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Volumn 27, Issue 7, 2019, Pages 2092-2104.e10

Guanylate-Binding Proteins 2 and 5 Exert Broad Antiviral Activity by Inhibiting Furin-Mediated Processing of Viral Envelope Proteins

(21)  Braun, Elisabeth a   Hotter, Dominik a   Koepke, Lennart a   Zech, Fabian a   Groß, Rüdiger a   Sparrer, Konstantin M J a   Müller, Janis A a   Pfaller, Christian K b   Heusinger, Elena a   Wombacher, Rebecka c   Sutter, Kathrin d   Dittmer, Ulf d   Winkler, Michael e   Simmons, Graham f   Jakobsen, Martin R g   Conzelmann, Karl Klaus h   Pöhlmann, Stefan e,i   Münch, Jan a   Fackler, Oliver T c,j   Kirchhoff, Frank a   more..


Author keywords

furin; GBPs; HIV; influenza A virus; measles virus; restriction factor; viral envelope proteins; Zika virus

Indexed keywords

FURIN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 160; GLYCOPROTEIN GP 41; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANYLATE BINDING PROTEIN 2; GUANYLATE BINDING PROTEIN 5; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; FURIN PROTEIN, HUMAN; GBP2 PROTEIN, HUMAN; GBP5 PROTEIN, HUMAN; GP120 PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; GP41 PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 85065235566     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2019.04.063     Document Type: Article
Times cited : (110)

References (80)
  • 1
    • 84999006511 scopus 로고    scopus 로고
    • Gene therapy with plasmids encoding IFN-β or IFN-α14 confers long-term resistance to HIV-1 in humanized mice
    • Abraham, S., Choi, J.-G., Ortega, N.M., Zhang, J., Shankar, P., Swamy, N.M., Gene therapy with plasmids encoding IFN-β or IFN-α14 confers long-term resistance to HIV-1 in humanized mice. Oncotarget 7 (2016), 78412–78420.
    • (2016) Oncotarget , vol.7 , pp. 78412-78420
    • Abraham, S.1    Choi, J.-G.2    Ortega, N.M.3    Zhang, J.4    Shankar, P.5    Swamy, N.M.6
  • 2
    • 0033616531 scopus 로고    scopus 로고
    • Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus
    • Anderson, S.L., Carton, J.M., Lou, J., Xing, L., Rubin, B.Y., Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus. Virology 256 (1999), 8–14.
    • (1999) Virology , vol.256 , pp. 8-14
    • Anderson, S.L.1    Carton, J.M.2    Lou, J.3    Xing, L.4    Rubin, B.Y.5
  • 3
    • 27644521904 scopus 로고    scopus 로고
    • Proprotein convertases: “master switches” in the regulation of tumor growth and progression
    • Bassi, D.E., Fu, J., Lopez de Cicco, R., Klein-Szanto, A.J.P., Proprotein convertases: “master switches” in the regulation of tumor growth and progression. Mol. Carcinog. 44 (2005), 151–161.
    • (2005) Mol. Carcinog. , vol.44 , pp. 151-161
    • Bassi, D.E.1    Fu, J.2    Lopez de Cicco, R.3    Klein-Szanto, A.J.P.4
  • 5
    • 84925321826 scopus 로고    scopus 로고
    • Processing by convertases is required for glypican-3-induced inhibition of Hedgehog signaling
    • Capurro, M., Shi, W., Izumikawa, T., Kitagawa, H., Filmus, J., Processing by convertases is required for glypican-3-induced inhibition of Hedgehog signaling. J. Biol. Chem. 290 (2015), 7576–7585.
    • (2015) J. Biol. Chem. , vol.290 , pp. 7576-7585
    • Capurro, M.1    Shi, W.2    Izumikawa, T.3    Kitagawa, H.4    Filmus, J.5
  • 6
    • 0020955866 scopus 로고
    • Interferon induction of fibroblast proteins with guanylate binding activity
    • Cheng, Y.S., Colonno, R.J., Yin, F.H., Interferon induction of fibroblast proteins with guanylate binding activity. J. Biol. Chem. 258 (1983), 7746–7750.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7746-7750
    • Cheng, Y.S.1    Colonno, R.J.2    Yin, F.H.3
  • 7
    • 0028302998 scopus 로고
    • Optimal infectivity in vitro of human immunodeficiency virus type 1 requires an intact nef gene
    • Chowers, M.Y., Spina, C.A., Kwoh, T.J., Fitch, N.J., Richman, D.D., Guatelli, J.C., Optimal infectivity in vitro of human immunodeficiency virus type 1 requires an intact nef gene. J. Virol. 68 (1994), 2906–2914.
    • (1994) J. Virol. , vol.68 , pp. 2906-2914
    • Chowers, M.Y.1    Spina, C.A.2    Kwoh, T.J.3    Fitch, N.J.4    Richman, D.D.5    Guatelli, J.C.6
  • 9
    • 0028842207 scopus 로고
    • Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes
    • Connor, R.I., Chen, B.K., Choe, S., Landau, N.R., Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes. Virology 206 (1995), 935–944.
    • (1995) Virology , vol.206 , pp. 935-944
    • Connor, R.I.1    Chen, B.K.2    Choe, S.3    Landau, N.R.4
  • 10
    • 41649118952 scopus 로고    scopus 로고
    • A small-molecule furin inhibitor inhibits cancer cell motility and invasiveness
    • Coppola, J.M., Bhojani, M.S., Ross, B.D., Rehemtulla, A., A small-molecule furin inhibitor inhibits cancer cell motility and invasiveness. Neoplasia 10 (2008), 363–370.
    • (2008) Neoplasia , vol.10 , pp. 363-370
    • Coppola, J.M.1    Bhojani, M.S.2    Ross, B.D.3    Rehemtulla, A.4
  • 11
    • 0033493228 scopus 로고    scopus 로고
    • Browsing protein families via the “Rich Family Description” format
    • Corpet, F., Gouzy, J., Kahn, D., Browsing protein families via the “Rich Family Description” format. Bioinforma. Oxf. Engl. 15 (1999), 1020–1027.
    • (1999) Bioinforma. Oxf. Engl. , vol.15 , pp. 1020-1027
    • Corpet, F.1    Gouzy, J.2    Kahn, D.3
  • 13
    • 0024449635 scopus 로고
    • Interactions of alpha- and gamma-interferon in the transcriptional regulation of the gene encoding a guanylate-binding protein
    • Decker, T., Lew, D.J., Cheng, Y.S., Levy, D.E., Darnell, J.E. Jr., Interactions of alpha- and gamma-interferon in the transcriptional regulation of the gene encoding a guanylate-binding protein. EMBO J. 8 (1989), 2009–2014.
    • (1989) EMBO J. , vol.8 , pp. 2009-2014
    • Decker, T.1    Lew, D.J.2    Cheng, Y.S.3    Levy, D.E.4    Darnell, J.E.5
  • 14
    • 0030997527 scopus 로고    scopus 로고
    • Comparative functional role of PC7 and furin in the processing of the HIV envelope glycoprotein gp160
    • Decroly, E., Benjannet, S., Savaria, D., Seidah, N.G., Comparative functional role of PC7 and furin in the processing of the HIV envelope glycoprotein gp160. FEBS Lett. 405 (1997), 68–72.
    • (1997) FEBS Lett. , vol.405 , pp. 68-72
    • Decroly, E.1    Benjannet, S.2    Savaria, D.3    Seidah, N.G.4
  • 15
    • 34648833266 scopus 로고    scopus 로고
    • A vectored measles virus induces hepatitis B surface antigen antibodies while protecting macaques against measles virus challenge
    • del Valle, J.R., Devaux, P., Hodge, G., Wegner, N.J., McChesney, M.B., Cattaneo, R., A vectored measles virus induces hepatitis B surface antigen antibodies while protecting macaques against measles virus challenge. J. Virol. 81 (2007), 10597–10605.
    • (2007) J. Virol. , vol.81 , pp. 10597-10605
    • del Valle, J.R.1    Devaux, P.2    Hodge, G.3    Wegner, N.J.4    McChesney, M.B.5    Cattaneo, R.6
  • 16
  • 17
    • 0029015314 scopus 로고
    • Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: requirement of precursor cleavage for glycoprotein incorporation
    • Dubay, J.W., Dubay, S.R., Shin, H.J., Hunter, E., Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: requirement of precursor cleavage for glycoprotein incorporation. J. Virol. 69 (1995), 4675–4682.
    • (1995) J. Virol. , vol.69 , pp. 4675-4682
    • Dubay, J.W.1    Dubay, S.R.2    Shin, H.J.3    Hunter, E.4
  • 18
  • 19
    • 0842313260 scopus 로고    scopus 로고
    • Prediction of proprotein convertase cleavage sites
    • Duckert, P., Brunak, S., Blom, N., Prediction of proprotein convertase cleavage sites. Protein Eng. Des. Sel. 17 (2004), 107–112.
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 107-112
    • Duckert, P.1    Brunak, S.2    Blom, N.3
  • 20
    • 60749114487 scopus 로고    scopus 로고
    • Comparative analysis of HIV-1-based lentiviral vectors bearing lyssavirus glycoproteins for neuronal gene transfer
    • Federici, T., Kutner, R., Zhang, X.-Y., Kuroda, H., Tordo, N., Boulis, N.M., Reiser, J., Comparative analysis of HIV-1-based lentiviral vectors bearing lyssavirus glycoproteins for neuronal gene transfer. Genet. Vaccines Ther., 7, 2009, 1.
    • (2009) Genet. Vaccines Ther. , vol.7 , pp. 1
    • Federici, T.1    Kutner, R.2    Zhang, X.-Y.3    Kuroda, H.4    Tordo, N.5    Boulis, N.M.6    Reiser, J.7
  • 22
    • 0030747461 scopus 로고    scopus 로고
    • HIV-1 infection of non-dividing cells: evidence that the amino-terminal basic region of the viral matrix protein is important for Gag processing but not for post-entry nuclear import
    • Fouchier, R.A., Meyer, B.E., Simon, J.H., Fischer, U., Malim, M.H., HIV-1 infection of non-dividing cells: evidence that the amino-terminal basic region of the viral matrix protein is important for Gag processing but not for post-entry nuclear import. EMBO J. 16 (1997), 4531–4539.
    • (1997) EMBO J. , vol.16 , pp. 4531-4539
    • Fouchier, R.A.1    Meyer, B.E.2    Simon, J.H.3    Fischer, U.4    Malim, M.H.5
  • 25
    • 0028074306 scopus 로고
    • Processing of viral glycoproteins by the subtilisin-like endoprotease furin and its inhibition by specific peptidylchloroalkylketones
    • Garten, W., Hallenberger, S., Ortmann, D., Schäfer, W., Vey, M., Angliker, H., Shaw, E., Klenk, H.D., Processing of viral glycoproteins by the subtilisin-like endoprotease furin and its inhibition by specific peptidylchloroalkylketones. Biochimie 76 (1994), 217–225.
    • (1994) Biochimie , vol.76 , pp. 217-225
    • Garten, W.1    Hallenberger, S.2    Ortmann, D.3    Schäfer, W.4    Vey, M.5    Angliker, H.6    Shaw, E.7    Klenk, H.D.8
  • 26
    • 84855974393 scopus 로고    scopus 로고
    • Significantly improved rescue of rabies virus from cDNA plasmids
    • Ghanem, A., Kern, A., Conzelmann, K.-K., Significantly improved rescue of rabies virus from cDNA plasmids. Eur. J. Cell Biol. 91 (2012), 10–16.
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 10-16
    • Ghanem, A.1    Kern, A.2    Conzelmann, K.-K.3
  • 27
    • 0029897676 scopus 로고    scopus 로고
    • Autocrine activation by interferon-gamma of STAT factors following T cell activation
    • Girdlestone, J., Wing, M., Autocrine activation by interferon-gamma of STAT factors following T cell activation. Eur. J. Immunol. 26 (1996), 704–709.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 704-709
    • Girdlestone, J.1    Wing, M.2
  • 28
    • 0028872463 scopus 로고
    • Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases
    • Gordon, V.M., Klimpel, K.R., Arora, N., Henderson, M.A., Leppla, S.H., Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases. Infect. Immun. 63 (1995), 82–87.
    • (1995) Infect. Immun. , vol.63 , pp. 82-87
    • Gordon, V.M.1    Klimpel, K.R.2    Arora, N.3    Henderson, M.A.4    Leppla, S.H.5
  • 29
    • 84925410974 scopus 로고    scopus 로고
    • Mx GTPases: dynamin-like antiviral machines of innate immunity
    • Haller, O., Staeheli, P., Schwemmle, M., Kochs, G., Mx GTPases: dynamin-like antiviral machines of innate immunity. Trends Microbiol. 23 (2015), 154–163.
    • (2015) Trends Microbiol. , vol.23 , pp. 154-163
    • Haller, O.1    Staeheli, P.2    Schwemmle, M.3    Kochs, G.4
  • 31
    • 85053561876 scopus 로고    scopus 로고
    • Proteolytic activation of flavivirus envelope proteins
    • E. Böttcher-Friebertshäuser W. Garten H.D. Klenk Springer
    • Heinz, F.X., Stiasny, K., Proteolytic activation of flavivirus envelope proteins. Böttcher-Friebertshäuser, E., Garten, W., Klenk, H.D., (eds.) Activation of Viruses by Host Proteases, 2018, Springer, 109–132.
    • (2018) Activation of Viruses by Host Proteases , pp. 109-132
    • Heinz, F.X.1    Stiasny, K.2
  • 32
    • 0028095251 scopus 로고
    • Proprotein-processing endoproteases PC6 and furin both activate hemagglutinin of virulent avian influenza viruses
    • Horimoto, T., Nakayama, K., Smeekens, S.P., Kawaoka, Y., Proprotein-processing endoproteases PC6 and furin both activate hemagglutinin of virulent avian influenza viruses. J. Virol. 68 (1994), 6074–6078.
    • (1994) J. Virol. , vol.68 , pp. 6074-6078
    • Horimoto, T.1    Nakayama, K.2    Smeekens, S.P.3    Kawaoka, Y.4
  • 33
    • 84976319552 scopus 로고    scopus 로고
    • Guanylate binding protein 5: Impairing virion infectivity by targeting retroviral envelope glycoproteins
    • Hotter, D., Sauter, D., Kirchhoff, F., Guanylate binding protein 5: Impairing virion infectivity by targeting retroviral envelope glycoproteins. Small GTPases 8 (2017), 31–37.
    • (2017) Small GTPases , vol.8 , pp. 31-37
    • Hotter, D.1    Sauter, D.2    Kirchhoff, F.3
  • 36
    • 68649097790 scopus 로고    scopus 로고
    • Glypican-3: a novel diagnostic marker for hepatocellular carcinoma and more
    • Kandil, D.H., Cooper, K., Glypican-3: a novel diagnostic marker for hepatocellular carcinoma and more. Adv. Anat. Pathol. 16 (2009), 125–129.
    • (2009) Adv. Anat. Pathol. , vol.16 , pp. 125-129
    • Kandil, D.H.1    Cooper, K.2
  • 38
    • 85020131888 scopus 로고    scopus 로고
    • Proprotein convertase inhibition: Paralyzing the cell's master switches
    • Klein-Szanto, A.J., Bassi, D.E., Proprotein convertase inhibition: Paralyzing the cell's master switches. Biochem. Pharmacol. 140 (2017), 8–15.
    • (2017) Biochem. Pharmacol. , vol.140 , pp. 8-15
    • Klein-Szanto, A.J.1    Bassi, D.E.2
  • 40
    • 0029941479 scopus 로고    scopus 로고
    • Purification and enzymatic characterization of recombinant prohormone convertase 2: stabilization of activity by 21 kDa 7B2
    • Lamango, N.S., Zhu, X., Lindberg, I., Purification and enzymatic characterization of recombinant prohormone convertase 2: stabilization of activity by 21 kDa 7B2. Arch. Biochem. Biophys. 330 (1996), 238–250.
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 238-250
    • Lamango, N.S.1    Zhu, X.2    Lindberg, I.3
  • 42
    • 0035940409 scopus 로고    scopus 로고
    • The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P
    • Lenz, O., ter Meulen, J., Klenk, H.D., Seidah, N.G., Garten, W., The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P. Proc. Natl. Acad. Sci. USA 98 (2001), 12701–12705.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12701-12705
    • Lenz, O.1    ter Meulen, J.2    Klenk, H.D.3    Seidah, N.G.4    Garten, W.5
  • 43
    • 0026069531 scopus 로고
    • Overlapping elements in the guanylate-binding protein gene promoter mediate transcriptional induction by alpha and gamma interferons
    • Lew, D.J., Decker, T., Strehlow, I., Darnell, J.E., Overlapping elements in the guanylate-binding protein gene promoter mediate transcriptional induction by alpha and gamma interferons. Mol. Cell. Biol. 11 (1991), 182–191.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 182-191
    • Lew, D.J.1    Decker, T.2    Strehlow, I.3    Darnell, J.E.4
  • 44
    • 0034634728 scopus 로고    scopus 로고
    • Maturation of HIV envelope glycoprotein precursors by cellular endoproteases
    • Moulard, M., Decroly, E., Maturation of HIV envelope glycoprotein precursors by cellular endoproteases. Biochim. Biophys. Acta 1469 (2000), 121–132.
    • (2000) Biochim. Biophys. Acta , vol.1469 , pp. 121-132
    • Moulard, M.1    Decroly, E.2
  • 45
    • 26244439665 scopus 로고    scopus 로고
    • The role of upstream U3 sequences in HIV-1 replication and CD4+ T cell depletion in human lymphoid tissue ex vivo
    • Münch, J., Rajan, D., Rücker, E., Wildum, S., Adam, N., Kirchhoff, F., The role of upstream U3 sequences in HIV-1 replication and CD4+ T cell depletion in human lymphoid tissue ex vivo. Virology 341 (2005), 313–320.
    • (2005) Virology , vol.341 , pp. 313-320
    • Münch, J.1    Rajan, D.2    Rücker, E.3    Wildum, S.4    Adam, N.5    Kirchhoff, F.6
  • 47
    • 84857732857 scopus 로고    scopus 로고
    • A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication
    • Nordmann, A., Wixler, L., Boergeling, Y., Wixler, V., Ludwig, S., A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication. FASEB J. 26 (2012), 1290–1300.
    • (2012) FASEB J. , vol.26 , pp. 1290-1300
    • Nordmann, A.1    Wixler, L.2    Boergeling, Y.3    Wixler, V.4    Ludwig, S.5
  • 48
    • 84857830668 scopus 로고    scopus 로고
    • Generation of transmitted/founder HIV-1 infectious molecular clones and characterization of their replication capacity in CD4 T lymphocytes and monocyte-derived macrophages
    • Ochsenbauer, C., Edmonds, T.G., Ding, H., Keele, B.F., Decker, J., Salazar, M.G., Salazar-Gonzalez, J.F., Shattock, R., Haynes, B.F., Shaw, G.M., et al. Generation of transmitted/founder HIV-1 infectious molecular clones and characterization of their replication capacity in CD4 T lymphocytes and monocyte-derived macrophages. J. Virol. 86 (2012), 2715–2728.
    • (2012) J. Virol. , vol.86 , pp. 2715-2728
    • Ochsenbauer, C.1    Edmonds, T.G.2    Ding, H.3    Keele, B.F.4    Decker, J.5    Salazar, M.G.6    Salazar-Gonzalez, J.F.7    Shattock, R.8    Haynes, B.F.9    Shaw, G.M.10
  • 49
    • 33744463639 scopus 로고    scopus 로고
    • In silico genomic analysis of the human and murine guanylate-binding protein (GBP) gene clusters
    • Olszewski, M.A., Gray, J., Vestal, D.J., In silico genomic analysis of the human and murine guanylate-binding protein (GBP) gene clusters. J. Interferon Cytokine Res. 26 (2006), 328–352.
    • (2006) J. Interferon Cytokine Res. , vol.26 , pp. 328-352
    • Olszewski, M.A.1    Gray, J.2    Vestal, D.J.3
  • 51
    • 0035868365 scopus 로고    scopus 로고
    • ‘Shed’ furin: mapping of the cleavage determinants and identification of its C-terminus
    • Plaimauer, B., Mohr, G., Wernhart, W., Himmelspach, M., Dorner, F., Schlokat, U., ‘Shed’ furin: mapping of the cleavage determinants and identification of its C-terminus. Biochem. J. 354 (2001), 689–695.
    • (2001) Biochem. J. , vol.354 , pp. 689-695
    • Plaimauer, B.1    Mohr, G.2    Wernhart, W.3    Himmelspach, M.4    Dorner, F.5    Schlokat, U.6
  • 52
    • 0031954686 scopus 로고    scopus 로고
    • Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1
    • Platt, E.J., Wehrly, K., Kuhmann, S.E., Chesebro, B., Kabat, D., Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1. J. Virol. 72 (1998), 2855–2864.
    • (1998) J. Virol. , vol.72 , pp. 2855-2864
    • Platt, E.J.1    Wehrly, K.2    Kuhmann, S.E.3    Chesebro, B.4    Kabat, D.5
  • 53
    • 79952616582 scopus 로고    scopus 로고
    • Hepatitis C virus-induced furin and thrombospondin-1 activate TGF-β1: role of TGF-β1 in HCV replication
    • Presser, L.D., Haskett, A., Waris, G., Hepatitis C virus-induced furin and thrombospondin-1 activate TGF-β1: role of TGF-β1 in HCV replication. Virology 412 (2011), 284–296.
    • (2011) Virology , vol.412 , pp. 284-296
    • Presser, L.D.1    Haskett, A.2    Waris, G.3
  • 55
    • 84931281975 scopus 로고    scopus 로고
    • Generation of a variety of stable Influenza A reporter viruses by genetic engineering of the NS gene segment
    • Reuther, P., Göpfert, K., Dudek, A.H., Heiner, M., Herold, S., Schwemmle, M., Generation of a variety of stable Influenza A reporter viruses by genetic engineering of the NS gene segment. Sci. Rep., 5, 2015, 11346.
    • (2015) Sci. Rep. , vol.5 , pp. 11346
    • Reuther, P.1    Göpfert, K.2    Dudek, A.H.3    Heiner, M.4    Herold, S.5    Schwemmle, M.6
  • 56
    • 78951472912 scopus 로고    scopus 로고
    • The proprotein convertase PC7: unique zymogen activation and trafficking pathways
    • Rousselet, E., Benjannet, S., Hamelin, J., Canuel, M., Seidah, N.G., The proprotein convertase PC7: unique zymogen activation and trafficking pathways. J. Biol. Chem. 286 (2011), 2728–2738.
    • (2011) J. Biol. Chem. , vol.286 , pp. 2728-2738
    • Rousselet, E.1    Benjannet, S.2    Hamelin, J.3    Canuel, M.4    Seidah, N.G.5
  • 57
    • 84876071883 scopus 로고    scopus 로고
    • Control of porcine reproductive and respiratory syndrome (PRRS) through genetic improvements in disease resistance and tolerance
    • Rowland, R.R.R., Lunney, J., Dekkers, J., Control of porcine reproductive and respiratory syndrome (PRRS) through genetic improvements in disease resistance and tolerance. Front. Genet., 3, 2012, 260.
    • (2012) Front. Genet. , vol.3 , pp. 260
    • Rowland, R.R.R.1    Lunney, J.2    Dekkers, J.3
  • 60
    • 0030577022 scopus 로고    scopus 로고
    • Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2
    • Sato, H., Kinoshita, T., Takino, T., Nakayama, K., Seiki, M., Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2. FEBS Lett. 393 (1996), 101–104.
    • (1996) FEBS Lett. , vol.393 , pp. 101-104
    • Sato, H.1    Kinoshita, T.2    Takino, T.3    Nakayama, K.4    Seiki, M.5
  • 61
    • 84935012627 scopus 로고    scopus 로고
    • In Silico Prediction and Experimental Confirmation of HA Residues Conferring Enhanced Human Receptor Specificity of H5N1 Influenza A Viruses
    • Schmier, S., Mostafa, A., Haarmann, T., Bannert, N., Ziebuhr, J., Veljkovic, V., Dietrich, U., Pleschka, S., In Silico Prediction and Experimental Confirmation of HA Residues Conferring Enhanced Human Receptor Specificity of H5N1 Influenza A Viruses. Sci. Rep., 5, 2015, 11434.
    • (2015) Sci. Rep. , vol.5 , pp. 11434
    • Schmier, S.1    Mostafa, A.2    Haarmann, T.3    Bannert, N.4    Ziebuhr, J.5    Veljkovic, V.6    Dietrich, U.7    Pleschka, S.8
  • 62
    • 0026742108 scopus 로고
    • Proprotein and prohormone convertases of the subtilisin family Recent developments and future perspectives
    • Seidah, N.G., Chrétien, M., Proprotein and prohormone convertases of the subtilisin family Recent developments and future perspectives. Trends Endocrinol. Metab. 3 (1992), 133–140.
    • (1992) Trends Endocrinol. Metab. , vol.3 , pp. 133-140
    • Seidah, N.G.1    Chrétien, M.2
  • 63
    • 84860383419 scopus 로고    scopus 로고
    • The biology and therapeutic targeting of the proprotein convertases
    • Seidah, N.G., Prat, A., The biology and therapeutic targeting of the proprotein convertases. Nat. Rev. Drug Discov. 11 (2012), 367–383.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 367-383
    • Seidah, N.G.1    Prat, A.2
  • 64
    • 0030128742 scopus 로고    scopus 로고
    • Survey of the hemagglutinin (HA) cleavage site sequence of H5 and H7 avian influenza viruses: amino acid sequence at the HA cleavage site as a marker of pathogenicity potential
    • Senne, D.A., Panigrahy, B., Kawaoka, Y., Pearson, J.E., Süss, J., Lipkind, M., Kida, H., Webster, R.G., Survey of the hemagglutinin (HA) cleavage site sequence of H5 and H7 avian influenza viruses: amino acid sequence at the HA cleavage site as a marker of pathogenicity potential. Avian Dis. 40 (1996), 425–437.
    • (1996) Avian Dis. , vol.40 , pp. 425-437
    • Senne, D.A.1    Panigrahy, B.2    Kawaoka, Y.3    Pearson, J.E.4    Süss, J.5    Lipkind, M.6    Kida, H.7    Webster, R.G.8
  • 66
  • 67
    • 0021220522 scopus 로고
    • Genetic control of interferon action: mouse strain distribution and inheritance of an induced protein with guanylate-binding property
    • Staeheli, P., Prochazka, M., Steigmeier, P.A., Haller, O., Genetic control of interferon action: mouse strain distribution and inheritance of an induced protein with guanylate-binding property. Virology 137 (1984), 135–142.
    • (1984) Virology , vol.137 , pp. 135-142
    • Staeheli, P.1    Prochazka, M.2    Steigmeier, P.A.3    Haller, O.4
  • 68
    • 0026643396 scopus 로고
    • Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease
    • Stieneke-Gröber, A., Vey, M., Angliker, H., Shaw, E., Thomas, G., Roberts, C., Klenk, H.D., Garten, W., Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J. 11 (1992), 2407–2414.
    • (1992) EMBO J. , vol.11 , pp. 2407-2414
    • Stieneke-Gröber, A.1    Vey, M.2    Angliker, H.3    Shaw, E.4    Thomas, G.5    Roberts, C.6    Klenk, H.D.7    Garten, W.8
  • 69
    • 44449092149 scopus 로고    scopus 로고
    • Molecular architecture of the bipartite fusion loops of vesicular stomatitis virus glycoprotein G, a class III viral fusion protein
    • Sun, X., Belouzard, S., Whittaker, G.R., Molecular architecture of the bipartite fusion loops of vesicular stomatitis virus glycoprotein G, a class III viral fusion protein. J. Biol. Chem. 283 (2008), 6418–6427.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6418-6427
    • Sun, X.1    Belouzard, S.2    Whittaker, G.R.3
  • 70
    • 33846022325 scopus 로고    scopus 로고
    • Analysis of furin ectodomain shedding in epididymal fluid of mammals: demonstration that shedding of furin occurs in vivo
    • Thimon, V., Belghazi, M., Dacheux, J.-L., Gatti, J.-L., Analysis of furin ectodomain shedding in epididymal fluid of mammals: demonstration that shedding of furin occurs in vivo. Reproduction 132 (2006), 899–908.
    • (2006) Reproduction , vol.132 , pp. 899-908
    • Thimon, V.1    Belghazi, M.2    Dacheux, J.-L.3    Gatti, J.-L.4
  • 71
    • 79952257801 scopus 로고    scopus 로고
    • FurinDB: A database of 20-residue furin cleavage site motifs, substrates and their associated drugs
    • Tian, S., Huang, Q., Fang, Y., Wu, J., FurinDB: A database of 20-residue furin cleavage site motifs, substrates and their associated drugs. Int. J. Mol. Sci. 12 (2011), 1060–1065.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 1060-1065
    • Tian, S.1    Huang, Q.2    Fang, Y.3    Wu, J.4
  • 73
    • 78651514940 scopus 로고    scopus 로고
    • The guanylate-binding proteins: emerging insights into the biochemical properties and functions of this family of large interferon-induced guanosine triphosphatase
    • Vestal, D.J., Jeyaratnam, J.A., The guanylate-binding proteins: emerging insights into the biochemical properties and functions of this family of large interferon-induced guanosine triphosphatase. J. Interferon Cytokine Res. 31 (2011), 89–97.
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 89-97
    • Vestal, D.J.1    Jeyaratnam, J.A.2
  • 74
    • 0034701943 scopus 로고    scopus 로고
    • Mutational analysis of the GPC3/GPC4 glypican gene cluster on Xq26 in patients with Simpson-Golabi-Behmel syndrome: identification of loss-of-function mutations in the GPC3 gene
    • Veugelers, M., Cat, B.D., Muyldermans, S.Y., Reekmans, G., Delande, N., Frints, S., Legius, E., Fryns, J.P., Schrander-Stumpel, C., Weidle, B., et al. Mutational analysis of the GPC3/GPC4 glypican gene cluster on Xq26 in patients with Simpson-Golabi-Behmel syndrome: identification of loss-of-function mutations in the GPC3 gene. Hum. Mol. Genet. 9 (2000), 1321–1328.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1321-1328
    • Veugelers, M.1    Cat, B.D.2    Muyldermans, S.Y.3    Reekmans, G.4    Delande, N.5    Frints, S.6    Legius, E.7    Fryns, J.P.8    Schrander-Stumpel, C.9    Weidle, B.10
  • 76
    • 0029868289 scopus 로고    scopus 로고
    • Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases
    • Vollenweider, F., Benjannet, S., Decroly, E., Savaria, D., Lazure, C., Thomas, G., Chrétien, M., Seidah, N.G., Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases. Biochem. J. 314 (1996), 521–532.
    • (1996) Biochem. J. , vol.314 , pp. 521-532
    • Vollenweider, F.1    Benjannet, S.2    Decroly, E.3    Savaria, D.4    Lazure, C.5    Thomas, G.6    Chrétien, M.7    Seidah, N.G.8
  • 77
    • 77951060977 scopus 로고    scopus 로고
    • Establishment and application of an infectious virus-like particle system for Marburg virus
    • Wenigenrath, J., Kolesnikova, L., Hoenen, T., Mittler, E., Becker, S., Establishment and application of an infectious virus-like particle system for Marburg virus. J. Gen. Virol. 91 (2010), 1325–1334.
    • (2010) J. Gen. Virol. , vol.91 , pp. 1325-1334
    • Wenigenrath, J.1    Kolesnikova, L.2    Hoenen, T.3    Mittler, E.4    Becker, S.5
  • 78
    • 84963657108 scopus 로고    scopus 로고
    • Fusion of Enveloped Viruses in Endosomes
    • White, J.M., Whittaker, G.R., Fusion of Enveloped Viruses in Endosomes. Traffic 17 (2016), 593–614.
    • (2016) Traffic , vol.17 , pp. 593-614
    • White, J.M.1    Whittaker, G.R.2
  • 79
    • 33746799703 scopus 로고    scopus 로고
    • Contribution of Vpu, Env, and Nef to CD4 down-modulation and resistance of human immunodeficiency virus type 1-infected T cells to superinfection
    • Wildum, S., Schindler, M., Münch, J., Kirchhoff, F., Contribution of Vpu, Env, and Nef to CD4 down-modulation and resistance of human immunodeficiency virus type 1-infected T cells to superinfection. J. Virol. 80 (2006), 8047–8059.
    • (2006) J. Virol. , vol.80 , pp. 8047-8059
    • Wildum, S.1    Schindler, M.2    Münch, J.3    Kirchhoff, F.4


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