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Volumn 13, Issue 7, 2015, Pages 426-437

Broad-spectrum antivirals against viral fusion

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; CONFORMATIONAL CHANGE INHIBITOR; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; PHOSPHOLIPID ANTIBODY; PHOSPHOLIPID SPECIFIC ANTIBODY; POLYPEPTIDE ANTIBIOTIC AGENT; RECEPTOR; UNCLASSIFIED DRUG; VIROLYTIC ANTIVIRAL PEPTIDE; VIRUS FUSION INHIBITOR;

EID: 84931576347     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro3475     Document Type: Review
Times cited : (195)

References (98)
  • 1
    • 34249089649 scopus 로고    scopus 로고
    • Origins of major human infectious diseases
    • Wolfe, N. D., Dunavan, C. P. & Diamond, J. Origins of major human infectious diseases. Nature 447, 279-283 (2007).
    • (2007) Nature , vol.447 , pp. 279-283
    • Wolfe, N.D.1    Dunavan, C.P.2    Diamond, J.3
  • 2
    • 84920794111 scopus 로고    scopus 로고
    • Evidence for henipavirus spillover into human populations in Africa
    • Pernet, O. et al. Evidence for henipavirus spillover into human populations in Africa. Nat. Commun. 5, 5342 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 5342
    • Pernet, O.1
  • 4
    • 84904438309 scopus 로고    scopus 로고
    • The 2014 Ebola virus disease outbreak in West Africa
    • Gatherer, D. The 2014 Ebola virus disease outbreak in West Africa. J. Gen. Virol. 95, 1619-1624 (2014).
    • (2014) J. Gen. Virol. , vol.95 , pp. 1619-1624
    • Gatherer, D.1
  • 5
    • 84959851955 scopus 로고    scopus 로고
    • Middle East respiratory syndrome coronavirus: Another zoonotic betacoronavirus causing SARS-like disease
    • Chan, J. F. et al. Middle East respiratory syndrome coronavirus: another zoonotic betacoronavirus causing SARS-like disease. Clin. Microbiol. Rev. 28, 465-522 (2015).
    • (2015) Clin. Microbiol. Rev. , vol.28 , pp. 465-522
    • Chan, J.F.1
  • 6
    • 78649856647 scopus 로고    scopus 로고
    • Impacts of biodiversity on the emergence and transmission of infectious diseases
    • Keesing, F. et al. Impacts of biodiversity on the emergence and transmission of infectious diseases. Nature 468, 647-652 (2010).
    • (2010) Nature , vol.468 , pp. 647-652
    • Keesing, F.1
  • 7
    • 84892715542 scopus 로고    scopus 로고
    • The human environment interface: Applying ecosystem concepts to health
    • Preston, N. D., Daszak, P. & Colwell, R. R. The human environment interface: applying ecosystem concepts to health. Curr. Top. Microbiol. Immunol. 365, 83-100 (2013).
    • (2013) Curr. Top. Microbiol. Immunol. , vol.365 , pp. 83-100
    • Preston, N.D.1    Daszak, P.2    Colwell, R.R.3
  • 8
    • 84885410330 scopus 로고    scopus 로고
    • A strategy to estimate unknown viral diversity in mammals
    • Anthony, S. J. et al. A strategy to estimate unknown viral diversity in mammals. mBio 4, e00598-13 (2013).
    • (2013) MBio , vol.4 , pp. e00598-e00613
    • Anthony, S.J.1
  • 9
    • 82955163230 scopus 로고    scopus 로고
    • Ribavirin for the treatment of chronic hepatitis C virus infection: A review of the proposed mechanisms of action
    • Paeshuyse, J., Dallmeier, K. & Neyts, J. Ribavirin for the treatment of chronic hepatitis C virus infection: a review of the proposed mechanisms of action. Curr. Opin. Virol. 1, 590-598 (2011).
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 590-598
    • Paeshuyse, J.1    Dallmeier, K.2    Neyts, J.3
  • 10
    • 79551639004 scopus 로고    scopus 로고
    • Cell entry of enveloped viruses
    • Cosset, F. L. & Lavillette, D. Cell entry of enveloped viruses. Adv. Genet. 73, 121-183 (2011).
    • (2011) Adv. Genet. , vol.73 , pp. 121-183
    • Cosset, F.L.1    Lavillette, D.2
  • 11
    • 84877898099 scopus 로고    scopus 로고
    • Virus entry at a glance
    • Yamauchi, Y. & Helenius, A. Virus entry at a glance. J. Cell Sci. 126, 1289-1295 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 1289-1295
    • Yamauchi, Y.1    Helenius, A.2
  • 12
    • 84855673964 scopus 로고    scopus 로고
    • Cell entry of enveloped viruses
    • Plemper, R. K. Cell entry of enveloped viruses. Curr. Opin. Virol. 1, 92-100 (2011).
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 92-100
    • Plemper, R.K.1
  • 14
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • White, J. M., Delos, S. E., Brecher, M. & Schornberg, K. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43, 189-219 (2008).
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 15
    • 84865974865 scopus 로고    scopus 로고
    • Hydration repulsion between biomembranes results from an interplay of dehydration and depolarization
    • Schneck, E., Sedlmeier, F. & Netz, R. R. Hydration repulsion between biomembranes results from an interplay of dehydration and depolarization. Proc. Natl Acad. Sci. USA 109, 14405-14409 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 14405-14409
    • Schneck, E.1    Sedlmeier, F.2    Netz, R.R.3
  • 16
    • 84870599997 scopus 로고    scopus 로고
    • Development of novel entry inhibitors targeting emerging viruses
    • Zhou, Y. & Simmons, G. Development of novel entry inhibitors targeting emerging viruses. Expert Rev. Anti Infect. Ther. 10, 1129-1138 (2012).
    • (2012) Expert Rev. Anti Infect. Ther. , vol.10 , pp. 1129-1138
    • Zhou, Y.1    Simmons, G.2
  • 17
    • 84873133718 scopus 로고    scopus 로고
    • Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry
    • El Omari, K., Iourin, O., Harlos, K., Grimes, J. M. & Stuart, D. I. Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry. Cell Rep. 3, 30-35 (2013).
    • (2013) Cell Rep. , vol.3 , pp. 30-35
    • El Omari, K.1    Iourin, O.2    Harlos, K.3    Grimes, J.M.4    Stuart, D.I.5
  • 18
    • 84876865608 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein E2 from bovine viral diarrhea virus
    • Li, Y., Wang, J., Kanai, R. & Modis, Y. Crystal structure of glycoprotein E2 from bovine viral diarrhea virus. Proc. Natl Acad. Sci. USA 110, 6805-6810 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 6805-6810
    • Li, Y.1    Wang, J.2    Kanai, R.3    Modis, Y.4
  • 19
    • 84888778890 scopus 로고    scopus 로고
    • Hepatitis C virus E2 envelope glycoprotein core structure
    • Kong, L. et al. Hepatitis C virus E2 envelope glycoprotein core structure. Science 342, 1090-1094 (2013).
    • (2013) Science , vol.342 , pp. 1090-1094
    • Kong, L.1
  • 20
    • 84897378275 scopus 로고    scopus 로고
    • A novel membrane fusion protein family in Flaviviridae?
    • Li, Y. & Modis, Y. A novel membrane fusion protein family in Flaviviridae? Trends Microbiol. 22, 176-182 (2014).
    • (2014) Trends Microbiol. , vol.22 , pp. 176-182
    • Li, Y.1    Modis, Y.2
  • 21
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein
    • Mothes, W., Boerger, A. L., Narayan, S., Cunningham, J. M. & Young, J. A. Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Cell 103, 679-689 (2000).
    • (2000) Cell , vol.103 , pp. 679-689
    • Mothes, W.1    Boerger, A.L.2    Narayan, S.3    Cunningham, J.M.4    Young, J.A.5
  • 22
    • 0037303326 scopus 로고    scopus 로고
    • Two retroviral entry pathways distinguished by lipid raft association of the viral receptor and differences in viral infectivity
    • Narayan, S., Barnard, R. J. & Young, J. A. Two retroviral entry pathways distinguished by lipid raft association of the viral receptor and differences in viral infectivity. J. Virol. 77, 1977-1983 (2003).
    • (2003) J. Virol. , vol.77 , pp. 1977-1983
    • Narayan, S.1    Barnard, R.J.2    Young, J.A.3
  • 23
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: Disparate players and common principles
    • Martens, S. & McMahon, H. T. Mechanisms of membrane fusion: disparate players and common principles. Nat. Rev. Mol. Cell Biol. 9, 543-556 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 24
    • 79960419904 scopus 로고    scopus 로고
    • Lipid acrobatics in the membrane fusion arena
    • Markvoort, A. J. & Marrink, S. J. Lipid acrobatics in the membrane fusion arena. Curr. Top. Membr. 68, 259-294 (2011).
    • (2011) Curr. Top. Membr. , vol.68 , pp. 259-294
    • Markvoort, A.J.1    Marrink, S.J.2
  • 25
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg, J. & Kozlov, M. M. How proteins produce cellular membrane curvature. Nat. Rev. Mol. Cell Biol. 7, 9-19 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 26
    • 84883672372 scopus 로고    scopus 로고
    • A cost-benefit analysis of the physical mechanisms of membrane curvature
    • Stachowiak, J. C., Brodsky, F. M. & Miller, E. A. A cost-benefit analysis of the physical mechanisms of membrane curvature. Nat. Cell Biol. 15, 1019-1027 (2013).
    • (2013) Nat. Cell Biol. , vol.15 , pp. 1019-1027
    • Stachowiak, J.C.1    Brodsky, F.M.2    Miller, E.A.3
  • 27
    • 84874660180 scopus 로고    scopus 로고
    • HIV-1 entry inhibitors: Recent development and clinical use
    • Henrich, T. J. & Kuritzkes, D. R. HIV-1 entry inhibitors: recent development and clinical use. Curr. Opin. Virol. 3, 51-57 (2013).
    • (2013) Curr. Opin. Virol. , vol.3 , pp. 51-57
    • Henrich, T.J.1    Kuritzkes, D.R.2
  • 28
    • 79960463354 scopus 로고    scopus 로고
    • Multifaceted action of Fuzeon as virus-cell membrane fusion inhibitor
    • Ashkenazi, A., Wexler-Cohen, Y. & Shai, Y. Multifaceted action of Fuzeon as virus-cell membrane fusion inhibitor. Biochim. Biophys. Acta 1808, 2352-2358 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2352-2358
    • Ashkenazi, A.1    Wexler-Cohen, Y.2    Shai, Y.3
  • 29
    • 1642494594 scopus 로고    scopus 로고
    • Putative role of membranes in the HIV fusion inhibitor enfuvirtide mode of action at the molecular level
    • Veiga, S., Henriques, S., Santos, N. C. & Castanho, M. Putative role of membranes in the HIV fusion inhibitor enfuvirtide mode of action at the molecular level. Biochem. J. 377, 107-110 (2004).
    • (2004) Biochem. J. , vol.377 , pp. 107-110
    • Veiga, S.1    Henriques, S.2    Santos, N.C.3    Castanho, M.4
  • 30
    • 84857363079 scopus 로고    scopus 로고
    • Is there a future for antiviral fusion inhibitors?
    • Berkhout, B., Eggink, D. & Sanders, R. W. Is there a future for antiviral fusion inhibitors? Curr. Opin. Virol. 2, 50-59 (2012).
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 50-59
    • Berkhout, B.1    Eggink, D.2    Sanders, R.W.3
  • 31
    • 26444506252 scopus 로고    scopus 로고
    • Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion
    • Liao, M. & Kielian, M. Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion. J. Cell Biol. 171, 111-120 (2005).
    • (2005) J. Cell Biol. , vol.171 , pp. 111-120
    • Liao, M.1    Kielian, M.2
  • 32
    • 84884679512 scopus 로고    scopus 로고
    • A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses
    • Koehler, J. W. et al. A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses. PLoS Negl. Trop. Dis. 7, e2430 (2013).
    • (2013) PLoS Negl. Trop. Dis. , vol.7 , pp. e2430
    • Koehler, J.W.1
  • 33
    • 80053257157 scopus 로고    scopus 로고
    • How viruses and toxins disassemble to enter host cells
    • Inoue, T., Moore, P. & Tsai, B. How viruses and toxins disassemble to enter host cells. Annu. Rev. Microbiol. 65, 287-305 (2011).
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 287-305
    • Inoue, T.1    Moore, P.2    Tsai, B.3
  • 34
    • 84876114193 scopus 로고
    • Post-translational control of protein function by disulfide bond cleavage
    • Cook, K. M. & Hogg, P. J. Post-translational control of protein function by disulfide bond cleavage. Antioxid. Redox Signal. 18, 1987-2015 (2013).
    • (1987) Antioxid. Redox Signal. , vol.18
    • Cook, K.M.1    Hogg, P.J.2
  • 35
    • 0346374729 scopus 로고    scopus 로고
    • Cross-strand disulphides in cell entry proteins: Poised to act
    • Wouters, M. A., Lau, K. K. & Hogg, P. J. Cross-strand disulphides in cell entry proteins: poised to act. Bioessays 26, 73-79 (2004).
    • (2004) Bioessays , vol.26 , pp. 73-79
    • Wouters, M.A.1    Lau, K.K.2    Hogg, P.J.3
  • 36
    • 79960601577 scopus 로고    scopus 로고
    • Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry
    • Bi, S., Hong, P. W., Lee, B. & Baum, L. G. Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry. Proc. Natl Acad. Sci. USA 108, 10650-10655 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 10650-10655
    • Bi, S.1    Hong, P.W.2    Lee, B.3    Baum, L.G.4
  • 37
    • 58149380783 scopus 로고    scopus 로고
    • Role of thiol/disulfide exchange in Newcastle disease virus entry
    • Jain, S., McGinnes, L. W. & Morrison, T. G. Role of thiol/disulfide exchange in Newcastle disease virus entry. J. Virol. 83, 241-249 (2009).
    • (2009) J. Virol. , vol.83 , pp. 241-249
    • Jain, S.1    McGinnes, L.W.2    Morrison, T.G.3
  • 38
    • 84870299409 scopus 로고    scopus 로고
    • Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infection
    • Stantchev, T. S. et al. Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infection. Retrovirology 9, 97 (2012).
    • (2012) Retrovirology , vol.9 , Issue.97
    • Stantchev, T.S.1
  • 39
    • 34447502257 scopus 로고    scopus 로고
    • Cell entry by enveloped viruses: Redox considerations for HIV and SARS-coronavirus
    • Fenouillet, E., Barbouche, R. & Jones, I. M. Cell entry by enveloped viruses: redox considerations for HIV and SARS-coronavirus. Antioxid. Redox Signal. 9, 1009-1034 (2007).
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 1009-1034
    • Fenouillet, E.1    Barbouche, R.2    Jones, I.M.3
  • 40
    • 33646698875 scopus 로고    scopus 로고
    • Extracellular disulfide exchange and the regulation of cellular function
    • Jordan, P. A. & Gibbins, J. M. Extracellular disulfide exchange and the regulation of cellular function. Antioxid. Redox Signal. 8, 312-324 (2006).
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 312-324
    • Jordan, P.A.1    Gibbins, J.M.2
  • 41
    • 59149097542 scopus 로고    scopus 로고
    • Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling
    • Garner, O. B. & Baum, L. G. Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling. Biochem. Soc. Trans. 36, 1472-1477 (2008).
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1472-1477
    • Garner, O.B.1    Baum, L.G.2
  • 42
    • 84860773241 scopus 로고    scopus 로고
    • Galectin-9 binding to Tim-3 renders activated human CD4+ T cells less susceptible to HIV-1 infection
    • Elahi, S., Niki, T., Hirashima, M. & Horton, H. Galectin-9 binding to Tim-3 renders activated human CD4+ T cells less susceptible to HIV-1 infection. Blood 119, 4192-4204 (2012).
    • (2012) Blood , vol.119 , pp. 4192-4204
    • Elahi, S.1    Niki, T.2    Hirashima, M.3    Horton, H.4
  • 43
    • 78649246847 scopus 로고    scopus 로고
    • Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins
    • Hoffstrom, B. G. et al. Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins. Nat. Chem. Biol. 6, 900-906 (2010).
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 900-906
    • Hoffstrom, B.G.1
  • 44
    • 84867095394 scopus 로고    scopus 로고
    • Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase for ovarian cancer treatment
    • Xu, S. et al. Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase for ovarian cancer treatment. Proc. Natl Acad. Sci. USA 109, 16348-16353 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 16348-16353
    • Xu, S.1
  • 45
    • 84861808529 scopus 로고    scopus 로고
    • Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents
    • Jasuja, R. et al. Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents. J. Clin. Invest. 122, 2104-2113 (2012).
    • (2012) J. Clin. Invest. , vol.122 , pp. 2104-2113
    • Jasuja, R.1
  • 46
    • 84859711349 scopus 로고    scopus 로고
    • The potential of protein disulfide isomerase as a therapeutic drug target
    • Khan, M. M., Simizu, S., Kawatani, M. & Osada, H. The potential of protein disulfide isomerase as a therapeutic drug target. Oncol. Res. 19, 445-453 (2011).
    • (2011) Oncol. Res. , vol.19 , pp. 445-453
    • Khan, M.M.1    Simizu, S.2    Kawatani, M.3    Osada, H.4
  • 47
    • 84891621364 scopus 로고    scopus 로고
    • Potential roles of protein disulphide isomerase in viral infections
    • Diwaker, D., Mishra, K. P. & Ganju, L. Potential roles of protein disulphide isomerase in viral infections. Acta Virol. 57, 293-304 (2013).
    • (2013) Acta Virol. , vol.57 , pp. 293-304
    • Diwaker, D.1    Mishra, K.P.2    Ganju, L.3
  • 48
    • 84884248924 scopus 로고    scopus 로고
    • Research perspective: Potential role of nitazoxanide in ovarian cancer treatment. Old drug, new purpose?
    • Di Santo, N. & Ehrisman, J. Research perspective: potential role of nitazoxanide in ovarian cancer treatment. Old drug, new purpose? Cancers 5, 1163-1176 (2013).
    • (2013) Cancers , vol.5 , pp. 1163-1176
    • Di Santo, N.1    Ehrisman, J.2
  • 49
    • 37349023592 scopus 로고    scopus 로고
    • Neospora caninum: Functional inhibition of protein disulfide isomerase by the broad-spectrum anti-parasitic drug nitazoxanide and other thiazolides
    • Muller, J., Naguleswaran, A., Muller, N. & Hemphill, A. Neospora caninum: functional inhibition of protein disulfide isomerase by the broad-spectrum anti-parasitic drug nitazoxanide and other thiazolides. Exp. Parasitol. 118, 80-88 (2008).
    • (2008) Exp. Parasitol. , vol.118 , pp. 80-88
    • Muller, J.1    Naguleswaran, A.2    Muller, N.3    Hemphill, A.4
  • 50
    • 84906669535 scopus 로고    scopus 로고
    • Nitazoxanide: A first-in-class broad-spectrum antiviral agent
    • Rossignol, J. F. Nitazoxanide: a first-in-class broad-spectrum antiviral agent. Antiviral Res. 110, 94-103 (2014).
    • (2014) Antiviral Res. , vol.110 , pp. 94-103
    • Rossignol, J.F.1
  • 51
    • 67651251216 scopus 로고    scopus 로고
    • Treatment of chronic viral hepatitis with nitazoxanide and second generation thiazolides
    • Keeffe, E. B. & Rossignol, J. F. Treatment of chronic viral hepatitis with nitazoxanide and second generation thiazolides. World J. Gastroenterol. 15, 1805-1808 (2009).
    • (2009) World J. Gastroenterol. , vol.15 , pp. 1805-1808
    • Keeffe, E.B.1    Rossignol, J.F.2
  • 52
    • 84869423899 scopus 로고    scopus 로고
    • Systematic identification of synergistic drug pairs targeting HIV
    • Tan, X. et al. Systematic identification of synergistic drug pairs targeting HIV. Nat. Biotechnol. 30, 1125-1130 (2012).
    • (2012) Nat. Biotechnol. , vol.30 , pp. 1125-1130
    • Tan, X.1
  • 53
    • 84901011755 scopus 로고    scopus 로고
    • Arbidol as a broad-spectrum antiviral: An update
    • Blaising, J., Polyak, S. J. & Pecheur, E. I. Arbidol as a broad-spectrum antiviral: an update. Antiviral Res. 107, 84-94 (2014).
    • (2014) Antiviral Res. , vol.107 , pp. 84-94
    • Blaising, J.1    Polyak, S.J.2    Pecheur, E.I.3
  • 54
    • 58249083139 scopus 로고    scopus 로고
    • Characteristics of arbidol-resistant mutants of influenza virus: Implications for the mechanism of anti-influenza action of arbidol
    • Leneva, I. A., Russell, R. J., Boriskin, Y. S. & Hay, A. J. Characteristics of arbidol-resistant mutants of influenza virus: implications for the mechanism of anti-influenza action of arbidol. Antiviral Res. 81, 132-140 (2009).
    • (2009) Antiviral Res. , vol.81 , pp. 132-140
    • Leneva, I.A.1    Russell, R.J.2    Boriskin, Y.S.3    Hay, A.J.4
  • 55
    • 84904740878 scopus 로고    scopus 로고
    • Effect of nitazoxanide in adults and adolescents with acute uncomplicated influenza: A double-blind, randomised, placebo-controlled, phase 2b/3 trial
    • Haffizulla, J. et al. Effect of nitazoxanide in adults and adolescents with acute uncomplicated influenza: a double-blind, randomised, placebo-controlled, phase 2b/3 trial. Lancet Infect. Dis. 14, 609-618 (2014).
    • (2014) Lancet Infect. Dis. , vol.14 , pp. 609-618
    • Haffizulla, J.1
  • 56
    • 84903717697 scopus 로고    scopus 로고
    • Peptide entry inhibitors of enveloped viruses: The importance of interfacial hydrophobicity
    • Badani, H., Garry, R. F. & Wimley, W. C. Peptide entry inhibitors of enveloped viruses: the importance of interfacial hydrophobicity. Biochim. Biophys. Acta 1838, 2180-2197 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 2180-2197
    • Badani, H.1    Garry, R.F.2    Wimley, W.C.3
  • 58
    • 42949173539 scopus 로고    scopus 로고
    • A virocidal amphipathic α-helical peptide that inhibits hepatitis C virus infection in vitro
    • Cheng, G. et al. A virocidal amphipathic α-helical peptide that inhibits hepatitis C virus infection in vitro. Proc. Natl Acad. Sci. USA 105, 3088-3093 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 3088-3093
    • Cheng, G.1
  • 59
    • 84886937495 scopus 로고    scopus 로고
    • A mastoparan-derived peptide has broad-spectrum antiviral activity against enveloped viruses
    • Sample, C. J. et al. A mastoparan-derived peptide has broad-spectrum antiviral activity against enveloped viruses. Peptides 48, 96-105 (2013).
    • (2013) Peptides , vol.48 , pp. 96-105
    • Sample, C.J.1
  • 60
    • 84859882976 scopus 로고    scopus 로고
    • Determining the mechanism of membrane permeabilizing peptides: Identification of potent, equilibrium pore-formers
    • Krauson, A. J., He, J. & Wimley, W. C. Determining the mechanism of membrane permeabilizing peptides: identification of potent, equilibrium pore-formers. Biochim. Biophys. Acta 1818, 1625-1632 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1625-1632
    • Krauson, A.J.1    He, J.2    Wimley, W.C.3
  • 61
    • 84856774559 scopus 로고    scopus 로고
    • Role of lipids in the interaction of antimicrobial peptides with membranes
    • Teixeira, V., Feio, M. J. & Bastos, M. Role of lipids in the interaction of antimicrobial peptides with membranes. Prog. Lipid Res. 51, 149-177 (2012).
    • (2012) Prog. Lipid Res. , vol.51 , pp. 149-177
    • Teixeira, V.1    Feio, M.J.2    Bastos, M.3
  • 62
    • 84891793411 scopus 로고    scopus 로고
    • AVPdb: A database of experimentally validated antiviral peptides targeting medically important viruses
    • Qureshi, A., Thakur, N., Tandon, H. & Kumar, M. AVPdb: a database of experimentally validated antiviral peptides targeting medically important viruses. Nucleic Acids Res. 42, D1147-D1153 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. D1147-D1153
    • Qureshi, A.1    Thakur, N.2    Tandon, H.3    Kumar, M.4
  • 63
    • 84870213151 scopus 로고    scopus 로고
    • Membrane-perturbing effect of fatty acids and lysolipids
    • Arouri, A. & Mouritsen, O. G. Membrane-perturbing effect of fatty acids and lysolipids. Prog. Lipid Res. 52, 130-140 (2013).
    • (2013) Prog. Lipid Res. , vol.52 , pp. 130-140
    • Arouri, A.1    Mouritsen, O.G.2
  • 64
    • 35748931458 scopus 로고    scopus 로고
    • Lipids as modulators of membrane fusion mediated by viral fusion proteins
    • Teissier, E. & Pecheur, E. I. Lipids as modulators of membrane fusion mediated by viral fusion proteins. Eur. Biophys. J. 36, 887-899 (2007).
    • (2007) Eur. Biophys. J. , vol.36 , pp. 887-899
    • Teissier, E.1    Pecheur, E.I.2
  • 65
    • 77953503043 scopus 로고    scopus 로고
    • Uptake and trafficking of liposomes to the endoplasmic reticulum
    • Pollock, S. et al. Uptake and trafficking of liposomes to the endoplasmic reticulum. FASEB J. 24, 1866-1878 (2010).
    • (2010) FASEB J. , vol.24 , pp. 1866-1878
    • Pollock, S.1
  • 66
    • 78049278777 scopus 로고    scopus 로고
    • Polyunsaturated liposomes are antiviral against hepatitis B and C viruses and HIV by decreasing cholesterol levels in infected cells
    • Pollock, S. et al. Polyunsaturated liposomes are antiviral against hepatitis B and C viruses and HIV by decreasing cholesterol levels in infected cells. Proc. Natl Acad. Sci. USA 107, 17176-17181 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 17176-17181
    • Pollock, S.1
  • 67
    • 84899865140 scopus 로고    scopus 로고
    • Lysophosphatidylcholine reversibly arrests pore expansion during syncytium formation mediated by diverse viral fusogens
    • Ciechonska, M. & Duncan, R. Lysophosphatidylcholine reversibly arrests pore expansion during syncytium formation mediated by diverse viral fusogens. J. Virol. 88, 6528-6531 (2014).
    • (2014) J. Virol. , vol.88 , pp. 6528-6531
    • Ciechonska, M.1    Duncan, R.2
  • 68
    • 78049306063 scopus 로고    scopus 로고
    • Rigid amphipathic fusion inhibitors, small molecule antiviral compounds against enveloped viruses
    • St Vincent, M. R. et al. Rigid amphipathic fusion inhibitors, small molecule antiviral compounds against enveloped viruses. Proc. Natl Acad. Sci. USA 107, 17339-17344 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 17339-17344
    • St Vincent, M.R.1
  • 69
    • 84875507361 scopus 로고    scopus 로고
    • 5-(Perylen-3-yl)ethynyl-arabino-uridine (aUY11), an arabino-based rigid amphipathic fusion inhibitor, targets virion envelope lipids to inhibit fusion of influenza virus, hepatitis C virus, and other enveloped viruses
    • Colpitts, C. C. et al. 5-(Perylen-3-yl)ethynyl-arabino-uridine (aUY11), an arabino-based rigid amphipathic fusion inhibitor, targets virion envelope lipids to inhibit fusion of influenza virus, hepatitis C virus, and other enveloped viruses. J. Virol. 87, 3640-3654 (2013).
    • (2013) J. Virol. , vol.87 , pp. 3640-3654
    • Colpitts, C.C.1
  • 70
    • 78049318430 scopus 로고    scopus 로고
    • Driving a wedge between viral lipids blocks infection
    • Melikyan, G. B. Driving a wedge between viral lipids blocks infection. Proc. Natl Acad. Sci. USA 107, 17069-17070 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 17069-17070
    • Melikyan, G.B.1
  • 71
    • 78049360426 scopus 로고    scopus 로고
    • Positive reinforcement for viruses
    • Vigant, F., Jung, M. & Lee, B. Positive reinforcement for viruses. Chem. Biol. 17, 1049-1051 (2010).
    • (2010) Chem. Biol. , vol.17 , pp. 1049-1051
    • Vigant, F.1    Jung, M.2    Lee, B.3
  • 72
    • 84876852255 scopus 로고    scopus 로고
    • A mechanistic paradigm for broad-spectrum antivirals that target virus-cell fusion
    • Vigant, F. et al. A mechanistic paradigm for broad-spectrum antivirals that target virus-cell fusion. PLoS Pathog. 9, e1003297 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. e1003297
    • Vigant, F.1
  • 73
    • 77649246144 scopus 로고    scopus 로고
    • A broad-spectrum antiviral targeting entry of enveloped viruses
    • Wolf, M. C. et al. A broad-spectrum antiviral targeting entry of enveloped viruses. Proc. Natl Acad. Sci. USA 107, 3157-3162 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 3157-3162
    • Wolf, M.C.1
  • 74
    • 84896119125 scopus 로고    scopus 로고
    • Singlet oxygen effects on lipid membranes: Implications for the mechanism of action of broad-spectrum viral fusion inhibitors
    • Hollmann, A., Castanho, M. A., Lee, B. & Santos, N. C. Singlet oxygen effects on lipid membranes: implications for the mechanism of action of broad-spectrum viral fusion inhibitors. Biochem. J. 459, 161-170 (2014).
    • (2014) Biochem. J. , vol.459 , pp. 161-170
    • Hollmann, A.1    Castanho, M.A.2    Lee, B.3    Santos, N.C.4
  • 75
    • 36048958468 scopus 로고    scopus 로고
    • Oxidation decomposition of unsaturated fatty acids by singlet oxygen in phospholipid bilayer membranes
    • Watabe, N., Ishida, Y., Ochiai, A., Tokuoka, Y. & Kawashima, N. Oxidation decomposition of unsaturated fatty acids by singlet oxygen in phospholipid bilayer membranes. J. Oleo Sci. 56, 73-80 (2007).
    • (2007) J. Oleo Sci. , vol.56 , pp. 73-80
    • Watabe, N.1    Ishida, Y.2    Ochiai, A.3    Tokuoka, Y.4    Kawashima, N.5
  • 76
    • 70349466662 scopus 로고    scopus 로고
    • Giant vesicles under oxidative stress induced by a membrane-anchored photosensitizer
    • Riske, K. A. et al. Giant vesicles under oxidative stress induced by a membrane-anchored photosensitizer. Biophys. J. 97, 1362-1370 (2009).
    • (2009) Biophys. J. , vol.97 , pp. 1362-1370
    • Riske, K.A.1
  • 77
    • 84901764653 scopus 로고    scopus 로고
    • Lipid oxidation induces structural changes in biomimetic membranes
    • Weber, G. et al. Lipid oxidation induces structural changes in biomimetic membranes. Soft Matter 10, 4241-4247 (2014).
    • (2014) Soft Matter , vol.10 , pp. 4241-4247
    • Weber, G.1
  • 78
    • 33748476306 scopus 로고    scopus 로고
    • Lipid peroxides promote large rafts: Effects of excitation of probes in fluorescence microscopy and electrochemical reactions during vesicle formation
    • Ayuyan, A. G. & Cohen, F. S. Lipid peroxides promote large rafts: effects of excitation of probes in fluorescence microscopy and electrochemical reactions during vesicle formation. Biophys. J. 91, 2172-2183 (2006).
    • (2006) Biophys. J. , vol.91 , pp. 2172-2183
    • Ayuyan, A.G.1    Cohen, F.S.2
  • 79
    • 84931067341 scopus 로고    scopus 로고
    • Effects of singlet oxygen generated by a broad-spectrum viral fusion inhibitor on membrane nanoarchitecture
    • Hollmann, A. et al. Effects of singlet oxygen generated by a broad-spectrum viral fusion inhibitor on membrane nanoarchitecture. Nanomedicine 11, 1163-1167 (2015).
    • (2015) Nanomedicine , vol.11 , pp. 1163-1167
    • Hollmann, A.1
  • 80
    • 84892460793 scopus 로고    scopus 로고
    • The rigid amphipathic fusion inhibitor dUY11 acts through photosensitization of viruses
    • Vigant, F. et al. The rigid amphipathic fusion inhibitor dUY11 acts through photosensitization of viruses. J. Virol. 88, 1849-1853 (2014).
    • (2014) J. Virol. , vol.88 , pp. 1849-1853
    • Vigant, F.1
  • 82
    • 84870294469 scopus 로고    scopus 로고
    • In vivo photodynamic therapy using upconversion nanoparticles as remote-controlled nanotransducers
    • Idris, N. M. et al. In vivo photodynamic therapy using upconversion nanoparticles as remote-controlled nanotransducers. Nat. Med. 18, 1580-1585 (2012).
    • (2012) Nat. Med. , vol.18 , pp. 1580-1585
    • Idris, N.M.1
  • 83
    • 77956914523 scopus 로고    scopus 로고
    • Phosphatidylserine targeting for diagnosis and treatment of human diseases
    • Schutters, K. & Reutelingsperger, C. Phosphatidylserine targeting for diagnosis and treatment of human diseases. Apoptosis 15, 1072-1082 (2010).
    • (2010) Apoptosis , vol.15 , pp. 1072-1082
    • Schutters, K.1    Reutelingsperger, C.2
  • 84
    • 57349140230 scopus 로고    scopus 로고
    • Targeting inside-out phosphatidylserine as a therapeutic strategy for viral diseases
    • Soares, M. M., King, S. W. & Thorpe, P. E. Targeting inside-out phosphatidylserine as a therapeutic strategy for viral diseases. Nat. Med. 14, 1357-1362 (2008).
    • (2008) Nat. Med. , vol.14 , pp. 1357-1362
    • Soares, M.M.1    King, S.W.2    Thorpe, P.E.3
  • 85
    • 84886071901 scopus 로고    scopus 로고
    • Lipids in innate antiviral defense
    • Schoggins, J. W. & Randall, G. Lipids in innate antiviral defense. Cell Host Microbe 14, 379-385 (2013).
    • (2013) Cell Host Microbe , vol.14 , pp. 379-385
    • Schoggins, J.W.1    Randall, G.2
  • 86
    • 78651095014 scopus 로고    scopus 로고
    • Lipid map of the mammalian cell
    • van Meer, G. & de Kroon, A. I. Lipid map of the mammalian cell. J. Cell Sci. 124, 5-8 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 5-8
    • Van Meer, G.1    De Kroon, A.I.2
  • 87
    • 0036050539 scopus 로고    scopus 로고
    • Strategies in the design of antiviral drugs
    • De Clercq, E. Strategies in the design of antiviral drugs. Nat. Rev. Drug Discov. 1, 13-25 (2002).
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 13-25
    • De Clercq, E.1
  • 88
    • 84931585584 scopus 로고    scopus 로고
    • Forum on Medical and Public Health Preparedness for Catastrophic Events, Forum on Drug Discovery, Development, and Translation, Board on Health Sciences Policy, Institute of Medicine. National Academies Press
    • Forum on Medical and Public Health Preparedness for Catastrophic Events, Forum on Drug Discovery, Development, and Translation, Board on Health Sciences Policy, Institute of Medicine. Advancing Regulatory Science for Medical Countermeasure Development: Workshop Summary (National Academies Press, 2011).
    • (2011) Advancing Regulatory Science for Medical Countermeasure Development: Workshop Summary
  • 89
    • 84905725612 scopus 로고    scopus 로고
    • 3D bioprinting of tissues and organs
    • Murphy, S. V. & Atala, A. 3D bioprinting of tissues and organs. Nat. Biotechnol. 32, 773-785 (2014).
    • (2014) Nat. Biotechnol. , vol.32 , pp. 773-785
    • Murphy, S.V.1    Atala, A.2
  • 90
    • 84905754409 scopus 로고    scopus 로고
    • Microfluidic organs-on-chips
    • Bhatia, S. N. & Ingber, D. E. Microfluidic organs-on-chips. Nat. Biotechnol. 32, 760-772 (2014).
    • (2014) Nat. Biotechnol. , vol.32 , pp. 760-772
    • Bhatia, S.N.1    Ingber, D.E.2
  • 91
    • 84876003028 scopus 로고    scopus 로고
    • Influenza virus resistance to neuraminidase inhibitors
    • Samson, M., Pizzorno, A., Abed, Y. & Boivin, G. Influenza virus resistance to neuraminidase inhibitors. Antiviral Res. 98, 174-185 (2013).
    • (2013) Antiviral Res. , vol.98 , pp. 174-185
    • Samson, M.1    Pizzorno, A.2    Abed, Y.3    Boivin, G.4
  • 92
    • 84870226652 scopus 로고    scopus 로고
    • A phase II study of DAS181, a novel host directed antiviral for the treatment of influenza infection
    • Moss, R. B. et al. A phase II study of DAS181, a novel host directed antiviral for the treatment of influenza infection. J. Infect. Dis. 206, 1844-1851 (2012).
    • (2012) J. Infect. Dis. , vol.206 , pp. 1844-1851
    • Moss, R.B.1
  • 93
    • 84893835937 scopus 로고    scopus 로고
    • DAS181 treatment of hematopoietic stem cell transplant patients with parainfluenza virus lung disease requiring mechanical ventilation
    • Chalkias, S. et al. DAS181 treatment of hematopoietic stem cell transplant patients with parainfluenza virus lung disease requiring mechanical ventilation. Transpl. Infect. Dis. 16, 141-144 (2014).
    • (2014) Transpl. Infect. Dis. , vol.16 , pp. 141-144
    • Chalkias, S.1
  • 96
    • 84890278211 scopus 로고    scopus 로고
    • Selective inhibitor of endosomal trafficking pathways exploited by multiple toxins and viruses
    • Gillespie, E. J. et al. Selective inhibitor of endosomal trafficking pathways exploited by multiple toxins and viruses. Proc. Natl Acad. Sci. USA 110, E4904-E4912 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E4904-E4912
    • Gillespie, E.J.1
  • 97
    • 84896955320 scopus 로고    scopus 로고
    • Role of phosphatidylserine receptors in enveloped virus infection
    • Morizono, K. & Chen, I. S. Role of phosphatidylserine receptors in enveloped virus infection. J. Virol. 88, 4275-4290 (2014).
    • (2014) J. Virol. , vol.88 , pp. 4275-4290
    • Morizono, K.1    Chen, I.S.2
  • 98
    • 84903885404 scopus 로고    scopus 로고
    • Inhibition of arenavirus infection by a glycoprotein-derived peptide with a novel mechanism
    • Spence, J. S., Melnik, L. I., Badani, H., Wimley, W. C. & Garry, R. F. Inhibition of arenavirus infection by a glycoprotein-derived peptide with a novel mechanism. J. Virol. 88, 8556-8564 (2014).
    • (2014) J. Virol. , vol.88 , pp. 8556-8564
    • Spence, J.S.1    Melnik, L.I.2    Badani, H.3    Wimley, W.C.4    Garry, R.F.5


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