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Volumn 1838, Issue 8, 2014, Pages 2026-2035

A peptide derived from the rotavirus outer capsid protein VP7 permeabilizes artificial membranes

Author keywords

ATR FTIR; Circular dichroism; Conformational rearrangement; Membranotropic peptide; NMR; Plasmon waveguide resonance

Indexed keywords

PEPTIDE DERIVATIVE; PROTEIN VP7;

EID: 84899771258     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.04.005     Document Type: Article
Times cited : (7)

References (80)
  • 1
    • 0001254548 scopus 로고    scopus 로고
    • Rotaviruses
    • K.D.N. B.N. Fields, P.M. Howley, R.M. Chanock, J.L. Melnick, T.P. Monath, B. Roizman, S.E. Straus, Lippincott-Raven Philadelphia, Pa
    • A.Z. Kapikian, and R.M. Chanock Rotaviruses K.D.N. B.N. Fields, P.M. Howley, R.M. Chanock, J.L. Melnick, T.P. Monath, B. Roizman, S.E. Straus, Fields virology 1996 Lippincott-Raven Philadelphia, Pa 1657 1708
    • (1996) Fields Virology , pp. 1657-1708
    • Kapikian, A.Z.1    Chanock, R.M.2
  • 2
    • 0000730162 scopus 로고    scopus 로고
    • Rotaviruses and their replication
    • K.D.N. B.N. Fields, P.M. Howley, R.M. Chanock, J.L. Melnick, T.P. Monath, B. Roizman, S.E. Straus, Lippincott-Raven Philadelphia, Pa
    • M.K. Estes Rotaviruses and their replication K.D.N. B.N. Fields, P.M. Howley, R.M. Chanock, J.L. Melnick, T.P. Monath, B. Roizman, S.E. Straus, Fields Virology 1996 Lippincott-Raven Philadelphia, Pa 1625 1655
    • (1996) Fields Virology , pp. 1625-1655
    • Estes, M.K.1
  • 5
    • 0018567957 scopus 로고
    • Structure of rotaviruses as studied by the freeze-drying technique
    • A. Roseto, J. Escaig, E. Delain, J. Cohen, and R. Scherrer Structure of rotaviruses as studied by the freeze-drying technique Virology 98 1979 471 475
    • (1979) Virology , vol.98 , pp. 471-475
    • Roseto, A.1    Escaig, J.2    Delain, E.3    Cohen, J.4    Scherrer, R.5
  • 7
    • 0025178591 scopus 로고
    • Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy
    • B.V. Prasad, J.W. Burns, E. Marietta, M.K. Estes, and W. Chiu Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy Nature 343 1990 476 479
    • (1990) Nature , vol.343 , pp. 476-479
    • Prasad, B.V.1    Burns, J.W.2    Marietta, E.3    Estes, M.K.4    Chiu, W.5
  • 8
    • 0028205688 scopus 로고
    • Three-dimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map analysis
    • M. Yeager, J.A. Berriman, T.S. Baker, and A.R. Bellamy Three-dimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map analysis Embo J. 13 1994 1011 1018
    • (1994) Embo J. , vol.13 , pp. 1011-1018
    • Yeager, M.1    Berriman, J.A.2    Baker, T.S.3    Bellamy, A.R.4
  • 9
    • 0033545985 scopus 로고    scopus 로고
    • Comparative structural analysis of transcriptionally competent and incompetent rotavirus-antibody complexes
    • J.A. Lawton, M.K. Estes, and B.V. Prasad Comparative structural analysis of transcriptionally competent and incompetent rotavirus-antibody complexes Proc. Natl. Acad. Sci. U. S. A. 96 1999 5428 5433
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5428-5433
    • Lawton, J.A.1    Estes, M.K.2    Prasad, B.V.3
  • 10
    • 0019440664 scopus 로고
    • Proteolytic enhancement of rotavirus infectivity: Molecular mechanisms
    • M.K. Estes, D.Y. Graham, and B.B. Mason Proteolytic enhancement of rotavirus infectivity: molecular mechanisms J. Virol. 39 1981 879 888
    • (1981) J. Virol. , vol.39 , pp. 879-888
    • Estes, M.K.1    Graham, D.Y.2    Mason, B.B.3
  • 11
    • 0026686139 scopus 로고
    • Interaction of rotavirus particles with liposomes
    • P. Nandi, A. Charpilienne, and J. Cohen Interaction of rotavirus particles with liposomes J. Virol. 66 1992 3363 3367
    • (1992) J. Virol. , vol.66 , pp. 3363-3367
    • Nandi, P.1    Charpilienne, A.2    Cohen, J.3
  • 13
    • 0025756384 scopus 로고
    • The VP8 fragment of VP4 is the rhesus rotavirus hemagglutinin
    • L. Fiore, H.B. Greenberg, and E.R. Mackow The VP8 fragment of VP4 is the rhesus rotavirus hemagglutinin Virology 181 1991 553 563
    • (1991) Virology , vol.181 , pp. 553-563
    • Fiore, L.1    Greenberg, H.B.2    Mackow, E.R.3
  • 15
    • 0036500085 scopus 로고    scopus 로고
    • The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site
    • P.R. Dormitzer, Z.Y. Sun, G. Wagner, and S.C. Harrison The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site Embo J. 21 2002 885 897
    • (2002) Embo J. , vol.21 , pp. 885-897
    • Dormitzer, P.R.1    Sun, Z.Y.2    Wagner, G.3    Harrison, S.C.4
  • 16
    • 4344695186 scopus 로고    scopus 로고
    • Structural rearrangements in the membrane penetration protein of a non-enveloped virus
    • P.R. Dormitzer, E.B. Nason, B.V. Prasad, and S.C. Harrison Structural rearrangements in the membrane penetration protein of a non-enveloped virus Nature 430 2004 1053 1058
    • (2004) Nature , vol.430 , pp. 1053-1058
    • Dormitzer, P.R.1    Nason, E.B.2    Prasad, B.V.3    Harrison, S.C.4
  • 18
    • 0034715826 scopus 로고    scopus 로고
    • Purified recombinant rotavirus VP7 forms soluble, calcium-dependent trimers
    • P.R. Dormitzer, H.B. Greenberg, and S.C. Harrison Purified recombinant rotavirus VP7 forms soluble, calcium-dependent trimers Virology 277 2000 420 428
    • (2000) Virology , vol.277 , pp. 420-428
    • Dormitzer, P.R.1    Greenberg, H.B.2    Harrison, S.C.3
  • 19
    • 0030998380 scopus 로고    scopus 로고
    • Rotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry into cells
    • B.S. Coulson, S.L. Londrigan, and D.J. Lee Rotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry into cells Proc. Natl. Acad. Sci. U. S. A. 94 1997 5389 5394
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5389-5394
    • Coulson, B.S.1    Londrigan, S.L.2    Lee, D.J.3
  • 20
    • 0141458927 scopus 로고    scopus 로고
    • Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 i domain via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7 during cell entry
    • K.L. Graham, P. Halasz, Y. Tan, M.J. Hewish, Y. Takada, E.R. Mackow, M.K. Robinson, and B.S. Coulson Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7 during cell entry J. Virol. 77 2003 9969 9978
    • (2003) J. Virol. , vol.77 , pp. 9969-9978
    • Graham, K.L.1    Halasz, P.2    Tan, Y.3    Hewish, M.J.4    Takada, Y.5    Mackow, E.R.6    Robinson, M.K.7    Coulson, B.S.8
  • 22
  • 23
    • 84861309287 scopus 로고    scopus 로고
    • Spike protein VP8* of human rotavirus recognizes histo-blood group antigens in a type-specific manner
    • P. Huang, M. Xia, M. Tan, W. Zhong, C. Wei, L. Wang, A. Morrow, and X. Jiang Spike protein VP8* of human rotavirus recognizes histo-blood group antigens in a type-specific manner J. Virol. 86 2012 4833 4843
    • (2012) J. Virol. , vol.86 , pp. 4833-4843
    • Huang, P.1    Xia, M.2    Tan, M.3    Zhong, W.4    Wei, C.5    Wang, L.6    Morrow, A.7    Jiang, X.8
  • 26
    • 33645750724 scopus 로고    scopus 로고
    • Alternative intermolecular contacts underlie the rotavirus VP5* two- to three-fold rearrangement
    • J.D. Yoder, and P.R. Dormitzer Alternative intermolecular contacts underlie the rotavirus VP5* two- to three-fold rearrangement Embo J. 25 2006 1559 1568
    • (2006) Embo J. , vol.25 , pp. 1559-1568
    • Yoder, J.D.1    Dormitzer, P.R.2
  • 27
    • 75449100099 scopus 로고    scopus 로고
    • A rotavirus spike protein conformational intermediate binds lipid bilayers
    • S.D. Trask, I.S. Kim, S.C. Harrison, and P.R. Dormitzer A rotavirus spike protein conformational intermediate binds lipid bilayers J. Virol. 84 2010 1764 1770
    • (2010) J. Virol. , vol.84 , pp. 1764-1770
    • Trask, S.D.1    Kim, I.S.2    Harrison, S.C.3    Dormitzer, P.R.4
  • 28
    • 79952111899 scopus 로고    scopus 로고
    • Flock house virus: A model system for understanding non-enveloped virus entry and membrane penetration
    • A. Odegard, M. Banerjee, and J.E. Johnson Flock house virus: a model system for understanding non-enveloped virus entry and membrane penetration Curr. Top. Microbiol. Immunol. 343 2010 1 22
    • (2010) Curr. Top. Microbiol. Immunol. , vol.343 , pp. 1-22
    • Odegard, A.1    Banerjee, M.2    Johnson, J.E.3
  • 32
    • 34547108622 scopus 로고    scopus 로고
    • Infectious bursal disease virus, a non-enveloped virus, possesses a capsid-associated peptide that deforms and perforates biological membranes
    • M. Galloux, S. Libersou, N. Morellet, S. Bouaziz, B. Da Costa, M. Ouldali, J. Lepault, and B. Delmas Infectious bursal disease virus, a non-enveloped virus, possesses a capsid-associated peptide that deforms and perforates biological membranes J. Biol. Chem. 282 2007 20774 20784
    • (2007) J. Biol. Chem. , vol.282 , pp. 20774-20784
    • Galloux, M.1    Libersou, S.2    Morellet, N.3    Bouaziz, S.4    Da Costa, B.5    Ouldali, M.6    Lepault, J.7    Delmas, B.8
  • 33
    • 42449151315 scopus 로고    scopus 로고
    • Peptides released from reovirus outer capsid form membrane pores that recruit virus particles
    • T. Ivanovic, M.A. Agosto, L. Zhang, K. Chandran, S.C. Harrison, and M.L. Nibert Peptides released from reovirus outer capsid form membrane pores that recruit virus particles Embo J. 27 2008 1289 1298
    • (2008) Embo J. , vol.27 , pp. 1289-1298
    • Ivanovic, T.1    Agosto, M.A.2    Zhang, L.3    Chandran, K.4    Harrison, S.C.5    Nibert, M.L.6
  • 34
    • 67650444363 scopus 로고    scopus 로고
    • Requirements for the formation of membrane pores by the reovirus myristoylated micro1N peptide
    • L. Zhang, M.A. Agosto, T. Ivanovic, D.S. King, M.L. Nibert, and S.C. Harrison Requirements for the formation of membrane pores by the reovirus myristoylated micro1N peptide J. Virol. 83 2009 7004 7014
    • (2009) J. Virol. , vol.83 , pp. 7004-7014
    • Zhang, L.1    Agosto, M.A.2    Ivanovic, T.3    King, D.S.4    Nibert, M.L.5    Harrison, S.C.6
  • 35
    • 33845419956 scopus 로고    scopus 로고
    • Reovirus mu1 structural rearrangements that mediate membrane penetration
    • L. Zhang, K. Chandran, M.L. Nibert, and S.C. Harrison Reovirus mu1 structural rearrangements that mediate membrane penetration J. Virol. 80 2006 12367 12376
    • (2006) J. Virol. , vol.80 , pp. 12367-12376
    • Zhang, L.1    Chandran, K.2    Nibert, M.L.3    Harrison, S.C.4
  • 36
    • 33750820630 scopus 로고    scopus 로고
    • Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR
    • R. Mani, S.D. Cady, M. Tang, A.J. Waring, R.I. Lehrer, and M. Hong Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR Proc. Natl. Acad. Sci. U. S. A. 103 2006 16242 16247
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 16242-16247
    • Mani, R.1    Cady, S.D.2    Tang, M.3    Waring, A.J.4    Lehrer, R.I.5    Hong, M.6
  • 38
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • B. Rost PHD: predicting one-dimensional protein structure by profile-based neural networks Methods Enzymol. 266 1996 525 539
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 40
    • 0014248563 scopus 로고
    • Resting and action potentials in experimental bimolecular lipid membranes
    • P. Mueller, and D.O. Rudin Resting and action potentials in experimental bimolecular lipid membranes J. Theor. Biol. 18 1968 222 258
    • (1968) J. Theor. Biol. , vol.18 , pp. 222-258
    • Mueller, P.1    Rudin, D.O.2
  • 41
    • 0031686552 scopus 로고    scopus 로고
    • Coupled plasmon-waveguide resonance spectroscopy studies of the cytochrome b6f/plastocyanin system in supported lipid bilayer membranes
    • Z. Salamon, D. Huang, W.A. Cramer, and G. Tollin Coupled plasmon-waveguide resonance spectroscopy studies of the cytochrome b6f/plastocyanin system in supported lipid bilayer membranes Biophys. J. 75 1998 1874 1885
    • (1998) Biophys. J. , vol.75 , pp. 1874-1885
    • Salamon, Z.1    Huang, D.2    Cramer, W.A.3    Tollin, G.4
  • 42
    • 1542781731 scopus 로고    scopus 로고
    • Direct observation of G-protein binding to the human delta-opioid receptor using plasmon-waveguide resonance spectroscopy
    • I.D. Alves, Z. Salamon, E. Varga, H.I. Yamamura, G. Tollin, and V.J. Hruby Direct observation of G-protein binding to the human delta-opioid receptor using plasmon-waveguide resonance spectroscopy J. Biol. Chem. 278 2003 48890 48897
    • (2003) J. Biol. Chem. , vol.278 , pp. 48890-48897
    • Alves, I.D.1    Salamon, Z.2    Varga, E.3    Yamamura, H.I.4    Tollin, G.5    Hruby, V.J.6
  • 43
    • 1942454801 scopus 로고    scopus 로고
    • Graphical analysis of mass and anisotropy changes observed by plasmon-waveguide resonance spectroscopy can provide useful insights into membrane protein function
    • Z. Salamon, and G. Tollin Graphical analysis of mass and anisotropy changes observed by plasmon-waveguide resonance spectroscopy can provide useful insights into membrane protein function Biophys. J. 86 2004 2508 2516
    • (2004) Biophys. J. , vol.86 , pp. 2508-2516
    • Salamon, Z.1    Tollin, G.2
  • 45
    • 64849112013 scopus 로고    scopus 로고
    • Structural studies of HIV-1 Gag p6ct and its interaction with Vpr determined by solution nuclear magnetic resonance
    • G.F. Salgado, R. Marquant, A. Vogel, I.D. Alves, S.E. Feller, N. Morellet, and S. Bouaziz Structural studies of HIV-1 Gag p6ct and its interaction with Vpr determined by solution nuclear magnetic resonance Biochemistry 48 2009 2355 2367
    • (2009) Biochemistry , vol.48 , pp. 2355-2367
    • Salgado, G.F.1    Marquant, R.2    Vogel, A.3    Alves, I.D.4    Feller, S.E.5    Morellet, N.6    Bouaziz, S.7
  • 46
    • 80052451032 scopus 로고    scopus 로고
    • Relationships between membrane binding, affinity and cell internalization efficacy of a cell-penetrating peptide: Penetratin as a case study
    • I.D. Alves, C. Bechara, A. Walrant, Y. Zaltsman, C.Y. Jiao, and S. Sagan Relationships between membrane binding, affinity and cell internalization efficacy of a cell-penetrating peptide: penetratin as a case study PLoS One 6 2011 e24096
    • (2011) PLoS One , vol.6 , pp. 24096
    • Alves, I.D.1    Bechara, C.2    Walrant, A.3    Zaltsman, Y.4    Jiao, C.Y.5    Sagan, S.6
  • 47
    • 0031752755 scopus 로고    scopus 로고
    • The effects of pH and intraliposomal buffer strength on the rate of liposome content release and intracellular drug delivery
    • R.J. Lee, S. Wang, M.J. Turk, and P.S. Low The effects of pH and intraliposomal buffer strength on the rate of liposome content release and intracellular drug delivery Biosci. Rep. 18 1998 69 78
    • (1998) Biosci. Rep. , vol.18 , pp. 69-78
    • Lee, R.J.1    Wang, S.2    Turk, M.J.3    Low, P.S.4
  • 48
    • 44949290287 scopus 로고
    • 2D homonuclear shift correlation phase sensitive using TPPI with double quantum filter phase cycle
    • A. Derome, and M. Williamson 2D homonuclear shift correlation phase sensitive using TPPI with double quantum filter phase cycle J. Magn. Reson. 88 1990 177 185
    • (1990) J. Magn. Reson. , vol.88 , pp. 177-185
    • Derome, A.1    Williamson, M.2
  • 50
    • 0343359244 scopus 로고
    • Investigation of exchange processes by 2-dimensional NMR-spectroscopy
    • J. Jeener, B.H. Meier, P. Bachmann, and R.R. Ernst investigation of exchange processes by 2-dimensional NMR-spectroscopy J. Chem. Phys. 71 1979 4546 4553
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 54
    • 17644366469 scopus 로고    scopus 로고
    • The C-terminal domain of the HIV-1 regulatory protein Vpr adopts an antiparallel dimeric structure in solution via its leucine-zipper-like domain
    • S. Bourbigot, H. Beltz, J. Denis, N. Morellet, B.P. Roques, Y. Mely, and S. Bouaziz The C-terminal domain of the HIV-1 regulatory protein Vpr adopts an antiparallel dimeric structure in solution via its leucine-zipper-like domain Biochem. J. 387 2005 333 341
    • (2005) Biochem. J. , vol.387 , pp. 333-341
    • Bourbigot, S.1    Beltz, H.2    Denis, J.3    Morellet, N.4    Roques, B.P.5    Mely, Y.6    Bouaziz, S.7
  • 55
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    Macarthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 58
    • 0030982689 scopus 로고    scopus 로고
    • Solubilized and cleaved VP7, the outer glycoprotein of rotavirus, induces permeabilization of cell membrane vesicles
    • A. Charpilienne, M.J. Abad, F. Michelangeli, F. Alvarado, M. Vasseur, J. Cohen, and M.C. Ruiz Solubilized and cleaved VP7, the outer glycoprotein of rotavirus, induces permeabilization of cell membrane vesicles J. Gen. Virol. 78 Pt 6 1997 1367 1371
    • (1997) J. Gen. Virol. , vol.78 , Issue.PART 6 , pp. 1367-1371
    • Charpilienne, A.1    Abad, M.J.2    Michelangeli, F.3    Alvarado, F.4    Vasseur, M.5    Cohen, J.6    Ruiz, M.C.7
  • 59
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • D.T. Jones Protein secondary structure prediction based on position-specific scoring matrices J. Mol. Biol. 292 1999 195 202
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 60
    • 63449087071 scopus 로고    scopus 로고
    • The interaction of cell-penetrating peptides with lipid model systems and subsequent lipid reorganization: Thermodynamic and structural characterization
    • I.D. Alves, I. Correia, C.Y. Jiao, E. Sachon, S. Sagan, S. Lavielle, G. Tollin, and G. Chassaing The interaction of cell-penetrating peptides with lipid model systems and subsequent lipid reorganization: thermodynamic and structural characterization J. Pept. Sci. 15 2009 200 209
    • (2009) J. Pept. Sci. , vol.15 , pp. 200-209
    • Alves, I.D.1    Correia, I.2    Jiao, C.Y.3    Sachon, E.4    Sagan, S.5    Lavielle, S.6    Tollin, G.7    Chassaing, G.8
  • 61
    • 70949106813 scopus 로고    scopus 로고
    • The role of membranes in the organization of HIV-1 Gag p6 and Vpr: P6 shows high affinity for membrane bilayers which substantially increases the interaction between p6 and Vpr
    • G.F. Salgado, A. Vogel, R. Marquant, S.E. Feller, S. Bouaziz, and I.D. Alves The role of membranes in the organization of HIV-1 Gag p6 and Vpr: p6 shows high affinity for membrane bilayers which substantially increases the interaction between p6 and Vpr J. Med. Chem. 52 2009 7157 7162
    • (2009) J. Med. Chem. , vol.52 , pp. 7157-7162
    • Salgado, G.F.1    Vogel, A.2    Marquant, R.3    Feller, S.E.4    Bouaziz, S.5    Alves, I.D.6
  • 64
    • 0033869955 scopus 로고    scopus 로고
    • Pressure effect on the dynamics of an isolated alpha-helix studied by 15 N-1H NMR relaxation
    • V.Y. Orekhov, P.V. Dubovskii, H. Yamada, K. Akasaka, and A.S. Arseniev Pressure effect on the dynamics of an isolated alpha-helix studied by 15 N-1H NMR relaxation J. Biomol. NMR 17 2000 257 263
    • (2000) J. Biomol. NMR , vol.17 , pp. 257-263
    • Orekhov, V.Y.1    Dubovskii, P.V.2    Yamada, H.3    Akasaka, K.4    Arseniev, A.S.5
  • 65
    • 0032811126 scopus 로고    scopus 로고
    • Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit
    • V.S. Pashkov, I.V. Maslennikov, L.D. Tchikin, R.G. Efremov, V.T. Ivanov, and A.S. Arseniev Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit FEBS Lett. 457 1999 117 121
    • (1999) FEBS Lett. , vol.457 , pp. 117-121
    • Pashkov, V.S.1    Maslennikov, I.V.2    Tchikin, L.D.3    Efremov, R.G.4    Ivanov, V.T.5    Arseniev, A.S.6
  • 66
    • 0344541116 scopus 로고    scopus 로고
    • Recent developments for the efficient crystallographic refinement of macromolecular structures
    • A.T. Brunger, P.D. Adams, and L.M. Rice Recent developments for the efficient crystallographic refinement of macromolecular structures Curr. Opin. Struct. Biol. 8 1998 606 611
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 606-611
    • Brunger, A.T.1    Adams, P.D.2    Rice, L.M.3
  • 67
    • 4644249737 scopus 로고    scopus 로고
    • VP7 mediates the interaction of rotaviruses with integrin alphavbeta3 through a novel integrin-binding site
    • S. Zarate, P. Romero, R. Espinosa, C.F. Arias, and S. Lopez VP7 mediates the interaction of rotaviruses with integrin alphavbeta3 through a novel integrin-binding site J. Virol. 78 2004 10839 10847
    • (2004) J. Virol. , vol.78 , pp. 10839-10847
    • Zarate, S.1    Romero, P.2    Espinosa, R.3    Arias, C.F.4    Lopez, S.5
  • 68
    • 0025900084 scopus 로고
    • Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture
    • F.M. Ruggeri, and H.B. Greenberg Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture J. Virol. 65 1991 2211 2219
    • (1991) J. Virol. , vol.65 , pp. 2211-2219
    • Ruggeri, F.M.1    Greenberg, H.B.2
  • 69
    • 0030813799 scopus 로고    scopus 로고
    • Rotaviruses induce an early membrane permeabilization of MA104 cells and do not require a low intracellular Ca2 + concentration to initiate their replication cycle
    • M.A. Cuadras, C.F. Arias, and S. Lopez Rotaviruses induce an early membrane permeabilization of MA104 cells and do not require a low intracellular Ca2 + concentration to initiate their replication cycle J. Virol. 71 1997 9065 9074
    • (1997) J. Virol. , vol.71 , pp. 9065-9074
    • Cuadras, M.A.1    Arias, C.F.2    Lopez, S.3
  • 72
    • 0032909033 scopus 로고    scopus 로고
    • Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra
    • B. Bechinger, J.M. Ruysschaert, and E. Goormaghtigh Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra Biophys. J. 76 1999 552 563
    • (1999) Biophys. J. , vol.76 , pp. 552-563
    • Bechinger, B.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 73
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y. Shai Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim. Biophys. Acta 1462 1999 55 70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 74
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • D.I. Chan, E.J. Prenner, and H.J. Vogel Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action Biochim. Biophys. Acta 1758 2006 1184 1202
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 76
    • 40149102160 scopus 로고    scopus 로고
    • Geometric mismatches within the concentric layers of rotavirus particles: A potential regulatory switch of viral particle transcription activity
    • S. Libersou, X. Siebert, M. Ouldali, L.F. Estrozi, J. Navaza, A. Charpilienne, P. Garnier, D. Poncet, and J. Lepault Geometric mismatches within the concentric layers of rotavirus particles: a potential regulatory switch of viral particle transcription activity J. Virol. 82 2008 2844 2852
    • (2008) J. Virol. , vol.82 , pp. 2844-2852
    • Libersou, S.1    Siebert, X.2    Ouldali, M.3    Estrozi, L.F.4    Navaza, J.5    Charpilienne, A.6    Garnier, P.7    Poncet, D.8    Lepault, J.9
  • 77
    • 0033168280 scopus 로고    scopus 로고
    • A highly membrane-active peptide in Flock House virus: Implications for the mechanism of nodavirus infection
    • D.T. Bong, C. Steinem, A. Janshoff, J.E. Johnson, and M. Reza Ghadiri A highly membrane-active peptide in Flock House virus: implications for the mechanism of nodavirus infection Chem. Biol. 6 1999 473 481
    • (1999) Chem. Biol. , vol.6 , pp. 473-481
    • Bong, D.T.1    Steinem, C.2    Janshoff, A.3    Johnson, J.E.4    Reza Ghadiri, M.5
  • 78
    • 33750819587 scopus 로고    scopus 로고
    • Mammalian reovirus, a nonfusogenic nonenveloped virus, forms size-selective pores in a model membrane
    • M.A. Agosto, T. Ivanovic, and M.L. Nibert Mammalian reovirus, a nonfusogenic nonenveloped virus, forms size-selective pores in a model membrane Proc. Natl. Acad. Sci. U. S. A. 103 2006 16496 16501
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 16496-16501
    • Agosto, M.A.1    Ivanovic, T.2    Nibert, M.L.3
  • 80
    • 27644563706 scopus 로고    scopus 로고
    • Trypsin is associated with the rotavirus capsid and is activated by solubilization of outer capsid proteins
    • Y. Benureau, J.C. Huet, A. Charpilienne, D. Poncet, and J. Cohen Trypsin is associated with the rotavirus capsid and is activated by solubilization of outer capsid proteins J. Gen. Virol. 86 2005 3143 3151
    • (2005) J. Gen. Virol. , vol.86 , pp. 3143-3151
    • Benureau, Y.1    Huet, J.C.2    Charpilienne, A.3    Poncet, D.4    Cohen, J.5


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