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Volumn 427, Issue 6, 2015, Pages 1224-1238

Cyclophilin-facilitated membrane translocation as pharmacological target to prevent intoxication of mammalian cells by binary clostridial actin ADP-ribosylated toxins

Author keywords

bacterial protein toxin; cellular uptake; cyclophilin 40; membrane transport; PPIase

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; BACTERIAL TOXIN; CLOSTRIDIUM BOTULINUM C2 TOXIN; CLOSTRIDIUM DIFFICILE TOXIN; CLOSTRIDIUM PERFRINGENS IOTA TOXIN; CYCLOPHILIN; CYCLOPHILIN 40; CYCLOPHILIN A; CYCLOSPORIN A; PEPTIDYLPROLYL ISOMERASE; UNCLASSIFIED DRUG; ACTIN-SPECIFIC ADP-RIBOSYLTRANSFERASE, CLOSTRIDIUM; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; BOTULINUM TOXIN; BOTULINUM TOXIN TYPE C; CYCLOSPORIN; IOTA TOXIN, CLOSTRIDIUM PERFRINGENS; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PPID PROTEIN, HUMAN;

EID: 84924239313     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.07.013     Document Type: Article
Times cited : (37)

References (86)
  • 1
    • 4544264417 scopus 로고    scopus 로고
    • Binary bacterial toxins: Biochemistry, biology, and applications of common Clostridium and Bacillus proteins
    • H. Barth, K. Aktories, M.R. Popoff, and B.G. Stiles Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins Microbiol Mol Biol Rev 8 2004 373 402
    • (2004) Microbiol Mol Biol Rev , vol.8 , pp. 373-402
    • Barth, H.1    Aktories, K.2    Popoff, M.R.3    Stiles, B.G.4
  • 3
    • 0022453775 scopus 로고
    • ADP-ribosylation of nonmuscle actin with component i of C2 toxin
    • I. Ohishi, and S. Tsuyama ADP-ribosylation of nonmuscle actin with component I of C2 toxin Biochem Biophys Res Commun 136 1986 802 806
    • (1986) Biochem Biophys Res Commun , vol.136 , pp. 802-806
    • Ohishi, I.1    Tsuyama, S.2
  • 4
    • 0023612455 scopus 로고
    • Clostridium perfringens iota toxin ADP-ribosylates skeletal muscle actin in Arg-177
    • J. Vandekerckhove, B. Schering, M. Bärmann, and K. Aktories Clostridium perfringens iota toxin ADP-ribosylates skeletal muscle actin in Arg-177 FEBS Lett 225 1987 48 52
    • (1987) FEBS Lett , vol.225 , pp. 48-52
    • Vandekerckhove, J.1    Schering, B.2    Bärmann, M.3    Aktories, K.4
  • 5
    • 0023848539 scopus 로고
    • Botulinum C2 toxin ADP-ribosylates cytoplasmic beta/gamma-actin in arginine 177
    • J. Vandekerckhove, B. Schering, M. Bärmann, and K. Aktories Botulinum C2 toxin ADP-ribosylates cytoplasmic beta/gamma-actin in arginine 177 J Biol Chem 263 1988 696 700
    • (1988) J Biol Chem , vol.263 , pp. 696-700
    • Vandekerckhove, J.1    Schering, B.2    Bärmann, M.3    Aktories, K.4
  • 6
    • 0024424942 scopus 로고
    • ADP-ribosylation of actin by clostridial toxins
    • K. Aktories, and A. Wegner ADP-ribosylation of actin by clostridial toxins J Cell Biol 109 1989 1385 1387
    • (1989) J Cell Biol , vol.109 , pp. 1385-1387
    • Aktories, K.1    Wegner, A.2
  • 7
    • 0023708116 scopus 로고
    • ADP-ribosylated actin caps the barbed ends of actin filaments
    • A. Wegner, and K. Aktories ADP-ribosylated actin caps the barbed ends of actin filaments J Biol Chem 263 1988 13739 13742
    • (1988) J Biol Chem , vol.263 , pp. 13739-13742
    • Wegner, A.1    Aktories, K.2
  • 8
    • 0024543962 scopus 로고
    • Nonmuscle actin ADP-ribosylated by botulinum C2 toxin caps actin filaments
    • C. Weigt, I. Just, A. Wegner, and K. Aktories Nonmuscle actin ADP-ribosylated by botulinum C2 toxin caps actin filaments FEBS Lett 246 1989 181 184
    • (1989) FEBS Lett , vol.246 , pp. 181-184
    • Weigt, C.1    Just, I.2    Wegner, A.3    Aktories, K.4
  • 9
    • 0025778012 scopus 로고
    • Alteration of the cytoskeleton of mammalian cells cultured in vitro by Clostridium botulinum C2 toxin and C3 ADP-ribosyltransferase
    • W. Wiegers, I. Just, H. Müller, A. Hellwig, P. Traub, and K. Aktories Alteration of the cytoskeleton of mammalian cells cultured in vitro by Clostridium botulinum C2 toxin and C3 ADP-ribosyltransferase Eur J Cell Biol 54 1991 237 245
    • (1991) Eur J Cell Biol , vol.54 , pp. 237-245
    • Wiegers, W.1    Just, I.2    Müller, H.3    Hellwig, A.4    Traub, P.5    Aktories, K.6
  • 10
    • 0023581950 scopus 로고
    • Response of tissue-cultured cynomolgus monkey kidney cells to botulinum C2 toxin
    • M. Miyake, and I. Ohishi Response of tissue-cultured cynomolgus monkey kidney cells to botulinum C2 toxin Microb Pathog 3 1987 279 286
    • (1987) Microb Pathog , vol.3 , pp. 279-286
    • Miyake, M.1    Ohishi, I.2
  • 11
    • 0019158135 scopus 로고
    • Purification and characterization of two components of botulinum C2 toxin
    • I. Ohishi, M. Iwasaki, and G. Sakaguchi Purification and characterization of two components of botulinum C2 toxin Infect Immun 30 1980 668 673
    • (1980) Infect Immun , vol.30 , pp. 668-673
    • Ohishi, I.1    Iwasaki, M.2    Sakaguchi, G.3
  • 12
    • 53649083009 scopus 로고    scopus 로고
    • ADP-ribosylation of actin by the Clostridium botulinum C2 toxin in mammalian cells results in delayed caspase-dependent apoptotic cell death
    • K. Heine, S. Pust, S. Enzenmüller, and H. Barth ADP-ribosylation of actin by the Clostridium botulinum C2 toxin in mammalian cells results in delayed caspase-dependent apoptotic cell death Infect Immun 76 2008 4600 4608
    • (2008) Infect Immun , vol.76 , pp. 4600-4608
    • Heine, K.1    Pust, S.2    Enzenmüller, S.3    Barth, H.4
  • 13
    • 72449140517 scopus 로고    scopus 로고
    • The long-lived nature of Clostridium perfringens iota toxin in mammalian cells induces delayed apoptosis
    • H. Hilger, S. Pust, G. von Figura, E. Kaiser, B.G. Stiles, and M.R. Popoff The long-lived nature of Clostridium perfringens iota toxin in mammalian cells induces delayed apoptosis Infect Immun 77 2009 5593 5601
    • (2009) Infect Immun , vol.77 , pp. 5593-5601
    • Hilger, H.1    Pust, S.2    Von Figura, G.3    Kaiser, E.4    Stiles, B.G.5    Popoff, M.R.6
  • 14
    • 0020539980 scopus 로고
    • Response of mouse intestinal loop to botulinum C2 toxin: Enterotoxic activity induced by cooperation of nonlinked protein components
    • I. Ohishi Response of mouse intestinal loop to botulinum C2 toxin: enterotoxic activity induced by cooperation of nonlinked protein components Infect Immun 40 1983 691 695
    • (1983) Infect Immun , vol.40 , pp. 691-695
    • Ohishi, I.1
  • 15
    • 0021358479 scopus 로고
    • Histopathological effect of botulinum C2 toxin on mouse intestines
    • I. Ohishi, and Y. Odagiri Histopathological effect of botulinum C2 toxin on mouse intestines Infect Immun 43 1984 54 58
    • (1984) Infect Immun , vol.43 , pp. 54-58
    • Ohishi, I.1    Odagiri, Y.2
  • 16
    • 0029915545 scopus 로고    scopus 로고
    • Clostridial enteric diseases of domestic animals
    • J.G. Songer Clostridial enteric diseases of domestic animals Clin Microbiol Rev 9 1996 216 234
    • (1996) Clin Microbiol Rev , vol.9 , pp. 216-234
    • Songer, J.G.1
  • 17
    • 4544379887 scopus 로고    scopus 로고
    • Distribution of Clostridium difficile variant toxinotypes and strains with binary toxin genes among clinical isolates in an American hospital
    • B. Geric, M. Rupnik, D.N. Gerding, M. Grabnar, and S. Johnson Distribution of Clostridium difficile variant toxinotypes and strains with binary toxin genes among clinical isolates in an American hospital J Med Microbiol 53 2004 887 894
    • (2004) J Med Microbiol , vol.53 , pp. 887-894
    • Geric, B.1    Rupnik, M.2    Gerding, D.N.3    Grabnar, M.4    Johnson, S.5
  • 19
    • 0023024730 scopus 로고
    • Purification and characterization of Clostridium perfringens iota toxin: Dependence on two nonlinked proteins for biological activity
    • B.G. Stiles, and T.D. Wilkins Purification and characterization of Clostridium perfringens iota toxin: dependence on two nonlinked proteins for biological activity Infect Immun 54 1986 683 688
    • (1986) Infect Immun , vol.54 , pp. 683-688
    • Stiles, B.G.1    Wilkins, T.D.2
  • 20
    • 0022993253 scopus 로고
    • Clostridium perfringens iota toxin: Synergism between two proteins
    • B.G. Stiles, and T.D. Wilkins Clostridium perfringens iota toxin: synergism between two proteins Toxicon 24 1986 767 773
    • (1986) Toxicon , vol.24 , pp. 767-773
    • Stiles, B.G.1    Wilkins, T.D.2
  • 21
    • 0031004306 scopus 로고    scopus 로고
    • Production of a complete binary toxin (actin-specific ADP-ribosyltransferase) by Clostridium difficile CD196
    • S. Perelle, M. Gibert, P. Bourlioux, G. Corthier, and M.R. Popoff Production of a complete binary toxin (actin-specific ADP-ribosyltransferase) by Clostridium difficile CD196 Infect Immun 65 1997 1402 1407
    • (1997) Infect Immun , vol.65 , pp. 1402-1407
    • Perelle, S.1    Gibert, M.2    Bourlioux, P.3    Corthier, G.4    Popoff, M.R.5
  • 22
    • 0023747353 scopus 로고
    • Actin-specific ADP-ribosyltransferase produced by a Clostridium difficile strain
    • M.R. Popoff, E.J. Rubin, D.M. Gill, and P. Boquet Actin-specific ADP-ribosyltransferase produced by a Clostridium difficile strain Infect Immun 56 1988 2299 2306
    • (1988) Infect Immun , vol.56 , pp. 2299-2306
    • Popoff, M.R.1    Rubin, E.J.2    Gill, D.M.3    Boquet, P.4
  • 23
    • 0034607782 scopus 로고    scopus 로고
    • Production of actin-specific ADP-ribosyltransferase (binary toxin) by strains of Clostridium difficile
    • S. Stubbs, M. Rupnik, M. Gibert, J. Brazier, B. Duerden, and M. Popoff Production of actin-specific ADP-ribosyltransferase (binary toxin) by strains of Clostridium difficile FEMS Microbiol Lett 186 2000 307 312
    • (2000) FEMS Microbiol Lett , vol.186 , pp. 307-312
    • Stubbs, S.1    Rupnik, M.2    Gibert, M.3    Brazier, J.4    Duerden, B.5    Popoff, M.6
  • 24
    • 0034819726 scopus 로고    scopus 로고
    • Characterization of the ADP-ribosyltransferase CDTa from Clostridium difficile by site directed mutagenesis
    • I. Gülke, G. Pfeifer, J. Liese, M. Fritz, F. Hofmann, and K. Aktories Characterization of the ADP-ribosyltransferase CDTa from Clostridium difficile by site directed mutagenesis Infect Immun 69 2001 6004 6011
    • (2001) Infect Immun , vol.69 , pp. 6004-6011
    • Gülke, I.1    Pfeifer, G.2    Liese, J.3    Fritz, M.4    Hofmann, F.5    Aktories, K.6
  • 25
    • 0023942902 scopus 로고
    • Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actin
    • M.R. Popoff, and P. Boquet Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actin Biochem Biophys Res Commun 152 1988 1361 1368
    • (1988) Biochem Biophys Res Commun , vol.152 , pp. 1361-1368
    • Popoff, M.R.1    Boquet, P.2
  • 26
    • 0031016925 scopus 로고    scopus 로고
    • Immunological and functional comparison between Clostridium perfringens iota toxin, C. Spiroforme toxin, and anthrax toxins
    • S. Perelle, S. Scalzo, S. Kochi, M. Mock, and M.R. Popoff Immunological and functional comparison between Clostridium perfringens iota toxin, C. spiroforme toxin, and anthrax toxins FEMS Microbiol Lett 146 1997 117 121
    • (1997) FEMS Microbiol Lett , vol.146 , pp. 117-121
    • Perelle, S.1    Scalzo, S.2    Kochi, S.3    Mock, M.4    Popoff, M.R.5
  • 27
    • 0023830603 scopus 로고
    • ADP-ribosylation of skeletal muscle and non- muscle actin by Clostridium perfringens iota toxin
    • B. Schering, M. Bärmann, G.S. Chhatwal, U. Geipel, and K. Aktories ADP-ribosylation of skeletal muscle and non- muscle actin by Clostridium perfringens iota toxin Eur J Biochem 171 1988 225 229
    • (1988) Eur J Biochem , vol.171 , pp. 225-229
    • Schering, B.1    Bärmann, M.2    Chhatwal, G.S.3    Geipel, U.4    Aktories, K.5
  • 28
    • 80053636077 scopus 로고    scopus 로고
    • Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase (CDT)
    • P. Papatheodorou, J.E. Carette, G.W. Bell, C. Schwan, G. Guttenberg, and T.R. Brummelkamp Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase (CDT) Proc Natl Acad Sci USA 108 2011 16422 16427
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 16422-16427
    • Papatheodorou, P.1    Carette, J.E.2    Bell, G.W.3    Schwan, C.4    Guttenberg, G.5    Brummelkamp, T.R.6
  • 30
    • 0034723205 scopus 로고    scopus 로고
    • Binding of Clostridium botulinum C2 toxin to asparagine-linked complex and hybrid carbohydrates
    • M. Eckhardt, H. Barth, D. Blöcker, and K. Aktories Binding of Clostridium botulinum C2 toxin to asparagine-linked complex and hybrid carbohydrates J Biol Chem 275 2000 2328 2334
    • (2000) J Biol Chem , vol.275 , pp. 2328-2334
    • Eckhardt, M.1    Barth, H.2    Blöcker, D.3    Aktories, K.4
  • 31
    • 0029962253 scopus 로고    scopus 로고
    • Characterization of component-I gene of botulinum C2 toxin and PCR detection of its gene in clostridial species
    • N. Fujii, T. Kubota, S. Shirakawa, K. Kimura, I. Ohishi, and K. Moriishi Characterization of component-I gene of botulinum C2 toxin and PCR detection of its gene in clostridial species Biochem Biophys Res Commun 220 1996 353 359
    • (1996) Biochem Biophys Res Commun , vol.220 , pp. 353-359
    • Fujii, N.1    Kubota, T.2    Shirakawa, S.3    Kimura, K.4    Ohishi, I.5    Moriishi, K.6
  • 32
    • 0032491480 scopus 로고    scopus 로고
    • Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis
    • H. Barth, J.C. Preiss, F. Hofmann, and K. Aktories Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis J Biol Chem 273 1998 29506 29511
    • (1998) J Biol Chem , vol.273 , pp. 29506-29511
    • Barth, H.1    Preiss, J.C.2    Hofmann, F.3    Aktories, K.4
  • 33
    • 0039003839 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium botulinum C2 toxin requires oligomerization and acidification
    • H. Barth, D. Blöcker, J. Behlke, W. Bergsma-Schutter, A. Brisson, and R. Benz Cellular uptake of Clostridium botulinum C2 toxin requires oligomerization and acidification J Biol Chem 275 2000 18704 18711
    • (2000) J Biol Chem , vol.275 , pp. 18704-18711
    • Barth, H.1    Blöcker, D.2    Behlke, J.3    Bergsma-Schutter, W.4    Brisson, A.5    Benz, R.6
  • 34
    • 77950217694 scopus 로고    scopus 로고
    • Functional characterization of an extended binding component of the actin-ADP-ribosylating C2 toxin detected in Clostridium botulinum strain (C) 2300
    • C. Sterthoff, A.E. Lang, C. Schwan, A. Tauch, and K. Aktories Functional characterization of an extended binding component of the actin-ADP-ribosylating C2 toxin detected in Clostridium botulinum strain (C) 2300 Infect Immun 78 2010 1468 1474
    • (2010) Infect Immun , vol.78 , pp. 1468-1474
    • Sterthoff, C.1    Lang, A.E.2    Schwan, C.3    Tauch, A.4    Aktories, K.5
  • 35
    • 0038208865 scopus 로고    scopus 로고
    • The C terminus of component C2II of Clostridium botulinum C2 toxin is essential for receptor binding
    • D. Blöcker, H. Barth, E. Maier, R. Benz, J.T. Barbieri, and K. Aktories The C terminus of component C2II of Clostridium botulinum C2 toxin is essential for receptor binding Infect Immun 68 2000 4566 4573
    • (2000) Infect Immun , vol.68 , pp. 4566-4573
    • Blöcker, D.1    Barth, H.2    Maier, E.3    Benz, R.4    Barbieri, J.T.5    Aktories, K.6
  • 36
    • 0035993546 scopus 로고    scopus 로고
    • Clostridium botulinum C2 toxin: Binding studies with fluorescence-activated cytometry
    • B.G. Stiles, D. Blöcker, M.L. Hale, M.A. Guetthoff, and H. Barth Clostridium botulinum C2 toxin: binding studies with fluorescence-activated cytometry Toxicon 40 2002 1135 1140
    • (2002) Toxicon , vol.40 , pp. 1135-1140
    • Stiles, B.G.1    Blöcker, D.2    Hale, M.L.3    Guetthoff, M.A.4    Barth, H.5
  • 37
    • 33751070013 scopus 로고    scopus 로고
    • Structure and action of the binary C2 toxin from Clostridium botulinum
    • C. Schleberger, H. Hochmann, H. Barth, K. Aktories, and G.E. Schulz Structure and action of the binary C2 toxin from Clostridium botulinum J Mol Biol 364 2006 705 715
    • (2006) J Mol Biol , vol.364 , pp. 705-715
    • Schleberger, C.1    Hochmann, H.2    Barth, H.3    Aktories, K.4    Schulz, G.E.5
  • 38
    • 0028286786 scopus 로고
    • Interaction of Clostridium botulinum C2 toxin with lipid bilayer membranes. Formation of cation-selective channels and inhibition of channel function by chloroquine
    • A. Schmid, R. Benz, I. Just, and K. Aktories Interaction of Clostridium botulinum C2 toxin with lipid bilayer membranes. Formation of cation-selective channels and inhibition of channel function by chloroquine J Biol Chem 269 1994 16706 16711
    • (1994) J Biol Chem , vol.269 , pp. 16706-16711
    • Schmid, A.1    Benz, R.2    Just, I.3    Aktories, K.4
  • 39
    • 0035404038 scopus 로고    scopus 로고
    • Interaction of C2 toxin with lipid bilayer membranes and Vero cells: Inhibition of channel function by chloroquine and related compounds in vitro and intoxification in vivo
    • C. Bachmeyer, R. Benz, H. Barth, K. Aktories, M. Gilbert, and M.R. Popoff Interaction of C2 toxin with lipid bilayer membranes and Vero cells: inhibition of channel function by chloroquine and related compounds in vitro and intoxification in vivo FASEB J 15 2001 1658 1660
    • (2001) FASEB J , vol.15 , pp. 1658-1660
    • Bachmeyer, C.1    Benz, R.2    Barth, H.3    Aktories, K.4    Gilbert, M.5    Popoff, M.R.6
  • 40
    • 18144441577 scopus 로고    scopus 로고
    • Clostridium botulinum C2 toxin: Low pH-induced pore formation is required for translocation of the enzyme component C2I into the cytosol of host cells
    • D. Blöcker, K. Pohlmann, G. Haug, C. Bachmeyer, R. Benz, and K. Aktories Clostridium botulinum C2 toxin: low pH-induced pore formation is required for translocation of the enzyme component C2I into the cytosol of host cells J Biol Chem 278 2003 37360 37367
    • (2003) J Biol Chem , vol.278 , pp. 37360-37367
    • Blöcker, D.1    Pohlmann, K.2    Haug, G.3    Bachmeyer, C.4    Benz, R.5    Aktories, K.6
  • 41
    • 0037881855 scopus 로고    scopus 로고
    • Channel formation by the binding component of Clostridium botulinum C2 toxin: Glutamate 307 of C2II affects channel properties in vitro and pH-dependent C2I translocation in vivo
    • D. Blöcker, C. Bachmeyer, R. Benz, K. Aktories, and H. Barth Channel formation by the binding component of Clostridium botulinum C2 toxin: glutamate 307 of C2II affects channel properties in vitro and pH-dependent C2I translocation in vivo Biochemistry 42 2003 5368 5377
    • (2003) Biochemistry , vol.42 , pp. 5368-5377
    • Blöcker, D.1    Bachmeyer, C.2    Benz, R.3    Aktories, K.4    Barth, H.5
  • 42
    • 0346333312 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium botulinum C2 toxin: Membrane translocation of a fusion toxin requires unfolding of its dihydrofolate reductase domain
    • G. Haug, C. Wilde, J. Leemhuis, D.K. Meyer, K. Aktories, and H. Barth Cellular uptake of Clostridium botulinum C2 toxin: membrane translocation of a fusion toxin requires unfolding of its dihydrofolate reductase domain Biochemistry 42 2003 15284 15291
    • (2003) Biochemistry , vol.42 , pp. 15284-15291
    • Haug, G.1    Wilde, C.2    Leemhuis, J.3    Meyer, D.K.4    Aktories, K.5    Barth, H.6
  • 43
    • 0035063194 scopus 로고    scopus 로고
    • Cellular uptake of the binary Clostridium perfringens iota-toxin
    • D. Blöcker, J. Behlke, K. Aktories, and H. Barth Cellular uptake of the binary Clostridium perfringens iota-toxin Infect Immun 69 2001 2980 2987
    • (2001) Infect Immun , vol.69 , pp. 2980-2987
    • Blöcker, D.1    Behlke, J.2    Aktories, K.3    Barth, H.4
  • 44
    • 0036845021 scopus 로고    scopus 로고
    • Clostridium perfringens iota toxin: Characterization of the cell-associated iota b complex
    • B.G. Stiles, M.L. Hale, J.C. Marvaud, and M.R. Popoff Clostridium perfringens iota toxin: characterization of the cell-associated iota b complex Biochem J 367 2002 801 808
    • (2002) Biochem J , vol.367 , pp. 801-808
    • Stiles, B.G.1    Hale, M.L.2    Marvaud, J.C.3    Popoff, M.R.4
  • 45
    • 0037155268 scopus 로고    scopus 로고
    • Interaction of the binding component of Clostridium perfringens iota-toxin with lipid bilayer membranes: Demonstration of channel formation by the activated binding component Ib and channel block by the enzyme component Ia
    • O. Knapp, R. Benz, M. Gibert, J.C. Marvaud, and M.R. Popoff Interaction of the binding component of Clostridium perfringens iota-toxin with lipid bilayer membranes: demonstration of channel formation by the activated binding component Ib and channel block by the enzyme component Ia J Biol Chem 277 2002 6143 6152
    • (2002) J Biol Chem , vol.277 , pp. 6143-6152
    • Knapp, O.1    Benz, R.2    Gibert, M.3    Marvaud, J.C.4    Popoff, M.R.5
  • 46
    • 0036130586 scopus 로고    scopus 로고
    • Binding component of Clostridium perfringens iota-toxin induces endocytosis in Vero cells
    • M. Nagahama, K. Nagayasu, K. Kobayashi, and J. Sakurai Binding component of Clostridium perfringens iota-toxin induces endocytosis in Vero cells Infect Immun 70 2002 1909 1914
    • (2002) Infect Immun , vol.70 , pp. 1909-1914
    • Nagahama, M.1    Nagayasu, K.2    Kobayashi, K.3    Sakurai, J.4
  • 47
    • 1842588541 scopus 로고    scopus 로고
    • Detergent-resistant membrane microdomains facilitate Ib oligomer formation and biological activity of Clostridium perfringens iota-toxin
    • M.L. Hale, J.C. Marvaud, M.R. Popoff, and B.G. Stiles Detergent-resistant membrane microdomains facilitate Ib oligomer formation and biological activity of Clostridium perfringens iota-toxin Infect Immun 72 2004 2186 2193
    • (2004) Infect Immun , vol.72 , pp. 2186-2193
    • Hale, M.L.1    Marvaud, J.C.2    Popoff, M.R.3    Stiles, B.G.4
  • 48
    • 33947393035 scopus 로고    scopus 로고
    • Differential requirement for the translocation of clostridial binary toxins: Iota toxin requires a membrane potential gradient
    • M. Gibert, J.C. Marvaud, Y. Pereira, M.L. Hale, B.G. Stiles, and P. Boquet Differential requirement for the translocation of clostridial binary toxins: iota toxin requires a membrane potential gradient FEBS Lett 581 2007 1287 1296
    • (2007) FEBS Lett , vol.581 , pp. 1287-1296
    • Gibert, M.1    Marvaud, J.C.2    Pereira, Y.3    Hale, M.L.4    Stiles, B.G.5    Boquet, P.6
  • 49
    • 0041856090 scopus 로고    scopus 로고
    • The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol
    • G. Haug, J. Leemhuis, D. Tiemann, D.K. Meyer, K. Aktories, and H. Barth The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol J Biol Chem 278 2003 32266 32274
    • (2003) J Biol Chem , vol.278 , pp. 32266-32274
    • Haug, G.1    Leemhuis, J.2    Tiemann, D.3    Meyer, D.K.4    Aktories, K.5    Barth, H.6
  • 50
    • 2142662149 scopus 로고    scopus 로고
    • The host cell chaperone Hsp90 is necessary for cytotoxic action of the binary iota-like toxins
    • G. Haug, K. Aktories, and H. Barth The host cell chaperone Hsp90 is necessary for cytotoxic action of the binary iota-like toxins Infect Immun 72 2004 3066 3068
    • (2004) Infect Immun , vol.72 , pp. 3066-3068
    • Haug, G.1    Aktories, K.2    Barth, H.3
  • 51
    • 64049084122 scopus 로고    scopus 로고
    • Cyclophilin A facilitates translocation of the Clostridium botulinum C2 toxin across membranes of acidified endosomes into the cytosol of mammalian cells
    • E. Kaiser, S. Pust, C. Kroll, and H. Barth Cyclophilin A facilitates translocation of the Clostridium botulinum C2 toxin across membranes of acidified endosomes into the cytosol of mammalian cells Cell Microbiol 11 2009 780 795
    • (2009) Cell Microbiol , vol.11 , pp. 780-795
    • Kaiser, E.1    Pust, S.2    Kroll, C.3    Barth, H.4
  • 52
    • 80855141250 scopus 로고    scopus 로고
    • Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90
    • E. Kaiser, C. Kroll, K. Ernst, C. Schwan, M.R. Popoff, and G. Fischer Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90 Infect Immun 79 2011 3913 3921
    • (2011) Infect Immun , vol.79 , pp. 3913-3921
    • Kaiser, E.1    Kroll, C.2    Ernst, K.3    Schwan, C.4    Popoff, M.R.5    Fischer, G.6
  • 53
    • 84863992806 scopus 로고    scopus 로고
    • FK506-binding protein 51 interacts with Clostridium botulinum C2 toxin and FK506 blocks membrane translocation of the toxin in mammalian cells
    • E. Kaiser, N. Böhm, K. Ernst, S. Langer, C. Schwan, and K. Aktories FK506-binding protein 51 interacts with Clostridium botulinum C2 toxin and FK506 blocks membrane translocation of the toxin in mammalian cells Cell Microbiol 14 2012 1193 1205
    • (2012) Cell Microbiol , vol.14 , pp. 1193-1205
    • Kaiser, E.1    Böhm, N.2    Ernst, K.3    Langer, S.4    Schwan, C.5    Aktories, K.6
  • 54
    • 0026319518 scopus 로고
    • Slow conformational changes in protein folding can be accelerated by enzymes
    • H. Bang, and G. Fischer Slow conformational changes in protein folding can be accelerated by enzymes Biomed Biochim Acta 50 1991 137 142
    • (1991) Biomed Biochim Acta , vol.50 , pp. 137-142
    • Bang, H.1    Fischer, G.2
  • 55
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • G. Fischer, B. Wittmann-Liebold, K. Lang, T. Kiefhaber, and F.X. Schmid Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins Nature 337 1989 476 478
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 56
    • 0027256737 scopus 로고
    • Prolyl isomerase: Enzymatic catalysis of slow protein-folding reactions
    • F.X. Schmid Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions Annu Rev Biophys Biomol Struct 22 1993 123 142
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 123-142
    • Schmid, F.X.1
  • 58
    • 0141707715 scopus 로고    scopus 로고
    • Peptidylprolyl cis/trans isomerases (immunophilins): Biological diversity-targets-functions
    • A. Galat Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity-targets-functions Curr Top Med Chem 3 2003 1315 1347
    • (2003) Curr Top Med Chem , vol.3 , pp. 1315-1347
    • Galat, A.1
  • 60
    • 0037438354 scopus 로고    scopus 로고
    • Thermodynamic characterization of the interaction of human cyclophilin 18 with cyclosporin A
    • J. Fanghänel, and G. Fischer Thermodynamic characterization of the interaction of human cyclophilin 18 with cyclosporin A Biophys Chem 100 2003 351 366
    • (2003) Biophys Chem , vol.100 , pp. 351-366
    • Fanghänel, J.1    Fischer, G.2
  • 61
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • W.B. Pratt, and D.O. Toft Steroid receptor interactions with heat shock protein and immunophilin chaperones Endocr Rev 18 1997 306 360
    • (1997) Endocr Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 62
    • 0034968225 scopus 로고    scopus 로고
    • Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40
    • F. Pirkl, and J. Buchner Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40 J Mol Biol 308 2001 795 806
    • (2001) J Mol Biol , vol.308 , pp. 795-806
    • Pirkl, F.1    Buchner, J.2
  • 63
    • 33750701808 scopus 로고    scopus 로고
    • Formation of a biologically active toxin complex of the binary Clostridium botulinum C2 toxin without cell membrane interaction
    • E. Kaiser, G. Haug, M. Hliscs, K. Aktories, and H. Barth Formation of a biologically active toxin complex of the binary Clostridium botulinum C2 toxin without cell membrane interaction Biochemistry 45 2006 13361 13368
    • (2006) Biochemistry , vol.45 , pp. 13361-13368
    • Kaiser, E.1    Haug, G.2    Hliscs, M.3    Aktories, K.4    Barth, H.5
  • 64
    • 1842411345 scopus 로고    scopus 로고
    • Energetic and entropic factors determining binding affinity in protein-ligand complexes
    • G. Klebe, and H.J. Böhm Energetic and entropic factors determining binding affinity in protein-ligand complexes J Recept Signal Transduct Res 17 1997 459 473
    • (1997) J Recept Signal Transduct Res , vol.17 , pp. 459-473
    • Klebe, G.1    Böhm, H.J.2
  • 66
    • 84871498469 scopus 로고    scopus 로고
    • Fine tuning the inhibition profile of cyclosporine A by derivatization of the MeBmt residue
    • E. Prell, V. Kahlert, K.P. Rücknagel, M. Malešević, and G. Fischer Fine tuning the inhibition profile of cyclosporine A by derivatization of the MeBmt residue ChemBioChem 14 2013 63 65
    • (2013) ChemBioChem , vol.14 , pp. 63-65
    • Prell, E.1    Kahlert, V.2    Rücknagel, K.P.3    Malešević, M.4    Fischer, G.5
  • 67
    • 0019271816 scopus 로고
    • Diphtheria toxin entry into cells is facilitated by low pH
    • K. Sandvig, and S. Olsnes Diphtheria toxin entry into cells is facilitated by low pH J Cell Biol 87 1980 828 832
    • (1980) J Cell Biol , vol.87 , pp. 828-832
    • Sandvig, K.1    Olsnes, S.2
  • 68
    • 84896403067 scopus 로고    scopus 로고
    • The chaperone Hsp90 and PPIases of the cyclophilin and FKBP families facilitate membrane translocation of Photorhabdus luminescens ADP-ribosyltransferases
    • A.E. Lang, K. Ernst, H. Lee, P. Papatheodorou, C. Schwan, and H. Barth The chaperone Hsp90 and PPIases of the cyclophilin and FKBP families facilitate membrane translocation of Photorhabdus luminescens ADP-ribosyltransferases Cell Microbiol 16 2013 490 503
    • (2013) Cell Microbiol , vol.16 , pp. 490-503
    • Lang, A.E.1    Ernst, K.2    Lee, H.3    Papatheodorou, P.4    Schwan, C.5    Barth, H.6
  • 69
    • 0345668477 scopus 로고    scopus 로고
    • The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex
    • R. Ratts, H. Zeng, E.A. Berg, C. Blue, M.E. McComb, and C.E. Costello The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex J Cell Biol 160 2003 1139 1150
    • (2003) J Cell Biol , vol.160 , pp. 1139-1150
    • Ratts, R.1    Zeng, H.2    Berg, E.A.3    Blue, C.4    McComb, M.E.5    Costello, C.E.6
  • 70
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • J. Liu, J.D. Farmer, W.S. Lane, J. Friedman, I. Weissman, and S.L. Schreiber Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes Cell 66 1991 807 815
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer, J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 71
    • 84904191299 scopus 로고    scopus 로고
    • Functional aspects of extracellular cyclophilins
    • H. Hoffmann, and C. Schiene-Fischer Functional aspects of extracellular cyclophilins Biol Chem 2014 10.1515/hsz-2014-0125
    • (2014) Biol Chem
    • Hoffmann, H.1    Schiene-Fischer, C.2
  • 72
  • 73
    • 0030050335 scopus 로고    scopus 로고
    • Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding
    • T. Ratajczak, and A. Carrello Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding J Biol Chem 271 1996 2961 2965
    • (1996) J Biol Chem , vol.271 , pp. 2961-2965
    • Ratajczak, T.1    Carrello, A.2
  • 75
    • 84885002888 scopus 로고    scopus 로고
    • Anti-inflammatory effects of extracellular cyclosporins are exclusively mediated by CD147
    • M. Malesevic, D. Gutknecht, E. Prell, C. Klein, M. Schumann, and R.A. Nowak Anti-inflammatory effects of extracellular cyclosporins are exclusively mediated by CD147 J Med Chem 56 2013 7302 7311
    • (2013) J Med Chem , vol.56 , pp. 7302-7311
    • Malesevic, M.1    Gutknecht, D.2    Prell, E.3    Klein, C.4    Schumann, M.5    Nowak, R.A.6
  • 76
    • 73449097193 scopus 로고    scopus 로고
    • Clostridium difficile toxin CDT induces formation of microtubule-based protrusions and increases adherence of bacteria
    • C. Schwan, B. Stecher, T. Tzivelekidis, M. van Ham, M. Rohde, and W.D. Hardt Clostridium difficile toxin CDT induces formation of microtubule-based protrusions and increases adherence of bacteria PLoS Pathog 5 2009 e1000626
    • (2009) PLoS Pathog , vol.5 , pp. e1000626
    • Schwan, C.1    Stecher, B.2    Tzivelekidis, T.3    Van Ham, M.4    Rohde, M.5    Hardt, W.D.6
  • 77
    • 77956871102 scopus 로고    scopus 로고
    • Clostridium difficile infection
    • L. Heinlen, and J.D. Ballard Clostridium difficile infection Am J Med Sci 340 2010 247 252
    • (2010) Am J Med Sci , vol.340 , pp. 247-252
    • Heinlen, L.1    Ballard, J.D.2
  • 78
    • 2442420091 scopus 로고    scopus 로고
    • Prevalence and characterization of a binary toxin (actin-specific ADP-ribosyltransferase) from Clostridium difficile
    • C. Goncalves, D. Decre, F. Barbut, B. Burghoffer, and J.C. Petit Prevalence and characterization of a binary toxin (actin-specific ADP-ribosyltransferase) from Clostridium difficile J Clin Microbiol 42 2004 1933 1939
    • (2004) J Clin Microbiol , vol.42 , pp. 1933-1939
    • Goncalves, C.1    Decre, D.2    Barbut, F.3    Burghoffer, B.4    Petit, J.C.5
  • 79
    • 53749091415 scopus 로고    scopus 로고
    • Characterization of Clostridium difficile strains isolated from patients in Ontario, Canada, from 2004 to 2006
    • H. Martin, B. Willey, D.E. Low, H.R. Staempfli, A. McGeer, and P. Boerlin Characterization of Clostridium difficile strains isolated from patients in Ontario, Canada, from 2004 to 2006 J Clin Microbiol 46 2008 2999 3004
    • (2008) J Clin Microbiol , vol.46 , pp. 2999-3004
    • Martin, H.1    Willey, B.2    Low, D.E.3    Staempfli, H.R.4    McGeer, A.5    Boerlin, P.6
  • 80
    • 33744964249 scopus 로고    scopus 로고
    • The specific FKBP38 inhibitor N-(N′, N′-dimethylcarboxamidomethyl)cycloheximide has potent neuroprotective and neurotrophic properties in brain ischemia
    • F. Edlich, M. Weiwad, D. Wildemann, F. Jarczowski, S. Kilka, and M.C. Moutty The specific FKBP38 inhibitor N-(N′, N′-dimethylcarboxamidomethyl)cycloheximide has potent neuroprotective and neurotrophic properties in brain ischemia J Biol Chem 281 2006 14961 14970
    • (2006) J Biol Chem , vol.281 , pp. 14961-14970
    • Edlich, F.1    Weiwad, M.2    Wildemann, D.3    Jarczowski, F.4    Kilka, S.5    Moutty, M.C.6
  • 81
    • 77649216057 scopus 로고    scopus 로고
    • Selective and specific internalization of clostridial C3 ADP-ribosyltransferases into macrophages and monocytes
    • J. Fahrer, J. Kuban, K. Heine, G. Rupps, E. Kaiser, and E. Felder Selective and specific internalization of clostridial C3 ADP-ribosyltransferases into macrophages and monocytes Cell Microbiol 12 2010 233 247
    • (2010) Cell Microbiol , vol.12 , pp. 233-247
    • Fahrer, J.1    Kuban, J.2    Heine, K.3    Rupps, G.4    Kaiser, E.5    Felder, E.6
  • 82
    • 0030597057 scopus 로고    scopus 로고
    • Evidence that Arg-295, Glu-378, and Glu-380 are active-site residues of the ADP-ribosyltransferase activity of iota toxin
    • S. Perelle, M. Domenighini, and M.R. Popoff Evidence that Arg-295, Glu-378, and Glu-380 are active-site residues of the ADP-ribosyltransferase activity of iota toxin FEBS Lett 395 1996 191 194
    • (1996) FEBS Lett , vol.395 , pp. 191-194
    • Perelle, S.1    Domenighini, M.2    Popoff, M.R.3
  • 84
    • 0021668676 scopus 로고
    • Determination of enzymatic catalysis for the cis-trans-isomerization of peptide bonds in proline-containing peptides
    • G. Fischer, H. Bang, and C. Mech Determination of enzymatic catalysis for the cis-trans-isomerization of peptide bonds in proline-containing peptides Biomed Biochim Acta 43 1984 1101 1111
    • (1984) Biomed Biochim Acta , vol.43 , pp. 1101-1111
    • Fischer, G.1    Bang, H.2    Mech, C.3
  • 86
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


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