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Volumn 1808, Issue 1, 2011, Pages 298-306

Laurdan and di-4-ANEPPDHQ do not respond to membrane-inserted peptides and are good probes for lipid packing

Author keywords

di 4 ANEPPDHQ; Laurdan; ld phase; Lipid rafts; lo phase; Membrane order

Indexed keywords

4 ALANYLASPARAGINYLGLUTAMYLPROLYLPROLYLASPARTYLHISTIDINYLGLUTAMINE; LAURDAN; MASTOPARAN; PEPTIDE; PRION PROTEIN; UNCLASSIFIED DRUG;

EID: 78649763791     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.10.002     Document Type: Article
Times cited : (58)

References (56)
  • 1
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 2
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • K. Simons, and G. van Meer Lipid sorting in epithelial cells Biochemistry 27 1988 6197 6202
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 3
    • 0026661612 scopus 로고
    • Membrane aging during cell growth ascertained by Laurdan generalized polarization
    • T. Parasassi, M. Di Stefano, G. Ravagnan, O. Sapora, and E. Gratton Membrane aging during cell growth ascertained by Laurdan generalized polarization Exp. Cell Res. 202 1992 432 439
    • (1992) Exp. Cell Res. , vol.202 , pp. 432-439
    • Parasassi, T.1    Di Stefano, M.2    Ravagnan, G.3    Sapora, O.4    Gratton, E.5
  • 4
    • 0026100432 scopus 로고
    • Characterization of lipid domains in erythrocyte membranes
    • W. Rodgers, and M. Glaser Characterization of lipid domains in erythrocyte membranes Proc. Natl. Acad. Sci. U. S. A. 88 1991 1364 1368
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 1364-1368
    • Rodgers, W.1    Glaser, M.2
  • 5
    • 0002391753 scopus 로고
    • Lateral diffusion of phospholipids in the plasma membrane of soybean protoplasts: Evidence for membrane lipid domains
    • T.N. Metcalf, J.L. Wang, and M. Schindler Lateral diffusion of phospholipids in the plasma membrane of soybean protoplasts: evidence for membrane lipid domains Proc. Natl. Acad. Sci. U. S. A. 83 1986 95 99
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 95-99
    • Metcalf, T.N.1    Wang, J.L.2    Schindler, M.3
  • 7
    • 58149473633 scopus 로고    scopus 로고
    • The liquid-ordered phase in membranes
    • P.J. Quinn, and C. Wolf The liquid-ordered phase in membranes Biochim. Biophys. Acta 1788 2009 33 46
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 33-46
    • Quinn, P.J.1    Wolf, C.2
  • 9
    • 29144531904 scopus 로고    scopus 로고
    • Seeing spots: Complex phase behavior in simple membranes
    • S.L. Veatch, and S.L. Keller Seeing spots: complex phase behavior in simple membranes Biochim. Biophys. Acta 1746 2005 172 185
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 172-185
    • Veatch, S.L.1    Keller, S.L.2
  • 10
    • 23244453354 scopus 로고    scopus 로고
    • Cholesterol-enriched lipid domains can be visualized by di-4-ANEPPDHQ with linear and nonlinear optics
    • L. Jin, A.C. Millard, J.P. Wuskell, H.A. Clark, and L.M. Loew Cholesterol-enriched lipid domains can be visualized by di-4-ANEPPDHQ with linear and nonlinear optics Biophys. J. 89 2005 L04 L06
    • (2005) Biophys. J. , vol.89
    • Jin, L.1    Millard, A.C.2    Wuskell, J.P.3    Clark, H.A.4    Loew, L.M.5
  • 11
    • 0022647019 scopus 로고
    • Time-resolved fluorescence emission spectra of Laurdan in phospholipid vesicles by multifrequency phase and modulation fluorometry
    • T. Parasassi, F. Conti, and E. Gratton Time-resolved fluorescence emission spectra of Laurdan in phospholipid vesicles by multifrequency phase and modulation fluorometry Cell. Mol. Biol. 32 1986 103 108
    • (1986) Cell. Mol. Biol. , vol.32 , pp. 103-108
    • Parasassi, T.1    Conti, F.2    Gratton, E.3
  • 12
    • 33646171689 scopus 로고    scopus 로고
    • Characterization and application of a new optical probe for membrane lipid domains
    • L. Jin, A.C. Millard, J.P. Wuskell, X. Dong, D. Wu, H.A. Clark, and L.M. Loew Characterization and application of a new optical probe for membrane lipid domains Biophys. J. 90 2006 2563 2575
    • (2006) Biophys. J. , vol.90 , pp. 2563-2575
    • Jin, L.1    Millard, A.C.2    Wuskell, J.P.3    Dong, X.4    Wu, D.5    Clark, H.A.6    Loew, L.M.7
  • 13
    • 0034815625 scopus 로고    scopus 로고
    • Use of cyclodextrins to monitor transbilayer movement and differential lipid affinities of cholesterol
    • R. Leventis, and J.R. Silvius Use of cyclodextrins to monitor transbilayer movement and differential lipid affinities of cholesterol Biophys. J. 81 2001 2257 2267
    • (2001) Biophys. J. , vol.81 , pp. 2257-2267
    • Leventis, R.1    Silvius, J.R.2
  • 14
    • 0017364675 scopus 로고
    • Molecular dynamics of the local anesthetic tetracaine in phospholipid vesicles
    • P.L. Yeagle, W.C. Hutton, and R.B. Martin Molecular dynamics of the local anesthetic tetracaine in phospholipid vesicles Biochim. Biophys. Acta 465 1977 173 178
    • (1977) Biochim. Biophys. Acta , vol.465 , pp. 173-178
    • Yeagle, P.L.1    Hutton, W.C.2    Martin, R.B.3
  • 15
    • 0025295884 scopus 로고
    • Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence
    • T. Parasassi, G. De Stasio, A. d'Ubaldo, and E. Gratton Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence Biophys. J. 57 1990 1179 1186
    • (1990) Biophys. J. , vol.57 , pp. 1179-1186
    • Parasassi, T.1    De Stasio, G.2    D'Ubaldo, A.3    Gratton, E.4
  • 17
    • 77649248897 scopus 로고    scopus 로고
    • Plasma membrane topography and interpretation of single-particle tracks
    • J. Adler, A.I. Shevchuk, P. Novak, Y.E. Korchev, and I. Parmryd Plasma membrane topography and interpretation of single-particle tracks Nat. Methods 7 2010 170 171
    • (2010) Nat. Methods , vol.7 , pp. 170-171
    • Adler, J.1    Shevchuk, A.I.2    Novak, P.3    Korchev, Y.E.4    Parmryd, I.5
  • 19
    • 0030950269 scopus 로고    scopus 로고
    • Two-photon fluorescence microscopy of laurdan generalized polarization domains in model and natural membranes
    • T. Parasassi, E. Gratton, W.M. Yu, P. Wilson, and M. Levi Two-photon fluorescence microscopy of laurdan generalized polarization domains in model and natural membranes Biophys. J. 72 1997 2413 2429
    • (1997) Biophys. J. , vol.72 , pp. 2413-2429
    • Parasassi, T.1    Gratton, E.2    Yu, W.M.3    Wilson, P.4    Levi, M.5
  • 20
    • 0027563626 scopus 로고
    • Modulation and dynamics of phase properties in phospholipid mixtures detected by Laurdan fluorescence
    • T. Parasassi, G. Ravagnan, R.M. Rusch, and E. Gratton Modulation and dynamics of phase properties in phospholipid mixtures detected by Laurdan fluorescence Photochem. Photobiol. 57 1993 403 410
    • (1993) Photochem. Photobiol. , vol.57 , pp. 403-410
    • Parasassi, T.1    Ravagnan, G.2    Rusch, R.M.3    Gratton, E.4
  • 21
    • 33749046710 scopus 로고    scopus 로고
    • To see or not to see: Lateral organization of biological membranes and fluorescence microscopy
    • L.A. Bagatolli To see or not to see: lateral organization of biological membranes and fluorescence microscopy Biochim. Biophys. Acta 1758 2006 1541 1556
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1541-1556
    • Bagatolli, L.A.1
  • 22
    • 67650391443 scopus 로고    scopus 로고
    • Monitoring biophysical properties of lipid membranes by environment-sensitive fluorescent probes
    • A.P. Demchenko, Y. Mely, G. Duportail, and A.S. Klymchenko Monitoring biophysical properties of lipid membranes by environment-sensitive fluorescent probes Biophys. J. 96 2009 3461 3470
    • (2009) Biophys. J. , vol.96 , pp. 3461-3470
    • Demchenko, A.P.1    Mely, Y.2    Duportail, G.3    Klymchenko, A.S.4
  • 23
    • 0031112791 scopus 로고    scopus 로고
    • Isotropic solutions of phospholipid bicelles: A new membrane mimetic for high-resolution NMR studies of polypeptides
    • R.R. Vold, R.S. Prosser, and A.J. Deese Isotropic solutions of phospholipid bicelles: a new membrane mimetic for high-resolution NMR studies of polypeptides J. Biomol. NMR 9 1997 329 335
    • (1997) J. Biomol. NMR , vol.9 , pp. 329-335
    • Vold, R.R.1    Prosser, R.S.2    Deese, A.J.3
  • 25
    • 27444443817 scopus 로고    scopus 로고
    • Membrane perturbation effects of peptides derived from the N-termini of unprocessed prion proteins
    • M. Magzoub, K. Oglecka, A. Pramanik, L.E. Goran Eriksson, and A. Graslund Membrane perturbation effects of peptides derived from the N-termini of unprocessed prion proteins Biochim. Biophys. Acta 1716 2005 126 136
    • (2005) Biochim. Biophys. Acta , vol.1716 , pp. 126-136
    • Magzoub, M.1    Oglecka, K.2    Pramanik, A.3    Goran Eriksson, L.E.4    Graslund, A.5
  • 26
    • 84934435581 scopus 로고    scopus 로고
    • Artificial membrane models for the study of macromolecular delivery
    • L. Maler, and A. Graslund Artificial membrane models for the study of macromolecular delivery Methods Mol. Biol. 480 2009 129 139
    • (2009) Methods Mol. Biol. , vol.480 , pp. 129-139
    • Maler, L.1    Graslund, A.2
  • 27
    • 68749083525 scopus 로고    scopus 로고
    • Biophysical studies of the membrane location of the voltage-gated sensors in the HsapBK and KvAP K(+) channels
    • H. Biverstahl, J. Lind, A. Bodor, and L. Maler Biophysical studies of the membrane location of the voltage-gated sensors in the HsapBK and KvAP K(+) channels Biochim. Biophys. Acta 1788 2009 1976 1986
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1976-1986
    • Biverstahl, H.1    Lind, J.2    Bodor, A.3    Maler, L.4
  • 28
    • 0023047980 scopus 로고
    • Vesicles of variable sizes produced by a rapid extrusion procedure
    • L.D. Mayer, M.J. Hope, and P.R. Cullis Vesicles of variable sizes produced by a rapid extrusion procedure Biochim. Biophys. Acta 858 1986 161 168
    • (1986) Biochim. Biophys. Acta , vol.858 , pp. 161-168
    • Mayer, L.D.1    Hope, M.J.2    Cullis, P.R.3
  • 29
    • 0029752766 scopus 로고    scopus 로고
    • Preparation of giant liposomes in physiological conditions and their characterization under an optical microscope
    • K. Akashi, H. Miyata, H. Itoh, and K. Kinosita Jr. Preparation of giant liposomes in physiological conditions and their characterization under an optical microscope Biophys. J. 71 1996 3242 3250
    • (1996) Biophys. J. , vol.71 , pp. 3242-3250
    • Akashi, K.1    Miyata, H.2    Itoh, H.3    Kinosita Jr., K.4
  • 30
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • A. Lobley, L. Whitmore, and B.A. Wallace DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra Bioinformatics 18 2002 211 212
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 31
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • L. Whitmore, and B.A. Wallace DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 32 2004 W668 W673
    • (2004) Nucleic Acids Res. , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 32
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • L. Whitmore, and B.A. Wallace Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases Biopolymers 89 2008 392 400
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 33
    • 77954760015 scopus 로고    scopus 로고
    • Lipid packing determines protein-membrane interactions: Challenges for apolipoprotein A-I and high density lipoproteins
    • S.A. Sanchez, M.A. Tricerri, G. Ossato, and E. Gratton Lipid packing determines protein-membrane interactions: challenges for apolipoprotein A-I and high density lipoproteins Biochim. Biophys. Acta 1798 2010 1399 1408
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1399-1408
    • Sanchez, S.A.1    Tricerri, M.A.2    Ossato, G.3    Gratton, E.4
  • 34
    • 77950600389 scopus 로고    scopus 로고
    • Limited cholesterol depletion causes aggregation of plasma membrane lipid rafts inducing T cell activation
    • S. Mahammad, J. Dinic, J. Adler, and I. Parmryd Limited cholesterol depletion causes aggregation of plasma membrane lipid rafts inducing T cell activation Biochim. Biophys. Acta 1801 2010 625 634
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 625-634
    • Mahammad, S.1    Dinic, J.2    Adler, J.3    Parmryd, I.4
  • 35
  • 37
    • 58149196187 scopus 로고    scopus 로고
    • Tracking microdomain dynamics in cell membranes
    • C.A. Day, and A.K. Kenworthy Tracking microdomain dynamics in cell membranes Biochim. Biophys. Acta 1788 2009 245 253
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 245-253
    • Day, C.A.1    Kenworthy, A.K.2
  • 38
    • 33746215054 scopus 로고    scopus 로고
    • Laurdan fluorescence senses mechanical strain in the lipid bilayer membrane
    • Y.L. Zhang, J.A. Frangos, and M. Chachisvilis Laurdan fluorescence senses mechanical strain in the lipid bilayer membrane Biochem. Biophys. Res. Commun. 347 2006 838 841
    • (2006) Biochem. Biophys. Res. Commun. , vol.347 , pp. 838-841
    • Zhang, Y.L.1    Frangos, J.A.2    Chachisvilis, M.3
  • 39
    • 19744373874 scopus 로고    scopus 로고
    • Influence of the curvature on the water structure in the headgroup region of phospholipid bilayer studied by the solvent relaxation technique
    • J. Sykora, P. Jurkiewicz, R.M. Epand, R. Kraayenhof, M. Langner, and M. Hof Influence of the curvature on the water structure in the headgroup region of phospholipid bilayer studied by the solvent relaxation technique Chem. Phys. Lipids 135 2005 213 221
    • (2005) Chem. Phys. Lipids , vol.135 , pp. 213-221
    • Sykora, J.1    Jurkiewicz, P.2    Epand, R.M.3    Kraayenhof, R.4    Langner, M.5    Hof, M.6
  • 41
    • 33750347409 scopus 로고    scopus 로고
    • Headgroup hydration and mobility of DOTAP/DOPC bilayers: A fluorescence solvent relaxation study
    • P. Jurkiewicz, A. Olzynska, M. Langner, and M. Hof Headgroup hydration and mobility of DOTAP/DOPC bilayers: a fluorescence solvent relaxation study Langmuir 22 2006 8741 8749
    • (2006) Langmuir , vol.22 , pp. 8741-8749
    • Jurkiewicz, P.1    Olzynska, A.2    Langner, M.3    Hof, M.4
  • 42
    • 33745448224 scopus 로고    scopus 로고
    • Laurdan in fluid bilayers: Position and structural sensitivity
    • C.C. De Vequi-Suplicy, C.R. Benatti, and M.T. Lamy Laurdan in fluid bilayers: position and structural sensitivity J. Fluoresc. 16 2006 431 439
    • (2006) J. Fluoresc. , vol.16 , pp. 431-439
    • De Vequi-Suplicy, C.C.1    Benatti, C.R.2    Lamy, M.T.3
  • 43
    • 0027731260 scopus 로고
    • Absence of lipid gel-phase domains in seven mammalian cell lines and in four primary cell types
    • T. Parasassi, M. Loiero, M. Raimondi, G. Ravagnan, and E. Gratton Absence of lipid gel-phase domains in seven mammalian cell lines and in four primary cell types Biochim. Biophys. Acta 1153 1993 143 154
    • (1993) Biochim. Biophys. Acta , vol.1153 , pp. 143-154
    • Parasassi, T.1    Loiero, M.2    Raimondi, M.3    Ravagnan, G.4    Gratton, E.5
  • 44
    • 70349591893 scopus 로고    scopus 로고
    • Segregated phases in pulmonary surfactant membranes do not show coexistence of lipid populations with differentiated dynamic properties
    • J.B. de la Serna, G. Oradd, L.A. Bagatolli, A.C. Simonsen, D. Marsh, G. Lindblom, and J. Perez-Gil Segregated phases in pulmonary surfactant membranes do not show coexistence of lipid populations with differentiated dynamic properties Biophys. J. 97 2009 1381 1389
    • (2009) Biophys. J. , vol.97 , pp. 1381-1389
    • De La Serna, J.B.1    Oradd, G.2    Bagatolli, L.A.3    Simonsen, A.C.4    Marsh, D.5    Lindblom, G.6    Perez-Gil, J.7
  • 45
    • 0025742883 scopus 로고
    • Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence
    • T. Parasassi, G. De Stasio, G. Ravagnan, R.M. Rusch, and E. Gratton Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence Biophys. J. 60 1991 179 189
    • (1991) Biophys. J. , vol.60 , pp. 179-189
    • Parasassi, T.1    De Stasio, G.2    Ravagnan, G.3    Rusch, R.M.4    Gratton, E.5
  • 46
    • 0030032803 scopus 로고    scopus 로고
    • Physical state of bulk and protein-associated lipid in nicotinic acetylcholine receptor-rich membrane studied by laurdan generalized polarization and fluorescence energy transfer
    • S.S. Antollini, M.A. Soto, I. Bonini de Romanelli, C. Gutierrez-Merino, P. Sotomayor, and F.J. Barrantes Physical state of bulk and protein-associated lipid in nicotinic acetylcholine receptor-rich membrane studied by laurdan generalized polarization and fluorescence energy transfer Biophys. J. 70 1996 1275 1284
    • (1996) Biophys. J. , vol.70 , pp. 1275-1284
    • Antollini, S.S.1    Soto, M.A.2    Bonini De Romanelli, I.3    Gutierrez-Merino, C.4    Sotomayor, P.5    Barrantes, F.J.6
  • 47
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: At a crossroad between cell biology and physics
    • K. Jacobson, O.G. Mouritsen, and R.G. Anderson Lipid rafts: at a crossroad between cell biology and physics Nat. Cell Biol. 9 2007 7 14
    • (2007) Nat. Cell Biol. , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.3
  • 48
    • 67349205034 scopus 로고    scopus 로고
    • Membrane order perturbation in the presence of antimicrobial peptides by (2)H solid-state NMR spectroscopy
    • E.S. Salnikov, A.J. Mason, and B. Bechinger Membrane order perturbation in the presence of antimicrobial peptides by (2)H solid-state NMR spectroscopy Biochimie 91 2009 734 743
    • (2009) Biochimie , vol.91 , pp. 734-743
    • Salnikov, E.S.1    Mason, A.J.2    Bechinger, B.3
  • 49
    • 0345305860 scopus 로고    scopus 로고
    • Bilayer localization of membrane-active peptides studied in biomimetic vesicles by visible and fluorescence spectroscopies
    • T. Sheynis, J. Sykora, A. Benda, S. Kolusheva, M. Hof, and R. Jelinek Bilayer localization of membrane-active peptides studied in biomimetic vesicles by visible and fluorescence spectroscopies Eur. J. Biochem. 270 2003 4478 4487
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4478-4487
    • Sheynis, T.1    Sykora, J.2    Benda, A.3    Kolusheva, S.4    Hof, M.5    Jelinek, R.6
  • 50
    • 77954758827 scopus 로고    scopus 로고
    • Impact of membrane-anchored fluorescent probes on the mechanical properties of lipid bilayers
    • H. Bouvrais, T. Pott, L.A. Bagatolli, J.H. Ipsen, and P. Meleard Impact of membrane-anchored fluorescent probes on the mechanical properties of lipid bilayers Biochim. Biophys. Acta 1798 2010 1333 1337
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1333-1337
    • Bouvrais, H.1    Pott, T.2    Bagatolli, L.A.3    Ipsen, J.H.4    Meleard, P.5
  • 51
    • 9744245200 scopus 로고    scopus 로고
    • NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein
    • H. Biverstahl, A. Andersson, A. Graslund, and L. Maler NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein Biochemistry 43 2004 14940 14947
    • (2004) Biochemistry , vol.43 , pp. 14940-14947
    • Biverstahl, H.1    Andersson, A.2    Graslund, A.3    Maler, L.4
  • 52
    • 0032508864 scopus 로고    scopus 로고
    • Binding of prothrombin and its fragment 1 to phospholipid membranes studied by the solvent relaxation technique
    • R. Hutterer, F.W. Schneider, W.T. Hermens, R. Wagenvoord, and M. Hof Binding of prothrombin and its fragment 1 to phospholipid membranes studied by the solvent relaxation technique Biochim. Biophys. Acta 1414 1998 155 164
    • (1998) Biochim. Biophys. Acta , vol.1414 , pp. 155-164
    • Hutterer, R.1    Schneider, F.W.2    Hermens, W.T.3    Wagenvoord, R.4    Hof, M.5
  • 54
    • 0030819703 scopus 로고    scopus 로고
    • Interaction of lipophilic peptides derived from mastoparan with phospholipid vesicles
    • T. Niidome, R. Kawakami, K. Okamoto, N. Ohmori, H. Mihara, and H. Aoyagi Interaction of lipophilic peptides derived from mastoparan with phospholipid vesicles J. Pept. Res. 50 1997 458 464
    • (1997) J. Pept. Res. , vol.50 , pp. 458-464
    • Niidome, T.1    Kawakami, R.2    Okamoto, K.3    Ohmori, N.4    Mihara, H.5    Aoyagi, H.6
  • 55
    • 0032803785 scopus 로고    scopus 로고
    • Pore-forming action of mastoparan peptides on liposomes: A quantitative analysis
    • A. Arbuzova, and G. Schwarz Pore-forming action of mastoparan peptides on liposomes: a quantitative analysis Biochim. Biophys. Acta 1420 1999 139 152
    • (1999) Biochim. Biophys. Acta , vol.1420 , pp. 139-152
    • Arbuzova, A.1    Schwarz, G.2


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