메뉴 건너뛰기




Volumn 55, Issue 2, 2011, Pages 696-702

Identification of high-affinity PB1-derived peptides with enhanced affinity to the PA protein of influenza A virus polymerase

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARTIC ACID; PROTEIN PA; PROTEIN PB1; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 78751681564     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01419-10     Document Type: Article
Times cited : (48)

References (23)
  • 1
    • 0029793810 scopus 로고    scopus 로고
    • Influenza virus polymerase basic protein 1 interacts with influenza virus polymerase basic protein 2 at multiple sites
    • Biswas, S. K., and D. P. Nayak. 1996. Influenza virus polymerase basic protein 1 interacts with influenza virus polymerase basic protein 2 at multiple sites. J. Virol. 70:6716-6722.
    • (1996) J. Virol. , vol.70 , pp. 6716-6722
    • Biswas, S.K.1    Nayak, D.P.2
  • 2
    • 67249130012 scopus 로고    scopus 로고
    • The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit
    • Dias, A., et al. 2009. The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit. Nature 458:914-918.
    • (2009) Nature , vol.458 , pp. 914-918
    • Dias, A.1
  • 3
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert, D. M., V. N. Malashkevich, L. H. Hong, P. A. Carr, and P. S. Kim. 1999. Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 99:103-115.
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 4
    • 0030329981 scopus 로고    scopus 로고
    • SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes
    • Frank, R., and H. Overwin. 1996. SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes. Methods Mol. Biol. 66:149-169.
    • (1996) Methods Mol. Biol. , vol.66 , pp. 149-169
    • Frank, R.1    Overwin, H.2
  • 6
    • 43249128376 scopus 로고    scopus 로고
    • The structural basis for cap binding by influenza virus polymerase subunit PB2
    • Guilligay, D., et al. 2008. The structural basis for cap binding by influenza virus polymerase subunit PB2. Nat. Struct. Mol. Biol. 15:500-506.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 500-506
    • Guilligay, D.1
  • 7
    • 77955369875 scopus 로고    scopus 로고
    • Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency
    • Harrison, R. S., et al. Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency. Proc. Natl. Acad. Sci. U. S. A. 107:11686-11691.
    • Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 11686-11691
    • Harrison, R.S.1
  • 8
    • 50649089174 scopus 로고    scopus 로고
    • Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus
    • He, X., et al. 2008. Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus. Nature 454:1123-1126.
    • (2008) Nature , vol.454 , pp. 1123-1126
    • He, X.1
  • 9
    • 64049093748 scopus 로고    scopus 로고
    • Detection and characterization of influenza a virus PA-PB2 interaction through a bimolecular fluorescence complementation assay
    • Hemerka, J. N., et al. 2009. Detection and characterization of influenza A virus PA-PB2 interaction through a bimolecular fluorescence complementation assay. J. Virol. 83:3944-3955.
    • (2009) J. Virol. , vol.83 , pp. 3944-3955
    • Hemerka, J.N.1
  • 10
    • 51649083754 scopus 로고    scopus 로고
    • Design of peptide inhibitors for the importin alpha/beta nuclear import pathway by activity-based profiling
    • Kosugi, S., et al. 2008. Design of peptide inhibitors for the importin alpha/beta nuclear import pathway by activity-based profiling. Chem. Biol. 15:940-949.
    • (2008) Chem. Biol. , vol.15 , pp. 940-949
    • Kosugi, S.1
  • 11
    • 76249105085 scopus 로고    scopus 로고
    • Molecular basis of the interaction for an essential subunit PA-PB1 in influenza virus RNA polymerase: Insights from molecular dynamics simulation and free energy calculation
    • Liu, H., and X. Yao. Molecular basis of the interaction for an essential subunit PA-PB1 in influenza virus RNA polymerase: insights from molecular dynamics simulation and free energy calculation. Mol. Pharm. 7:75-85.
    • Mol. Pharm. , vol.7 , pp. 75-85
    • Liu, H.1    Yao, X.2
  • 12
    • 34147137981 scopus 로고    scopus 로고
    • Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide
    • Munch, J., et al. 2007. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. Cell 129:263-275.
    • (2007) Cell , vol.129 , pp. 263-275
    • Munch, J.1
  • 13
    • 50649122962 scopus 로고    scopus 로고
    • The structural basis for an essential subunit interaction in influenza virus RNA polymerase
    • Obayashi, E., et al. 2008. The structural basis for an essential subunit interaction in influenza virus RNA polymerase. Nature 454:1127-1131.
    • (2008) Nature , vol.454 , pp. 1127-1131
    • Obayashi, E.1
  • 14
    • 0036219058 scopus 로고    scopus 로고
    • Fine mapping of the subunit binding sites of influenza virus RNA polymerase
    • Ohtsu, Y., Y. Honda, Y. Sakata, H. Kato, and T. Toyoda. 2002. Fine mapping of the subunit binding sites of influenza virus RNA polymerase. Microbiol. Immunol. 46:167-175.
    • (2002) Microbiol. Immunol. , vol.46 , pp. 167-175
    • Ohtsu, Y.1    Honda, Y.2    Sakata, Y.3    Kato, H.4    Toyoda, T.5
  • 15
    • 0028865474 scopus 로고
    • A 48-amino-acid region of influenza a virus PB1 protein is sufficient for complex formation with PA
    • Perez, D. R., and R. O. Donis. 1995. A 48-amino-acid region of influenza A virus PB1 protein is sufficient for complex formation with PA. J. Virol. 69:6932-6939.
    • (1995) J. Virol. , vol.69 , pp. 6932-6939
    • Perez, D.R.1    Donis, R.O.2
  • 16
    • 0034864841 scopus 로고    scopus 로고
    • Functional analysis of PA binding by influenza a virus PB1: Effects on polymerase activity and viral infectivity
    • Perez, D. R., and R. O. Donis. 2001. Functional analysis of PA binding by influenza A virus PB1: effects on polymerase activity and viral infectivity. J. Virol. 75:8127-8136.
    • (2001) J. Virol. , vol.75 , pp. 8127-8136
    • Perez, D.R.1    Donis, R.O.2
  • 17
    • 77749322610 scopus 로고    scopus 로고
    • Towards an atomic resolution understanding of the influenza virus replication machinery
    • Ruigrok, R. W., T. Crepin, D. J. Hart, and S. Cusack. Towards an atomic resolution understanding of the influenza virus replication machinery. Curr. Opin. Struct. Biol. 20:104-113.
    • Curr. Opin. Struct. Biol. , vol.20 , pp. 104-113
    • Ruigrok, R.W.1    Crepin, T.2    Hart, D.J.3    Cusack, S.4
  • 18
    • 59049093098 scopus 로고    scopus 로고
    • The influenza virus enigma
    • Salomon, R., and R. G. Webster. 2009. The influenza virus enigma. Cell 136:402-410.
    • (2009) Cell , vol.136 , pp. 402-410
    • Salomon, R.1    Webster, R.G.2
  • 19
    • 67649552964 scopus 로고    scopus 로고
    • Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase
    • Sugiyama, K., et al. 2009. Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase. EMBO J. 28:1803-1811.
    • (2009) EMBO J. , vol.28 , pp. 1803-1811
    • Sugiyama, K.1
  • 20
    • 21044441799 scopus 로고    scopus 로고
    • Rapid and quantitative cyclization of multiple peptide loops onto synthetic scaffolds for structural mimicry of protein surfaces
    • Timmerman, P., J. Beld, W. C. Puijk, and R. H. Meloen. 2005. Rapid and quantitative cyclization of multiple peptide loops onto synthetic scaffolds for structural mimicry of protein surfaces. Chembiochem 6:821-824.
    • (2005) Chembiochem , vol.6 , pp. 821-824
    • Timmerman, P.1    Beld, J.2    Puijk, W.C.3    Meloen, R.H.4
  • 21
    • 77952786167 scopus 로고    scopus 로고
    • Limited compatibility of polymerase subunit interactions in influenza a and B viruses
    • Wunderlich, K., et al. Limited compatibility of polymerase subunit interactions in influenza A and B viruses. J. Biol. Chem. 285:16704-16712.
    • J. Biol. Chem. , vol.285 , pp. 16704-16712
    • Wunderlich, K.1
  • 22
    • 70449571952 scopus 로고    scopus 로고
    • Identification of a PA-binding peptide with inhibitory activity against influenza a and B virus replication
    • Wunderlich, K., et al. 2009. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication. PLoS One 4:e7517.
    • (2009) PLoS One , vol.4
    • Wunderlich, K.1
  • 23
    • 67249100913 scopus 로고    scopus 로고
    • Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site
    • Yuan, P., et al. 2009. Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site. Nature 458:909-913.
    • (2009) Nature , vol.458 , pp. 909-913
    • Yuan, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.