메뉴 건너뛰기




Volumn 70, Issue 2 I, 1996, Pages 723-732

Optical single-channel analysis of the aerolysin pore in erythrocyte membranes

Author keywords

[No Author keywords available]

Indexed keywords

AEROLYSIN; BACTERIAL TOXIN; UNCLASSIFIED DRUG;

EID: 0030032367     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79612-1     Document Type: Article
Times cited : (26)

References (31)
  • 1
    • 0027058138 scopus 로고
    • Range of messenger action of calcium ion and inositol 1,4,5-triphosphate
    • Allbriton, N. L., T. Meyer, and L Stryer. 1992 Range of messenger action of calcium ion and inositol 1,4,5-triphosphate. Science. 258:1812-1815.
    • (1992) Science , vol.258 , pp. 1812-1815
    • Allbriton, N.L.1    Meyer, T.2    Stryer, L.3
  • 2
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod, D., D. E. Koppel, J. Schlessinger, E. Elson, and W. W. Webb. 1976. Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J. 16:1055-1069.
    • (1976) Biophys. J. , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Schlessinger, J.3    Elson, E.4    Webb, W.W.5
  • 3
    • 0027466791 scopus 로고
    • Fluorescence photobleaching recovery in the confocal scanning microscope
    • Blonk, J. C. G., A. Don, H. van Alst. and J. J. Birmingham. 1993. Fluorescence photobleaching recovery in the confocal scanning microscope. J. Microsc. 169:363-374.
    • (1993) J. Microsc. , vol.169 , pp. 363-374
    • Blonk, J.C.G.1    Don, A.2    Van Alst, H.3    Birmingham, J.J.4
  • 4
    • 0025004421 scopus 로고
    • Purification of cloned proaerolysin released by a low protease mutant of Aeromonas salmonicida
    • Buckley, J. T. 1990. Purification of cloned proaerolysin released by a low protease mutant of Aeromonas salmonicida, Biochem. Cell Biol. 68: 221-224.
    • (1990) Biochem. Cell Biol. , vol.68 , pp. 221-224
    • Buckley, J.T.1
  • 5
    • 0020532081 scopus 로고
    • Cytolysis by H-2-specific T killer cells
    • Dennert, G., and E. R. Podack. 1983. Cytolysis by H-2-specific T killer cells. J. Exp. Med. 157:1483-1495.
    • (1983) J. Exp. Med. , vol.157 , pp. 1483-1495
    • Dennert, G.1    Podack, E.R.2
  • 6
    • 0020071103 scopus 로고
    • Membrane glycoprotein receptor and hole-forming properties of a cytolytic protein toxin
    • Howard, S. P., and J. T. Buckley. 1982. Membrane glycoprotein receptor and hole-forming properties of a cytolytic protein toxin. Biochemistry. 21:1662-1667.
    • (1982) Biochemistry , vol.21 , pp. 1662-1667
    • Howard, S.P.1    Buckley, J.T.2
  • 7
    • 0017253004 scopus 로고
    • Measurement of the translational mobility of concanavalin a in glycerol-saline solutions and on the cell surface by fluorescence recovery after photobleaching
    • Jacobson, K., E. Wu, and G. Poste. 1976. Measurement of the translational mobility of concanavalin A in glycerol-saline solutions and on the cell surface by fluorescence recovery after photobleaching. Biochim. Biophys. Acta. 433:215-222.
    • (1976) Biochim. Biophys. Acta , vol.433 , pp. 215-222
    • Jacobson, K.1    Wu, E.2    Poste, G.3
  • 8
    • 0017867017 scopus 로고
    • Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: Utilization by the Na:K pump of human red blood cell ghosts
    • Kaplan, J. H., B. Forbush, and J. F. Hoffman. 1978. Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: utilization by the Na:K pump of human red blood cell ghosts. Biochemistry. 17:1929-1935.
    • (1978) Biochemistry , vol.17 , pp. 1929-1935
    • Kaplan, J.H.1    Forbush, B.2    Hoffman, J.F.3
  • 9
    • 0029002426 scopus 로고
    • Calcium pump kinetics determined in single erythrocyte ghosts by microphotolysis and confocal imaging
    • Kubitscheck, U., L. Pratsch, H. Passow, and R. Peters. 1995. Calcium pump kinetics determined in single erythrocyte ghosts by microphotolysis and confocal imaging. Biophys. J. 69:30-41.
    • (1995) Biophys. J. , vol.69 , pp. 30-41
    • Kubitscheck, U.1    Pratsch, L.2    Passow, H.3    Peters, R.4
  • 10
    • 9044224161 scopus 로고
    • Pore-forming toxins and antimicrobial polypeptides
    • Menestrina, G. 1994. Pore-forming toxins and antimicrobial polypeptides. Toxicol. Appl. Pharmacol. 87:1-268.
    • (1994) Toxicol. Appl. Pharmacol. , vol.87 , pp. 1-268
    • Menestrina, G.1
  • 11
    • 0028024397 scopus 로고
    • Nuclear calcium transport and the role of calcium in apoptosis
    • Nicotera, P., B. Zhivotovsky, and S. Orrenius. 1994. Nuclear calcium transport and the role of calcium in apoptosis. Cell Calcium. 16: 279-288.
    • (1994) Cell Calcium , vol.16 , pp. 279-288
    • Nicotera, P.1    Zhivotovsky, B.2    Orrenius, S.3
  • 13
    • 0016751324 scopus 로고
    • Drag coefficients for the movement of rigid spheres through liquid-filled cylindrical pores
    • Paine, P. L., and P. Scherr. 1975. Drag coefficients for the movement of rigid spheres through liquid-filled cylindrical pores. Biophys. J. 15: 1087-1091.
    • (1975) Biophys. J. , vol.15 , pp. 1087-1091
    • Paine, P.L.1    Scherr, P.2
  • 14
    • 84957794434 scopus 로고
    • Filtration, diffusion and molecular sieving through peripheral capillary membranes
    • Pappenheimer, J. R., E. M. Renkin, and L. M. Borrero. 1951. Filtration, diffusion and molecular sieving through peripheral capillary membranes. Am. J. Physiol. 167:13-23.
    • (1951) Am. J. Physiol. , vol.167 , pp. 13-23
    • Pappenheimer, J.R.1    Renkin, E.M.2    Borrero, L.M.3
  • 16
    • 0021100162 scopus 로고
    • Nuclear envelope permeability measured by fluorescence microphotoiysis of single liver cell nuclei
    • Peters, R. 1983. Nuclear envelope permeability measured by fluorescence microphotoiysis of single liver cell nuclei. J. Cell Biol. 258: 11427-11429.
    • (1983) J. Cell Biol. , vol.258 , pp. 11427-11429
    • Peters, R.1
  • 17
    • 0021471078 scopus 로고
    • Nucleo-cytoplasmic flux and intracellular mobility in single hepatocytes measured by fluorescence microphotolysis
    • Peters, R. 1984. Nucleo-cytoplasmic flux and intracellular mobility in single hepatocytes measured by fluorescence microphotolysis. EMBO J. 3:1831-1836.
    • (1984) EMBO J. , vol.3 , pp. 1831-1836
    • Peters, R.1
  • 18
    • 0016272796 scopus 로고
    • A microfluorimetric study of translational diffusion in erythrocyte membranes
    • Peters, R . J. Peters, K. H. Tews, and W. Bähr. 1974. A microfluorimetric study of translational diffusion in erythrocyte membranes. Biochim Biophys. Acta. 367:282-294.
    • (1974) Biochim Biophys. Acta , vol.367 , pp. 282-294
    • Peters, R.1    Peters, J.2    Tews, K.H.3    Bähr, W.4
  • 19
    • 0025289854 scopus 로고
    • Transients of perform pore formation observed by fluorescence microscopic single channel recording
    • Peters, R., H. Sauer, J- Tschopp, and G. Fritzsch. 1990. Transients of perform pore formation observed by fluorescence microscopic single channel recording. EMBO J. 9:2447-2451.
    • (1990) EMBO J. , vol.9 , pp. 2447-2451
    • Peters, R.1    Sauer, H.2    Tschopp, J.3    Fritzsch, G.4
  • 20
    • 0000063170 scopus 로고
    • Fluorescence photobleaching techniques
    • R. J. Cherry, editor. Macmillan Press, Houndsmill
    • Peters, R., and M. Scholz. 1991. Fluorescence photobleaching techniques. In New Techniques of Optical Microscopy and Microspectroscopy. R. J. Cherry, editor. Macmillan Press, Houndsmill. 199-228.
    • (1991) New Techniques of Optical Microscopy and Microspectroscopy , pp. 199-228
    • Peters, R.1    Scholz, M.2
  • 22
    • 0000560829 scopus 로고
    • Filtration, diffusion, and molecular sieving through porous cellulose membrane
    • Renkin, E. M. 1954. Filtration, diffusion, and molecular sieving through porous cellulose membrane. J. Gen. Physiol. 38:225-243.
    • (1954) J. Gen. Physiol. , vol.38 , pp. 225-243
    • Renkin, E.M.1
  • 24
    • 0025822681 scopus 로고
    • Complement pore genesis observed in erythrocyte membranes by fluorescence microscopic single-channel recording
    • Sauer, H., L. Pratsch, G. Fritzsch, S. Bhakdi, and R. Peters. 1991. Complement pore genesis observed in erythrocyte membranes by fluorescence microscopic single-channel recording. Biochem. J. 276:395-399.
    • (1991) Biochem. J. , vol.276 , pp. 395-399
    • Sauer, H.1    Pratsch, L.2    Fritzsch, G.3    Bhakdi, S.4    Peters, R.5
  • 25
    • 0015764378 scopus 로고
    • Preparation and properties of human erythrocyte ghosts
    • Schwoch, G., and H. Passow. 1973. Preparation and properties of human erythrocyte ghosts. Mol. Cell. Biochem. 2:197-218.
    • (1973) Mol. Cell. Biochem. , vol.2 , pp. 197-218
    • Schwoch, G.1    Passow, H.2
  • 27
    • 0028231277 scopus 로고
    • The cytolytic toxin aerolysin. From the soluble form to the transmembrane channel
    • van der Goot, F. G., F. Pattus, M. Parker, and J. T. Buckley. 1994. The cytolytic toxin aerolysin. from the soluble form to the transmembrane channel. Toxicology. 87:19-28.
    • (1994) Toxicology , vol.87 , pp. 19-28
    • Van Der Goot, F.G.1    Pattus, F.2    Parker, M.3    Buckley, J.T.4
  • 28
    • 0028149090 scopus 로고
    • Scanning microphotolysis: A new photobleaching technique based on fast intensity modulation of a scanned laser beam and confocal imaging
    • Wedekind, P., U. Kubitscheck, and R. Peters. 1994. Scanning microphotolysis: a new photobleaching technique based on fast intensity modulation of a scanned laser beam and confocal imaging. J. Microsc 176:23-33
    • (1994) J. Microsc , vol.176 , pp. 23-33
    • Wedekind, P.1    Kubitscheck, U.2    Peters, R.3
  • 29
    • 0025932268 scopus 로고
    • Site-directed mutagenesis at histidines of aerolysin from Aeromonas hydrophila: A lipid planar bilayer study
    • Wilmsen, H. U., J. T. Buckley, and F. Pattus. 1991. Site-directed mutagenesis at histidines of aerolysin from Aeromonas hydrophila: a lipid planar bilayer study. Mol. Microbiol. 5:2745-2751.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2745-2751
    • Wilmsen, H.U.1    Buckley, J.T.2    Pattus, F.3
  • 30
    • 0026721371 scopus 로고
    • The aerolysin membrane channel is formed by heptamerization of the monomer
    • Wilmsen, H. U., K. R. Leonard, W. Tichelaar, J. T. Buckley, and F. Pattus. 1992. The aerolysin membrane channel is formed by heptamerization of the monomer. EMBO J. 11:2457-2463.
    • (1992) EMBO J. , vol.11 , pp. 2457-2463
    • Wilmsen, H.U.1    Leonard, K.R.2    Tichelaar, W.3    Buckley, J.T.4    Pattus, F.5
  • 31
    • 0025357554 scopus 로고
    • Aerolysin. A hemolysin from Aeromonas hydrophilia, forms voltage-gated channels in planar lipid bilayers
    • Wilmsen, H. U., F. Pattus, and J. T. Buckley. 1990. Aerolysin. a hemolysin from Aeromonas hydrophilia, forms voltage-gated channels in planar lipid bilayers. J. Membr. Biol. 115:71-81.
    • (1990) J. Membr. Biol. , vol.115 , pp. 71-81
    • Wilmsen, H.U.1    Pattus, F.2    Buckley, J.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.