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Volumn 4, Issue 7, 1998, Pages 413-425

Microscopic observations of the different morphological changes caused by anti-bacterial peptides on Klebsiella pneumoniae and HL-60 leukemia cells

Author keywords

Anti bacterial; Cecropins; Modes of action; Morphology

Indexed keywords

BACTERIA (MICROORGANISMS); KLEBSIELLA PNEUMONIAE;

EID: 0032200757     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1387(199811)4:7<413::AID-PSC160>3.0.CO;2-W     Document Type: Article
Times cited : (50)

References (29)
  • 1
    • 0019386682 scopus 로고
    • Sequence and specificity of 2 anti-bacterial proteins involved in insect immunity
    • H. Steiner, H. Bennich, H.G. Boman, A. Engstrom and D. Hultmark (1981). Sequence and specificity of 2 anti-bacterial proteins involved in insect immunity. Nature 292, 246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Bennich, H.2    Boman, H.G.3    Engstrom, A.4    Hultmark, D.5
  • 2
    • 0025818448 scopus 로고
    • Antibacterial peptides: Key components needed in immunity
    • H.G. Boman (1991). Antibacterial peptides: key components needed in immunity. Cell 65, 205-207.
    • (1991) Cell , vol.65 , pp. 205-207
    • Boman, H.G.1
  • 3
    • 0027318549 scopus 로고
    • Immune-reactions in Drosophila and other insects - A model for innate immunity
    • D. Hultmark (1993). Immune-reactions in Drosophila and other insects - a model for innate immunity. Trends Genet. 9, 178-183.
    • (1993) Trends Genet. , vol.9 , pp. 178-183
    • Hultmark, D.1
  • 5
    • 0020366780 scopus 로고
    • Insect immunity: Isolation and structure of cecropin D and four minor antibacterial components from cecropia pupae
    • D. Hultmark, A. Engstrom, H. Bennich, R. Kapur and H.G. Boman (1982). Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from cecropia pupae. Eur. J. Biochem. 127, 207-217.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 207-217
    • Hultmark, D.1    Engstrom, A.2    Bennich, H.3    Kapur, R.4    Boman, H.G.5
  • 6
    • 0028805651 scopus 로고
    • Extraction of the synthetic lytic peptide, cecropin B, from biological fluid and analysis using reversed-phase high performance liquid chromatography
    • A.J. Moore, P.M. Loadman, D.A. Devine and M.C. Bibby (1995). Extraction of the synthetic lytic peptide, cecropin B, from biological fluid and analysis using reversed-phase high performance liquid chromatography. J. Chromatgr. B 672, 225-231.
    • (1995) J. Chromatgr. B , vol.672 , pp. 225-231
    • Moore, A.J.1    Loadman, P.M.2    Devine, D.A.3    Bibby, M.C.4
  • 7
    • 0020395778 scopus 로고
    • Synthesis of the antibacterial peptide cecropin A (1-33)
    • R.B. Merrifield, H.G. Boman and L.D. Vizioli (1982). Synthesis of the antibacterial peptide cecropin A (1-33). Biochemistry 21, 5020-5031.
    • (1982) Biochemistry , vol.21 , pp. 5020-5031
    • Merrifield, R.B.1    Boman, H.G.2    Vizioli, L.D.3
  • 11
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • H.G. Boman (1995). Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13, 61-92.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 12
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • C.E. Dempsy (1990). The actions of melittin on membranes. Biochim. Biophys. Acta 1031, 143-161.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsy, C.E.1
  • 13
    • 0025935264 scopus 로고
    • The biophysics of peptide models of ion channels
    • M.S.P. Sansom (1991). The biophysics of peptide models of ion channels. Prog. Biophys. Mol. Biol. 55, 139-235.
    • (1991) Prog. Biophys. Mol. Biol. , vol.55 , pp. 139-235
    • Sansom, M.S.P.1
  • 14
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin - Isolation, characterization of 2 active forms, and partial cDNA sequence of a precursor
    • M. Zasloff (1987). Magainins, a class of antimicrobial peptides from Xenopus skin - isolation, characterization of 2 active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 84, 5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 16
    • 0028504387 scopus 로고
    • Preliminary experimental anticancer activity of cecropins
    • A.J. Moore, D.A. Devine and M.C. Bibby (1994). Preliminary experimental anticancer activity of cecropins. Peptide Res. 7, 65-269.
    • (1994) Peptide Res. , vol.7 , pp. 65-269
    • Moore, A.J.1    Devine, D.A.2    Bibby, M.C.3
  • 17
    • 0030746525 scopus 로고    scopus 로고
    • Effects of the anti-bacterial peptide cecropin B and its analogs cecropin B-1 and B-2, on liposomes, bacteria and cancer cells
    • H.M. Chen, W. Wang, D. Smith and S.C. Chan (1997). Effects of the anti-bacterial peptide cecropin B and its analogs cecropin B-1 and B-2, on liposomes, bacteria and cancer cells. Biochim. Biophys. Acta 1336, 171-179.
    • (1997) Biochim. Biophys. Acta , vol.1336 , pp. 171-179
    • Chen, H.M.1    Wang, W.2    Smith, D.3    Chan, S.C.4
  • 18
    • 0004099105 scopus 로고
    • ACS Professional Reference Book, American Chemical Society, Washington, DC
    • W.O. Foye: Cancer Chemotherapeutic Agents, ACS Professional Reference Book, American Chemical Society, Washington, DC 1995.
    • (1995) Cancer Chemotherapeutic Agents
    • Foye, W.O.1
  • 19
    • 0028275743 scopus 로고
    • Induction of cecropin-like and attacin-like antibacterial but not antiviral activity in heliothis virescens larvae
    • D.D. Ourth, T.D. Lockey and H.E. Renis (1994). Induction of cecropin-like and attacin-like antibacterial but not antiviral activity in heliothis virescens larvae. Biochem. Biophys. Res. Commun. 200, 35-44.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 35-44
    • Ourth, D.D.1    Lockey, T.D.2    Renis, H.E.3
  • 20
    • 0024841875 scopus 로고
    • Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids
    • H.G. Boman, D. Wade, I.A. Boman, B. Wahlin and R.B. Merrifield (1989). Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids. FEBS Lett. 259, 103-106.
    • (1989) FEBS Lett. , vol.259 , pp. 103-106
    • Boman, H.G.1    Wade, D.2    Boman, I.A.3    Wahlin, B.4    Merrifield, R.B.5
  • 21
    • 0028800158 scopus 로고
    • The morphological effects of two antimicrobial peptides, hecate-1 and melittin, on Escherichia coli
    • W.G. Henk, W.J. Todd, F.M. Enright and P.S. Mitchell (1995). The morphological effects of two antimicrobial peptides, hecate-1 and melittin, on Escherichia coli. Scanning Microsc. 9, 510-507.
    • (1995) Scanning Microsc. , vol.9 , pp. 510-1507
    • Henk, W.G.1    Todd, W.J.2    Enright, F.M.3    Mitchell, P.S.4
  • 22
    • 0030007916 scopus 로고    scopus 로고
    • Formation of pores in Escherichia cold cell membranes by a cecropin isolated from hemolymph of heliothis virescens larvae
    • T.D. Lockey and D.D. Ourth (1996). Formation of pores in Escherichia cold cell membranes by a cecropin isolated from hemolymph of heliothis virescens larvae. Eur. J. Biochem. 236, 263-271.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 263-271
    • Lockey, T.D.1    Ourth, D.D.2
  • 23
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • B. Christensen, J. Fink, R.B. Merrifield and D. Mauzerall (1988). Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Natl. Acad. Sci. USA 85, 5072-5076.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 24
    • 0029115961 scopus 로고
    • Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A
    • M. Oblatt-Montal, M. Yamazaki, R. Nelson and M. Montal (1995). Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A. Protein Sci. 4, 1490-1497.
    • (1995) Protein Sci. , vol.4 , pp. 1490-1497
    • Oblatt-Montal, M.1    Yamazaki, M.2    Nelson, R.3    Montal, M.4
  • 25
    • 0019904731 scopus 로고
    • Comparative lipid analysis of purified plasma membranes and shed extracellular membrane vesicles from normal murine thymocytes and leukemic GRSL cells
    • W.J. Van Blitterswijk, G. De Veer, J.H. Krol and P. Emmelot (1982). Comparative lipid analysis of purified plasma membranes and shed extracellular membrane vesicles from normal murine thymocytes and leukemic GRSL cells. Biochim. Biophys. Acta 688, 495-504.
    • (1982) Biochim. Biophys. Acta , vol.688 , pp. 495-504
    • Van Blitterswijk, W.J.1    De Veer, G.2    Krol, J.H.3    Emmelot, P.4
  • 26
    • 0029765758 scopus 로고    scopus 로고
    • Release of lipid vesicle contents by an antibacterial cecropin A-melittin hybrid peptide
    • J.M. Mancheno, M. Onaderra, A.M. Delpozo, P. Diaz-Achirica and D. Andreu (1996). Release of lipid vesicle contents by an antibacterial cecropin A-melittin hybrid peptide. Biochemistry 35, 9892-9899.
    • (1996) Biochemistry , vol.35 , pp. 9892-9899
    • Mancheno, J.M.1    Onaderra, M.2    Delpozo, A.M.3    Diaz-Achirica, P.4    Andreu, D.5
  • 27
    • 0027288625 scopus 로고
    • Electric potentiation, cooperativity and synergism of magainin peptide in protein-free liposomes
    • A.V. Gomes, A. Dewaal, J.A. Berden and H.V. Westerhoff (1993). Electric potentiation, cooperativity and synergism of magainin peptide in protein-free liposomes. Biochemistry 32, 5356-5372.
    • (1993) Biochemistry , vol.32 , pp. 5356-5372
    • Gomes, A.V.1    Dewaal, A.2    Berden, J.A.3    Westerhoff, H.V.4
  • 28
    • 0030886178 scopus 로고
    • The concentration-dependent membrane activity of cecropin A
    • L. Silvestro, K. Gupta, J.N. Weiser and P.H. Axelsen (1993). The concentration-dependent membrane activity of cecropin A. Biochemistry 36, 11452-11460.
    • (1993) Biochemistry , vol.36 , pp. 11452-11460
    • Silvestro, L.1    Gupta, K.2    Weiser, J.N.3    Axelsen, P.H.4
  • 29
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogs with phospholipid-membranes
    • Y. Pouny, D. Rapaport, A. Mor, P. Nicolas and Y. Shai (1992). Interaction of antimicrobial dermaseptin and its fluorescently labeled analogs with phospholipid-membranes. Biochemistry 31, 12416-12423.
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.