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Volumn 3, Issue , 2015, Pages

Characterizing alpha helical properties of Ebola viral proteins as potential targets for inhibition of alpha-helix mediated protein-protein interactions

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; MEMBRANE FUSION PROTEIN; NEUTRALIZING ANTIBODY; VIRUS GLYCOPROTEIN;

EID: 84925014192     PISSN: 20461402     EISSN: 1759796X     Source Type: Journal    
DOI: 10.12688/f1000research.5573.3     Document Type: Article
Times cited : (5)

References (56)
  • 1
    • 0017772926 scopus 로고
    • Isolation of Marburg-like virus from a case of haemorrhagic fever in Zaire
    • 65663
    • Pattyn S van der Groen G Courteille G: Isolation of Marburg-like virus from a case of haemorrhagic fever in Zaire. Lancet. 1977;1(8011):573-574. 65663 10.1016/S0140-6736(77)92002-5
    • (1977) Lancet , vol.1 , Issue.8011 , pp. 573-574
    • Pattyn, S.1    van der Groen, G.2    Courteille, G.3
  • 2
    • 0034060436 scopus 로고    scopus 로고
    • Ebola haemorrhagic fever-a review
    • 10762106
    • Colebunders R Borchert M: Ebola haemorrhagic fever-a review. J Infect. 2000;40(1):16-20. 10762106 10.1053/jinf.1999.0603
    • (2000) J Infect , vol.40 , Issue.1 , pp. 16-20
    • Colebunders, R.1    Borchert, M.2
  • 3
    • 84907210934 scopus 로고    scopus 로고
    • Ebola's perfect storm
    • 25214580
    • Piot P: Ebola's perfect storm. Science. 2014;345(6202):1221. 25214580 10.1126/science.1260695
    • (2014) Science , vol.345 , Issue.6202 , pp. 1221
    • Piot, P.1
  • 4
    • 84908287083 scopus 로고    scopus 로고
    • Ebola in west Africa: from disease outbreak to humanitarian crisis
    • 25282665
    • Piot P Muyembe JJ Edmunds WJ: Ebola in west Africa: from disease outbreak to humanitarian crisis. Lancet Infect Dis. 2014;14(11):1034-1035. 25282665 10.1016/S1473-3099(14)70956-9
    • (2014) Lancet Infect Dis , vol.14 , Issue.11 , pp. 1034-1035
    • Piot, P.1    Muyembe, J.J.2    Edmunds, W.J.3
  • 5
    • 0019986131 scopus 로고
    • Filoviridae: a taxonomic home for Marburg and Ebola Viruses?
    • 7118520
    • Kiley M Bowen E Eddy G: Filoviridae: a taxonomic home for Marburg and Ebola Viruses? Intervirology. 1982;18(1-2):24-32. 7118520 10.1159/000149300
    • (1982) Intervirology , vol.18 , Issue.1-2 , pp. 24-32
    • Kiley, M.1    Bowen, E.2    Eddy, G.3
  • 6
    • 84921997533 scopus 로고    scopus 로고
    • How a virus blocks a cellular emergency access lane to the nucleus, STAT!
    • 25121743
    • Daugherty MD Malik HS: How a virus blocks a cellular emergency access lane to the nucleus, STAT! Cell Host Microbe. 2014;16(2):150-152. 25121743 10.1016/j.chom.2014.07.013
    • (2014) Cell Host Microbe , vol.16 , Issue.2 , pp. 150-152
    • Daugherty, M.D.1    Malik, H.S.2
  • 7
    • 0022375091 scopus 로고
    • Descriptive analysis of Ebola virus proteins
    • 4060597
    • Elliott LH Kiley MP McCormick JB: Descriptive analysis of Ebola virus proteins. Virology. 1985;147(1):169-176. 4060597 10.1016/0042-6822(85)90236-3
    • (1985) Virology , vol.147 , Issue.1 , pp. 169-176
    • Elliott, L.H.1    Kiley, M.P.2    McCormick, J.B.3
  • 8
    • 84882787658 scopus 로고    scopus 로고
    • Structural basis for ebolavirus matrix assembly and budding; protein plasticity allows multiple functions
    • 23953110
    • Bornholdt ZA Noda T Abelson DM: Structural basis for ebolavirus matrix assembly and budding; protein plasticity allows multiple functions. Cell. 2013;154:763. 23953110 10.1016/j.cell.2013.07.015 4138722
    • (2013) Cell , vol.154 , pp. 763
    • Bornholdt, Z.A.1    Noda, T.2    Abelson, D.M.3
  • 9
    • 84924987424 scopus 로고    scopus 로고
    • Conformational plasticity of the Ebola virus matrix protein
    • 25159197
    • Radzimanowski J Effantin G Weissenhorn W: Conformational plasticity of the Ebola virus matrix protein. Protein Sci. 2014;23(11):1519-1527. 25159197 10.1002/pro.2541
    • (2014) Protein Sci , vol.23 , Issue.11 , pp. 1519-1527
    • Radzimanowski, J.1    Effantin, G.2    Weissenhorn, W.3
  • 10
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • 7937889
    • Wild CT Shugars DC Greenwell TK: Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc Natl Acad Sci U S A. 1994;91(21):9770-9774. 7937889 10.1073/pnas.91.21.9770 44898
    • (1994) Proc Natl Acad Sci U S A , vol.91 , Issue.21 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3
  • 11
    • 0031473771 scopus 로고    scopus 로고
    • Inhibition of HIV type 1 infectivity by constrained alpha-helical peptides: implications for the viral fusion mechanism
    • 9391041
    • Judice JK Tom JY Huang W: Inhibition of HIV type 1 infectivity by constrained alpha-helical peptides: implications for the viral fusion mechanism. Proc Natl Acad Sci U S A. 1997;94(25):13426-13430. 9391041 10.1073/pnas.94.25.13426 28321
    • (1997) Proc Natl Acad Sci U S A , vol.94 , Issue.25 , pp. 13426-13430
    • Judice, J.K.1    Tom, J.Y.2    Huang, W.3
  • 12
    • 0037126834 scopus 로고    scopus 로고
    • Design of a protein surface antagonist based on α-helix mimicry: inhibition of gp41 assembly and viral fusion
    • 12491408
    • Ernst JT Kutzki O Debnath AK: Design of a protein surface antagonist based on α-helix mimicry: inhibition of gp41 assembly and viral fusion. Angew Chem Int Ed Engl. 2002;41(2):278-281. 12491408 10.1002/1521-3773(20020118)41:2&278::AID-ANIE278&3.0.CO;2-A
    • (2002) Angew Chem Int Ed Engl , vol.41 , Issue.2 , pp. 278-281
    • Ernst, J.T.1    Kutzki, O.2    Debnath, A.K.3
  • 13
    • 0026604244 scopus 로고
    • Computer programs to identify and classify amphipathic alpha helical domains
    • 1569380
    • Jones MK Anantharamaiah GM Segrest JP: Computer programs to identify and classify amphipathic alpha helical domains. J Lipid Res. 1992;33(2):287-296. 1569380
    • (1992) J Lipid Res , vol.33 , Issue.2 , pp. 287-296
    • Jones, M.K.1    Anantharamaiah, G.M.2    Segrest, J.P.3
  • 14
    • 84923239653 scopus 로고    scopus 로고
    • Pagal - Properties and corresponding graphics of alpha helical structures in proteins
    • 25352981
    • Chakraborty S Rao B Dandekar A: Pagal - Properties and corresponding graphics of alpha helical structures in proteins. F1000Res. 2014;3:206. 25352981 10.12688/f1000research.4952.2 4207245
    • (2014) F1000Res , vol.3 , pp. 206
    • Chakraborty, S.1    Rao, B.2    Dandekar, A.3
  • 15
    • 78651277458 scopus 로고    scopus 로고
    • A series of PDB related databases for everyday needs
    • 21071423
    • Joosten RP te Beek TA Krieger E: A series of PDB related databases for everyday needs. Nucleic Acids Res. 2011;39(Database issue):D411-419. 21071423 10.1093/nar/gkq1105 3013697
    • (2011) Nucleic Acids Res , vol.39 , Issue.DATABASE ISSUE , pp. D411-419
    • Joosten, R.P.1    te Beek, T.A.2    Krieger, E.3
  • 16
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • 9844633
    • Weissenhorn W Carfi A Lee KH: Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol Cell. 1998;2(5):605-616. 9844633 10.1016/S1097-2765(00)80159-8
    • (1998) Mol Cell , vol.2 , Issue.5 , pp. 605-616
    • Weissenhorn, W.1    Carfi, A.2    Lee, K.H.3
  • 17
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor
    • 18615077
    • Lee JE Fusco ML Hessell AJ: Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature. 2008;454(7201):177-182. 18615077 10.1038/nature07082 2700032
    • (2008) Nature , vol.454 , Issue.7201 , pp. 177-182
    • Lee, J.E.1    Fusco, M.L.2    Hessell, A.J.3
  • 18
    • 84908332680 scopus 로고    scopus 로고
    • Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of phosphorylated STAT1
    • 25121748
    • Xu W Edwards MR Borek DM: Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of phosphorylated STAT1. Cell Host Microbe. 2014;16(2):187-200. 25121748 10.1016/j.chom.2014.07.008 4188415
    • (2014) Cell Host Microbe , vol.16 , Issue.2 , pp. 187-200
    • Xu, W.1    Edwards, M.R.2    Borek, D.M.3
  • 19
    • 33646754920 scopus 로고    scopus 로고
    • Ebola virus VP24 binds karyopherin alpha1 and blocks STAT1 nuclear accumulation
    • 16698996
    • Reid SP Leung LW Hartman AL: Ebola virus VP24 binds karyopherin alpha1 and blocks STAT1 nuclear accumulation. J Virol. 2006;80(11):5156-5167. 16698996 10.1128/JVI.02349-05 1472181
    • (2006) J Virol , vol.80 , Issue.11 , pp. 5156-5167
    • Reid, S.P.1    Leung, L.W.2    Hartman, A.L.3
  • 20
    • 84875436143 scopus 로고    scopus 로고
    • Inhibition of α-helix-mediated protein-protein interactions using designed molecules
    • 23422557
    • Azzarito V Long K Murphy NS: Inhibition of α-helix-mediated protein-protein interactions using designed molecules. Nat Chem. 2013;5(3):161-173. 23422557 10.1038/nchem.1568
    • (2013) Nat Chem , vol.5 , Issue.3 , pp. 161-173
    • Azzarito, V.1    Long, K.2    Murphy, N.S.3
  • 21
    • 0030877537 scopus 로고    scopus 로고
    • The origin and evolution of Ebola and Marburg viruses
    • 9254917
    • Suzuki Y Gojobori T: The origin and evolution of Ebola and Marburg viruses. Mol Biol Evol. 1997;14(8):800-806. 9254917 10.1093/oxfordjournals.molbev.a025820
    • (1997) Mol Biol Evol , vol.14 , Issue.8 , pp. 800-806
    • Suzuki, Y.1    Gojobori, T.2
  • 22
    • 0028246971 scopus 로고
    • Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein
    • 8122375
    • Feldmann H Nichol ST Klenk HD: Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein. Virology. 1994;199(2):469-473. 8122375 10.1006/viro.1994.1147
    • (1994) Virology , vol.199 , Issue.2 , pp. 469-473
    • Feldmann, H.1    Nichol, S.T.2    Klenk, H.D.3
  • 23
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2.0
    • 17846036
    • Larkin MA Blackshields G Brown NP: Clustal W and Clustal X version 2.0. Bioinformatics. 2007;23(21):2947-2948. 17846036 10.1093/bioinformatics/btm404
    • (2007) Bioinformatics , vol.23 , Issue.21 , pp. 2947-2948
    • Larkin, M.A.1    Blackshields, G.2    Brown, N.P.3
  • 24
    • 74549125386 scopus 로고    scopus 로고
    • SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building
    • 19854763
    • Gouy M Guindon S Gascuel O: SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building. Mol Biol Evol. 2010;27(2):221-224. 19854763 10.1093/molbev/msp259
    • (2010) Mol Biol Evol , vol.27 , Issue.2 , pp. 221-224
    • Gouy, M.1    Guindon, S.2    Gascuel, O.3
  • 25
    • 33746218852 scopus 로고    scopus 로고
    • MUSTANG: a multiple structural alignment algorithm
    • 16736488
    • Konagurthu AS Whisstock JC Stuckey PJ: MUSTANG: a multiple structural alignment algorithm. Proteins. 2006;64(3):559-574. 16736488 10.1002/prot.20921
    • (2006) Proteins , vol.64 , Issue.3 , pp. 559-574
    • Konagurthu, A.S.1    Whisstock, J.C.2    Stuckey, P.J.3
  • 26
    • 84903717697 scopus 로고    scopus 로고
    • Peptide entry inhibitors of enveloped viruses: the importance of interfacial hydrophobicity
    • 24780375
    • Badani H Garry RF Wimley WC: Peptide entry inhibitors of enveloped viruses: the importance of interfacial hydrophobicity. Biochim Biophys Acta. 2014;1838(9):2180-97. 24780375 10.1016/j.bbamem.2014.04.015
    • (2014) Biochim Biophys Acta , vol.1838 , Issue.9 , pp. 2180-2197
    • Badani, H.1    Garry, R.F.2    Wimley, W.C.3
  • 27
    • 0032568634 scopus 로고    scopus 로고
    • The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil
    • 9600912
    • Weissenhorn W Calder LJ Wharton SA: The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil. Proc Natl Acad Sci U S A. 1998;95(11):6032-6036. 9600912 10.1073/pnas.95.11.6032 27580
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.11 , pp. 6032-6036
    • Weissenhorn, W.1    Calder, L.J.2    Wharton, S.A.3
  • 28
    • 84860903741 scopus 로고    scopus 로고
    • The Ebola virus interferon antagonist VP24 directly binds STAT1 and has a novel, pyramidal fold
    • 22383882
    • Zhang AP Bornholdt ZA Liu T: The Ebola virus interferon antagonist VP24 directly binds STAT1 and has a novel, pyramidal fold. PLoS Pathog. 2012;8(2):e1002550. 22383882 10.1371/journal.ppat.1002550 3285596
    • (2012) PLoS Pathog , vol.8 , Issue.2 , pp. e1002550
    • Zhang, A.P.1    Bornholdt, Z.A.2    Liu, T.3
  • 29
    • 84924970701 scopus 로고    scopus 로고
    • Correlating the ability of VP24 protein from Ebola and Marburg viruses to bind human karyopherin to their immune suppression mechanism and pathogenicity using computational methods [v1; ref status: awaiting peer review
    • Chakraborty S Rao B Asgeirsson B: Correlating the ability of VP24 protein from Ebola and Marburg viruses to bind human karyopherin to their immune suppression mechanism and pathogenicity using computational methods [v1; ref status: awaiting peer review, http://f1000r.es/4o3]. F1000Res. 2014;3:265. 10.12688/f1000research.5666.1
    • (2014) F1000Res , vol.3 , pp. 265
    • Chakraborty, S.1    Rao, B.2    Asgeirsson, B.3
  • 30
    • 0026034332 scopus 로고
    • Seroepidemiological study of filovirus related to Ebola in the Philippines
    • 1671441
    • Miranda ME White ME Dayrit MM: Seroepidemiological study of filovirus related to Ebola in the Philippines. Lancet. 1991;337(8738):425-426. 1671441 10.1016/0140-6736(91)91199-5
    • (1991) Lancet , vol.337 , Issue.8738 , pp. 425-426
    • Miranda, M.E.1    White, M.E.2    Dayrit, M.M.3
  • 31
    • 80054768375 scopus 로고    scopus 로고
    • Reston Ebolavirus in humans and animals in the Philippines: a review
    • 21987747
    • Miranda ME Miranda NL: Reston Ebolavirus in humans and animals in the Philippines: a review. J Infect Dis. 2011;204(Suppl 3):S757-S760. 21987747 10.1093/infdis/jir296
    • (2011) J Infect Dis , vol.204 , pp. S757-S760
    • Miranda, M.E.1    Miranda, N.L.2
  • 32
    • 77649195743 scopus 로고    scopus 로고
    • Marburg virus evades interferon responses by a mechanism distinct from Ebola virus
    • 20084112
    • Valmas C Grosch MN Schumann M: Marburg virus evades interferon responses by a mechanism distinct from Ebola virus. PLoS Pathog. 2010;6(1):e1000721. 20084112 10.1371/journal.ppat.1000721 2799553
    • (2010) PLoS Pathog , vol.6 , Issue.1 , pp. e1000721
    • Valmas, C.1    Grosch, M.N.2    Schumann, M.3
  • 33
    • 58849098002 scopus 로고    scopus 로고
    • Structure of the Ebola VP35 interferon inhibitory domain
    • 19122151
    • Leung DW Ginder ND Fulton DB: Structure of the Ebola VP35 interferon inhibitory domain. Proc Natl Acad Sci U S A. 2009;106(2):411-416. 19122151 10.1073/pnas.0807854106 2626716
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.2 , pp. 411-416
    • Leung, D.W.1    Ginder, N.D.2    Fulton, D.B.3
  • 34
    • 76249120477 scopus 로고    scopus 로고
    • Ebolavirus VP35 uses a bimodal strategy to bind dsRNA for innate immune suppression
    • 20018665
    • Kimberlin CR Bornholdt ZA Li S: Ebolavirus VP35 uses a bimodal strategy to bind dsRNA for innate immune suppression. Proc Natl Acad Sci U S A. 2010;107(1):314-319. 20018665 10.1073/pnas.0910547107 2806767
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.1 , pp. 314-319
    • Kimberlin, C.R.1    Bornholdt, Z.A.2    Li, S.3
  • 35
    • 0035179356 scopus 로고    scopus 로고
    • Crystal structure of transcription factor malt domain iii: a novel helix repeat fold implicated in regulated oligomerization
    • 11709169
    • Steegborn C Danot O Huber R: Crystal structure of transcription factor malt domain iii: a novel helix repeat fold implicated in regulated oligomerization. Structure. 2001;9(11):1051-1060. 11709169 10.1016/S0969-2126(01)00665-7
    • (2001) Structure , vol.9 , Issue.11 , pp. 1051-1060
    • Steegborn, C.1    Danot, O.2    Huber, R.3
  • 36
    • 77956231836 scopus 로고    scopus 로고
    • Genetic factors of Ebola virus virulence in guinea pigs
    • 20654661
    • Subbotina E Dadaeva A Kachko A: Genetic factors of Ebola virus virulence in guinea pigs. Virus Res. 2010;153(1):121-133. 20654661 10.1016/j.virusres.2010.07.015
    • (2010) Virus Res , vol.153 , Issue.1 , pp. 121-133
    • Subbotina, E.1    Dadaeva, A.2    Kachko, A.3
  • 37
    • 84899641278 scopus 로고    scopus 로고
    • In silico derived small molecules bind the filovirus VP35 protein and inhibit its polymerase cofactor activity
    • 24495995
    • Brown CS Lee MS Leung DW: In silico derived small molecules bind the filovirus VP35 protein and inhibit its polymerase cofactor activity. J Mol Biol. 2014;426(10):2045-2048. 24495995 10.1016/j.jmb.2014.01.010
    • (2014) J Mol Biol , vol.426 , Issue.10 , pp. 2045-2048
    • Brown, C.S.1    Lee, M.S.2    Leung, D.W.3
  • 38
    • 84923345145 scopus 로고    scopus 로고
    • A common feature pharmacophore for FDA-approved drugs inhibiting the Ebola virus[v2; ref status: indexed
    • Ekins S Freundlich JS Coffee DW: A common feature pharmacophore for FDA-approved drugs inhibiting the Ebola virus [v2; ref status: indexed, http://f1000r.es/4wt]. F1000 Res. 2014;3:277. 10.12688/f1000research.5741.2
    • (2014) F1000 Res , vol.3 , pp. 277
    • Ekins, S.1    Freundlich, J.S.2    Coffee, D.W.3
  • 39
    • 79958741408 scopus 로고    scopus 로고
    • Intrinsically disordered proteins from A to Z
    • 21501695
    • Uversky VN: Intrinsically disordered proteins from A to Z. Int J Biochem Cell Biol. 2011;43(8):1090-1103. 21501695 10.1016/j.biocel.2011.04.001
    • (2011) Int J Biochem Cell Biol , vol.43 , Issue.8 , pp. 1090-1103
    • Uversky, V.N.1
  • 40
    • 84878483268 scopus 로고    scopus 로고
    • The secret life of viral entry glycoproteins: moonlighting in immune evasion
    • 23696729
    • Cook JD Lee JE: The secret life of viral entry glycoproteins: moonlighting in immune evasion. PLoS Pathog. 2013;9(5):e1003258. 23696729 10.1371/journal.ppat.1003258 3656028
    • (2013) PLoS Pathog , vol.9 , Issue.5 , pp. e1003258
    • Cook, J.D.1    Lee, J.E.2
  • 41
    • 84907017637 scopus 로고    scopus 로고
    • The structure of the C-terminal domain of the Zaire ebolavirus nucleoprotein
    • 25195755
    • Dziubanska PJ Derewenda U Ellena JF: The structure of the C-terminal domain of the Zaire ebolavirus nucleoprotein. Acta Crystallogr D Biol Crystallogr. 2014;70(Pt 9):2420-2429. 25195755 10.1107/S1399004714014710 4157450
    • (2014) Acta Crystallogr D Biol Crystallogr , vol.70 , pp. 2420-2429
    • Dziubanska, P.J.1    Derewenda, U.2    Ellena, J.F.3
  • 42
    • 84907537018 scopus 로고    scopus 로고
    • The alphabet of intrinsic disorder: II. various roles of glutamic acid in ordered and intrinsically disordered proteins
    • Uversky VN: The alphabet of intrinsic disorder: II. various roles of glutamic acid in ordered and intrinsically disordered proteins. Intrinsically Disord Proteins. 2013;1:18-40. 10.4161/idp.24684
    • (2013) Intrinsically Disord Proteins , vol.1 , pp. 18-40
    • Uversky, V.N.1
  • 43
    • 33644777658 scopus 로고    scopus 로고
    • Global suppression of the host antiviral response by Ebola- and Marburgviruses: increased antagonism of the type i interferon response is associated with enhanced virulence
    • 16501110
    • Kash JC Mühlberger E Carter V: Global suppression of the host antiviral response by Ebola- and Marburgviruses: increased antagonism of the type i interferon response is associated with enhanced virulence. J Virol. 2006;80(6):3009-3020. 16501110 10.1128/JVI.80.6.3009-3020.2006 1395418
    • (2006) J Virol , vol.80 , Issue.6 , pp. 3009-3020
    • Kash, J.C.1    Mühlberger, E.2    Carter, V.3
  • 44
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • 18075579
    • Wells JA McClendon CL: Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature. 2007;450(7172):1001-1009. 18075579 10.1038/nature06526
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 45
    • 0142149164 scopus 로고    scopus 로고
    • Oligomerization of Ebola virus VP30 is essential for viral transcription and can be inhibited by a synthetic peptide
    • 12912982
    • Hartlieb B Modrof J Mühlberger E: Oligomerization of Ebola virus VP30 is essential for viral transcription and can be inhibited by a synthetic peptide. J Biol Chem. 2003;278(43):41830-41836. 12912982 10.1074/jbc.M307036200
    • (2003) J Biol Chem , vol.278 , Issue.43 , pp. 41830-41836
    • Hartlieb, B.1    Modrof, J.2    Mühlberger, E.3
  • 46
    • 34447263302 scopus 로고    scopus 로고
    • Peptide-mediated interference with influenza A virus polymerase
    • 17494067
    • Ghanem A Mayer D Chase G: Peptide-mediated interference with influenza A virus polymerase. J Virol. 2007;81(14):7801-7804. 17494067 10.1128/JVI.00724-07 1933368
    • (2007) J Virol , vol.81 , Issue.14 , pp. 7801-7804
    • Ghanem, A.1    Mayer, D.2    Chase, G.3
  • 47
    • 4644308020 scopus 로고    scopus 로고
    • A highly stable short alpha-helix constrained by a main-chain hydrogen-bond surrogate
    • 15453743
    • Chapman RN Dimartino G Arora PS: A highly stable short alpha-helix constrained by a main-chain hydrogen-bond surrogate. J Am Chem Soc. 2004;126(39):12252-12253. 15453743 10.1021/ja0466659
    • (2004) J Am Chem Soc , vol.126 , Issue.39 , pp. 12252-12253
    • Chapman, R.N.1    Dimartino, G.2    Arora, P.S.3
  • 48
    • 77956294635 scopus 로고    scopus 로고
    • Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic
    • 20660316
    • Bird GH Madani N Perry AF: Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic. Proc Natl Acad Sci U S A. 2010;107(32):14093-14098. 20660316 10.1073/pnas.1002713107 2922607
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.32 , pp. 14093-14098
    • Bird, G.H.1    Madani, N.2    Perry, A.F.3
  • 49
    • 84899715084 scopus 로고    scopus 로고
    • Mucosal delivery of a double-stapled RSV peptide prevents nasopulmonary infection
    • 24743147
    • Bird GH Boyapalle S Wong T: Mucosal delivery of a double-stapled RSV peptide prevents nasopulmonary infection. J Clin Invest. 2014;124(5):2113-24. 24743147 10.1172/JCI71856 4001541
    • (2014) J Clin Invest , vol.124 , Issue.5 , pp. 2113-2124
    • Bird, G.H.1    Boyapalle, S.2    Wong, T.3
  • 50
    • 77955369875 scopus 로고    scopus 로고
    • Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency
    • 20543141
    • Harrison RS Shepherd NE Hoang HN: Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency. Proc Natl Acad Sci U S A. 2010;107(26):11686-11691. 20543141 10.1073/pnas.1002498107 2900680
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.26 , pp. 11686-11691
    • Harrison, R.S.1    Shepherd, N.E.2    Hoang, H.N.3
  • 51
    • 0037229321 scopus 로고    scopus 로고
    • Identification of protective epitopes on Ebola virus glycoprotein at the single amino acid level by using recombinant vesicular stomatitis viruses
    • 12502822
    • Takada A Feldmann H Stroeher U: Identification of protective epitopes on Ebola virus glycoprotein at the single amino acid level by using recombinant vesicular stomatitis viruses. J Virol. 2003;77(2):1069-1074. 12502822 10.1128/JVI.77.2.1069-1074.2003 140786
    • (2003) J Virol , vol.77 , Issue.2 , pp. 1069-1074
    • Takada, A.1    Feldmann, H.2    Stroeher, U.3
  • 52
    • 0034051595 scopus 로고    scopus 로고
    • Epitopes involved in antibody-mediated protection from Ebola virus
    • 10698744
    • Wilson JA Hevey M Bakken R: Epitopes involved in antibody-mediated protection from Ebola virus. Science. 2000;287(5458):1664-1666. 10698744 10.1126/science.287.5458.1664
    • (2000) Science , vol.287 , Issue.5458 , pp. 1664-1666
    • Wilson, J.A.1    Hevey, M.2    Bakken, R.3
  • 53
    • 33845584363 scopus 로고    scopus 로고
    • Protective efficacy of neutralizing antibodies against Ebola Virus infection
    • 17055127
    • Takada A Ebihara H Jones S: Protective efficacy of neutralizing antibodies against Ebola Virus infection. Vaccine. 2007;25(6):993-999. 17055127 10.1016/j.vaccine.2006.09.076
    • (2007) Vaccine , vol.25 , Issue.6 , pp. 993-999
    • Takada, A.1    Ebihara, H.2    Jones, S.3
  • 54
    • 80054837546 scopus 로고    scopus 로고
    • Characterization of Zaire ebolavirus glycoprotein-specific monoclonal antibodies
    • 21925951
    • Qiu X Alimonti JB Melito PL: Characterization of Zaire ebolavirus glycoprotein-specific monoclonal antibodies. Clin Immunol. 2011;141(2):218-227. 21925951 10.1016/j.clim.2011.08.008
    • (2011) Clin Immunol , vol.141 , Issue.2 , pp. 218-227
    • Qiu, X.1    Alimonti, J.B.2    Melito, P.L.3
  • 55
    • 84907263545 scopus 로고    scopus 로고
    • Reversion of advanced Ebola virus disease in nonhuman primates with ZMapp
    • 25171469
    • Qiu X Wong G Audet J: Reversion of advanced Ebola virus disease in nonhuman primates with ZMapp. Nature. 2014;514(7520):47-53. 25171469 10.1038/nature13777 4214273
    • (2014) Nature , vol.514 , Issue.7520 , pp. 47-53
    • Qiu, X.1    Wong, G.2    Audet, J.3
  • 56
    • 84868149422 scopus 로고    scopus 로고
    • Delayed treatment of Ebola virus infection with plant-derived monoclonal antibodies provides protection in rhesus macaques
    • 23071322, 3497800
    • Olinger GG Jr Pettitt J Kim D: Delayed treatment of Ebola virus infection with plant-derived monoclonal antibodies provides protection in rhesus macaques. Proc Natl Acad Sci U S A. 2012;109(44):18030-18035. 23071322 10.1073/pnas.1213709109 3497800
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.44 , pp. 18030-18035
    • Olinger Jr, G.G.1    Pettitt, J.2    Kim, D.3


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