메뉴 건너뛰기




Volumn 106, Issue 7, 2014, Pages 1447-1456

PH-ontrolled two-step uncoating of influenza virus

Author keywords

[No Author keywords available]

Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ; LIPOSOME; M2 PROTEIN, INFLUENZA A VIRUS; MATRIX PROTEIN; RIBONUCLEOPROTEIN; VIRUS PROTEIN;

EID: 84897425911     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.02.018     Document Type: Article
Times cited : (102)

References (42)
  • 1
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • J.J. Skehel, and D.C. Wiley Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin Annu. Rev. Biochem. 69 2000 531 569
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 3
    • 31444441789 scopus 로고    scopus 로고
    • Architecture of ribonucleoprotein complexes in influenza A virus particles
    • DOI 10.1038/nature04378, PII NATURE04378
    • T. Noda, and H. Sagara Y. Kawaoka Architecture of ribonucleoprotein complexes in influenza A virus particles Nature 439 2006 490 492 (Pubitemid 43152841)
    • (2006) Nature , vol.439 , Issue.7075 , pp. 490-492
    • Noda, T.1    Sagara, H.2    Yen, A.3    Takada, A.4    Kida, H.5    Cheng, R.H.6    Kawaoka, Y.7
  • 4
    • 0033946767 scopus 로고    scopus 로고
    • Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins
    • DOI 10.1128/JVI.74.4.1781-1786.2000
    • M. Bui, and E.G. Wills G.R. Whittaker Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins J. Virol. 74 2000 1781 1786 (Pubitemid 30434036)
    • (2000) Journal of Virology , vol.74 , Issue.4 , pp. 1781-1786
    • Bui, M.1    Wills, E.G.2    Helenius, A.3    Whittaker, G.R.4
  • 5
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleoproteins: The viral matrix protein (M1) promotes export and inhibits import
    • K. Martin, and A. Helenius Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import Cell 67 1991 117 130 (Pubitemid 121001429)
    • (1991) Cell , vol.67 , Issue.1 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 6
    • 0037690744 scopus 로고    scopus 로고
    • Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses
    • S.B. Sieczkarski, and G.R. Whittaker Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses Traffic 4 2003 333 343 (Pubitemid 36588337)
    • (2003) Traffic , vol.4 , Issue.5 , pp. 333-343
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 8
    • 84857981961 scopus 로고    scopus 로고
    • Structural changes in Influenza virus at low pH characterized by cryo-electron tomography
    • J. Fontana, and G. Cardone A.C. Steven Structural changes in Influenza virus at low pH characterized by cryo-electron tomography J. Virol. 86 2012 2919 2929
    • (2012) J. Virol. , vol.86 , pp. 2919-2929
    • Fontana, J.1    Cardone, G.2    Steven, A.C.3
  • 9
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • DOI 10.1146/annurev.biochem.72.121801.161504
    • L.V. Chernomordik, and M.M. Kozlov Protein-lipid interplay in fusion and fission of biological membranes Annu. Rev. Biochem. 72 2003 175 207 (Pubitemid 36930445)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 11
    • 10244229625 scopus 로고    scopus 로고
    • Deformation and collapse of microtubules on the nanometer scale
    • P.J. de Pablo, and I.A. Schaap C.F. Schmidt Deformation and collapse of microtubules on the nanometer scale Phys. Rev. Lett. 91 2003 098101
    • (2003) Phys. Rev. Lett. , vol.91 , pp. 098101
    • De Pablo, P.J.1    Schaap, I.A.2    Schmidt, C.F.3
  • 13
    • 80054763139 scopus 로고    scopus 로고
    • How to perform a nanoindentation experiment on a virus
    • W.H. Roos How to perform a nanoindentation experiment on a virus Methods Mol. Biol. 783 2011 251 264
    • (2011) Methods Mol. Biol. , vol.783 , pp. 251-264
    • Roos, W.H.1
  • 14
    • 79551677164 scopus 로고    scopus 로고
    • Bending and puncturing the influenza lipid envelope
    • S. Li, and F. Eghiaian I.A. Schaap Bending and puncturing the influenza lipid envelope Biophys. J. 100 2011 637 645
    • (2011) Biophys. J. , vol.100 , pp. 637-645
    • Li, S.1    Eghiaian, F.2    Schaap, I.A.3
  • 15
    • 84870362776 scopus 로고    scopus 로고
    • Effect of envelope proteins on the mechanical properties of influenza virus
    • I.A. Schaap, and F. Eghiaian C. Veigel Effect of envelope proteins on the mechanical properties of influenza virus J. Biol. Chem. 287 2012 41078 41088
    • (2012) J. Biol. Chem. , vol.287 , pp. 41078-41088
    • Schaap, I.A.1    Eghiaian, F.2    Veigel, C.3
  • 17
    • 0015491828 scopus 로고
    • Crystalline antigen from the influenza virus envelope
    • C.M. Brand, and J.J. Skehel Crystalline antigen from the influenza virus envelope Nat. New Biol. 238 1972 145 147
    • (1972) Nat. New Biol. , vol.238 , pp. 145-147
    • Brand, C.M.1    Skehel, J.J.2
  • 18
    • 80054756416 scopus 로고    scopus 로고
    • Structural and dynamic characterization of biochemical processes by atomic force microscopy
    • F. Eghiaian, and I.A. Schaap Structural and dynamic characterization of biochemical processes by atomic force microscopy Methods Mol. Biol. 778 2011 71 95
    • (2011) Methods Mol. Biol. , vol.778 , pp. 71-95
    • Eghiaian, F.1    Schaap, I.A.2
  • 19
    • 33845792555 scopus 로고    scopus 로고
    • CellProfiler: Image analysis software for identifying and quantifying cell phenotypes
    • A.E. Carpenter, and T.R. Jones D.M. Sabatini CellProfiler: image analysis software for identifying and quantifying cell phenotypes Genome Biol. 7 2006 R100
    • (2006) Genome Biol. , vol.7 , pp. 100
    • Carpenter, A.E.1    Jones, T.R.2    Sabatini, D.M.3
  • 20
    • 65249164886 scopus 로고    scopus 로고
    • The capillarity of nanometric water menisci confined inside closed-geometry viral cages
    • C. Carrasco, and M. Douas P.J. de Pablo The capillarity of nanometric water menisci confined inside closed-geometry viral cages Proc. Natl. Acad. Sci. USA 106 2009 5475 5480
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5475-5480
    • Carrasco, C.1    Douas, M.2    De Pablo, P.J.3
  • 21
    • 0028053969 scopus 로고
    • Kinetics of the low pH-induced conformational changes and fusogenic activity of influenza hemagglutinin
    • M. Krumbiegel, A. Herrmann, and R. Blumenthal Kinetics of the low pH-induced conformational changes and fusogenic activity of influenza hemagglutinin Biophys. J. 67 1994 2355 2360 (Pubitemid 24369658)
    • (1994) Biophysical Journal , vol.67 , Issue.6 , pp. 2355-2360
    • Krumbiegel, M.1    Herrmann, A.2    Blumenthal, R.3
  • 22
  • 23
    • 77950528480 scopus 로고    scopus 로고
    • Architecture of a nascent viral fusion pore
    • K.K. Lee Architecture of a nascent viral fusion pore EMBO J. 29 2010 1299 1311
    • (2010) EMBO J. , vol.29 , pp. 1299-1311
    • Lee, K.K.1
  • 25
    • 84857926431 scopus 로고    scopus 로고
    • The molten globule state is unusually deformable under mechanical force
    • P.J. Elms, and J.D. Chodera S. Marqusee The molten globule state is unusually deformable under mechanical force Proc. Natl. Acad. Sci. USA 109 2012 3796 3801
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 3796-3801
    • Elms, P.J.1    Chodera, J.D.2    Marqusee, S.3
  • 26
    • 34250792678 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles
    • DOI 10.1128/JVI.00361-07
    • B.J. Chen, and G.P. Leser R.A. Lamb Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles J. Virol. 81 2007 7111 7123 (Pubitemid 46986647)
    • (2007) Journal of Virology , vol.81 , Issue.13 , pp. 7111-7123
    • Chen, B.J.1    Leser, G.P.2    Morita, E.3    Lamb, R.A.4
  • 27
    • 0035264603 scopus 로고    scopus 로고
    • In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
    • DOI 10.1006/viro.2000.0804
    • F. Baudin, and I. Petit R.W. Ruigrok In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein Virology 281 2001 102 108 (Pubitemid 32911530)
    • (2001) Virology , vol.281 , Issue.1 , pp. 102-108
    • Baudin, F.1    Petit, I.2    Weissenhorn, W.3    Ruigrok, R.W.H.4
  • 29
    • 84863393147 scopus 로고    scopus 로고
    • A supramolecular assembly formed by influenza A virus genomic RNA segments
    • E. Fournier, and V. Moules R. Marquet A supramolecular assembly formed by influenza A virus genomic RNA segments Nucleic Acids Res. 40 2012 2197 2209
    • (2012) Nucleic Acids Res. , vol.40 , pp. 2197-2209
    • Fournier, E.1    Moules, V.2    Marquet, R.3
  • 30
    • 84856704565 scopus 로고    scopus 로고
    • Three-dimensional analysis of ribonucleoprotein complexes in influenza A virus
    • T. Noda, and Y. Sugita Y. Kawaoka Three-dimensional analysis of ribonucleoprotein complexes in influenza A virus Nat. Commun. 3 2012 639
    • (2012) Nat. Commun. , vol.3 , pp. 639
    • Noda, T.1    Sugita, Y.2    Kawaoka, Y.3
  • 32
    • 0033060915 scopus 로고    scopus 로고
    • Conformational intermediates and fusion activity of influenza virus hemagglutinin
    • T. Korte, and K. Ludwig A. Herrmann Conformational intermediates and fusion activity of influenza virus hemagglutinin J. Virol. 73 1999 4567 4574 (Pubitemid 29246714)
    • (1999) Journal of Virology , vol.73 , Issue.6 , pp. 4567-4574
    • Korte, T.1    Ludwig, K.2    Booy, F.P.3    Blumenthal, R.4    Herrmann, A.5
  • 33
    • 0039114981 scopus 로고    scopus 로고
    • Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope
    • D.J. Müller, and D. Fotiadis A. Engel Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope Biophys. J. 76 1999 1101 1111 (Pubitemid 29264591)
    • (1999) Biophysical Journal , vol.76 , Issue.2 , pp. 1101-1111
    • Muller, D.J.1    Fotiadis, D.2    Scheuring, S.3    Muller, S.A.4    Engel, A.5
  • 34
    • 0036151820 scopus 로고    scopus 로고
    • Protonation and stability of the globular domain of influenza virus hemagglutinin
    • Q. Huang, and R. Opitz A. Herrmann Protonation and stability of the globular domain of influenza virus hemagglutinin Biophys. J. 82 2002 1050 1058 (Pubitemid 34111241)
    • (2002) Biophysical Journal , vol.82 , Issue.2 , pp. 1050-1058
    • Huang, Q.1    Opitz, R.2    Knapp, E.-W.3    Herrmann, A.4
  • 36
    • 0028176704 scopus 로고
    • The intrinsic pKa values for phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine in monolayers deposited on mercury electrodes
    • M.R. Moncelli, L. Becucci, and R. Guidelli The intrinsic pKa values for phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine in monolayers deposited on mercury electrodes Biophys. J. 66 1994 1969 1980
    • (1994) Biophys. J. , vol.66 , pp. 1969-1980
    • Moncelli, M.R.1    Becucci, L.2    Guidelli, R.3
  • 40
    • 0028170284 scopus 로고
    • PH-dependent binding of the fluorophore bis-ANS to influenza virus reflects the conformational change of hemagglutinin
    • T. Korte, and A. Herrmann pH-dependent binding of the fluorophore bis-ANS to influenza virus reflects the conformational change of hemagglutinin Eur. Biophys. J. 23 1994 105 113
    • (1994) Eur. Biophys. J. , vol.23 , pp. 105-113
    • Korte, T.1    Herrmann, A.2
  • 41
    • 0028198382 scopus 로고
    • On the validity of lipid dequenching assays for estimating virus fusion kinetics
    • DOI 10.1016/0005-2736(94)90095-7
    • A. Arbuzova, and T. Korte A. Herrmann On the validity of lipid dequenching assays for estimating virus fusion kinetics Biochim. Biophys. Acta 1190 1994 360 366 (Pubitemid 24098499)
    • (1994) Biochimica et Biophysica Acta - Biomembranes , vol.1190 , Issue.2 , pp. 360-366
    • Arbuzova, A.1    Korte, T.2    Muller, P.3    Herrmann, A.4
  • 42
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • DOI 10.1016/0003-2697(87)90587-2
    • H. Schägger, and G. von Jagow Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 166 1987 368 379 (Pubitemid 18004907)
    • (1987) Analytical Biochemistry , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.