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Volumn 1788, Issue 9, 2009, Pages 1797-1803

The circular bacteriocin, carnocyclin A, forms anion-selective channels in lipid bilayers

Author keywords

Antimicrobial peptide; Bacterial toxin; Ion channel; Lipid bilayer; Membrane; Pore formation

Indexed keywords

AMINO ACID; BACTERIOCIN; CARNOCYCLIN A; ION CHANNEL; SODIUM CHLORIDE; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 68749095929     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.05.008     Document Type: Article
Times cited : (50)

References (26)
  • 3
    • 33745145802 scopus 로고    scopus 로고
    • Inducing endogenous antimicrobial peptides to battle infections
    • Zasloff M. Inducing endogenous antimicrobial peptides to battle infections. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 8913-8914
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 8913-8914
    • Zasloff, M.1
  • 5
    • 33846913393 scopus 로고    scopus 로고
    • Bacteriocin diversity in Streptococcus and Enterococcus
    • Nes I.F., Diep D.B., and Holo H. Bacteriocin diversity in Streptococcus and Enterococcus. J. Bacteriol. 189 (2007) 1189-1198
    • (2007) J. Bacteriol. , vol.189 , pp. 1189-1198
    • Nes, I.F.1    Diep, D.B.2    Holo, H.3
  • 6
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: developing innate immunity for food
    • Cotter P.D., Hill C., and Ross R.P. Bacteriocins: developing innate immunity for food. Nat. Rev. Microbiol. 3 (2005) 777-788
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 7
    • 0036418802 scopus 로고    scopus 로고
    • Production of class II bacteriocins by lactic acid bacteria; an example of biological warfare and communication
    • Eijsink V.G., Axelsson L., Diep D.B., Håvarstein L.S., Holo H., and Nes I.F. Production of class II bacteriocins by lactic acid bacteria; an example of biological warfare and communication. Antonie Van Leeuwenhoek 81 (2002) 639-654
    • (2002) Antonie Van Leeuwenhoek , vol.81 , pp. 639-654
    • Eijsink, V.G.1    Axelsson, L.2    Diep, D.B.3    Håvarstein, L.S.4    Holo, H.5    Nes, I.F.6
  • 10
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • Hancock R.E., and Rozek A. Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol. Lett. 206 (2002) 143-149
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 143-149
    • Hancock, R.E.1    Rozek, A.2
  • 11
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
    • Dathe M., and Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1462 (1999) 71-87
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 13
    • 0026786899 scopus 로고
    • Collapse of the proton motive force in Listeria monocytogenes caused by a bacteriocin produced by Pediococcus acidilactici
    • Christensen D.P., and Hutkins R.W. Collapse of the proton motive force in Listeria monocytogenes caused by a bacteriocin produced by Pediococcus acidilactici. Appl. Environ. Microbiol. 58 (1992) 3312-3315
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3312-3315
    • Christensen, D.P.1    Hutkins, R.W.2
  • 16
    • 43049150421 scopus 로고    scopus 로고
    • Structure and ion channel activity of the human respiratory syncytial virus (hRSV) small hydrophobic protein transmembrane domain
    • Gan S.W., Ng L., Lin X., Gong X., and Torres J. Structure and ion channel activity of the human respiratory syncytial virus (hRSV) small hydrophobic protein transmembrane domain. Protein Sci. 17 (2008) 813-820
    • (2008) Protein Sci. , vol.17 , pp. 813-820
    • Gan, S.W.1    Ng, L.2    Lin, X.3    Gong, X.4    Torres, J.5
  • 19
    • 0027817476 scopus 로고
    • Structure and function of channel-forming peptaibols
    • Sansom M.S. Structure and function of channel-forming peptaibols. Q. Rev. Biophys. 26 (1993) 365-421
    • (1993) Q. Rev. Biophys. , vol.26 , pp. 365-421
    • Sansom, M.S.1
  • 23
    • 0026097976 scopus 로고
    • Permeation of bacterial cells, permeation of cytoplasmic and artificial membrane vesicles, and channel formation on lipid bilayers by peptide antibiotic AS-48
    • Gálvez A., Maqueda M., Martínez-Bueno M., and Valdivia E. Permeation of bacterial cells, permeation of cytoplasmic and artificial membrane vesicles, and channel formation on lipid bilayers by peptide antibiotic AS-48. J. Bacteriol. 173 (1991) 886-892
    • (1991) J. Bacteriol. , vol.173 , pp. 886-892
    • Gálvez, A.1    Maqueda, M.2    Martínez-Bueno, M.3    Valdivia, E.4
  • 24
    • 0032738115 scopus 로고    scopus 로고
    • Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin
    • Miteva M., Andersson M., Karshikoff A., and Otting G. Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin. FEBS Lett. 462 (1999) 155-158
    • (1999) FEBS Lett. , vol.462 , pp. 155-158
    • Miteva, M.1    Andersson, M.2    Karshikoff, A.3    Otting, G.4
  • 25
    • 33744812969 scopus 로고    scopus 로고
    • Disulfonic stilbene permeation and block of the anion channel from the sarcoplasmic reticulum of rabbit skeletal muscle
    • Laver D.R., and Bradley K.M. Disulfonic stilbene permeation and block of the anion channel from the sarcoplasmic reticulum of rabbit skeletal muscle. Am. J. Physiol. Cell Physiol. 290 (2006) C1666-C1677
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290
    • Laver, D.R.1    Bradley, K.M.2
  • 26
    • 0037340702 scopus 로고    scopus 로고
    • Regulation of the calcium release channel from skeletal muscle by suramin and the disulfonated stilbene derivatives DIDS, DBDS, and DNDS
    • O'Neill E.R., Sakowska M.M., and Laver D.R. Regulation of the calcium release channel from skeletal muscle by suramin and the disulfonated stilbene derivatives DIDS, DBDS, and DNDS. Biophys. J. 84 (2003) 1674-1689
    • (2003) Biophys. J. , vol.84 , pp. 1674-1689
    • O'Neill, E.R.1    Sakowska, M.M.2    Laver, D.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.