus in vitro and in vivo. J. Virol. 69, 7001-7005.
    • (1995) J. Virol. , vol.69 , pp. 7001-7005
    • Akarid, K.1    Sinet, M.2    Desforges, B.3    Gougerot-Pocidalo, M.A.4
  • 3
    • 0028338583 scopus 로고
    • Naegleria fowleri: Characterization of a secreted histolytic cysteine protease
    • Aldape, K., Huizinga, H., Bouvier, J., and McKerrow, J. (1994). Naegleria fowleri: Characterization of a secreted histolytic cysteine protease. Exper. Parasitol. 78, 230-241.
    • (1994) Exper. Parasitol. , vol.78 , pp. 230-241
    • Aldape, K.1    Huizinga, H.2    Bouvier, J.3    McKerrow, J.4
  • 4
    • 0030691114 scopus 로고    scopus 로고
    • Viral proteases: Evolution of diverse structural motifs to optimize function
    • Babe, L.M., and Craik, C.S. (1997). Viral proteases: Evolution of diverse structural motifs to optimize function. Cell 91, 427-430.
    • (1997) Cell , vol.91 , pp. 427-430
    • Babe, L.M.1    Craik, C.S.2
  • 5
    • 0026915311 scopus 로고
    • Plasmodium falciparum: Differential sensitivity in vitro to E-64 (cysteine protease inhibitor) and Pepstatin A (aspartyl protease inhibitor)
    • Bailly, E., Jambou, R., Savel, J., and Jaureguiberry, G. (1992). Plasmodium falciparum: Differential sensitivity in vitro to E-64 (cysteine protease inhibitor) and Pepstatin A (aspartyl protease inhibitor). J. Protozool. 39, 593-599.
    • (1992) J. Protozool. , vol.39 , pp. 593-599
    • Bailly, E.1    Jambou, R.2    Savel, J.3    Jaureguiberry, G.4
  • 6
    • 0028118622 scopus 로고
    • Purification and characterization of a collagen-degrading protease from Porphyromonas gingivalis
    • Bedi, G.S., and Williams, T. (1994). Purification and characterization of a collagen-degrading protease from Porphyromonas gingivalis. J. Biol. Chem. 269, 599-606.
    • (1994) J. Biol. Chem. , vol.269 , pp. 599-606
    • Bedi, G.S.1    Williams, T.2
  • 7
    • 0028920702 scopus 로고
    • Inhibition of vesicular stomatitis virus infection by nitric oxide
    • Bi, Z., and Reiss, C.S. (1995). Inhibition of vesicular stomatitis virus infection by nitric oxide. J. Virol. 69, 2208-2213.
    • (1995) J. Virol. , vol.69 , pp. 2208-2213
    • Bi, Z.1    Reiss, C.S.2
  • 8
    • 0028966205 scopus 로고
    • Regulation of nitric oxide synthase activity in human immuno-deficiency virus type 1 (HIV-1)-infected monocytes: Implications for HIV-associated neurological disease
    • Bukrinsky, M.I., Nottet, H.S., Schmidtmayerova, H., Dubrovsky, L., Flanagan, C.R., Mullins, M.E., Lipton, S.A., and Gendelman, H.E. (1995). Regulation of nitric oxide synthase activity in human immuno-deficiency virus type 1 (HIV-1)-infected monocytes: Implications for HIV-associated neurological disease. J. Exper. Med. 181, 735-745.
    • (1995) J. Exper. Med. , vol.181 , pp. 735-745
    • Bukrinsky, M.I.1    Nottet, H.S.2    Schmidtmayerova, H.3    Dubrovsky, L.4    Flanagan, C.R.5    Mullins, M.E.6    Lipton, S.A.7    Gendelman, H.E.8
  • 9
    • 0027258651 scopus 로고
    • Evidence for antiviral effect of nitric oxide. Inhibition of herpes simplex virus type 1 replication
    • Croen, K.D. (1993). Evidence for antiviral effect of nitric oxide. Inhibition of herpes simplex virus type 1 replication. J. Clin. Invest. 91, 2446-2452.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2446-2452
    • Croen, K.D.1
  • 10
    • 0030758238 scopus 로고    scopus 로고
    • Synthesis and antimalarial effects of phenothiazine inhibitors of a Plasmodium falciparum cysteine protease
    • Dominguez, J.N., Lopez, S., Charris, J., Iarruso, L., Lobo, G., Semenov, A., Olson, J.E., and Rosenthal, P.J. (1997). Synthesis and antimalarial effects of phenothiazine inhibitors of a Plasmodium falciparum cysteine protease. J. Med. Chem. 40, 2726-2732.
    • (1997) J. Med. Chem. , vol.40 , pp. 2726-2732
    • Dominguez, J.N.1    Lopez, S.2    Charris, J.3    Iarruso, L.4    Lobo, G.5    Semenov, A.6    Olson, J.E.7    Rosenthal, P.J.8
  • 11
    • 0027138172 scopus 로고
    • Expression of virus encoded proteinases: Functional and structural similarities with cellular enzymes
    • Dougherty, W.G., and Semler, B.L. (1993). Expression of virus encoded proteinases: Functional and structural similarities with cellular enzymes. Microbiol. Rev. 57, 781-822.
    • (1993) Microbiol. Rev. , vol.57 , pp. 781-822
    • Dougherty, W.G.1    Semler, B.L.2
  • 12
    • 0026781519 scopus 로고
    • The sequence, organization, and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi
    • Eakin, A.E., Mills, A.A., Harth, G., McKerrow, J.H., and Craik, C.S. (1992). The sequence, organization, and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi. J. Biol. Chem. 267, 7411-7420.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7411-7420
    • Eakin, A.E.1    Mills, A.A.2    Harth, G.3    McKerrow, J.H.4    Craik, C.S.5
  • 14
    • 0031570501 scopus 로고    scopus 로고
    • Mechanisms of nitric oxide related antimicrobial activity
    • Fang, F.C. (1997). Mechanisms of nitric oxide related antimicrobial activity. J. Clin. Invest. 99, 2818-2825.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2818-2825
    • Fang, F.C.1
  • 16
    • 0018342066 scopus 로고
    • Properties of coxsackievirus B3 variants which are amyocarditic or myocarditic for mice
    • Gauntt, C.J., Trousdale, M.D., Labadie, D.R., Paque, R.E., and Nealon, T. (1979). Properties of coxsackievirus B3 variants which are amyocarditic or myocarditic for mice. J. Med. Virol. 3, 207-220.
    • (1979) J. Med. Virol. , vol.3 , pp. 207-220
    • Gauntt, C.J.1    Trousdale, M.D.2    Labadie, D.R.3    Paque, R.E.4    Nealon, T.5
  • 17
    • 0030591758 scopus 로고    scopus 로고
    • A multifunctional vector system for heterologous expression of proteins in E. coli
    • Ghosh, S., and Lowenstein, J.M. (1996). A multifunctional vector system for heterologous expression of proteins in E.coli. Gene 176, 249-255.
    • (1996) Gene , vol.176 , pp. 249-255
    • Ghosh, S.1    Lowenstein, J.M.2
  • 19
    • 0013625411 scopus 로고
    • Protease of encephalomyocarditis virus: Purification and role of SH groups in processing of the structural proteins precursor
    • Gorbalenya, A.E., and Svitkin, Y.V. (1983). Protease of encephalomyocarditis virus: Purification and role of SH groups in processing of the structural proteins precursor. Biochemistry (USSR) 48, 385-395.
    • (1983) Biochemistry (USSR) , vol.48 , pp. 385-395
    • Gorbalenya, A.E.1    Svitkin, Y.V.2
  • 20
    • 0031930829 scopus 로고    scopus 로고
    • Expression and characterization of group A streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes
    • Gubba, S., Low, D.E., and Mussen, J.M. (1998). Expression and characterization of group A streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes. Infect. Immun. 66, 765-770.
    • (1998) Infect. Immun. , vol.66 , pp. 765-770
    • Gubba, S.1    Low, D.E.2    Mussen, J.M.3
  • 22
    • 0026095274 scopus 로고
    • Site-directed mutagenesis of the putative catalytic triad of poliovirus 3C proteinase
    • Hammerle, T., Hellen, C.U., and Wimmer, E. (1991). Site-directed mutagenesis of the putative catalytic triad of poliovirus 3C proteinase. J. Biol. Chem. 266, 5412-5416.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5412-5416
    • Hammerle, T.1    Hellen, C.U.2    Wimmer, E.3
  • 23
    • 0027398184 scopus 로고
    • Peptide-fluoromethyl ketones arrest intracellular replication and intercellular transmission of trypanosoma cruzi
    • Harth, G., Andrews, N., Mills, A.A., Engel, J.C., Smith, R., and McKerrow, J.H. (1993). Peptide-fluoromethyl ketones arrest intracellular replication and intercellular transmission of trypanosoma cruzi. Mol. Biochem. Parasitol. 58, 17-24.
    • (1993) Mol. Biochem. Parasitol. , vol.58 , pp. 17-24
    • Harth, G.1    Andrews, N.2    Mills, A.A.3    Engel, J.C.4    Smith, R.5    McKerrow, J.H.6
  • 24
    • 0024830949 scopus 로고
    • Proteolytic processing of polyproteins in the replication of RNA viruses
    • Hellen, C.U., Kräusslich, H.G., and Wimmer, E. (1989). Proteolytic processing of polyproteins in the replication of RNA viruses. BioChemistry 28, 9881-9890.
    • (1989) Biochemistry , vol.28 , pp. 9881-9890
    • Hellen, C.U.1    Kräusslich, H.G.2    Wimmer, E.3
  • 25
    • 0019085525 scopus 로고
    • Proteolytic inactivation of luciferases from three species of luminous marine bacteria, Beneckea harveyi, photobacterium fischeri, and photobacterium phosphoreum: Evidence of a conserved structural feature
    • Holzman, T.F., and Baldwin, T.O. (1980). Proteolytic inactivation of luciferases from three species of luminous marine bacteria, Beneckea harveyi, photobacterium fischeri, and photobacterium phosphoreum: Evidence of a conserved structural feature. Proc. Natl. Acad. Sci. USA 77, 6363-6367.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 6363-6367
    • Holzman, T.F.1    Baldwin, T.O.2
  • 27
    • 0004134524 scopus 로고
    • Expression and site-specific mutagenesis of the poliovirus 3C protease in Escherichia coli
    • Ivanoff, L.A., Towatari, T., Ray, J., Korant, B.D., and Petteway, S.R., Jr. (1986). Expression and site-specific mutagenesis of the poliovirus 3C protease in Escherichia coli. Proc. Natl. Acad. Sci. USA 83, 5392-5396.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5392-5396
    • Ivanoff, L.A.1    Towatari, T.2    Ray, J.3    Korant, B.D.4    Petteway S.R., Jr.5
  • 28
    • 0027290733 scopus 로고
    • Cleavage of interleukin 1 beta (IL-1 beta) precursor to produce active IL-1 beta by a conserved extracellular cysteine protease from streptococcus pyogenes
    • Kapur, V., Majesky, M.W., Li, L.L., Black, R.A., and Musser, J.M. (1993a). Cleavage of interleukin 1 beta (IL-1 beta) precursor to produce active IL-1 beta by a conserved extracellular cysteine protease from streptococcus pyogenes. Proc. Natl. Acad. Sci. USA 90, 7676-7680.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7676-7680
    • Kapur, V.1    Majesky, M.W.2    Li, L.L.3    Black, R.A.4    Musser, J.M.5
  • 29
    • 0027893017 scopus 로고
    • A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin
    • Kapur, V., Topouzis, S., Majesky, M.W., Li, L.L., Hamrick, M.R., Hamill, R.J., Patti, J.M., and Musser, J.M. (1993b). A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin. Microb. Pathog. 15, 327-346.
    • (1993) Microb. Pathog. , vol.15 , pp. 327-346
    • Kapur, V.1    Topouzis, S.2    Majesky, M.W.3    Li, L.L.4    Hamrick, M.R.5    Hamill, R.J.6    Patti, J.M.7    Musser, J.M.8
  • 30
    • 0027488067 scopus 로고
    • Inhibition of viral replication by interferon-gamma-induced nitric oxide synthase
    • Karupiah, G., Xie, Q.W., Buller, R.M., Nathan, C., Duarte, C., and MacMicking, J.D. (1993). Inhibition of viral replication by interferon-gamma-induced-induced nitric oxide synthase. Science 261, 1445-1448.
    • (1993) Science , vol.261 , pp. 1445-1448
    • Karupiah, G.1    Xie, Q.W.2    Buller, R.M.3    Nathan, C.4    Duarte, C.5    MacMicking, J.D.6
  • 31
    • 0030662226 scopus 로고    scopus 로고
    • Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms
    • Kim, Y.M., Talanian, R.V., and Billiar, T.R. (1997). Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms. J. Biol. Chem. 272, 31138-31148.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31138-31148
    • Kim, Y.M.1    Talanian, R.V.2    Billiar, T.R.3
  • 32
    • 0025212682 scopus 로고
    • Complete nucleotide sequence of infectious Coxsackievirus B3 cDNA: Two initial 5′ uridine residues are regained during plusstrand RNA synthesis
    • Klump, W.M., Bergmann, I., Muller, B.C., Ameis, D., and Kandolf, R. (1990). Complete nucleotide sequence of infectious Coxsackievirus B3 cDNA: Two initial 5′ uridine residues are regained during plusstrand RNA synthesis. J. Virol. 64, 1573-1583.
    • (1990) J. Virol. , vol.64 , pp. 1573-1583
    • Klump, W.M.1    Bergmann, I.2    Muller, B.C.3    Ameis, D.4    Kandolf, R.5
  • 33
    • 0030217887 scopus 로고    scopus 로고
    • Interferon-gamma induced type I nitric oxide synthase activity inhibits viral replication in neurons
    • Komatsu, T., Bi, Z., and Reiss, C.S. (1996). Interferon-gamma induced type I nitric oxide synthase activity inhibits viral replication in neurons. J. Neuroimmunol. 68, 101-108.
    • (1996) J. Neuroimmunol. , vol.68 , pp. 101-108
    • Komatsu, T.1    Bi, Z.2    Reiss, C.S.3
  • 34
    • 0029952366 scopus 로고    scopus 로고
    • Nitric oxide and viral infection: NO antiviral activity against a flavivirus in vitro, and evidence for contribution to pathogenesis in experimental infection in vivo
    • Kreil, T.R., and Eibl, M.M. (1996). Nitric oxide and viral infection: NO antiviral activity against a flavivirus in vitro, and evidence for contribution to pathogenesis in experimental infection in vivo. VirolOgy 219, 304-306.
    • (1996) Virology , vol.219 , pp. 304-306
    • Kreil, T.R.1    Eibl, M.M.2
  • 36
    • 0028199880 scopus 로고
    • Effects of hormones and cysteine protease modulators on infection of HepG2 cells by Plasmodium berghei sporozoites in vitro determined by ELISA immunoassay
    • Kumar, S., Van Pelt, J.F., O'Dowd, C.A., Hollingdale, M.R., and Sinden, R.E. (1994). Effects of hormones and cysteine protease modulators on infection of HepG2 cells by Plasmodium berghei sporozoites in vitro determined by ELISA immunoassay. J. Parasitol. 80, 414-420.
    • (1994) J. Parasitol. , vol.80 , pp. 414-420
    • Kumar, S.1    Van Pelt, J.F.2    O'Dowd, C.A.3    Hollingdale, M.R.4    Sinden, R.E.5
  • 37
    • 0030623609 scopus 로고    scopus 로고
    • Multiple colonization defects in a cysteine protease mutant of Porphyromonas gingivalis
    • Kuramitsu, H., Tokuda, M., Yoneda, M., Duncan, M., and Cho, M.I. (1997). Multiple colonization defects in a cysteine protease mutant of Porphyromonas gingivalis. J. Period. Res. 32, 140-142.
    • (1997) J. Period. Res. , vol.32 , pp. 140-142
    • Kuramitsu, H.1    Tokuda, M.2    Yoneda, M.3    Duncan, M.4    Cho, M.I.5
  • 38
    • 0025335389 scopus 로고
    • Picornavirus protein processing - Enzymes, substrates, and genetic regulation
    • Lawson, M.A., and Semler, B.L. (1990). Picornavirus protein processing - Enzymes, substrates, and genetic regulation. Curr. Top. Microbiol. Immunol. 161, 49-80.
    • (1990) Curr. Top. Microbiol. Immunol. , vol.161 , pp. 49-80
    • Lawson, M.A.1    Semler, B.L.2
  • 40
    • 0031576527 scopus 로고    scopus 로고
    • Nitric oxide reversibly inhibits seven members of the caspase family via S-nitrosylation
    • Li, J., Billiar, T.R., Talanian, R.V., and Kim, Y.M. (1997). Nitric oxide reversibly inhibits seven members of the caspase family via S-nitrosylation. Biochem. Biophys. Res. Commun. 240, 419-424.
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 419-424
    • Li, J.1    Billiar, T.R.2    Talanian, R.V.3    Kim, Y.M.4
  • 41
    • 0026703183 scopus 로고
    • Nitrite and nitrosamine synthesis by hepatocytes isolated from normal woodchucks (Marmota monax) and woodchucks chronically infected with woodchuck hepatitis virus
    • Liu, R.H., Jacob, J.R., Tennant, B.C., and Hotchkiss, J.H. (1992). Nitrite and nitrosamine synthesis by hepatocytes isolated from normal woodchucks (Marmota monax) and woodchucks chronically infected with woodchuck hepatitis virus. Cancer Res. 52, 4139-4143.
    • (1992) Cancer Res. , vol.52 , pp. 4139-4143
    • Liu, R.H.1    Jacob, J.R.2    Tennant, B.C.3    Hotchkiss, J.H.4
  • 43
    • 0030960001 scopus 로고    scopus 로고
    • Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serotype M3 and M49 strains
    • Lukomski, S., Sreevatsan, S., Amberg, C., Reichardt, W., Woischnik, M., Podbielski, A., and Musser, J.M. (1997). Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serotype M3 and M49 strains. J. Clin. Invest. 99, 2574-2580.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2574-2580
    • Lukomski, S.1    Sreevatsan, S.2    Amberg, C.3    Reichardt, W.4    Woischnik, M.5    Podbielski, A.6    Musser, J.M.7
  • 44
    • 0030937832 scopus 로고    scopus 로고
    • Nitric oxide and macrophage function
    • W.E. Paul, C.G. Fathman, and H. Metzger, eds. (Palo Alto, CA: Annual Reviews, Inc.)
    • MacMicking, J.D., Xie, Q.W., and Nathan, C. (1997). Nitric oxide and macrophage function. In Annual Review Of Immunology, W.E. Paul, C.G. Fathman, and H. Metzger, eds. (Palo Alto, CA: Annual Reviews, Inc.), pp. 323-350.
    • (1997) Annual Review of Immunology , pp. 323-350
    • MacMicking, J.D.1    Xie, Q.W.2    Nathan, C.3
  • 45
    • 0029613299 scopus 로고
    • The antiviral role of nitric oxide
    • Mannick, J.B. (1995). The antiviral role of nitric oxide. Res. Immunol. 146, 693-697.
    • (1995) Res. Immunol. , vol.146 , pp. 693-697
    • Mannick, J.B.1
  • 46
    • 0028658374 scopus 로고
    • Nitric oxide produced by human B lymphocytes inhibits apoptosis and Epstein-Barr virus reactivation
    • Mannick, J.B., Asano, K., Izumi, K., Kieff, E., and Stamler, J.S. (1994). Nitric oxide produced by human B lymphocytes inhibits apoptosis and Epstein-Barr virus reactivation. Cell 79, 1137-1146.
    • (1994) Cell , vol.79 , pp. 1137-1146
    • Mannick, J.B.1    Asano, K.2    Izumi, K.3    Kieff, E.4    Stamler, J.S.5
  • 47
    • 0030827880 scopus 로고    scopus 로고
    • Nitric oxide inhibits Fas-induced apoptosis
    • Mannick, J.B., Miao, X.Q., and Stamler, J.S. (1997). Nitric oxide inhibits Fas-induced apoptosis. J. Biol. Chem. 272, 24125-24128.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24125-24128
    • Mannick, J.B.1    Miao, X.Q.2    Stamler, J.S.3
  • 49
    • 0028892235 scopus 로고
    • Inhibition of vaccinia virus DNA replication by inducible expression of nitric oxide synthase
    • Melkova, Z., and Esteban, M. (1995). Inhibition of vaccinia virus DNA replication by inducible expression of nitric oxide synthase. J. Immunol. 155, 5711-5718.
    • (1995) J. Immunol. , vol.155 , pp. 5711-5718
    • Melkova, Z.1    Esteban, M.2
  • 51
    • 0027416762 scopus 로고
    • Site-directed mutagenesis of the putative active site residues of 3C proteinase of coxsackievirus B3: Evidence of a functional relationship with trypsin-like serine proteinases
    • Miyashita, K., Kusumi, M., Utsumi, R., Katayama, S., Noda, M., Komano, T., and Satoh, N. (1993). Site-directed mutagenesis of the putative active site residues of 3C proteinase of coxsackievirus B3: Evidence of a functional relationship with trypsin-like serine proteinases. Protein. Eng. 6, 189-193.
    • (1993) Protein. Eng. , vol.6 , pp. 189-193
    • Miyashita, K.1    Kusumi, M.2    Utsumi, R.3    Katayama, S.4    Noda, M.5    Komano, T.6    Satoh, N.7
  • 52
    • 0031577534 scopus 로고    scopus 로고
    • Inhibition of caspase-3 by S-nitrosation and oxidation caused by nitric oxide
    • Mohr, S., Zech, B., Lapetina, E.G., and Brune, B. (1997). Inhibition of caspase-3 by S-nitrosation and oxidation caused by nitric oxide. Biochem. Biophys. Res. Commun. 238, 387-391.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 387-391
    • Mohr, S.1    Zech, B.2    Lapetina, E.G.3    Brune, B.4
  • 53
    • 0029889570 scopus 로고    scopus 로고
    • Substitution of cysteine 192 in a highly conserved streptococcus pyogenes extracellular cysteine protease (interleukin 1beta convertase) alters proteolytic activity and ablates zymogen processing
    • Musser, J.M., Stockbauer, K., Kapur, V., and Rudgers, G.W. (1996). Substitution of cysteine 192 in a highly conserved streptococcus pyogenes extracellular cysteine protease (interleukin 1beta convertase) alters proteolytic activity and ablates zymogen processing. Infect. Immun. 64, 1913-1917.
    • (1996) Infect. Immun. , vol.64 , pp. 1913-1917
    • Musser, J.M.1    Stockbauer, K.2    Kapur, V.3    Rudgers, G.W.4
  • 54
    • 0024468899 scopus 로고
    • Hydrolysis of a series of synthetic peptide substrates by the human rhinovirus 14 3C proteinase, cloned and expressed in Escherichia coli
    • Orr, D.C., Long, A.C., Kay, J., Dunn, B.M., and Cameron, J.M. (1989). Hydrolysis of a series of synthetic peptide substrates by the human rhinovirus 14 3C proteinase, cloned and expressed in Escherichia coli. J. Gen. Virol. 70, 2931-2942.
    • (1989) J. Gen. Virol. , vol.70 , pp. 2931-2942
    • Orr, D.C.1    Long, A.C.2    Kay, J.3    Dunn, B.M.4    Cameron, J.M.5
  • 55
    • 0025011840 scopus 로고
    • Proteolytic processing of picornaviral polyprotein
    • Palmberg, A. (1990). Proteolytic processing of picornaviral polyprotein. Annu. Rev. Microbiol. 44, 603-623.
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 603-623
    • Palmberg, A.1
  • 56
    • 0031903001 scopus 로고    scopus 로고
    • Does nitric oxide play a critical role in viral infections
    • Reiss, C.S., and Komatsu, T. (1998). Does nitric oxide play a critical role in viral infections? J. Virol. 72, 4547-4551.
    • (1998) J. Virol. , vol.72 , pp. 4547-4551
    • Reiss, C.S.1    Komatsu, T.2
  • 57
    • 0029985795 scopus 로고    scopus 로고
    • Nitric oxide production is increased during murine vaccinia virus infection, but may not be essential for virus clearance
    • Rolph, M.S., Ramshaw, I.A., Rockett, K.A., Ruby, J., and Cowden, W.B. (1996). Nitric oxide production is increased during murine vaccinia virus infection, but may not be essential for virus clearance. Virology 217, 470-477.
    • (1996) Virology , vol.217 , pp. 470-477
    • Rolph, M.S.1    Ramshaw, I.A.2    Rockett, K.A.3    Ruby, J.4    Cowden, W.B.5
  • 58
    • 37049066149 scopus 로고
    • A scheme for the colorimetric determination of microgram amounts of thiols
    • Saville, B. (1958). A scheme for the colorimetric determination of microgram amounts of thiols. Analyst 83, 670-672.
    • (1958) Analyst , vol.83 , pp. 670-672
    • Saville, B.1
  • 60
    • 0028132836 scopus 로고
    • Redox signaling: Nitrosylation and related target interactions of nitric oxide
    • Stamler, J.S. (1994). Redox signaling: Nitrosylation and related target interactions of nitric oxide. Cell 78, 931-936.
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 62
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • Stamler, J.S., Singel, D.J., and Loscalzo, J. (1992b). Biochemistry of nitric oxide and its redox-activated forms. Science 258, 1898-1902.
    • (1992) Science , vol.258 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 63
    • 0030956929 scopus 로고    scopus 로고
    • (S)NO signals: Translocation, regulation, and a consensus motif
    • Stamler, J.S., Toone, E.J., Lipton, S.A., and Sucher, N.J. (1997). (S)NO signals: Translocation, regulation, and a consensus motif. Neuron 18, 691-696.
    • (1997) Neuron , vol.18 , pp. 691-696
    • Stamler, J.S.1    Toone, E.J.2    Lipton, S.A.3    Sucher, N.J.4
  • 65
    • 0030029769 scopus 로고    scopus 로고
    • Inhibition of nitric oxide synthesis increases mortality in Sindbis virus encephalitis
    • Tucker, P.C., Griffin, D.E., Choi, S., Bui, N., and Wesselingh, S. (1996). Inhibition of nitric oxide synthesis increases mortality in Sindbis virus encephalitis. J. Virol. 70, 3972-3977.
    • (1996) J. Virol. , vol.70 , pp. 3972-3977
    • Tucker, P.C.1    Griffin, D.E.2    Choi, S.3    Bui, N.4    Wesselingh, S.5
  • 66
    • 0028797229 scopus 로고
    • Appearance of inducible nitric oxide synthase in the rat central nervous system after rabies virus infection and during experimental allergic encephalomyelitis but not after peripheral administration of endotoxin
    • Van Dam, A.M., Bauer, J., Man-A-Hing, W.K., Marquette, C., Tilders, F.J., and Berkenbosch, F. (1995). Appearance of inducible nitric oxide synthase in the rat central nervous system after rabies virus infection and during experimental allergic encephalomyelitis but not after peripheral administration of endotoxin. J. Neurosci. Res. 40, 251-260.
    • (1995) J. Neurosci. Res. , vol.40 , pp. 251-260
    • Van Dam, A.M.1    Bauer, J.2    Man-A-Hing, W.K.3    Marquette, C.4    Tilders, F.J.5    Berkenbosch, F.6
  • 67
    • 0030607410 scopus 로고    scopus 로고
    • Cysteine protease inhibitors block schistosome hemoglobin degradation in vitro and decrease worm burden and egg production in vivo
    • Wasilewski, M.M., Lim, K.C., Phillips, J., and McKerrow, J.H. (1996). Cysteine protease inhibitors block schistosome hemoglobin degradation in vitro and decrease worm burden and egg production in vivo. Mol. Biochem. Parasitol. 81, 179-189.
    • (1996) Mol. Biochem. Parasitol. , vol.81 , pp. 179-189
    • Wasilewski, M.M.1    Lim, K.C.2    Phillips, J.3    McKerrow, J.H.4
  • 70
    • 0029893843 scopus 로고    scopus 로고
    • Nitrosation of tryptophan residue(s) in serumalbumion and model dipeptides
    • Zhang, Y., Xu, A., Nomen, M., Walsh, M., Keaney, J.F., and Loscalzo, J. (1996). Nitrosation of tryptophan residue(s) in serumalbumion and model dipeptides. J. Biol. Chem. 271, 14271-14279.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14271-14279
    • Zhang, Y.1    Xu, A.2    Nomen, M.3    Walsh, M.4    Keaney, J.F.5    Loscalzo, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.