乳链菌肽的抑菌机制

[1] Translocation of a channel-forming antimicrobial peptide,magainin2,across lipid bilayers by forming a pore. Matsuzaki K,Murase O,Fujii N et al. Biochemistry . 1995

[2] Structure-function relations of variant and fragment nisins studied with model membrane systems. Giffard CJ,Dodd HM,Horn N et al. Biochemistry . 1997

[3] Mode of action of modified and unmodified bacteriocins from gram-positive bacteria. Héchard Y,Sahl HG. Biochimie . 2002

[4] The orientation of nisin in membranes. Breukink E,Van Kraaij C,Van Dalen A et al. Biochemistry . 1998

[5] Characterization of permeability and Morphological perturbations induced by nisin on phosphatidylcholine membrances. El Jastimi R,Edwards K,Lafleur M. Biophysical Journal . 1999

[6] Structure-activity relationships in the peptide antibiotic nisin:antibacterial activity of fragments of nisin. Chan WC,Leyland ML,ClarkJ et al. FEBS Letters . 1996

[7] Specific binding of nisin to peptidoglycan precursor lipid II com-bines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. Wiedemann I,Breukink E,Van Kraaij C et al. Journal of Biological Chemistry . 2001

[8] Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin,epidermin and other lantibiotics. Br"tz H,Josten M,Wiedemann I et al. Molecular Microbiology . 1998

[9] Lantibiotics:structure,biosynthesis and mode of action. McAuliffe O,Ross RP,Hill C. FEMS Microbiology Reviews . 2001

[10] Lipid II-mediated pore formation by the peptide antibiotic nisin:a black lipid membrane study. Wiedemann I,Benz R,Sahl HG. Journal of Bacteriology . 2004

[1] Translocation of a channel-forming antimicrobial peptide,magainin2,across lipid bilayers by forming a pore. Matsuzaki K,Murase O,Fujii N et al. Biochemistry . 1995

[2] Structure-function relations of variant and fragment nisins studied with model membrane systems. Giffard CJ,Dodd HM,Horn N et al. Biochemistry . 1997

[3] Mode of action of modified and unmodified bacteriocins from gram-positive bacteria. Héchard Y,Sahl HG. Biochimie . 2002

[4] The orientation of nisin in membranes. Breukink E,Van Kraaij C,Van Dalen A et al. Biochemistry . 1998

[5] Characterization of permeability and Morphological perturbations induced by nisin on phosphatidylcholine membrances. El Jastimi R,Edwards K,Lafleur M. Biophysical Journal . 1999

[6] Structure-activity relationships in the peptide antibiotic nisin:antibacterial activity of fragments of nisin. Chan WC,Leyland ML,ClarkJ et al. FEBS Letters . 1996

[7] Specific binding of nisin to peptidoglycan precursor lipid II com-bines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. Wiedemann I,Breukink E,Van Kraaij C et al. Journal of Biological Chemistry . 2001

[8] Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin,epidermin and other lantibiotics. Br"tz H,Josten M,Wiedemann I et al. Molecular Microbiology . 1998

[9] Lantibiotics:structure,biosynthesis and mode of action. McAuliffe O,Ross RP,Hill C. FEMS Microbiology Reviews . 2001

[10] Lipid II-mediated pore formation by the peptide antibiotic nisin:a black lipid membrane study. Wiedemann I,Benz R,Sahl HG. Journal of Bacteriology . 2004