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Volumn 1418, Issue 1, 1999, Pages 106-116

Stabilizing effect of an S-layer on liposomes towards thermal or mechanical stress

Author keywords

Crystalline bacterial surface layer; Liposome; S layer

Indexed keywords

ALIPHATIC AMINE; CELL SURFACE PROTEIN; CHOLESTEROL; DIPALMITOYLPHOSPHATIDYLCHOLINE; HEXADECYLAMINE; LIPOSOME; UNCLASSIFIED DRUG;

EID: 0345435047     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(99)00030-9     Document Type: Article
Times cited : (63)

References (35)
  • 3
    • 0018195592 scopus 로고
    • Regular arrays of macromolecules on bacterial cell walls: Structure, chemistry, assembly and function
    • U.B. Sleytr, Regular arrays of macromolecules on bacterial cell walls: structure, chemistry, assembly and function, Int. Rev. Cytol. 53 (1978) 1-64.
    • (1978) Int. Rev. Cytol. , vol.53 , pp. 1-64
    • Sleytr, U.B.1
  • 4
    • 0027167476 scopus 로고
    • Relevance of charged groups for the integrity of the S-layer from Bacillus coagulans E38-66 and for molecular interactions
    • M. Sára, U.B. Sleytr, Relevance of charged groups for the integrity of the S-layer from Bacillus coagulans E38-66 and for molecular interactions, J. Bacteriol. 175 (1993) 2248-2254.
    • (1993) J. Bacteriol. , vol.175 , pp. 2248-2254
    • Sára, M.1    Sleytr, U.B.2
  • 5
    • 0027189904 scopus 로고
    • Large scale recrystallization of the S-layer of Bacillus coagulans E38-66 at the air/water interface and on lipid films
    • D. Pum, M. Weinhandel, C. Hödel, U.B. Sleytr, Large scale recrystallization of the S-layer of Bacillus coagulans E38-66 at the air/water interface and on lipid films, J. Bacteriol. 195 (1993) 2762-2766.
    • (1993) J. Bacteriol. , vol.195 , pp. 2762-2766
    • Pum, D.1    Weinhandel, M.2    Hödel, C.3    Sleytr, U.B.4
  • 6
    • 0028433572 scopus 로고
    • Large-scale reconstitution of crystalline bacterial surface layer proteins at air/water interface and on lipid films
    • D. Pum, U.B. Sleytr, Large-scale reconstitution of crystalline bacterial surface layer proteins at air/water interface and on lipid films, Thin Solid Films 244 (1994) 882-886.
    • (1994) Thin Solid Films , vol.244 , pp. 882-886
    • Pum, D.1    Sleytr, U.B.2
  • 7
    • 0024456474 scopus 로고
    • Structure, surface charge, and self-assembly of the S-layer lattice from Bacillus coagulans E38-66
    • D. Pum, M. Sára, U.B. Sleytr, Structure, surface charge, and self-assembly of the S-layer lattice from Bacillus coagulans E38-66, J. Bacteriol. 171 (1989) 5296-5303.
    • (1989) J. Bacteriol. , vol.171 , pp. 5296-5303
    • Pum, D.1    Sára, M.2    Sleytr, U.B.3
  • 9
    • 0032513080 scopus 로고    scopus 로고
    • Self-assembled α-hemolysin pores in an S-layer-supported lipid bilayer
    • B. Schuster, D. Pum, O. Braha, H. Bayley, U.B. Sleytr, Self-assembled α-hemolysin pores in an S-layer-supported lipid bilayer, Biochim. Biophys. Acta 1370 (1998) 280-288.
    • (1998) Biochim. Biophys. Acta , vol.1370 , pp. 280-288
    • Schuster, B.1    Pum, D.2    Braha, O.3    Bayley, H.4    Sleytr, U.B.5
  • 10
    • 0032472790 scopus 로고    scopus 로고
    • Voltage clamp studies on S-layer supported tetraether lipid membranes
    • B. Schuster, D. Pum, U.B. Sleytr, Voltage clamp studies on S-layer supported tetraether lipid membranes, Biochim. Biophys. Acta 1369 (1998) 51-60.
    • (1998) Biochim. Biophys. Acta , vol.1369 , pp. 51-60
    • Schuster, B.1    Pum, D.2    Sleytr, U.B.3
  • 11
    • 0029040954 scopus 로고
    • Liposomes coated with crystalline bacterial cell surface protein (S-layer) as immobilization structures for macromolecules
    • S. Küpcü, M. Sára, U.B. Sleytr, Liposomes coated with crystalline bacterial cell surface protein (S-layer) as immobilization structures for macromolecules, Biochim. Biophys. Acta 1235 (1995) 263-269.
    • (1995) Biochim. Biophys. Acta , vol.1235 , pp. 263-269
    • Küpcü, S.1    Sára, M.2    Sleytr, U.B.3
  • 12
    • 0031038990 scopus 로고    scopus 로고
    • Molecular characterization of the second S-layer gene sbsB of Bacillus stearothermophilus PV72 expressed by oxidative stress
    • B. Kuen, A. Koch, E. Asenbauer, M. Sára, W. Lubitz, Molecular characterization of the second S-layer gene sbsB of Bacillus stearothermophilus PV72 expressed by oxidative stress, J. Bacteriol. 179 (1997) 1664-1670.
    • (1997) J. Bacteriol. , vol.179 , pp. 1664-1670
    • Kuen, B.1    Koch, A.2    Asenbauer, E.3    Sára, M.4    Lubitz, W.5
  • 13
    • 0021704080 scopus 로고
    • Dehydration-rehydration vesicles: A simple method for high yield drug entrapment in liposomes
    • C. Kirby, G. Gregoriadis, Dehydration-rehydration vesicles: a simple method for high yield drug entrapment in liposomes, Bio/technology 2 (1984) 979-984.
    • (1984) Bio/Technology , vol.2 , pp. 979-984
    • Kirby, C.1    Gregoriadis, G.2
  • 15
    • 0029876584 scopus 로고    scopus 로고
    • Dynamics in oxygen-induced changes in S-layer protein synthesis and cell wall composition in continuous culture from Bacillus stearothermophilus PV72 and its S-layer-deficient variant T5
    • M. Sára, B. Kuen, H.F. Mayer, F. Mandel, K.C. Schuster, U.B. Sleytr, Dynamics in oxygen-induced changes in S-layer protein synthesis and cell wall composition in continuous culture from Bacillus stearothermophilus PV72 and its S-layer-deficient variant T5, J. Bacteriol. 178 (1996) 2108-2117.
    • (1996) J. Bacteriol. , vol.178 , pp. 2108-2117
    • Sára, M.1    Kuen, B.2    Mayer, H.F.3    Mandel, F.4    Schuster, K.C.5    Sleytr, U.B.6
  • 16
    • 0030615947 scopus 로고    scopus 로고
    • Oxygen-triggered synchronized variant formation of the S-layer carrying Bacillus stearothermophilus PV72 during continuous cultivation
    • K.C. Schuster, T. Pink, H.F. Mayer, W.A. Hampel, M. Sara, Oxygen-triggered synchronized variant formation of the S-layer carrying Bacillus stearothermophilus PV72 during continuous cultivation, J. Biotechnol. 54 (1997) 15-28.
    • (1997) J. Biotechnol. , vol.54 , pp. 15-28
    • Schuster, K.C.1    Pink, T.2    Mayer, H.F.3    Hampel, W.A.4    Sara, M.5
  • 17
    • 0017128465 scopus 로고
    • Self-assembly of the hexagonally and tetragonally arranged subunits of bacterial surface layers and their reattachment to cell walls
    • U.B. Sleytr, A.M. Glauert, Self-assembly of the hexagonally and tetragonally arranged subunits of bacterial surface layers and their reattachment to cell walls, J. Ultrastruct. Res. 55 (1975) 360-377.
    • (1975) J. Ultrastruct. Res. , vol.55 , pp. 360-377
    • Sleytr, U.B.1    Glauert, A.M.2
  • 19
    • 0025970192 scopus 로고
    • Determination of vesicle size distributions by freeze-fracture electron microscopy
    • F.R. Hallett, B. Nickel, C. Samuels, P.H. Krygsman, Determination of vesicle size distributions by freeze-fracture electron microscopy, J. Electron Microsc. Techn. 17 (1991) 459-466.
    • (1991) J. Electron Microsc. Techn. , vol.17 , pp. 459-466
    • Hallett, F.R.1    Nickel, B.2    Samuels, C.3    Krygsman, P.H.4
  • 20
    • 0002031860 scopus 로고
    • Low temperature methods in electron microscopy
    • A.M. Glauert (Ed.), Elsevier, Amsterdam
    • A. Robards, U.B. Sleytr, Low temperature methods in electron microscopy, in: A.M. Glauert (Ed.), Practical Methods in Electron Microscopy, vol. 10, Elsevier, Amsterdam, 1985, pp. 309-459.
    • (1985) Practical Methods in Electron Microscopy , vol.10 , pp. 309-459
    • Robards, A.1    Sleytr, U.B.2
  • 21
    • 0021261426 scopus 로고
    • Paracrystalline cell wall surface layers of different Bacillus stearothermophilus strains
    • P. Messner, F. Hollaus, U.B. Sleytr, Paracrystalline cell wall surface layers of different Bacillus stearothermophilus strains, Int. J. Syst. Bacteriol. 34 (1984) 202-210.
    • (1984) Int. J. Syst. Bacteriol. , vol.34 , pp. 202-210
    • Messner, P.1    Hollaus, F.2    Sleytr, U.B.3
  • 22
    • 77957004481 scopus 로고
    • The rapid determination of amino groups with TNBS
    • C.H.W. Hirs, S.N. Timasheff (Eds.), Academic Press, San Diego
    • R. Fields, The rapid determination of amino groups with TNBS, in: C.H.W. Hirs, S.N. Timasheff (Eds.), Methods in Enzymology Enzyme Structure (part B), vol. 25, Academic Press, San Diego, 1972, pp. 464-468.
    • (1972) Methods in Enzymology Enzyme Structure (Part B) , vol.25 , pp. 464-468
    • Fields, R.1
  • 23
    • 0000751621 scopus 로고
    • Molecular packing in steroid-lecithin monolayers, part II: Mixed films of cholesterol with dipalmitoylphosphatidylcholine and tetradecanoic acid
    • F. Müller-Landau, D.A. Cadenhead, Molecular packing in steroid-lecithin monolayers, part II: Mixed films of cholesterol with dipalmitoylphosphatidylcholine and tetradecanoic acid, Chem. Phys. Lipids 25 (1979) 315-328.
    • (1979) Chem. Phys. Lipids , vol.25 , pp. 315-328
    • Müller-Landau, F.1    Cadenhead, D.A.2
  • 25
    • 0031819387 scopus 로고    scopus 로고
    • Microcalorimetric study on the phase behaviour of S-layer-coated liposomes
    • S. Küpcü, K. Lohner, C. Mader, U.B. Sleytr, Microcalorimetric study on the phase behaviour of S-layer-coated liposomes, Mol. Membr. Biol. 15 (1998) 69-74.
    • (1998) Mol. Membr. Biol. , vol.15 , pp. 69-74
    • Küpcü, S.1    Lohner, K.2    Mader, C.3    Sleytr, U.B.4
  • 26
    • 0024039744 scopus 로고
    • Mechanism of fluorescence concentration quenching of carboxyfluoresceine in liposomes: Energy transfer to nonfluorescent dimers
    • R.T. Chen, J.R. Knutson, Mechanism of fluorescence concentration quenching of carboxyfluoresceine in liposomes: Energy transfer to nonfluorescent dimers, Anal. Biochem. 172 (1988) 61-77.
    • (1988) Anal. Biochem. , vol.172 , pp. 61-77
    • Chen, R.T.1    Knutson, J.R.2
  • 27
    • 0024504913 scopus 로고
    • Aqueous two-phase polymer partitioning of lipid vesicles of defined size and composition
    • C. Tilcock, P. Cullis, T. Dempsey, B.N. Youens, D. Fisher, Aqueous two-phase polymer partitioning of lipid vesicles of defined size and composition, Biochim. Biophys. Acta 979 (1989) 208-214.
    • (1989) Biochim. Biophys. Acta , vol.979 , pp. 208-214
    • Tilcock, C.1    Cullis, P.2    Dempsey, T.3    Youens, B.N.4    Fisher, D.5
  • 28
    • 0029367707 scopus 로고
    • Monomolecular reassembly of a crystalline bacterial cell surface layer (S-layer) on untreated and modified silicon surfaces
    • D. Pum, U.B. Sleytr, Monomolecular reassembly of a crystalline bacterial cell surface layer (S-layer) on untreated and modified silicon surfaces, Supramol. Sci. 2 (1995) 193-197.
    • (1995) Supramol. Sci. , vol.2 , pp. 193-197
    • Pum, D.1    Sleytr, U.B.2
  • 29
    • 0002073950 scopus 로고
    • Crystalline protein layers as isoporous molecular sieves and immobilization and affinity matrices
    • U.B. Sleytr, P. Messner, D. Pum, M. Sára (Eds.), Springer, Berlin
    • M. Sára, S. Küpcü, C. Weiner, S. Weigert, U.B. Sleytr, Crystalline protein layers as isoporous molecular sieves and immobilization and affinity matrices, in: U.B. Sleytr, P. Messner, D. Pum, M. Sára (Eds.), Immobilized Macromolecules: Application Potentials, Springer, Berlin, 1993, pp. 71-86.
    • (1993) Immobilized Macromolecules: Application Potentials , pp. 71-86
    • Sára, M.1    Küpcü, S.2    Weiner, C.3    Weigert, S.4    Sleytr, U.B.5
  • 30
    • 0015795402 scopus 로고
    • Phase transitions in phospholipid vesicles. Fluorescence polarization and permeability measurements concerning the effects of temperature and cholesterol
    • D. Papahadjopoulos, K. Jacobsen, S. Nir, T. Isac, Phase transitions in phospholipid vesicles. Fluorescence polarization and permeability measurements concerning the effects of temperature and cholesterol, Biochim. Biophys. Acta 311 (1973) 330-348.
    • (1973) Biochim. Biophys. Acta , vol.311 , pp. 330-348
    • Papahadjopoulos, D.1    Jacobsen, K.2    Nir, S.3    Isac, T.4
  • 31
    • 0029891834 scopus 로고    scopus 로고
    • Reciprocal influence between the protein and lipid components of a lipid-protein membrane model
    • A. Diederich, C. Sponer, D. Pum, U.B. Sleytr, M. Lösche, Reciprocal influence between the protein and lipid components of a lipid-protein membrane model, Colloids Surf. B: Biointerfaces 6 (1996) 335-346.
    • (1996) Colloids Surf. B: Biointerfaces , vol.6 , pp. 335-346
    • Diederich, A.1    Sponer, C.2    Pum, D.3    Sleytr, U.B.4    Lösche, M.5
  • 32
    • 0026492596 scopus 로고
    • Shear stress-facilitated calcium ion transport across lipid bilayers
    • S.R. Chakravarthy, T.D. Giorgio, Shear stress-facilitated calcium ion transport across lipid bilayers, Biochim. Biophys. Acta 1112 (1992) 197-204.
    • (1992) Biochim. Biophys. Acta , vol.1112 , pp. 197-204
    • Chakravarthy, S.R.1    Giorgio, T.D.2
  • 33
    • 0029793574 scopus 로고    scopus 로고
    • Two-dimensional protein crystals (S-layers) as novel matrix for immobilization of IgG and applicability of S-layers as microparticles in immunoassays
    • S. Küpcü, U.B. Sleytr, M. Sara, Two-dimensional protein crystals (S-layers) as novel matrix for immobilization of IgG and applicability of S-layers as microparticles in immunoassays, J. Immunol. Methods 196 (1996) 73-84.
    • (1996) J. Immunol. Methods , vol.196 , pp. 73-84
    • Küpcü, S.1    Sleytr, U.B.2    Sara, M.3
  • 34
    • 0028972983 scopus 로고
    • Surface modification of an ultrafiltration membrane with crystalline structure and studying interactions with selected protein molecules
    • S. Weigert, M. Sara, Surface modification of an ultrafiltration membrane with crystalline structure and studying interactions with selected protein molecules, J. Membr. Sci. 106 (1995) 147-159.
    • (1995) J. Membr. Sci. , vol.106 , pp. 147-159
    • Weigert, S.1    Sara, M.2
  • 35
    • 0343145679 scopus 로고    scopus 로고
    • Bacterial and archaeal S-layer proteins: Structure-function relationships and their biotechnological applications
    • U.B. Sleytr, M. Sara, Bacterial and archaeal S-layer proteins: structure-function relationships and their biotechnological applications, Trends Biotechnol. 15 (1997) 20-26.
    • (1997) Trends Biotechnol. , vol.15 , pp. 20-26
    • Sleytr, U.B.1    Sara, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.