메뉴 건너뛰기




Volumn 46, Issue 40, 2007, Pages 11253-11262

Self-promoted cellular uptake of peptide/DNA transfection complexes

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPATHIC PEPTIDES; CELLULAR UPTAKE; TRANSFECTION COMPLEXES;

EID: 35248823164     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700766j     Document Type: Article
Times cited : (46)

References (59)
  • 1
    • 0032580348 scopus 로고    scopus 로고
    • Human gene therapy
    • Anderson, W. F. (1998) Human gene therapy, Nature 392, 25-30.
    • (1998) Nature , vol.392 , pp. 25-30
    • Anderson, W.F.1
  • 2
    • 0027351450 scopus 로고
    • Synthesis and characterization of a trigalactosylated bisacridine compound to target DNA to hepatocytes
    • Haensler, J., and Szoka, F. C., Jr. (1993) Synthesis and characterization of a trigalactosylated bisacridine compound to target DNA to hepatocytes, Bioconjugate Chem. 4, 85-93.
    • (1993) Bioconjugate Chem , vol.4 , pp. 85-93
    • Haensler, J.1    Szoka Jr., F.C.2
  • 3
    • 0028464351 scopus 로고
    • Strategies to achieve targeted gene delivery via the receptor-mediated endocytosis pathway
    • Michael, S. I., and Curiel, D. T. (1994) Strategies to achieve targeted gene delivery via the receptor-mediated endocytosis pathway, Gene Ther. 1, 223-232.
    • (1994) Gene Ther , vol.1 , pp. 223-232
    • Michael, S.I.1    Curiel, D.T.2
  • 5
    • 0030729180 scopus 로고    scopus 로고
    • ExGen 500 is an efficient vector for gene delivery to lung epithelial cells in vitro and in vivo
    • Ferrari, S., Moro, E., Pettenazzo, A., Behr, J. P., Zacchello, F., and Scarpa, M. (1997) ExGen 500 is an efficient vector for gene delivery to lung epithelial cells in vitro and in vivo, Gene Ther. 4, 1100-1106.
    • (1997) Gene Ther , vol.4 , pp. 1100-1106
    • Ferrari, S.1    Moro, E.2    Pettenazzo, A.3    Behr, J.P.4    Zacchello, F.5    Scarpa, M.6
  • 6
    • 0029801424 scopus 로고    scopus 로고
    • Characterization of vectors for gene therapy formed by self-assembly of DNA with synthetic block co-polymers
    • Wolfert, M. A., Schacht, E. H., Toncheva, V., Ulbrich, K., Nazarova, O., and Seymour, L. W. (1996) Characterization of vectors for gene therapy formed by self-assembly of DNA with synthetic block co-polymers, Hum. Gene Ther. 7, 2123-2133.
    • (1996) Hum. Gene Ther , vol.7 , pp. 2123-2133
    • Wolfert, M.A.1    Schacht, E.H.2    Toncheva, V.3    Ulbrich, K.4    Nazarova, O.5    Seymour, L.W.6
  • 7
    • 0029558004 scopus 로고
    • Cationic liposome-mediated gene transfer
    • Gao, X., and Huang, L. (1995) Cationic liposome-mediated gene transfer, Gene Ther. 2, 710-722.
    • (1995) Gene Ther , vol.2 , pp. 710-722
    • Gao, X.1    Huang, L.2
  • 8
    • 0028501007 scopus 로고
    • Gene transfer with synthetic cationic amphiphiles: Prospects for gene therapy
    • Behr, J. P. (1994) Gene transfer with synthetic cationic amphiphiles: Prospects for gene therapy, Bioconjugate Chem. 5, 382-389.
    • (1994) Bioconjugate Chem , vol.5 , pp. 382-389
    • Behr, J.P.1
  • 9
    • 0030890748 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of a cationic peptide that binds to nucleic acids and permeabilizes bilayers
    • Wyman, T. B., Nicol, F., Zelphati, O., Scaria, P. V., Plank, C., and Szoka, F. C., Jr. (1997) Design, synthesis, and characterization of a cationic peptide that binds to nucleic acids and permeabilizes bilayers, Biochemistry 36, 3008-3017.
    • (1997) Biochemistry , vol.36 , pp. 3008-3017
    • Wyman, T.B.1    Nicol, F.2    Zelphati, O.3    Scaria, P.V.4    Plank, C.5    Szoka Jr., F.C.6
  • 10
    • 0034328409 scopus 로고    scopus 로고
    • An optimized amphiphilic cationic peptide as an efficient non-viral gene delivery vector
    • Fominaya, J., Gasset, M., Garcia, R., Roncal, F., Albar, J. P., and Bernad, A. (2000) An optimized amphiphilic cationic peptide as an efficient non-viral gene delivery vector, J. Gene Med. 2, 455-464.
    • (2000) J. Gene Med , vol.2 , pp. 455-464
    • Fominaya, J.1    Gasset, M.2    Garcia, R.3    Roncal, F.4    Albar, J.P.5    Bernad, A.6
  • 11
    • 0030777569 scopus 로고    scopus 로고
    • Integrin-mediated transfection with peptides containing arginine-glycine- aspartic acid domains
    • Hart, S. L., Collins, L., Gustafsson, K., and Fabre, J. W. (1997) Integrin-mediated transfection with peptides containing arginine-glycine- aspartic acid domains, Gene Ther. 4, 1225-1230.
    • (1997) Gene Ther , vol.4 , pp. 1225-1230
    • Hart, S.L.1    Collins, L.2    Gustafsson, K.3    Fabre, J.W.4
  • 13
    • 0028199067 scopus 로고
    • The influence of endosome-disruptive peptides on gene transfer using synthetic virus-like gene transfer systems
    • Plank, C., Oberhauser, B., Mechtler, K., Koch, C., and Wagner, E. (1994) The influence of endosome-disruptive peptides on gene transfer using synthetic virus-like gene transfer systems, J. Biol. Chem. 269, 12918-12924.
    • (1994) J. Biol. Chem , vol.269 , pp. 12918-12924
    • Plank, C.1    Oberhauser, B.2    Mechtler, K.3    Koch, C.4    Wagner, E.5
  • 14
    • 0033524453 scopus 로고    scopus 로고
    • Gene delivery: A single nuclear localization signal peptide is sufficient to carry DNA to the cell nucleus
    • Zanta, M. A., Belguise-Valladier, P., and Behr, J. P. (1999) Gene delivery: A single nuclear localization signal peptide is sufficient to carry DNA to the cell nucleus, Proc. Natl. Acad. Sci. U.S.A. 96, 91-96.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 91-96
    • Zanta, M.A.1    Belguise-Valladier, P.2    Behr, J.P.3
  • 15
    • 0037452787 scopus 로고    scopus 로고
    • Histidine-rich amphipathic peptide antibiotics promote efficient delivery of DNA into mammalian cells
    • Kichler, A., Leborgne, C., Marz, J., Danos, O., and Bechinger, B. (2003) Histidine-rich amphipathic peptide antibiotics promote efficient delivery of DNA into mammalian cells, Proc. Natl. Acad. Sci. U.S.A. 100, 1564-1568.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 1564-1568
    • Kichler, A.1    Leborgne, C.2    Marz, J.3    Danos, O.4    Bechinger, B.5
  • 16
    • 0032849898 scopus 로고    scopus 로고
    • The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers: The effects of charges and pH
    • Vogt, T. C. B., and Bechinger, B. (1999) The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers: The effects of charges and pH, J. Biol. Chem. 274, 29115-29121.
    • (1999) J. Biol. Chem , vol.274 , pp. 29115-29121
    • Vogt, T.C.B.1    Bechinger, B.2
  • 17
    • 0030589158 scopus 로고    scopus 로고
    • Towards membrane protein design: PH dependent topology of histidine-containing polypeptides
    • Bechinger, B. (1996) Towards membrane protein design: pH dependent topology of histidine-containing polypeptides, J. Mol. Biol. 263, 768-775.
    • (1996) J. Mol. Biol , vol.263 , pp. 768-775
    • Bechinger, B.1
  • 18
    • 33646474970 scopus 로고    scopus 로고
    • Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy
    • Porcelli, F., Buck-Koehntop, B. A., Thennarasu, S., Ramamoorthy, A., and Veglia, G. (2006) Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy, Biochemistry 45, 5793-5799.
    • (2006) Biochemistry , vol.45 , pp. 5793-5799
    • Porcelli, F.1    Buck-Koehntop, B.A.2    Thennarasu, S.3    Ramamoorthy, A.4    Veglia, G.5
  • 19
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37
    • Henzler Wildman, K. A., Lee, D. K., and Ramamoorthy, A. (2003) Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37, Biochemistry 42, 6545-6558.
    • (2003) Biochemistry , vol.42 , pp. 6545-6558
    • Henzler Wildman, K.A.1    Lee, D.K.2    Ramamoorthy, A.3
  • 22
    • 0042166066 scopus 로고    scopus 로고
    • DNA binding of a non-sequence-specific HMG-D protein is entropy driven with a substantial non-electrostatic contribution
    • Dragan, A. I., Klass, J., Read, C., Churchill, M. E., Crane-Robinson, C., and Privalov, P. L. (2003) DNA binding of a non-sequence-specific HMG-D protein is entropy driven with a substantial non-electrostatic contribution, J. Mol. Biol. 331, 795-813.
    • (2003) J. Mol. Biol , vol.331 , pp. 795-813
    • Dragan, A.I.1    Klass, J.2    Read, C.3    Churchill, M.E.4    Crane-Robinson, C.5    Privalov, P.L.6
  • 23
    • 0037080014 scopus 로고    scopus 로고
    • Biophysical characterization of the DNA binding and condensing properties of adenoviral core peptide μ
    • Keller, M., Tagawa, T., Preuss, M., and Miller, A. D. (2002) Biophysical characterization of the DNA binding and condensing properties of adenoviral core peptide μ, Biochemistry 41, 652-659.
    • (2002) Biochemistry , vol.41 , pp. 652-659
    • Keller, M.1    Tagawa, T.2    Preuss, M.3    Miller, A.D.4
  • 24
    • 0032489503 scopus 로고    scopus 로고
    • Thermodynamic characterization of non-sequence-specific DNA-binding to the Sso7d protein from Sulfolobus solfataricus
    • Lundbäck, T., Hansson, H., Knapp, S., Adenstein, R., and Hard, T. (1998) Thermodynamic characterization of non-sequence-specific DNA-binding to the Sso7d protein from Sulfolobus solfataricus, J. Mol. Biol. 276, 775-786.
    • (1998) J. Mol. Biol , vol.276 , pp. 775-786
    • Lundbäck, T.1    Hansson, H.2    Knapp, S.3    Adenstein, R.4    Hard, T.5
  • 25
    • 0031567121 scopus 로고    scopus 로고
    • Titration calorimetry of lipid-peptide interactions
    • Seelig, J. (1997) Titration calorimetry of lipid-peptide interactions, Biochim. Biophys. Acta 1331, 103-116.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 103-116
    • Seelig, J.1
  • 26
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • Seelig, J. (2004) Thermodynamics of lipid-peptide interactions, Biochim. Biophys. Acta 1666, 40-50.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 40-50
    • Seelig, J.1
  • 27
    • 0038016473 scopus 로고    scopus 로고
    • Thermodynamic analysis of binding and protonation in DOTAP/DOPE (1:1): DNA complexes using isothermal titration calorimetry
    • Lobo, B. A., Koe, G. S., Koe, J. G., and Middaugh, C. R. (2003) Thermodynamic analysis of binding and protonation in DOTAP/DOPE (1:1): DNA complexes using isothermal titration calorimetry, Biophys. Chem. 104, 67-78.
    • (2003) Biophys. Chem , vol.104 , pp. 67-78
    • Lobo, B.A.1    Koe, G.S.2    Koe, J.G.3    Middaugh, C.R.4
  • 29
    • 0036159271 scopus 로고    scopus 로고
    • Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to Tat
    • Silhol, M., Tyagi, M., Giacca, M., Lebleu, B., and Vives, E. (2002) Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to Tat, Eur. J. Biochem. 269, 494-501.
    • (2002) Eur. J. Biochem , vol.269 , pp. 494-501
    • Silhol, M.1    Tyagi, M.2    Giacca, M.3    Lebleu, B.4    Vives, E.5
  • 30
    • 0036169073 scopus 로고    scopus 로고
    • New basic membrane-destabilizing peptides for plasmid-based gene delivery in vitro and in vivo
    • Rittner, K., Benavente, A., Bompard-Sorlet, A., Heitz, F., Divita, G., Brasseur, R., and Jacobs, E. (2002) New basic membrane-destabilizing peptides for plasmid-based gene delivery in vitro and in vivo, Mol. Ther. 5, 104-114.
    • (2002) Mol. Ther , vol.5 , pp. 104-114
    • Rittner, K.1    Benavente, A.2    Bompard-Sorlet, A.3    Heitz, F.4    Divita, G.5    Brasseur, R.6    Jacobs, E.7
  • 31
    • 0038719684 scopus 로고    scopus 로고
    • The cationic amphipathic α-helix of HIV-1 viral protein R (Vpr) binds to nucleic acids, permeabilizes membranes, and efficiently transfects cells
    • Coeytaux, E., Coulaud, D., Le Cam, E., Danos, O., and Kichler, A. (2003) The cationic amphipathic α-helix of HIV-1 viral protein R (Vpr) binds to nucleic acids, permeabilizes membranes, and efficiently transfects cells, J. Biol. Chem. 278, 18110-18116.
    • (2003) J. Biol. Chem , vol.278 , pp. 18110-18116
    • Coeytaux, E.1    Coulaud, D.2    Le Cam, E.3    Danos, O.4    Kichler, A.5
  • 32
    • 0035286969 scopus 로고    scopus 로고
    • Polyethylenimine-mediated gene delivery: A mechanistic study
    • Kichler, A., Leborgne, C., Coeytaux, E., and Danos, O. (2001) Polyethylenimine-mediated gene delivery: A mechanistic study, J. Gene Med. 3, 135-144.
    • (2001) J. Gene Med , vol.3 , pp. 135-144
    • Kichler, A.1    Leborgne, C.2    Coeytaux, E.3    Danos, O.4
  • 33
    • 36849106840 scopus 로고
    • Proton-enhanced NMR of dilute spins in solids
    • Pines, A., Gibby, M. G., and Waugh, J. S. (1973) Proton-enhanced NMR of dilute spins in solids, J. Chem. Phys. 59, 569-590.
    • (1973) J. Chem. Phys , vol.59 , pp. 569-590
    • Pines, A.1    Gibby, M.G.2    Waugh, J.S.3
  • 34
    • 33845550898 scopus 로고
    • 13C NMR cross polarization/magic angle spinning spectroscopic characterization of solid polypeptides
    • 13C NMR cross polarization/magic angle spinning spectroscopic characterization of solid polypeptides, Macromolecules 16, 615-623.
    • (1983) Macromolecules , vol.16 , pp. 615-623
    • Kricheldorf, H.R.M.D.1
  • 36
    • 77956853496 scopus 로고
    • High-resolution solid-state NMR studies of synthetic and biological macromolecules
    • Webb, E. A, Ed, pp, Academic Press, New York
    • Saito, H., and Ando, I. (1989) High-resolution solid-state NMR studies of synthetic and biological macromolecules, in Annual Reports on NMR Spectroscopy (Webb, E. A., Ed.) pp 209-290, Academic Press, New York.
    • (1989) Annual Reports on NMR Spectroscopy , pp. 209-290
    • Saito, H.1    Ando, I.2
  • 38
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set, Anal. Biochem. 252-260.
    • (2000) Anal. Biochem , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 39
    • 0025356901 scopus 로고
    • Interactions of mammalian cells with lipid dispersions containing novel metabolizable cationic amphiphiles
    • Leventis, R., and Silvius, J. R. (1990) Interactions of mammalian cells with lipid dispersions containing novel metabolizable cationic amphiphiles, Biochim. Biophys. Acta 1023, 124-132.
    • (1990) Biochim. Biophys. Acta , vol.1023 , pp. 124-132
    • Leventis, R.1    Silvius, J.R.2
  • 40
    • 0034152683 scopus 로고    scopus 로고
    • Systemic linear polyethylenimine (L-PEI)-mediated gene delivery in the mouse
    • Zou, S. M., Erbacher, P., Remy, J. S., and Behr, J. P. (2000) Systemic linear polyethylenimine (L-PEI)-mediated gene delivery in the mouse, J. Gene Med. 2, 128-134.
    • (2000) J. Gene Med , vol.2 , pp. 128-134
    • Zou, S.M.1    Erbacher, P.2    Remy, J.S.3    Behr, J.P.4
  • 41
    • 0038719684 scopus 로고    scopus 로고
    • The cationic amphipathic α-helix of HIV-1 viral protein R (Vpr) binds to nucleic acids, permeabilizes membranes, and efficiently transfects cells
    • Coeytaux, E., Coulaud, D., Le Cam, E., Danos, O., and Kichler, A. (2003) The cationic amphipathic α-helix of HIV-1 viral protein R (Vpr) binds to nucleic acids, permeabilizes membranes, and efficiently transfects cells, J. Biol. Chem. 278, 18110-18116.
    • (2003) J. Biol. Chem , vol.278 , pp. 18110-18116
    • Coeytaux, E.1    Coulaud, D.2    Le Cam, E.3    Danos, O.4    Kichler, A.5
  • 42
    • 0018798032 scopus 로고
    • Physicochemical studies of the protein-lipid interactions in melittin-containing micelles
    • Lauterwein, J., Bosch, C., Brown, L. R., and Wüthrich, K. (1979) Physicochemical studies of the protein-lipid interactions in melittin-containing micelles, Biochim. Biophys. Acta 556, 244-264.
    • (1979) Biochim. Biophys. Acta , vol.556 , pp. 244-264
    • Lauterwein, J.1    Bosch, C.2    Brown, L.R.3    Wüthrich, K.4
  • 43
    • 0020479083 scopus 로고
    • The structure of melittin. I. Structure determination and partial refinement
    • Terwilliger, T. C., and Eisenberg, D. (1982) The structure of melittin. I. Structure determination and partial refinement, J. Biol. Chem. 257, 6010-6015.
    • (1982) J. Biol. Chem , vol.257 , pp. 6010-6015
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 44
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity
    • Oren, Z., Lerman, J. C., Gudmundsson, G. H., Agerberth, B., and Shai, Y. (1999) Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity, Biochem. J. 341, 501-513.
    • (1999) Biochem. J , vol.341 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 45
    • 0034846331 scopus 로고    scopus 로고
    • Secondary chemical shifts in immobilized peptides and proteins: A qualitative basis for structure refinement under magic angle spinning
    • Luca, S., Filippov, D. V., van Boom, J. H., Oschkinat, H., de Groot, H. J., and Baldus, M. (2001) Secondary chemical shifts in immobilized peptides and proteins: A qualitative basis for structure refinement under magic angle spinning, J. Biomol. NMR 20, 325-331.
    • (2001) J. Biomol. NMR , vol.20 , pp. 325-331
    • Luca, S.1    Filippov, D.V.2    van Boom, J.H.3    Oschkinat, H.4    de Groot, H.J.5    Baldus, M.6
  • 46
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology, J Biomol. NMR 13, 289-302.
    • (1999) J Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 47
    • 0001427112 scopus 로고    scopus 로고
    • Determination of the solid-state conformations of polyalanine using magic-angle spinning NMR spectroscopy
    • Lee, D. K., and Ramamoorthy, A. (1999) Determination of the solid-state conformations of polyalanine using magic-angle spinning NMR spectroscopy, J. Phys. Chem. 103, 271-275.
    • (1999) J. Phys. Chem , vol.103 , pp. 271-275
    • Lee, D.K.1    Ramamoorthy, A.2
  • 48
    • 0037102901 scopus 로고    scopus 로고
    • Determination of α-helix and β-sheet stability in the solid state: A solid-state NMR investigation of poly(L-alanine)
    • Henzler Wildman, K. A., Lee, D. K., and Ramamoorthy, A. (2002) Determination of α-helix and β-sheet stability in the solid state: A solid-state NMR investigation of poly(L-alanine), Biopolymers 64, 246-254.
    • (2002) Biopolymers , vol.64 , pp. 246-254
    • Henzler Wildman, K.A.1    Lee, D.K.2    Ramamoorthy, A.3
  • 50
    • 0030478012 scopus 로고    scopus 로고
    • Coupled folding and site-specific binding of the GCN4-bZIP transcription factor to the AP-1 and ATC/CREB DNA studied by microcalorimetry
    • Berger, C., Jelesarov, I., and Bosshard, H. R. (1996) Coupled folding and site-specific binding of the GCN4-bZIP transcription factor to the AP-1 and ATC/CREB DNA studied by microcalorimetry, Biochemistry 35, 14984-14991.
    • (1996) Biochemistry , vol.35 , pp. 14984-14991
    • Berger, C.1    Jelesarov, I.2    Bosshard, H.R.3
  • 51
    • 0035965868 scopus 로고    scopus 로고
    • Heat does not come in different colours: Entropy-enthalpy compensation, free energy windows, quantum confinement, pressure perturbation calorimetry, solvation and the multiple causes of heat capacity effects in biomolecular interactions
    • Cooper, A., Johnson, C. M., Lakey, J. H., and Nollmann, M. (2001) Heat does not come in different colours: Entropy-enthalpy compensation, free energy windows, quantum confinement, pressure perturbation calorimetry, solvation and the multiple causes of heat capacity effects in biomolecular interactions, Biophys. Chem. 93, 215-230.
    • (2001) Biophys. Chem , vol.93 , pp. 215-230
    • Cooper, A.1    Johnson, C.M.2    Lakey, J.H.3    Nollmann, M.4
  • 52
    • 33846597010 scopus 로고    scopus 로고
    • Characterisation of gene transfer processes mediated by histidine-rich peptides
    • Kichler, A., Leborgne, C., Danos, O., and Bechinger, B. (2007) Characterisation of gene transfer processes mediated by histidine-rich peptides, J. Mol. Med. 85, 191-201.
    • (2007) J. Mol. Med , vol.85 , pp. 191-201
    • Kichler, A.1    Leborgne, C.2    Danos, O.3    Bechinger, B.4
  • 53
    • 0035408714 scopus 로고    scopus 로고
    • Different behavior of branched and linear polyethylenimine for gene delivery in vitro and in vivo
    • Wightman, L., Kircheis, R., Rossler, V., Carotta, S., Ruzicka, R., Kursa, M., and Wagner, E. (2001) Different behavior of branched and linear polyethylenimine for gene delivery in vitro and in vivo, J. Gene Med. 3, 362-372.
    • (2001) J. Gene Med , vol.3 , pp. 362-372
    • Wightman, L.1    Kircheis, R.2    Rossler, V.3    Carotta, S.4    Ruzicka, R.5    Kursa, M.6    Wagner, E.7
  • 54
    • 0035442411 scopus 로고    scopus 로고
    • Leavitt, S., and Freire, E. (2001) Direct measurement of protein binding energetics by isothermal titration calorimetry 22, Curr. Opin. Struct. Biol. 11, 560-566.
    • Leavitt, S., and Freire, E. (2001) Direct measurement of protein binding energetics by isothermal titration calorimetry 22, Curr. Opin. Struct. Biol. 11, 560-566.
  • 55
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like action of linear cationic membrane-active antibiotic peptides
    • Bechinger, B., and Lohner, K. (2006) Detergent-like action of linear cationic membrane-active antibiotic peptides, Biochim. Biophys. Acta 1758, 1529-1539.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 56
    • 33644925279 scopus 로고    scopus 로고
    • The antibiotic and DNA transfecting peptide LAH4 selectively associates with, and disorders, anionic lipids in mixed membranes
    • Mason, A. J., Martinez, A., Glaubitz, C., Danos, O., Kichler, A., and Bechinger, B. (2005) The antibiotic and DNA transfecting peptide LAH4 selectively associates with, and disorders, anionic lipids in mixed membranes, FASEB J. 20, 320-322.
    • (2005) FASEB J , vol.20 , pp. 320-322
    • Mason, A.J.1    Martinez, A.2    Glaubitz, C.3    Danos, O.4    Kichler, A.5    Bechinger, B.6
  • 57
    • 33646870619 scopus 로고    scopus 로고
    • A spectroscopic study of the membrane interaction of the antimicrobial peptide pleurocidin
    • Mason, A. J., Husnal-Chotimah, I. N., Bertani, P., and Bechinger, B. (2006) A spectroscopic study of the membrane interaction of the antimicrobial peptide pleurocidin, Mol. Membr. Biol. 23, 185-194.
    • (2006) Mol. Membr. Biol , vol.23 , pp. 185-194
    • Mason, A.J.1    Husnal-Chotimah, I.N.2    Bertani, P.3    Bechinger, B.4
  • 58
    • 20444400818 scopus 로고    scopus 로고
    • Detergent-like properties of magainin antibiotic peptides: A 31P solid-state NMR study
    • Bechinger, B. (2005) Detergent-like properties of magainin antibiotic peptides: A 31P solid-state NMR study, Biochim. Biophys. Acta 1712, 101-108.
    • (2005) Biochim. Biophys. Acta , vol.1712 , pp. 101-108
    • Bechinger, B.1
  • 59
    • 0038719684 scopus 로고    scopus 로고
    • The cationic amphipathic α-helix of HIV-1 viral protein R (Vpr) binds to nucleic acids, permeabilizes membranes, and efficiently transfects cells
    • Coeytaux, E., Coulaud, D., Le Cam, E., Danos, O., and Kichler, A. (2003) The cationic amphipathic α-helix of HIV-1 viral protein R (Vpr) binds to nucleic acids, permeabilizes membranes, and efficiently transfects cells, J. Biol. Chem. 278, 18110-18116.
    • (2003) J. Biol. Chem , vol.278 , pp. 18110-18116
    • Coeytaux, E.1    Coulaud, D.2    Le Cam, E.3    Danos, O.4    Kichler, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.