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Volumn 128, Issue 1, 2007, Pages 75-86

Fluorescence study of protein-lipid complexes with a new symmetric squarylium probe

Author keywords

Lipid demixing; Lysozyme; Protein lipid interactions; Ribonuclease A; Squarylium dye

Indexed keywords

AMPHOLYTE; ANION; CARDIOLIPIN; DYE; LYSOZYME; PHOSPHATIDYLCHOLINE; RIBONUCLEASE A; SQUARIC ACID DERIVATIVE;

EID: 34247637186     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2007.03.007     Document Type: Article
Times cited : (26)

References (87)
  • 1
    • 0033807597 scopus 로고    scopus 로고
    • Lipid demixing and protein-protein interactions in the adsorption of charged proteins on mixed membranes
    • May S., Harries D., and Ben-Shaul A. Lipid demixing and protein-protein interactions in the adsorption of charged proteins on mixed membranes. Biophys. J. 79 (2000) 1747-1760
    • (2000) Biophys. J. , vol.79 , pp. 1747-1760
    • May, S.1    Harries, D.2    Ben-Shaul, A.3
  • 2
    • 0030754783 scopus 로고    scopus 로고
    • Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles
    • Ben-Tal N., Honig B., Miller C., and McLaughlin S. Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles. Biophys. J. 73 (1997) 1717-1727
    • (1997) Biophys. J. , vol.73 , pp. 1717-1727
    • Ben-Tal, N.1    Honig, B.2    Miller, C.3    McLaughlin, S.4
  • 3
    • 77956852054 scopus 로고
    • Protein-lipid interactions with peripheral membrane proteins
    • Elsevier
    • Sankaram M., and Marsh D. Protein-lipid interactions with peripheral membrane proteins. Protein-Lipid Interactions (1993), Elsevier 127-162
    • (1993) Protein-Lipid Interactions , pp. 127-162
    • Sankaram, M.1    Marsh, D.2
  • 4
    • 0031030031 scopus 로고    scopus 로고
    • Interaction of bee venom melittin with zwitterionic and negatively charged phospholipid bilayers: a spin-label electron spin resonance study
    • Kleinschmidt J., Mahaney J., Thomas D., and Marsh D. Interaction of bee venom melittin with zwitterionic and negatively charged phospholipid bilayers: a spin-label electron spin resonance study. Biophys. J. 72 (1997) 767-778
    • (1997) Biophys. J. , vol.72 , pp. 767-778
    • Kleinschmidt, J.1    Mahaney, J.2    Thomas, D.3    Marsh, D.4
  • 5
    • 0032842512 scopus 로고    scopus 로고
    • The transmembrane protein bacterioopsin affects the polarity of the hydrophobic core of the host lipid bilayer
    • Dumas F., Lebrun M., Peyron P., Lopez A., and Tocanne J. The transmembrane protein bacterioopsin affects the polarity of the hydrophobic core of the host lipid bilayer. Biochim. Biophys. Acta 1421 (1999) 295-305
    • (1999) Biochim. Biophys. Acta , vol.1421 , pp. 295-305
    • Dumas, F.1    Lebrun, M.2    Peyron, P.3    Lopez, A.4    Tocanne, J.5
  • 6
    • 0024589502 scopus 로고
    • Conformational changes of phospholipid headgroups induced by a cationic integral membrane peptide as seen by deuterium magnetic resonance
    • Roux M., Newmann Y., and Hodges R. Conformational changes of phospholipid headgroups induced by a cationic integral membrane peptide as seen by deuterium magnetic resonance. Biochemistry 28 (1989) 2313-2321
    • (1989) Biochemistry , vol.28 , pp. 2313-2321
    • Roux, M.1    Newmann, Y.2    Hodges, R.3
  • 7
    • 0000284138 scopus 로고
    • Interaction of melittin with mixed phospholipid membranes composed of dimyristoylphosphatidylserine studied by deuterium NMR
    • Dempsey C., Bitbol M., and Watts A. Interaction of melittin with mixed phospholipid membranes composed of dimyristoylphosphatidylserine studied by deuterium NMR. Biochemistry 28 (1989) 6590-6595
    • (1989) Biochemistry , vol.28 , pp. 6590-6595
    • Dempsey, C.1    Bitbol, M.2    Watts, A.3
  • 8
    • 0023615921 scopus 로고
    • A study of the structure of polymyxin B - dipalmitoylphosphatidylglycerol complexes by vibrational spectroscopy
    • Babin Y., D'Amour J., Pigeon M., and Pezolet M. A study of the structure of polymyxin B - dipalmitoylphosphatidylglycerol complexes by vibrational spectroscopy. Biochim. Biophys. Acta 903 (1987) 78-88
    • (1987) Biochim. Biophys. Acta , vol.903 , pp. 78-88
    • Babin, Y.1    D'Amour, J.2    Pigeon, M.3    Pezolet, M.4
  • 9
    • 0024591992 scopus 로고
    • Thermodynamic and kinetic studies on the association of melittin with a phospholipid bilayer
    • Schwarz G., and Beschiachvili G. Thermodynamic and kinetic studies on the association of melittin with a phospholipid bilayer. Biochim. Biophys. Acta 979 (1989) 82-90
    • (1989) Biochim. Biophys. Acta , vol.979 , pp. 82-90
    • Schwarz, G.1    Beschiachvili, G.2
  • 10
    • 0019891830 scopus 로고
    • Fluorescence quenching in model membranes: 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics
    • Caffrey M., and Feigenson G.W. Fluorescence quenching in model membranes: 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics. Biochemistry 20 (1981) 1949-1961
    • (1981) Biochemistry , vol.20 , pp. 1949-1961
    • Caffrey, M.1    Feigenson, G.W.2
  • 11
    • 0033552653 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy analysis of the hydrophobic interactions of protein 4.1 with phosphatidylserine liposomes
    • Takakuwa Y., Pack C.G., An X.L., Manno S., Ito E., and Kinjo M. Fluorescence correlation spectroscopy analysis of the hydrophobic interactions of protein 4.1 with phosphatidylserine liposomes. Biophys. Chemist. 82 (1999) 149-155
    • (1999) Biophys. Chemist. , vol.82 , pp. 149-155
    • Takakuwa, Y.1    Pack, C.G.2    An, X.L.3    Manno, S.4    Ito, E.5    Kinjo, M.6
  • 13
    • 33745151952 scopus 로고    scopus 로고
    • Membrane interactions of cell-penetrating peptides probed by tryptophan fluorescence and dichroism techniques: correlations of structure to cellular uptake
    • Caesar C.E., Esbjorner E.K., Lincoln P., and Norden B. Membrane interactions of cell-penetrating peptides probed by tryptophan fluorescence and dichroism techniques: correlations of structure to cellular uptake. Biochemistry 45 (2006) 7682-7692
    • (2006) Biochemistry , vol.45 , pp. 7682-7692
    • Caesar, C.E.1    Esbjorner, E.K.2    Lincoln, P.3    Norden, B.4
  • 14
    • 33646582344 scopus 로고    scopus 로고
    • Targeting membrane proteins to liquid-ordered phases: molecular self-organization explored by fluorescence correlation spectroscopy
    • Kahya N. Targeting membrane proteins to liquid-ordered phases: molecular self-organization explored by fluorescence correlation spectroscopy. Chem. Phys. Lipids 141 (2006) 158-168
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 158-168
    • Kahya, N.1
  • 15
    • 33744788870 scopus 로고    scopus 로고
    • Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy
    • Rhoades E., Ramlall T.F., Webb W.W., and Eliezer D. Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy. Biophys. J. 90 (2006) 4692-4700
    • (2006) Biophys. J. , vol.90 , pp. 4692-4700
    • Rhoades, E.1    Ramlall, T.F.2    Webb, W.W.3    Eliezer, D.4
  • 16
    • 17144422439 scopus 로고    scopus 로고
    • Lysozyme effect on structural state of model membranes as revealed by pyrene excimerization studies
    • Ioffe V.M., and Gorbenko G.P. Lysozyme effect on structural state of model membranes as revealed by pyrene excimerization studies. Biophys. Chemist. 114 (2005) 199-204
    • (2005) Biophys. Chemist. , vol.114 , pp. 199-204
    • Ioffe, V.M.1    Gorbenko, G.P.2
  • 17
    • 0033559170 scopus 로고    scopus 로고
    • A fluorescence resonance energy transfer approach for monitoring protein-mediated glycolipid transfer between vesicle membranes
    • Mattjus P., Molotkovsky J.G., Smaby J.M., and Brown R.E. A fluorescence resonance energy transfer approach for monitoring protein-mediated glycolipid transfer between vesicle membranes. Anal. Biochem. 268 (1999) 297-304
    • (1999) Anal. Biochem. , vol.268 , pp. 297-304
    • Mattjus, P.1    Molotkovsky, J.G.2    Smaby, J.M.3    Brown, R.E.4
  • 18
    • 0028836142 scopus 로고
    • Reversibility of the binding of cytochrome c to liposomes. Implications for lipid-protein interactions
    • Rytömaa M., and Kinnunen P.K.J. Reversibility of the binding of cytochrome c to liposomes. Implications for lipid-protein interactions. J. Biol. Chem. 270 (1995) 3197-3202
    • (1995) J. Biol. Chem. , vol.270 , pp. 3197-3202
    • Rytömaa, M.1    Kinnunen, P.K.J.2
  • 19
    • 33745830875 scopus 로고    scopus 로고
    • Lipid-induced conformational transitions of beta-lactoglobulin
    • Zhang X., and Keiderling T.A. Lipid-induced conformational transitions of beta-lactoglobulin. Biochemistry 45 (2006) 8444-8452
    • (2006) Biochemistry , vol.45 , pp. 8444-8452
    • Zhang, X.1    Keiderling, T.A.2
  • 20
    • 33644854069 scopus 로고    scopus 로고
    • Scanning the membrane-bound conformation of helix 1 in the colicin E1 channel domain by site-directed fluorescence labelling
    • Musse A.A., Wang J., Deleon G.P., Prentice G.A., London E., and Merrill A.R. Scanning the membrane-bound conformation of helix 1 in the colicin E1 channel domain by site-directed fluorescence labelling. J. Biol. Chem. 281 (2006) 885-895
    • (2006) J. Biol. Chem. , vol.281 , pp. 885-895
    • Musse, A.A.1    Wang, J.2    Deleon, G.P.3    Prentice, G.A.4    London, E.5    Merrill, A.R.6
  • 21
    • 0037466114 scopus 로고    scopus 로고
    • Cytochrome c location in phosphatidylcholine/cardiolipin model membranes: resonance energy transfer study
    • Gorbenko G.P., and Domanov Ye.A. Cytochrome c location in phosphatidylcholine/cardiolipin model membranes: resonance energy transfer study. Biophys. Chemist. 103 (2003) 239-249
    • (2003) Biophys. Chemist. , vol.103 , pp. 239-249
    • Gorbenko, G.P.1    Domanov, Ye.A.2
  • 22
    • 0032476687 scopus 로고    scopus 로고
    • Resonance energy transfer study of hemoglobin and cytochrome c complexes with lipids
    • Gorbenko G.P. Resonance energy transfer study of hemoglobin and cytochrome c complexes with lipids. Biochim. Biophys. Acta 1409 (1998) 12-24
    • (1998) Biochim. Biophys. Acta , vol.1409 , pp. 12-24
    • Gorbenko, G.P.1
  • 23
    • 0043234255 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of cytochromes P450, 2C2 and 2E1 molecular interactions in living cells
    • Szczesna-Skorupa E., Mallah B., and Kemper B. Fluorescence resonance energy transfer analysis of cytochromes P450, 2C2 and 2E1 molecular interactions in living cells. J. Biol. Chem. 278 (2003) 31269-31276
    • (2003) J. Biol. Chem. , vol.278 , pp. 31269-31276
    • Szczesna-Skorupa, E.1    Mallah, B.2    Kemper, B.3
  • 24
    • 0141785142 scopus 로고    scopus 로고
    • Dependence of M13 major coat protein oligomerization and lateral segregation on bilayer composition
    • Fernandes F., Loura L.M.S., Prieto M., Koehorst R., Spruijt R.B., and Hemminga M.A. Dependence of M13 major coat protein oligomerization and lateral segregation on bilayer composition. Biophys. J. 85 (2003) 2430-2441
    • (2003) Biophys. J. , vol.85 , pp. 2430-2441
    • Fernandes, F.1    Loura, L.M.S.2    Prieto, M.3    Koehorst, R.4    Spruijt, R.B.5    Hemminga, M.A.6
  • 25
    • 33745714410 scopus 로고    scopus 로고
    • FRET study of membrane proteins: simulation-based fitting for analysis of membrane protein embedment and association
    • Nazarov P.V., Koehorst R.B., Vos W.L., Apanasovich V.V., and Hemminga M.A. FRET study of membrane proteins: simulation-based fitting for analysis of membrane protein embedment and association. Biophys. J. 91 (2006) 454-466
    • (2006) Biophys. J. , vol.91 , pp. 454-466
    • Nazarov, P.V.1    Koehorst, R.B.2    Vos, W.L.3    Apanasovich, V.V.4    Hemminga, M.A.5
  • 26
    • 33646870619 scopus 로고    scopus 로고
    • A spectroscopic study of the membrane interaction of the antimicrobial peptide Pleurocidin
    • Mason A.J., Chotimah I.N., Bertani P., and Bechinger B.A. A spectroscopic study of the membrane interaction of the antimicrobial peptide Pleurocidin. Mol. Membr. Biol. 23 (2006) 185-194
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 185-194
    • Mason, A.J.1    Chotimah, I.N.2    Bertani, P.3    Bechinger, B.A.4
  • 28
    • 4043100348 scopus 로고    scopus 로고
    • Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
    • Zhao H., Tuominen E.K.J., and Kinnunen P.K.J. Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry 43 (2004) 10302-10307
    • (2004) Biochemistry , vol.43 , pp. 10302-10307
    • Zhao, H.1    Tuominen, E.K.J.2    Kinnunen, P.K.J.3
  • 29
    • 14344250143 scopus 로고    scopus 로고
    • Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers
    • Zhao H., Jutila A., Nurminen T., Wickstrom S.A., Keski-Oja J., and Kinnunen P.K.J. Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers. Biochemistry 44 (2005) 2857-2863
    • (2005) Biochemistry , vol.44 , pp. 2857-2863
    • Zhao, H.1    Jutila, A.2    Nurminen, T.3    Wickstrom, S.A.4    Keski-Oja, J.5    Kinnunen, P.K.J.6
  • 31
    • 33745923547 scopus 로고    scopus 로고
    • Examining protein-lipid interactions in model systems with a new squarylium fluorescent dye
    • Ioffe V.M., Gorbenko G.P., Tatarets A.L., Patsenker L.D., and Terpechnig E.A. Examining protein-lipid interactions in model systems with a new squarylium fluorescent dye. J. Fluoresc. 16 (2006) 547-554
    • (2006) J. Fluoresc. , vol.16 , pp. 547-554
    • Ioffe, V.M.1    Gorbenko, G.P.2    Tatarets, A.L.3    Patsenker, L.D.4    Terpechnig, E.A.5
  • 32
    • 0025844368 scopus 로고
    • Synthesis and characterization of 1,3-bis-(2-dialkylamino-5-thienyl)-substituted squaraines - a novel class of intensively coloured panchromatic dyes
    • Keil D., Hartmann H., and Moschny T. Synthesis and characterization of 1,3-bis-(2-dialkylamino-5-thienyl)-substituted squaraines - a novel class of intensively coloured panchromatic dyes. Dyes Pigm. 17 (1991) 19-27
    • (1991) Dyes Pigm. , vol.17 , pp. 19-27
    • Keil, D.1    Hartmann, H.2    Moschny, T.3
  • 33
    • 0842291515 scopus 로고    scopus 로고
    • Squaraine dyes for photodynamic therapy: mechanism of cytotoxicity and DNA damage induced by halogenated squaraine dyes plus light (> 600 nm)
    • Ramaiah D., Eckert I., Arun K.T., Weidenfeller L., and Epe B. Squaraine dyes for photodynamic therapy: mechanism of cytotoxicity and DNA damage induced by halogenated squaraine dyes plus light (> 600 nm). Photochem. photobiol. 79 (2004) 99-104
    • (2004) Photochem. photobiol. , vol.79 , pp. 99-104
    • Ramaiah, D.1    Eckert, I.2    Arun, K.T.3    Weidenfeller, L.4    Epe, B.5
  • 34
    • 0023379625 scopus 로고
    • Squaraine chemistry: effect of synthesis on the morphological and xerographic properties of photoconductive squaraines
    • Law K.Y., and Bailey F.C. Squaraine chemistry: effect of synthesis on the morphological and xerographic properties of photoconductive squaraines. J. Imag. Sci. 31 (1987) 172-175
    • (1987) J. Imag. Sci. , vol.31 , pp. 172-175
    • Law, K.Y.1    Bailey, F.C.2
  • 35
    • 34247625391 scopus 로고    scopus 로고
    • Polaroid Corporation, US Patent 5795981.
  • 36
    • 36749114561 scopus 로고
    • Organic solar cells of hydroxysquarylium
    • Merritt V.Y., and Hovel H.J. Organic solar cells of hydroxysquarylium. Appl. Phys. Lett. 29 (1976) 414-416
    • (1976) Appl. Phys. Lett. , vol.29 , pp. 414-416
    • Merritt, V.Y.1    Hovel, H.J.2
  • 37
    • 0028071629 scopus 로고
    • Enhanced bactericidal action of lysozyme to Escherichia coli by inserting a hydrophobic pentapeptide into its C terminus
    • Ibrahim H.R., Yamada M., Matsushita K., Kobayashi K., and Kato A. Enhanced bactericidal action of lysozyme to Escherichia coli by inserting a hydrophobic pentapeptide into its C terminus. J. Biol. Chem. 269 (1994) 5053-5063
    • (1994) J. Biol. Chem. , vol.269 , pp. 5053-5063
    • Ibrahim, H.R.1    Yamada, M.2    Matsushita, K.3    Kobayashi, K.4    Kato, A.5
  • 39
    • 0035941271 scopus 로고    scopus 로고
    • A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action
    • Ibrahim H.R., Thomas U., and Pellegrini A. A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. J. Biol. Chem. 276 (2001) 43767-43774
    • (2001) J. Biol. Chem. , vol.276 , pp. 43767-43774
    • Ibrahim, H.R.1    Thomas, U.2    Pellegrini, A.3
  • 40
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines R.T. Ribonuclease A. Chem. Rev. 98 (1998) 1045-1065
    • (1998) Chem. Rev. , vol.98 , pp. 1045-1065
    • Raines, R.T.1
  • 42
    • 0015239056 scopus 로고
    • Interactions of basic proteins with phospholipid membranes. Binding and changes in the sodium permeability of phosphotidylserine vesicles
    • Kimelberg H.K., and Papahadjopoulos D. Interactions of basic proteins with phospholipid membranes. Binding and changes in the sodium permeability of phosphotidylserine vesicles. J. Biol. Chem. 246 (1971) 1142-1148
    • (1971) J. Biol. Chem. , vol.246 , pp. 1142-1148
    • Kimelberg, H.K.1    Papahadjopoulos, D.2
  • 43
    • 0004155427 scopus 로고
    • W.H. Freeman, New York
    • Stryer L. Biochemistry (1995), W.H. Freeman, New York
    • (1995) Biochemistry
    • Stryer, L.1
  • 44
    • 0017253898 scopus 로고
    • Protein-liposome interactions and their relevance to the structure and function of cell membranes
    • Kimelberg H.K. Protein-liposome interactions and their relevance to the structure and function of cell membranes. Mol. Cell. Biochem. 10 (1976) 171-190
    • (1976) Mol. Cell. Biochem. , vol.10 , pp. 171-190
    • Kimelberg, H.K.1
  • 45
  • 46
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world
    • Stefani M. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta 1739 (2004) 5-25
    • (2004) Biochim. Biophys. Acta , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 47
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: structure and assembly
    • Serpell L.C. Alzheimer's amyloid fibrils: structure and assembly. Biochim. Biophys. Acta 1502 (2000) 16-30
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 48
    • 0028179865 scopus 로고
    • Alzheimer Aβ-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes
    • Terzi E., Höelzemann G., and Seelig J. Alzheimer Aβ-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes. Biochemistry 33 (1994) 7434-7441
    • (1994) Biochemistry , vol.33 , pp. 7434-7441
    • Terzi, E.1    Höelzemann, G.2    Seelig, J.3
  • 49
    • 33646557678 scopus 로고    scopus 로고
    • The role of lipid-protein interactions in amyloid-type protein fibril formation
    • Gorbenko G.P., and Kinnunen P.K.J. The role of lipid-protein interactions in amyloid-type protein fibril formation. Chem. Phys. Lipids 141 (2006) 72-82
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 72-82
    • Gorbenko, G.P.1    Kinnunen, P.K.J.2
  • 50
    • 1642452936 scopus 로고    scopus 로고
    • Formation of amyloid fibrils from fully reduced hen egg white lysozyme
    • Cao A., Hu D., and Lai L. Formation of amyloid fibrils from fully reduced hen egg white lysozyme. Protein Sci. 13 (2004) 319-324
    • (2004) Protein Sci. , vol.13 , pp. 319-324
    • Cao, A.1    Hu, D.2    Lai, L.3
  • 52
    • 24644510813 scopus 로고    scopus 로고
    • Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure
    • Sambashivan S., Liu Y., Sawaya M.R., Gingery M., and Eisenberg D. Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure. Nature 437 (2005) 266-269
    • (2005) Nature , vol.437 , pp. 266-269
    • Sambashivan, S.1    Liu, Y.2    Sawaya, M.R.3    Gingery, M.4    Eisenberg, D.5
  • 53
    • 0019201689 scopus 로고
    • Cardiolipin, a major phospholipid of Gram-positive bacteria that is not readily extractable
    • Filgueiras M.H., and Op den Kamp J.A. Cardiolipin, a major phospholipid of Gram-positive bacteria that is not readily extractable. Biochim. Biophys. Acta 620 (1980) 332-337
    • (1980) Biochim. Biophys. Acta , vol.620 , pp. 332-337
    • Filgueiras, M.H.1    Op den Kamp, J.A.2
  • 54
    • 2142642612 scopus 로고    scopus 로고
    • Synthesis and characterization of heptamethine cyanine dyes
    • Li Q., Ji T., and Bi-Xian P. Synthesis and characterization of heptamethine cyanine dyes. Molecules 2 (1997) 91-98
    • (1997) Molecules , vol.2 , pp. 91-98
    • Li, Q.1    Ji, T.2    Bi-Xian, P.3
  • 55
    • 0032035848 scopus 로고    scopus 로고
    • Synthesis and properties of functional aminosquarylium dyes
    • Kim S.H., Hwang S.H., Kim J.J., Yoon C.M., and Keun S.R. Synthesis and properties of functional aminosquarylium dyes. Dyes Pigm. 37 (1998) 145-154
    • (1998) Dyes Pigm. , vol.37 , pp. 145-154
    • Kim, S.H.1    Hwang, S.H.2    Kim, J.J.3    Yoon, C.M.4    Keun, S.R.5
  • 56
    • 0242380856 scopus 로고    scopus 로고
    • Extrusion technique to generate liposomes of defined size
    • Mui B., Chow L., and Hope M.J. Extrusion technique to generate liposomes of defined size. Methods Enzymol. 367 (2003) 3-14
    • (2003) Methods Enzymol. , vol.367 , pp. 3-14
    • Mui, B.1    Chow, L.2    Hope, M.J.3
  • 57
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett G. Phosphorus assay in column chromatography. J. Biol. Chem. 234 (1959) 466-468
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.1
  • 58
    • 0026551529 scopus 로고
    • Refinement of an enzyme complex with inhibitor bound at partial occupancy. Hen egg-white lysozyme and tri-N-acetylchitotriose at 1.75 Å resolution
    • Cheetham J.C., Artymiuk P.J., and Phillips D.C. Refinement of an enzyme complex with inhibitor bound at partial occupancy. Hen egg-white lysozyme and tri-N-acetylchitotriose at 1.75 Å resolution. J. Mol. Biol. 224 (1992) 613-628
    • (1992) J. Mol. Biol. , vol.224 , pp. 613-628
    • Cheetham, J.C.1    Artymiuk, P.J.2    Phillips, D.C.3
  • 59
    • 0026606219 scopus 로고
    • Effects of temperature on protein structure and dynamics: X-ray crystallographic of the protein ribonuclease A at nine different temperatures from 98 to 320 K
    • Tilton R.F., Dewan J.C., and Petsko G.A. Effects of temperature on protein structure and dynamics: X-ray crystallographic of the protein ribonuclease A at nine different temperatures from 98 to 320 K. Biochemistry 31 (1992) 2469-2481
    • (1992) Biochemistry , vol.31 , pp. 2469-2481
    • Tilton, R.F.1    Dewan, J.C.2    Petsko, G.A.3
  • 60
    • 0038392423 scopus 로고    scopus 로고
    • Quantifying molecular partition into model systems of biomembranes: an emphasis on optical spectroscopic methods
    • Santos N.C., Prieto M., and Castanho M.A.R.B. Quantifying molecular partition into model systems of biomembranes: an emphasis on optical spectroscopic methods. Biochim. Biophys. Acta 1612 (2003) 123-135
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 123-135
    • Santos, N.C.1    Prieto, M.2    Castanho, M.A.R.B.3
  • 65
    • 0028287424 scopus 로고
    • Significant stabilization of the phosphatidylcholine bilayer structure by incorporation of small amounts of cardiolipin
    • Shibata A., Ikawa K., Shimooka T., and Terada H. Significant stabilization of the phosphatidylcholine bilayer structure by incorporation of small amounts of cardiolipin. Biochim. Biophys. Acta 1192 (1994) 71-78
    • (1994) Biochim. Biophys. Acta , vol.1192 , pp. 71-78
    • Shibata, A.1    Ikawa, K.2    Shimooka, T.3    Terada, H.4
  • 66
    • 0014673553 scopus 로고
    • Interactions of proteins and lipids: structure and polymorphism of protein-lipid-water phases
    • Gulik-Krzywicki T., Shechter E., Luzzati V., and Faure M. Interactions of proteins and lipids: structure and polymorphism of protein-lipid-water phases. Nature 223 (1969) 1116-1120
    • (1969) Nature , vol.223 , pp. 1116-1120
    • Gulik-Krzywicki, T.1    Shechter, E.2    Luzzati, V.3    Faure, M.4
  • 67
    • 0027981591 scopus 로고
    • Lysozyme interactions with phospholipid vesicles: relationships with fusion and release of aqueous content
    • Posse E., de Arcuri B.F., and Morero d.R.D. Lysozyme interactions with phospholipid vesicles: relationships with fusion and release of aqueous content. Biochim. Biophys. Acta 1193 (1994) 101-106
    • (1994) Biochim. Biophys. Acta , vol.1193 , pp. 101-106
    • Posse, E.1    de Arcuri, B.F.2    Morero, d.R.D.3
  • 69
    • 0036169327 scopus 로고    scopus 로고
    • Binding of globular proteins to lipid membranes studied by isothermal titration calorimetry and fluorescence
    • Dimitrova M.N., Matsumura H., Terezova N., and Neytchev V. Binding of globular proteins to lipid membranes studied by isothermal titration calorimetry and fluorescence. Colloids Surf. B Biointerfaces 24 (2002) 53-61
    • (2002) Colloids Surf. B Biointerfaces , vol.24 , pp. 53-61
    • Dimitrova, M.N.1    Matsumura, H.2    Terezova, N.3    Neytchev, V.4
  • 70
    • 0016712926 scopus 로고
    • Effects of proteins on thermotropic phase transitions of phospholipid membranes
    • Papahadjopoulos D., Moscarello M., Eylar E.H., and Isac T. Effects of proteins on thermotropic phase transitions of phospholipid membranes. Biochim. Biophys. Acta 401 (1975) 317-335
    • (1975) Biochim. Biophys. Acta , vol.401 , pp. 317-335
    • Papahadjopoulos, D.1    Moscarello, M.2    Eylar, E.H.3    Isac, T.4
  • 71
    • 0029014955 scopus 로고
    • Protein location in liposomes, a drug carriers: a prediction by differential scanning calorimetry
    • Lo Y.L., and Rahman Y.E. Protein location in liposomes, a drug carriers: a prediction by differential scanning calorimetry. J. Pharm. Sci. 84 (1995) 805-814
    • (1995) J. Pharm. Sci. , vol.84 , pp. 805-814
    • Lo, Y.L.1    Rahman, Y.E.2
  • 72
    • 0026942482 scopus 로고
    • A thermodynamic study of protein-lipid lateral phase separation. Effect of lysozyme on mixed lipid vesicles
    • Raudino A., and Castelli F. A thermodynamic study of protein-lipid lateral phase separation. Effect of lysozyme on mixed lipid vesicles. Colloid Polym. Sci. 270 (1992) 1116-1123
    • (1992) Colloid Polym. Sci. , vol.270 , pp. 1116-1123
    • Raudino, A.1    Castelli, F.2
  • 73
    • 0031927361 scopus 로고    scopus 로고
    • Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: an electrostatic model and experimental results
    • Denisov G., Wanaski S., Luan P., Glaser M., and McLaughlin S. Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: an electrostatic model and experimental results. Biophys. J. 74 (1998) 731-744
    • (1998) Biophys. J. , vol.74 , pp. 731-744
    • Denisov, G.1    Wanaski, S.2    Luan, P.3    Glaser, M.4    McLaughlin, S.5
  • 74
    • 0034152715 scopus 로고    scopus 로고
    • Association of lysozyme with phospholipid vesicles is accompanied by membrane surface dehydration
    • Zschornig O., Paasche G., Thieme C., Korb N., Fahrwald A., and Arnold K. Association of lysozyme with phospholipid vesicles is accompanied by membrane surface dehydration. Gen. Physiol. Biophys. 19 (2000) 85-101
    • (2000) Gen. Physiol. Biophys. , vol.19 , pp. 85-101
    • Zschornig, O.1    Paasche, G.2    Thieme, C.3    Korb, N.4    Fahrwald, A.5    Arnold, K.6
  • 75
    • 0025974966 scopus 로고
    • On the principles of functional ordering in biological membranes
    • Kinnunen P.J.K. On the principles of functional ordering in biological membranes. Chem. Phys. Lipids 57 (1991) 375-399
    • (1991) Chem. Phys. Lipids , vol.57 , pp. 375-399
    • Kinnunen, P.J.K.1
  • 76
    • 0030947939 scopus 로고    scopus 로고
    • Cholesterol and ergosterol superlattices in three-component liquid crystalline lipid bilayers as revealed by dehydroergosterol fluorescence
    • Liu F., Sugar I.P., and Chong L.G. Cholesterol and ergosterol superlattices in three-component liquid crystalline lipid bilayers as revealed by dehydroergosterol fluorescence. Biophys. J. 72 (1997) 2243-2254
    • (1997) Biophys. J. , vol.72 , pp. 2243-2254
    • Liu, F.1    Sugar, I.P.2    Chong, L.G.3
  • 78
    • 0344981517 scopus 로고    scopus 로고
    • Hydration, structure, and molecular interactions in the headgroup region of dioleoylphosphatidylcholine bilayers: an electron spin resonance study
    • Ge M., and Freed J.H. Hydration, structure, and molecular interactions in the headgroup region of dioleoylphosphatidylcholine bilayers: an electron spin resonance study. Biophys. J. 85 (2003) 4023-4040
    • (2003) Biophys. J. , vol.85 , pp. 4023-4040
    • Ge, M.1    Freed, J.H.2
  • 80
    • 3042587512 scopus 로고    scopus 로고
    • Electronic structure and photochemistry of squaraine dyes: basic theoretical analysis and direct detection of the photoisomer of a symmetrical squarylium cyanine
    • Momicchioli F., Tatikolov A.S., Vanossi D., and Ponterini G. Electronic structure and photochemistry of squaraine dyes: basic theoretical analysis and direct detection of the photoisomer of a symmetrical squarylium cyanine. Photochem. photobiol. Sci. 3 (2004) 396-402
    • (2004) Photochem. photobiol. Sci. , vol.3 , pp. 396-402
    • Momicchioli, F.1    Tatikolov, A.S.2    Vanossi, D.3    Ponterini, G.4
  • 82
    • 0031982611 scopus 로고    scopus 로고
    • Permeation of halide anions through phospholipid bilayers occurs by the solubility-diffusion mechanism
    • Paula S., Volkov A.G., and Deamer D.W. Permeation of halide anions through phospholipid bilayers occurs by the solubility-diffusion mechanism. Biophys. J. 74 (1998) 319-327
    • (1998) Biophys. J. , vol.74 , pp. 319-327
    • Paula, S.1    Volkov, A.G.2    Deamer, D.W.3
  • 83
    • 0018814426 scopus 로고
    • Chlorinated hydrocarbon-cell membrane interactions studied by the fluorescence quenching of carbazole-labeled phospholipids: probe synthesis and characterization of the quenching methodology
    • Lakowicz J.R., and Hogen D. Chlorinated hydrocarbon-cell membrane interactions studied by the fluorescence quenching of carbazole-labeled phospholipids: probe synthesis and characterization of the quenching methodology. Chem. Phys. Lipids 26 (1980) 1-40
    • (1980) Chem. Phys. Lipids , vol.26 , pp. 1-40
    • Lakowicz, J.R.1    Hogen, D.2
  • 84
    • 33751158845 scopus 로고
    • Simulation of water transport through a lipid membrane
    • Marrink S.J., and Berendsen H.J.C. Simulation of water transport through a lipid membrane. J. Phys. Chem. 98 (1994) 4155-4168
    • (1994) J. Phys. Chem. , vol.98 , pp. 4155-4168
    • Marrink, S.J.1    Berendsen, H.J.C.2
  • 85
    • 0025679188 scopus 로고
    • Facilitated ion transport through thin bilayers
    • Hamilton R.T., and Kaler E.W. Facilitated ion transport through thin bilayers. J. Membr. Sci. 54 (1990) 259-269
    • (1990) J. Membr. Sci. , vol.54 , pp. 259-269
    • Hamilton, R.T.1    Kaler, E.W.2
  • 87
    • 2942692314 scopus 로고    scopus 로고
    • Membrane perturbation induced by interfacially absorbed peptides
    • Zemel A., Ben-Shaul S., and May. Membrane perturbation induced by interfacially absorbed peptides. Biophys. J. 86 (2004) 3607-3619
    • (2004) Biophys. J. , vol.86 , pp. 3607-3619
    • Zemel, A.1    Ben-Shaul, S.2    May3


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