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Volumn 89, Issue 5, 1997, Pages 685-692

Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; CYTOLYSIN; LIPID BINDING PROTEIN;

EID: 0030666371     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80251-2     Document Type: Article
Times cited : (414)

References (58)
  • 1
    • 0002027172 scopus 로고
    • The family of the antigenically-related cholesterol-binding ('sulphydryl-activated') cytolytic toxins
    • J.E. Alouf and J.H. Freer, eds. (London: Academic Press)
    • Alouf, J.E., and Geoffroy, C. (1991). The family of the antigenically-related cholesterol-binding ('sulphydryl-activated') cytolytic toxins. In Sourcebook of Bacterial Toxins, J.E. Alouf and J.H. Freer, eds. (London: Academic Press), pp. 147-186.
    • (1991) Sourcebook of Bacterial Toxins , pp. 147-186
    • Alouf, J.E.1    Geoffroy, C.2
  • 2
    • 0027514827 scopus 로고
    • Structure-function analysis of the ion channel selectivity filter in human annexin V
    • Berendes, R., Voges, D., Demange, P., Huber, R., and Burger, A. (1993). Structure-function analysis of the ion channel selectivity filter in human annexin V. Science 262, 427-430.
    • (1993) Science , vol.262 , pp. 427-430
    • Berendes, R.1    Voges, D.2    Demange, P.3    Huber, R.4    Burger, A.5
  • 3
    • 0023901550 scopus 로고
    • Damage to cell membranes by pore-forming bacterial cytolysins
    • Bhakdi, S., and Tranum-Jensen, J. (1988). Damage to cell membranes by pore-forming bacterial cytolysins. Prog. Allergy 40, 1-43.
    • (1988) Prog. Allergy , vol.40 , pp. 1-43
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 4
    • 0027183815 scopus 로고
    • A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes
    • Bhakdi, S., Weller, U., Walev, I., Martin, E., Jonas, D., and Palmer, M. (1993). A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes. Med. Microbiol. Immunol. 182, 167-175.
    • (1993) Med. Microbiol. Immunol. , vol.182 , pp. 167-175
    • Bhakdi, S.1    Weller, U.2    Walev, I.3    Martin, E.4    Jonas, D.5    Palmer, M.6
  • 5
    • 0005819964 scopus 로고
    • Structure and function of pneumolysin, the thiolactivated toxin from Streptococcus pneumoniae
    • R. Rappuoli, J.E. Alouf, F. Falmagne, J. Fehrenbach, J. Freer, R. Gross, J. Jeljaszewicz, C. Montecucco, T. Tomasi, T. Wadström, and B. Witholt, eds. (Stuttgart: Gustav Verlag)
    • Boulnois, G.J., Mitchell, T.J., Saunders, F.K., Mendez, F.J., and Andrew, P.W. (1990). Structure and function of pneumolysin, the thiolactivated toxin from Streptococcus pneumoniae. In Bacterial Protein Toxins, R. Rappuoli, J.E. Alouf, F. Falmagne, J. Fehrenbach, J. Freer, R. Gross, J. Jeljaszewicz, C. Montecucco, T. Tomasi, T. Wadström, and B. Witholt, eds. (Stuttgart: Gustav Verlag), pp. 43-51.
    • (1990) Bacterial Protein Toxins , pp. 43-51
    • Boulnois, G.J.1    Mitchell, T.J.2    Saunders, F.K.3    Mendez, F.J.4    Andrew, P.W.5
  • 7
    • 0037877123 scopus 로고
    • New Haven, Connecticut: Department of Molecular Biophysics and Biochemistry, Yale University
    • Brünger, AT. (1993). X-PLOR: A system for X-ray Crystallography and NMR (New Haven, Connecticut: Department of Molecular Biophysics and Biochemistry, Yale University).
    • (1993) X-PLOR: A System for X-ray Crystallography and NMR
    • Brünger, A.T.1
  • 8
    • 0026240806 scopus 로고
    • Ribbons 2.0
    • Carson, M. (1991). Ribbons 2.0. J. Appl. Cryst. 24, 958-961.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 958-961
    • Carson, M.1
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (Collaborative Computational Project) Program Suite. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D50, 750-763.
    • (1994) Acta Cryst. , vol.D50 , pp. 750-763
  • 11
    • 0017837578 scopus 로고
    • Alteration by cereolysin of the structure of cholesterol-containing membranes
    • Cowell, J.L., Kim, K-S., and Bernheimer, A.W. (1978). Alteration by cereolysin of the structure of cholesterol-containing membranes. Biochim. Biophys. Acta 507, 230-241.
    • (1978) Biochim. Biophys. Acta , vol.507 , pp. 230-241
    • Cowell, J.L.1    Kim, K.-S.2    Bernheimer, A.W.3
  • 12
    • 0029902726 scopus 로고    scopus 로고
    • Neutralizing monoclonal antibodies against listeriolysin: Mapping of epitopes involved in pore formation
    • Darji, A., Niebuhr, K., Hense, M., Wehland, J., Chakraborty, T., and Weiss, S. (1996). Neutralizing monoclonal antibodies against listeriolysin: mapping of epitopes involved in pore formation. Infect. Immun. 64, 2356-2358.
    • (1996) Infect. Immun. , vol.64 , pp. 2356-2358
    • Darji, A.1    Niebuhr, K.2    Hense, M.3    Wehland, J.4    Chakraborty, T.5    Weiss, S.6
  • 13
    • 0028670509 scopus 로고
    • Orientation of the α-helices of apocytochrome c and derived fragments at membrane interfaces, as studied by circular dichroism
    • De Jongh, H.H., Brasseur, R., and Killian, J.A. (1994). Orientation of the α-helices of apocytochrome c and derived fragments at membrane interfaces, as studied by circular dichroism. Biochemistry 33, 14529-14535.
    • (1994) Biochemistry , vol.33 , pp. 14529-14535
    • De Jongh, H.H.1    Brasseur, R.2    Killian, J.A.3
  • 14
    • 0029996132 scopus 로고    scopus 로고
    • The structural homology between uteroglobin and the pore-forming domain of colicin a suggests a possible mechanism of action of uteroglobin
    • De La Cruz, X., and Lee, B. (1996). The structural homology between uteroglobin and the pore-forming domain of colicin A suggests a possible mechanism of action of uteroglobin. Prot. Sci. 5, 857-861.
    • (1996) Prot. Sci. , vol.5 , pp. 857-861
    • De La Cruz, X.1    Lee, B.2
  • 16
    • 0016715847 scopus 로고
    • Effect of streptolysin O on erythrocyte membranes, liposomes, and lipid dispersions. A protein-cholesterol interaction
    • Duncan, J.L., and Schlegel, R. (1975). Effect of streptolysin O on erythrocyte membranes, liposomes, and lipid dispersions. A protein-cholesterol interaction. J. Cell Biol. 67, 160-173.
    • (1975) J. Cell Biol. , vol.67 , pp. 160-173
    • Duncan, J.L.1    Schlegel, R.2
  • 17
    • 0030592696 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of a thiol-activated cytolysin
    • Feil, S.C., Rossjohn, J., Rohde, K., Tweten, R.K., and Parker, M.W. (1996). Crystallization and preliminary X-ray analysis of a thiol-activated cytolysin. FEBS Lett. 397, 290-292.
    • (1996) FEBS Lett. , vol.397 , pp. 290-292
    • Feil, S.C.1    Rossjohn, J.2    Rohde, K.3    Tweten, R.K.4    Parker, M.W.5
  • 19
    • 0027476367 scopus 로고
    • The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30 → Met variant to 1.7-Å resolution
    • Hamilton, J.A., Steinrauf, L.K., Braden, B.C., Liepnieks, J., Benson, M.D., Holmgren, G., Sandgren, O., and Steen, L. (1993). The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30 → Met variant to 1.7-Å resolution. J. Biol. Chem. 268, 2416-2424.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2416-2424
    • Hamilton, J.A.1    Steinrauf, L.K.2    Braden, B.C.3    Liepnieks, J.4    Benson, M.D.5    Holmgren, G.6    Sandgren, O.7    Steen, L.8
  • 20
    • 0025739648 scopus 로고
    • Kinetic aspects of the aggregation of Clostridium perfringens θ-toxin on erythrocyte membranes
    • Harris, R.W., Sims, P.J., and Tweten, R.K. (1991). Kinetic aspects of the aggregation of Clostridium perfringens θ-toxin on erythrocyte membranes. J. Biol. Chem. 266, 6936-6941.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6936-6941
    • Harris, R.W.1    Sims, P.J.2    Tweten, R.K.3
  • 21
    • 0027976487 scopus 로고
    • Amino acids in pneumolysin important for hemolytic activity identified by random mutagenesis
    • Hill, J., Andrew, P.W., and Mitchell, T.J. (1994). Amino acids in pneumolysin important for hemolytic activity identified by random mutagenesis. Infect. Immun. 62, 757-758.
    • (1994) Infect. Immun. , vol.62 , pp. 757-758
    • Hill, J.1    Andrew, P.W.2    Mitchell, T.J.3
  • 22
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L., and Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 23
  • 24
    • 0025244264 scopus 로고
    • Effect of isolated C-terminal fragment of 6-toxin (perfringolysin O) on toxin assembly and membrane lysis
    • Iwamoto, M., Ohno-Iwashita, Y., and Ando, S. (1990). Effect of isolated C-terminal fragment of 6-toxin (perfringolysin O) on toxin assembly and membrane lysis. Eur. J. Biochem. 794, 25-31.
    • (1990) Eur. J. Biochem. , vol.794 , pp. 25-31
    • Iwamoto, M.1    Ohno-Iwashita, Y.2    Ando, S.3
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for building models in electron density maps and the location of errors in these models. Acta Cryst. A47, 110-119.
    • (1991) Acta Cryst. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0026572775 scopus 로고
    • Molecular surface recognition: Determination of geometric fit between proteins and their ligands by correlation techniques
    • Katchalski-Katzir, E., Shariv, I., Eisenstein, M., Friesem, A.A., Aflalo, C., and Vasker, I.A. (1992). Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques. Proc. Natl. Acad. Sci. USA 89, 2195-2199.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2195-2199
    • Katchalski-Katzir, E.1    Shariv, I.2    Eisenstein, M.3    Friesem, A.A.4    Aflalo, C.5    Vasker, I.A.6
  • 27
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., McArthur, M.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 282-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 282-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 28
    • 0026050639 scopus 로고
    • Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution
    • Li, J., Carroll, J., and Ellar, D.J. (1991). Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution. Nature 353, 815-821.
    • (1991) Nature , vol.353 , pp. 815-821
    • Li, J.1    Carroll, J.2    Ellar, D.J.3
  • 29
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Lüthy, R., Bowie, J.U., and Eisenberg, D. (1992). Assessment of protein models with three-dimensional profiles. Nature 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 30
    • 0025685253 scopus 로고
    • Attentuated mutants of the intracellular bacterium Listeria monocytogenes obtained by single amino acid substitutions in listeriolysin O
    • Michel, E., Reich, K.A., Favier, R., Berche, P., and Cossart, P. (1990). Attentuated mutants of the intracellular bacterium Listeria monocytogenes obtained by single amino acid substitutions in listeriolysin O. Mol. Microbiol. 4, 2167-2178.
    • (1990) Mol. Microbiol. , vol.4 , pp. 2167-2178
    • Michel, E.1    Reich, K.A.2    Favier, R.3    Berche, P.4    Cossart, P.5
  • 31
    • 0018763938 scopus 로고
    • Alteration of human erythrocyte plasma membranes by perfringolysin O as revealed by freeze-fracture electron microscopy
    • Mitsui, K., Sekiya, T., Nozawa, Y., and Hase, J. (1979a). Alteration of human erythrocyte plasma membranes by perfringolysin O as revealed by freeze-fracture electron microscopy. Biochem. Biophys. Acta 554, 68-75.
    • (1979) Biochem. Biophys. Acta , vol.554 , pp. 68-75
    • Mitsui, K.1    Sekiya, T.2    Nozawa, Y.3    Hase, J.4
  • 32
    • 0018789078 scopus 로고
    • Ring formation of perfringolysin O as revealed by negative stain electron microscopy
    • Mitsui, K., Sekiya, T., Okamura, S., Nozawa, Y., and Hase, J. (1979b). Ring formation of perfringolysin O as revealed by negative stain electron microscopy. Biochem. Biophys. Acta 558, 307-313.
    • (1979) Biochem. Biophys. Acta , vol.558 , pp. 307-313
    • Mitsui, K.1    Sekiya, T.2    Okamura, S.3    Nozawa, Y.4    Hase, J.5
  • 33
    • 0028062876 scopus 로고
    • Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form
    • Morgan, P.J., Hyman, S.C., Byron, O., Andrew, P.W., Mitchell, T.J., and Rowe, A.J. (1994). Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form. J. Biol. Chem. 269, 25315-25320.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25315-25320
    • Morgan, P.J.1    Hyman, S.C.2    Byron, O.3    Andrew, P.W.4    Mitchell, T.J.5    Rowe, A.J.6
  • 36
    • 0028988973 scopus 로고
    • Interaction of θ-toxin (perfringolysin O), acholesterol-binding cytolysin, with liposomal membranes: Change in the aromatic side chains upon binding and insertion
    • Nakamura, M., Sekino, N., Iwamoto, M., and Ohno-Iwashita, Y. (1995). Interaction of θ-toxin (perfringolysin O), acholesterol-binding cytolysin, with liposomal membranes: change in the aromatic side chains upon binding and insertion. Biochemistry 34, 6513-6520.
    • (1995) Biochemistry , vol.34 , pp. 6513-6520
    • Nakamura, M.1    Sekino, N.2    Iwamoto, M.3    Ohno-Iwashita, Y.4
  • 37
    • 0026434570 scopus 로고
    • Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein
    • Nambudripad, R., Stark, W., Opella, S.J., and Makowski, L. (1991). Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein. Science 252, 1305-1308.
    • (1991) Science , vol.252 , pp. 1305-1308
    • Nambudripad, R.1    Stark, W.2    Opella, S.J.3    Makowski, L.4
  • 38
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Prot. Struct. Funct. Genet. 11, 281-293.
    • (1991) Prot. Struct. Funct. Genet. , vol.11 , pp. 281-293
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 39
    • 0021831999 scopus 로고
    • Interaction of streptolysin-O with biomembranes: Kinetic and morphological studies on erythrocyte membranes
    • Niedermeyer, W. (1985). Interaction of streptolysin-O with biomembranes: kinetic and morphological studies on erythrocyte membranes, Toxicon 23, 425-439.
    • (1985) Toxicon , vol.23 , pp. 425-439
    • Niedermeyer, W.1
  • 40
    • 0026785987 scopus 로고
    • Effect of lipidic factors on membrane cholesterol topology - Mode of binding of θ-toxin to cholesterol in liposomes
    • Ohno-Iwashita, Y., Iwamoto, M., Ando, S., and Iwashita, S. (1992). Effect of lipidic factors on membrane cholesterol topology - mode of binding of θ-toxin to cholesterol in liposomes. Biochim. Biophys. Acta 1109, 81-90.
    • (1992) Biochim. Biophys. Acta , vol.1109 , pp. 81-90
    • Ohno-Iwashita, Y.1    Iwamoto, M.2    Ando, S.3    Iwashita, S.4
  • 41
    • 0027526035 scopus 로고
    • The projection structure of perfringolysin O
    • Olofsson, A., Hebert, H., and Thelestam, M. (1993). The projection structure of perfringolysin O. FEBS Lett. 319, 125-127.
    • (1993) FEBS Lett. , vol.319 , pp. 125-127
    • Olofsson, A.1    Hebert, H.2    Thelestam, M.3
  • 42
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, and S. Bailey, eds. (Warrington, U.K.: SERC Daresbury Laboratory)
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Data Collection and Processing, L. Sawyer, N. Isaacs, and S. Bailey, eds. (Warrington, U.K.: SERC Daresbury Laboratory), pp. 56-62.
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 43
    • 0028001461 scopus 로고
    • A role in cell-binding for the C-terminus of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae
    • Owen, R.H.G., Boulnois, G.J., Andrew, P.W., and Mitchell, T.J. (1994). A role in cell-binding for the C-terminus of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae. FEMS Microbiol. Lett. 121, 217-221.
    • (1994) FEMS Microbiol. Lett. , vol.121 , pp. 217-221
    • Owen, R.H.G.1    Boulnois, G.J.2    Andrew, P.W.3    Mitchell, T.J.4
  • 45
    • 0027976196 scopus 로고
    • Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
    • Parker, M.W., Buckley, J.T., Postma, J.P.M., Tucker, A.D., Leonard, K., Pattus, F., and Tsernoglou, D. (1994). Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature 367, 292-295.
    • (1994) Nature , vol.367 , pp. 292-295
    • Parker, M.W.1    Buckley, J.T.2    Postma, J.P.M.3    Tucker, A.D.4    Leonard, K.5    Pattus, F.6    Tsernoglou, D.7
  • 46
    • 0024961641 scopus 로고
    • Structure of the membrane-pore-forming fragment of colicin A
    • Parker, M.W., Pattus, F., Tucker, A.D., and Tsernoglou, D. (1989). Structure of the membrane-pore-forming fragment of colicin A. Nature 337, 93-96.
    • (1989) Nature , vol.337 , pp. 93-96
    • Parker, M.W.1    Pattus, F.2    Tucker, A.D.3    Tsernoglou, D.4
  • 49
    • 0024720325 scopus 로고
    • The thiol-activated toxin streptolysin O does not require a thiol group for cytolytic activity
    • Pinkney, M., Beachey, E., and Kehoe, M. (1989). The thiol-activated toxin streptolysin O does not require a thiol group for cytolytic activity. Infect. Immun. 57, 2553-2558.
    • (1989) Infect. Immun. , vol.57 , pp. 2553-2558
    • Pinkney, M.1    Beachey, E.2    Kehoe, M.3
  • 50
    • 0020422130 scopus 로고
    • Structural characteristics of tetanolysin and its binding to lipid vesicles
    • Rottem, S., Cole, R.M., Habig, W.H., Barile, M.F., and Hardegree, M.C. (1982). Structural characteristics of tetanolysin and its binding to lipid vesicles. J. Bacteriol. 752, 888-892.
    • (1982) J. Bacteriol. , vol.752 , pp. 888-892
    • Rottem, S.1    Cole, R.M.2    Habig, W.H.3    Barile, M.F.4    Hardegree, M.C.5
  • 51
    • 0024407229 scopus 로고
    • Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require athiol group for in vitro activity
    • Saunders, F.K., Mitchell, T.J., Walker, J.A., Andrew, P.W., and Boulnois, G.J. (1989). Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require athiol group for in vitro activity. Infect. Immun. 57, 2547-2552.
    • (1989) Infect. Immun. , vol.57 , pp. 2547-2552
    • Saunders, F.K.1    Mitchell, T.J.2    Walker, J.A.3    Andrew, P.W.4    Boulnois, G.J.5
  • 52
    • 0027169048 scopus 로고
    • A ring-shaped structure with a crown formed by streptolysin O on the erthrocyte membrane
    • Sekiya, K., Satoh, R., Danbara, H., and Futaesaku, Y. (1993). A ring-shaped structure with a crown formed by streptolysin O on the erthrocyte membrane. J. Bacteriol. 175, 5953-5961.
    • (1993) J. Bacteriol. , vol.175 , pp. 5953-5961
    • Sekiya, K.1    Satoh, R.2    Danbara, H.3    Futaesaku, Y.4
  • 53
    • 0030447720 scopus 로고    scopus 로고
    • Structure of Staphyloccal α-hemolysin, a heptameric transmembrane pore
    • Song, L., Hobaugh, M.R., Shustak, C., Cheley, S., Bayley, H., and Gouaux, J.E. (1996). Structure of Staphyloccal α-hemolysin, a heptameric transmembrane pore. Science 274, 1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 55
    • 0023757453 scopus 로고
    • Nucleotide sequence of the gene for perfringolysin O (theta-toxin) from Clostridium perfringens: Significant homology with the genes for streptolysin O and pneumolysin
    • Tweten, R.K. (1988). Nucleotide sequence of the gene for perfringolysin O (theta-toxin) from Clostridium perfringens: significant homology with the genes for streptolysin O and pneumolysin. Infect. Immun. 56, 3235-3240.
    • (1988) Infect. Immun. , vol.56 , pp. 3235-3240
    • Tweten, R.K.1
  • 56
    • 0002832111 scopus 로고
    • Pore-forming toxins in gram-positive bacteria
    • J.A. Roth, C.A. Bolin, K.A. Brogden, C.Minion, and M.J. Wannemuehler, eds. (Washington, D.C.: American Soc. Microbiol.)
    • Tweten, R.K. (1995). Pore-forming toxins in gram-positive bacteria. In Virulence Mechanisms of Bacterial Pathogens, J.A. Roth, C.A. Bolin, K.A. Brogden, C.Minion, and M.J. Wannemuehler, eds. (Washington, D.C.: American Soc. Microbiol.), pp. 207-229.
    • (1995) Virulence Mechanisms of Bacterial Pathogens , pp. 207-229
    • Tweten, R.K.1
  • 57
    • 0025821214 scopus 로고
    • Isolation of a tryptic fragment from Clostridium perfringens theta-toxin that contains sites for membrane binding and self-aggregation
    • Tweten, R.K., Harris, R.W., and Sims, P.J. (1991). Isolation of a tryptic fragment from Clostridium perfringens theta-toxin that contains sites for membrane binding and self-aggregation. J. Biol. Chem. 266, 12449-12454.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12449-12454
    • Tweten, R.K.1    Harris, R.W.2    Sims, P.J.3
  • 58
    • 0028915098 scopus 로고
    • Binding, oligomerization, and pore formation by streptolysin O in erythrocytes and fibroblast membranes: Detection of nonlytic polymers
    • Walev, I., Palmer, M., Valeva, A., Weller, U., and Bhakdi, S. (1995). Binding, oligomerization, and pore formation by streptolysin O in erythrocytes and fibroblast membranes: detection of nonlytic polymers. Infect. Immun. 63, 1188-1194.
    • (1995) Infect. Immun. , vol.63 , pp. 1188-1194
    • Walev, I.1    Palmer, M.2    Valeva, A.3    Weller, U.4    Bhakdi, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.