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Volumn 9, Issue 8, 2017, Pages

Cellular entry of Clostridium perfringens iota-toxin and Clostridium botulinum C2 toxin

Author keywords

C2 toxin; Cellular internalization; Clostridial binary toxin; Iota toxin

Indexed keywords

BACTERIAL TOXIN; CLOSTRIDIUM BOTULINUM C2 TOXIN; CLOSTRIDIUM PERFRINGENS IOTA TOXIN; LIPOPROTEIN RECEPTOR; SPHINGOMYELIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR; ACTIN; BOTULINUM TOXIN; BOTULINUM TOXIN TYPE C; IOTA TOXIN, CLOSTRIDIUM PERFRINGENS; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE;

EID: 85027414793     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins9080247     Document Type: Review
Times cited : (24)

References (51)
  • 1
    • 0033934871 scopus 로고    scopus 로고
    • Clostridium perfringens iota-toxin requires activation of both binding and enzymatic components for cytopathic activity
    • [CrossRef] [PubMed]
    • Gibert, M.; Petit, L.; Raffestin, S.; Okabe, A.; Popoff, M. R. Clostridium perfringens iota-toxin requires activation of both binding and enzymatic components for cytopathic activity. Infect. Immun. 2000, 68, 3848-3853. [CrossRef] [PubMed]
    • (2000) Infect. Immun , vol.68 , pp. 3848-3853
    • Gibert, M.1    Petit, L.2    Raffestin, S.3    Okabe, A.4    Popoff, M.R.5
  • 2
    • 70449380358 scopus 로고    scopus 로고
    • Clostridial toxins
    • [CrossRef] [PubMed]
    • Popoff, M. R.; Boquet, P. Clostridial toxins. Future Microbiol. 2009, 4, 1021-1064. [CrossRef] [PubMed]
    • (2009) Future Microbiol , vol.4 , pp. 1021-1064
    • Popoff, M.R.1    Boquet, P.2
  • 3
    • 84979834040 scopus 로고    scopus 로고
    • Clostridium perfringens iota-toxin: Structure and function
    • [CrossRef] [PubMed]
    • Sakurai, J.; Nagahama, M.; Oda, M.; Tsuge, H.; Kobayashi, K. Clostridium perfringens iota-toxin: Structure and function. Toxins 2009, 1, 208-228. [CrossRef] [PubMed]
    • (2009) Toxins , vol.1 , pp. 208-228
    • Sakurai, J.1    Nagahama, M.2    Oda, M.3    Tsuge, H.4    Kobayashi, K.5
  • 5
    • 0034819726 scopus 로고    scopus 로고
    • Characterization of the enzymatic component of the ADP-ribosyltransferase toxin. CDTa from Clostridium difficile
    • [CrossRef] [PubMed]
    • Gülke, I.; Pfeifer, G.; Liese, J.; Fritz, M.; Hofmann, F.; Aktories, K.; Barth, H. Characterization of the enzymatic component of the ADP-ribosyltransferase toxin. CDTa from Clostridium difficile. Infect. Immun. 2001, 69, 6004-6011. [CrossRef] [PubMed]
    • (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    Barth, H.7
  • 6
    • 0023942902 scopus 로고
    • Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actin
    • [CrossRef]
    • Popoff, M. R.; Boquet, P. Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actin. Biochem. Biophys. Res. Commun. 1988, 152, 1361-1368. [CrossRef]
    • (1988) Biochem. Biophys. Res. Commun , vol.152 , pp. 1361-1368
    • Popoff, M.R.1    Boquet, P.2
  • 8
    • 0036130586 scopus 로고    scopus 로고
    • Binding component of Clostridium perfringens iota-toxin induces endocytosis in Vero cells
    • [CrossRef] [PubMed]
    • Nagahama, M.; Nagayasu, K.; Kobayashi, K.; Sakurai, J. Binding component of Clostridium perfringens iota-toxin induces endocytosis in Vero cells. Infect. Immun. 2002, 70, 1909-1914. [CrossRef] [PubMed]
    • (2002) Infect. Immun , vol.70 , pp. 1909-1914
    • Nagahama, M.1    Nagayasu, K.2    Kobayashi, K.3    Sakurai, J.4
  • 9
    • 2542583975 scopus 로고    scopus 로고
    • Binding and internalization of Clostridium perfringens iota-toxin in lipid rafts
    • [CrossRef] [PubMed]
    • Nagahama, M.; Yamaguchi, A.; Hagiyama, T.; Ohkubo, N.; Kobayashi, K.; Sakurai, J. Binding and internalization of Clostridium perfringens iota-toxin in lipid rafts. Infect. Immun. 2004, 72, 3267-3275. [CrossRef] [PubMed]
    • (2004) Infect. Immun , vol.72 , pp. 3267-3275
    • Nagahama, M.1    Yamaguchi, A.2    Hagiyama, T.3    Ohkubo, N.4    Kobayashi, K.5    Sakurai, J.6
  • 10
    • 80051693604 scopus 로고    scopus 로고
    • Actin as target for modification by bacterial protein toxins
    • [CrossRef] [PubMed]
    • Aktories, K.; Lang, A. E.; Schwan, C.; Mannherz, H. G. Actin as target for modification by bacterial protein toxins. FEBS J. 2011, 278, 4526-4543. [CrossRef] [PubMed]
    • (2011) FEBS J , vol.278 , pp. 4526-4543
    • Aktories, K.1    Lang, A.E.2    Schwan, C.3    Mannherz, H.G.4
  • 11
    • 84956739494 scopus 로고    scopus 로고
    • Pore-forming activity of clostridial binary toxins
    • [CrossRef] [PubMed]
    • Knapp, O.; Benz, R.; Popoff, M. R. Pore-forming activity of clostridial binary toxins. Biochim. Biophys. Acta 2016, 1858, 512-525. [CrossRef] [PubMed]
    • (2016) Biochim. Biophys. Acta , vol.1858 , pp. 512-525
    • Knapp, O.1    Benz, R.2    Popoff, M.R.3
  • 12
    • 0025242426 scopus 로고
    • ADP-ribosylation of actin isoforms by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin
    • [CrossRef] [PubMed]
    • Mauss, S.; Chaponnier, C.; Just, I.; Aktories, K.; Gabbiani, G. ADP-ribosylation of actin isoforms by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin. Eur. J. Biochem. 1990, 194, 237-241. [CrossRef] [PubMed]
    • (1990) Eur. J. Biochem , vol.194 , pp. 237-241
    • Mauss, S.1    Chaponnier, C.2    Just, I.3    Aktories, K.4    Gabbiani, G.5
  • 13
    • 78650271034 scopus 로고    scopus 로고
    • Endocytosis and toxicity of clostridial binary toxins depend on a clathrin-independent pathway regulated by Rho-GDI
    • [CrossRef] [PubMed]
    • Gibert, M.; Monier, M. N.; Ruez, R.; Hale, M. L.; Stiles, B. G.; Benmerah, A.; Johannes, L.; Lamaze, C.; Popoff, M. R. Endocytosis and toxicity of clostridial binary toxins depend on a clathrin-independent pathway regulated by Rho-GDI. Cell. Microbiol. 2011, 13, 154-170. [CrossRef] [PubMed]
    • (2011) Cell. Microbiol , vol.13 , pp. 154-170
    • Gibert, M.1    Monier, M.N.2    Ruez, R.3    Hale, M.L.4    Stiles, B.G.5    Benmerah, A.6    Johannes, L.7    Lamaze, C.8    Popoff, M.R.9
  • 14
    • 0029915545 scopus 로고    scopus 로고
    • Clostridial enteric diseases of domestic animals
    • [PubMed]
    • Songer, J. G. Clostridial enteric diseases of domestic animals. Clin. Microbiol. Rev. 1996, 9, 216-234. [PubMed]
    • (1996) Clin. Microbiol. Rev , vol.9 , pp. 216-234
    • Songer, J.G.1
  • 16
    • 0037225397 scopus 로고    scopus 로고
    • Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens iota-toxin
    • [CrossRef]
    • Tsuge, H.; Nagahama, M.; Nishimura, H.; Hisatsune, J.; Sakaguchi, Y.; Itogawa, Y.; Katunuma, N.; Sakurai, J. Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens iota-toxin. J. Mol. Biol. 2003, 325, 471-483. [CrossRef]
    • (2003) J. Mol. Biol , vol.325 , pp. 471-483
    • Tsuge, H.1    Nagahama, M.2    Nishimura, H.3    Hisatsune, J.4    Sakaguchi, Y.5    Itogawa, Y.6    Katunuma, N.7    Sakurai, J.8
  • 18
    • 84875045406 scopus 로고    scopus 로고
    • Arginine ADP-ribosylation mechanism based on structural snapshots of iota-toxin and actin complex
    • [CrossRef] [PubMed]
    • Tsurumura, T.; Tsumori, Y.; Qiu, H.; Oda, M.; Sakurai, J.; Nagahama, M.; Tsuge, H. Arginine ADP-ribosylation mechanism based on structural snapshots of iota-toxin and actin complex. Proc. Natl. Acad. Sci. USA 2013, 110, 4267-4272. [CrossRef] [PubMed]
    • (2013) "');"> , vol.110 , pp. 4267-4272
    • Tsurumura, T.1    Tsumori, Y.2    Qiu, H.3    Oda, M.4    Sakurai, J.5    Nagahama, M.6    Tsuge, H.7
  • 19
    • 4544264417 scopus 로고    scopus 로고
    • Binary bacterial toxins: Biochemistry, biology, and applications of common Clostridium and Bacillus proteins
    • [CrossRef] [PubMed]
    • Barth, H.; Aktories, K.; Popoff, M. R.; Stiles, B. G. Binary bacterial toxins: Biochemistry, biology, and applications of common Clostridium and Bacillus proteins. Microbiol. Mol. Biol. Rev. 2004, 68, 373-402. [CrossRef] [PubMed]
    • (2004) Microbiol. Mol. Biol. Rev , vol.68 , pp. 373-402
    • Barth, H.1    Aktories, K.2    Popoff, M.R.3    Stiles, B.G.4
  • 20
    • 80053636077 scopus 로고    scopus 로고
    • Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase (CDT)
    • [CrossRef] [PubMed]
    • Papatheodorou, P.; Carette, J. E.; Bell, G. W.; Schwan, C.; Guttenberg, G.; Brummelkamp, T. R.; Aktories, K. Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase (CDT). Proc. Natl. Acad. Sci. USA 2011, 108, 16422-16427. [CrossRef] [PubMed]
    • (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    Aktories, K.7
  • 21
    • 84918544522 scopus 로고    scopus 로고
    • Novel receptors for bacterial protein toxins
    • [CrossRef] [PubMed]
    • Schmidt, G.; Papatheodorou, P.; Aktories, K. Novel receptors for bacterial protein toxins. Curr. Opin. Microbiol. 2015, 23, 55-61. [CrossRef] [PubMed]
    • (2015) Curr. Opin. Microbiol , vol.23 , pp. 55-61
    • Schmidt, G.1    Papatheodorou, P.2    Aktories, K.3
  • 24
    • 0142197614 scopus 로고    scopus 로고
    • Pathogens: Raft hijackers
    • [CrossRef] [PubMed]
    • Mañes, S.; del Real, G.; Martínez-A C. Pathogens: Raft hijackers. Nat. Rev. Immunol. 2003, 3, 557-568. [CrossRef] [PubMed]
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 557-568
    • Mañes, S.1    Del Real, G.2    Martínez, C.3
  • 25
    • 29144525990 scopus 로고    scopus 로고
    • The role of lipid rafts in the pathogenesis of bacterial infections
    • [CrossRef] [PubMed]
    • Zaas, D. W.; Duncan, M. ;Wright, J. R.; Abraham, S. N. The role of lipid rafts in the pathogenesis of bacterial infections. Biochim. Biophys. Acta 2005, 1746, 305-313. [CrossRef] [PubMed]
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 305-313
    • Zaas, D.W.1    Duncan, M.2    Wright, J.R.3    Abraham, S.N.4
  • 27
    • 1842588541 scopus 로고    scopus 로고
    • Detergent-resistant membrane microdomains facilitate Ib oligomer formation and biological activity of Clostridium perfringens iota-toxin
    • [CrossRef] [PubMed]
    • Hale, M. L.; Marvaud, J. C.; Popoff, M. R.; Stiles, B. G. Detergent-resistant membrane microdomains facilitate Ib oligomer formation and biological activity of Clostridium perfringens iota-toxin. Infect. Immun. 2004, 72, 2186-2193. [CrossRef] [PubMed]
    • (2004) Infect. Immun , vol.72 , pp. 2186-2193
    • Hale, M.L.1    Marvaud, J.C.2    Popoff, M.R.3    Stiles, B.G.4
  • 28
    • 0035081307 scopus 로고    scopus 로고
    • Clostridium perfringens iota-toxin: Mapping of receptor binding and Ia docking domains on Ib
    • [CrossRef] [PubMed]
    • Marvaud, J. C.; Smith, T.; Hale, M. L.; Popoff, M. R.; Smith, L. A.; Stiles, B. G. Clostridium perfringens iota-toxin: Mapping of receptor binding and Ia docking domains on Ib. Infect. Immun. 2001, 69, 2435-2441. [CrossRef] [PubMed]
    • (2001) Infect. Immun , vol.69 , pp. 2435-2441
    • Marvaud, J.C.1    Smith, T.2    Hale, M.L.3    Popoff, M.R.4    Smith, L.A.5    Stiles, B.G.6
  • 30
    • 84879571965 scopus 로고    scopus 로고
    • Clostridium difficile binary toxin CDT induces clustering of the lipolysis-stimulated lipoprotein receptor into lipid rafts
    • [CrossRef] [PubMed]
    • Papatheodorou, P.; Hornuss, D.; Nölke, T.; Hemmasi, S.; Castonguay, J.; Picchianti, M.; Aktories, K. Clostridium difficile binary toxin CDT induces clustering of the lipolysis-stimulated lipoprotein receptor into lipid rafts. mBio 2013, 4, e00244-13. [CrossRef] [PubMed]
    • (2013) . Mbio , vol.4 , pp. e00244-e00313
    • Papatheodorou, P.1    Hornuss, D.2    Nölke, T.3    Hemmasi, S.4    Castonguay, J.5    Picchianti, M.6    Aktories, K.7
  • 31
    • 33947393035 scopus 로고    scopus 로고
    • Differential requirement for the translocation of clostridial binary toxins: Iota toxin requires a membrane potential gradient
    • [CrossRef] [PubMed]
    • Gibert, M.; Marvaud, J. C.; Pereira, Y.; Hale, M. L.; Stiles, B. G.; Boquet, P.; Lamaze, C.; Popoff, M. R. Differential requirement for the translocation of clostridial binary toxins: Iota toxin requires a membrane potential gradient. FEBS Lett. 2007, 581, 1287-1296. [CrossRef] [PubMed]
    • (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    Lamaze, C.7    Popoff, M.R.8
  • 33
    • 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
    • [CrossRef] [PubMed]
    • Kaiser, E.; Kroll, C.; Ernst, K.; Schwan, C.; Popoff, M.; Fischer, G.; Buchner, J.; Aktories, K.; Barth, H. Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90. Infect. Immun. 2011, 79, 3913-3921. [CrossRef] [PubMed]
    • (2011) Infect. Immun , vol.79 , pp. 3913-3921
    • Kaiser, E.1    Kroll, C.2    Ernst, K.3    Schwan, C.4    Popoff, M.5    Fischer, G.6    Buchner, J.7    Aktories, K.8    Barth, H.9
  • 34
    • 84957837635 scopus 로고    scopus 로고
    • A novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens iota toxin
    • [CrossRef] [PubMed]
    • Ernst, K.; Liebscher, M.; Mathea, S.; Granzhan, A.; Schmid, J.; Popoff, M. R.; Ihmels, H.; Barth, H.; Schiene-Fischer, C. A novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens iota toxin. Sci. Rep. 2016, 6, 20301. [CrossRef] [PubMed]
    • (2016) Sci. Rep , vol.6 , pp. 20301
    • Ernst, K.1    Liebscher, M.2    Mathea, S.3    Granzhan, A.4    Schmid, J.5    Popoff, M.R.6    Ihmels, H.7    Barth, H.8    Schiene-Fischer, C.9
  • 35
    • 85019974593 scopus 로고    scopus 로고
    • Hsp70 facilitates trans-membrane transport of bacterial ADP-ribosylating toxins into the cytosol of mammalian cells
    • [CrossRef] [PubMed]
    • Ernst, K.; Schmid, J.; Beck, M.; Hägele, M.; Hohwieler, M.; Hauff, P.; Ückert, A. K.; Anastasia, A.; Fauler, M.; Jank, T. et al. Hsp70 facilitates trans-membrane transport of bacterial ADP-ribosylating toxins into the cytosol of mammalian cells. Sci. Rep. 2017, 7, 2724. [CrossRef] [PubMed]
    • (2017) Sci. Rep , vol.2724 , pp. 7
    • Ernst, K.1    Schmid, J.2    Beck, M.3    Hägele, M.4    Hohwieler, M.5    Hauff, P.6    Ückert, A.K.7    Anastasia, A.8    Fauler, M.9    Jank, T.10
  • 36
    • 0037155268 scopus 로고    scopus 로고
    • Interaction 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
    • [CrossRef] [PubMed]
    • Knapp, O.; Benz, R.; Gibert, M.; Marvaud, J. C.; Popoff, M. R. Interaction 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. 2002, 277, 6143-6152. [CrossRef] [PubMed]
    • (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
  • 39
    • 33751070013 scopus 로고    scopus 로고
    • Structure and action of the binary C2 toxin from Clostridium botulinum
    • [CrossRef] [PubMed]
    • Schleberger, C.; Hochmann, H.; Barth, H.; Aktories, K.; Schulz, G. E. Structure and action of the binary C2 toxin from Clostridium botulinum. J. Mol. Biol. 2006, 364, 705-715. [CrossRef] [PubMed]
    • (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
  • 40
    • 0034723205 scopus 로고    scopus 로고
    • Binding of Clostridium botulinum C2 toxin to asparagine-linked complex and hybrid carbohydrates
    • [CrossRef] [PubMed]
    • Eckhardt, M.; Barth, H.; Blöcker, D.; Aktories, K. Binding of Clostridium botulinum C2 toxin to asparagine-linked complex and hybrid carbohydrates. J. Biol. Chem. 2000, 275, 2328-2334. [CrossRef] [PubMed]
    • (2000) J. Biol. Chem , vol.275 , pp. 2328-2334
    • Eckhardt, M.1    Barth, H.2    Blöcker, D.3    Aktories, K.4
  • 41
    • 85016173980 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium botulinum C2 toxin requires acid sphingomyelinase activity
    • [CrossRef] [PubMed]
    • Nagahama, M.; Takehara, M.; Takagishi, T.; Seike, S.; Miyamoto, K.; Kobayashi, K. Cellular uptake of Clostridium botulinum C2 toxin requires acid sphingomyelinase activity. Infect. Immun. 2017, 85, e00966-16. [CrossRef] [PubMed]
    • (2017) Infect. Immun , vol.85 , pp. e00966-e01016
    • Nagahama, M.1    Takehara, M.2    Takagishi, T.3    Seike, S.4    Miyamoto, K.5    Kobayashi, K.6
  • 42
    • 54049109535 scopus 로고    scopus 로고
    • Two-way traffic on the road to plasma membrane repair
    • [CrossRef] [PubMed]
    • Idone, V.; Tam, C.; Andrews, N. W. Two-way traffic on the road to plasma membrane repair. Trends Cell Biol. 2008, 18, 552-559. [CrossRef] [PubMed]
    • (2008) Trends Cell Biol , vol.18 , pp. 552-559
    • Idone, V.1    Tam, C.2    Andrews, N.W.3
  • 43
    • 84878253590 scopus 로고    scopus 로고
    • Role of pore-forming toxins in bacterial infectious diseases
    • [CrossRef] [PubMed]
    • Los, F. C.; Randis, T. M.; Aroian, R. V.; Ratner, A. J. Role of pore-forming toxins in bacterial infectious diseases. Microbiol. Mol. Biol. Rev. 2013, 77, 173-207. [CrossRef] [PubMed]
    • (2013) Microbiol. Mol. Biol. Rev , vol.77 , pp. 173-207
    • Los, F.C.1    Randis, T.M.2    Aroian, R.V.3    Ratner, A.J.4
  • 44
    • 77953576191 scopus 로고    scopus 로고
    • Exocytosis of acid sphingomyelinase by wounded cells promotes endocytosis and plasma membrane repair
    • [CrossRef] [PubMed]
    • Tam, C.; Idone, V.; Devlin, C.; Fernandes, M. C.; Flannery, A.; He, X.; Schuchman, E.; Tabas, I.; Andrews, N. W. Exocytosis of acid sphingomyelinase by wounded cells promotes endocytosis and plasma membrane repair. J. Cell Biol. 2010, 189, 1027-1038. [CrossRef] [PubMed]
    • (2010) J. Cell Biol , vol.189 , pp. 1027-1038
    • Tam, C.1    Idone, V.2    Devlin, C.3    Fernandes, M.C.4    Flannery, A.5    He, X.6    Schuchman, E.7    Tabas, I.8    Andrews, N.W.9
  • 45
    • 84856787672 scopus 로고    scopus 로고
    • Toxin pores endocytosed during plasma membrane repair traffic into the lumen of MVBs for degradation
    • [CrossRef] [PubMed]
    • Corrotte, M.; Fernandes, M. C.; Tam, C.; Andrews, N. W. Toxin pores endocytosed during plasma membrane repair traffic into the lumen of MVBs for degradation. Traffic 2012, 13, 483-494. [CrossRef] [PubMed]
    • (2012) Traffic , vol.13 , pp. 483-494
    • Corrotte, M.1    Fernandes, M.C.2    Tam, C.3    Andrews, N.W.4
  • 47
    • 33845292007 scopus 로고    scopus 로고
    • Ceramide 1-phosphate/ceramide, a switch between life and death
    • [CrossRef] [PubMed]
    • Gómez-Muñoz, A. Ceramide 1-phosphate/ceramide, a switch between life and death. Biochim. Biophys. Acta 2006, 1758, 2049-2056. [CrossRef] [PubMed]
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 2049-2056
    • Gómez-Muñoz, A.1
  • 49
    • 79953252238 scopus 로고    scopus 로고
    • Exploring the role of host cell chaperones/PPIases during cellular up-take of bacterial ADP-ribosylating toxins as basis for novel pharmacological strategies to protect mammalian cells against these virulence factors
    • [CrossRef] [PubMed]
    • Barth, H. Exploring the role of host cell chaperones/PPIases during cellular up-take of bacterial ADP-ribosylating toxins as basis for novel pharmacological strategies to protect mammalian cells against these virulence factors. Naunyn-Schmiedebergs Arch. Pharmacol. 2011, 383, 237-245. [CrossRef] [PubMed]
    • (2011) Naunyn-Schmiedebergs Arch. Pharmacol , vol.383 , pp. 237-245
    • Barth, H.1
  • 50
    • 84863992806 scopus 로고    scopus 로고
    • FK506-binding protein 51 interacts with Clostridium botulinum C2 toxin and FK506 inhibits membrane translocation of the toxin in mammalian cells
    • [CrossRef] [PubMed]
    • Kaiser, E.; Böhm, N.; Ernst, K.; Langer, S.; Schwan, C.; Aktories, K.; Popoff, M.; Fischer, G.; Barth, H. FK506-binding protein 51 interacts with Clostridium botulinum C2 toxin and FK506 inhibits membrane translocation of the toxin in mammalian cells. Cell. Microbiol. 2012, 14, 1193-1205. [CrossRef] [PubMed]
    • (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    Popoff, M.7    Fischer, G.8    Barth, H.9


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