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Volumn 54, Issue 5, 2010, Pages 1922-1929

Peptide fragments of a β-defensin derivative with potent bactericidal activity

Author keywords

[No Author keywords available]

Indexed keywords

BETA DEFENSIN; DIMER; MONOMER; PEPTIDE LIBRARY;

EID: 77951216438     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01568-09     Document Type: Article
Times cited : (12)

References (24)
  • 2
    • 10344240423 scopus 로고    scopus 로고
    • Structure-activity relationships in defensin dimers: A novel link between beta-defensin tertiary structure and antimicrobial activity
    • Campopiano, D. J., D. J. Clarke, N. C. Polfer, P. E. Barran, R. J. Langley, J. R. Govan, A. Maxwell, and J. R. Dorin. 2004. Structure-activity relationships in defensin dimers: a novel link between beta-defensin tertiary structure and antimicrobial activity. J. Biol. Chem. 279:48671-48679.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48671-48679
    • Campopiano, D.J.1    Clarke, D.J.2    Polfer, N.C.3    Barran, P.E.4    Langley, R.J.5    Govan, J.R.6    Maxwell, A.7    Dorin, J.R.8
  • 3
    • 67650081577 scopus 로고    scopus 로고
    • Structure, dynamics, and activity of an all-cysteine mutated human beta defensin-3 peptide analogue
    • Chandrababu, K. B., B. Ho, and D. Yang. 2009. Structure, dynamics, and activity of an all-cysteine mutated human beta defensin-3 peptide analogue. Biochemistry 48:6052-6061.
    • (2009) Biochemistry , vol.48 , pp. 6052-6061
    • Chandrababu, K.B.1    Ho, B.2    Yang, D.3
  • 4
    • 0036297453 scopus 로고    scopus 로고
    • Structural and functional characterization of hBD-1(Ser35), a peptide deduced from a DEFB1 polymorphism
    • Circo, R., B. Skerlavaj, R. Gennaro, A. Amoroso, and M. Zanetti. 2002. Structural and functional characterization of hBD-1(Ser35), a peptide deduced from a DEFB1 polymorphism. Biochem. Biophys. Res. Commun. 293:586-592.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 586-592
    • Circo, R.1    Skerlavaj, B.2    Gennaro, R.3    Amoroso, A.4    Zanetti, M.5
  • 9
    • 22244480342 scopus 로고    scopus 로고
    • Structure-activity relation of human beta-defensin 3: Influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity
    • Kluver, E., S. Schulz-Maronde, S. Scheid, B. Meyer, W. G. Forssmann, and K. Adermann. 2005. Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity. Biochemistry 44:9804-9816.
    • (2005) Biochemistry , vol.44 , pp. 9804-9816
    • Kluver, E.1    Schulz-Maronde, S.2    Scheid, S.3    Meyer, B.4    Forssmann, W.G.5    Adermann, K.6
  • 10
    • 70350461418 scopus 로고    scopus 로고
    • Electropositive charge in alpha-defensin bactericidal activity: Functional effects of Lys-for-Arg substitutions vary with the peptide primary structure
    • Llenado, R. A., C. S. Weeks, M. J. Cocco, and A. J. Ouellette. 2009. Electropositive charge in alpha-defensin bactericidal activity: functional effects of Lys-for-Arg substitutions vary with the peptide primary structure. Infect. Immun. 77:5035-5043.
    • (2009) Infect. Immun. , vol.77 , pp. 5035-5043
    • Llenado, R.A.1    Weeks, C.S.2    Cocco, M.J.3    Ouellette, A.J.4
  • 12
    • 37249076371 scopus 로고    scopus 로고
    • Evaluation of the inhibitory effects of human serum components on bactericidal activity of human beta defensin 3
    • Maisetta, G., L. M. Di, S. Esin, W. Florio, F. L. Brancatisano, D. Bottai, M. Campa, and G. Batoni. 2008. Evaluation of the inhibitory effects of human serum components on bactericidal activity of human beta defensin 3. Peptides 29:1-6.
    • (2008) Peptides , vol.29 , pp. 1-6
    • Maisetta, G.1    Di, L.M.2    Esin, S.3    Florio, W.4    Brancatisano, F.L.5    Bottai, D.6    Campa, M.7    Batoni, G.8
  • 15
    • 33847298627 scopus 로고    scopus 로고
    • Studies of the biological properties of human beta-defensin 1
    • Pazgier, M., A. Prahl, D. M. Hoover, and J. Lubkowski. 2007. Studies of the biological properties of human beta-defensin 1. J. Biol. Chem. 282:1819-1829.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1819-1829
    • Pazgier, M.1    Prahl, A.2    Hoover, D.M.3    Lubkowski, J.4
  • 16
    • 41949115565 scopus 로고    scopus 로고
    • Identification and biological characterization of mouse beta-defensin 14, the orthologue of human beta-defensin 3
    • Rohrl, J., D. Yang, J. J. Oppenheim, and T. Hehlgans. 2008. Identification and biological characterization of mouse beta-defensin 14, the orthologue of human beta-defensin 3. J. Biol. Chem. 283:5414-5419.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5414-5419
    • Rohrl, J.1    Yang, D.2    Oppenheim, J.J.3    Hehlgans, T.4
  • 17
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus
    • Schibli, D. J., H. N. Hunter, V. Aseyev, T. D. Starner, J. M. Wiencek, P. B. McCray, Jr., B. F. Tack, and H. J. Vogel. 2002. The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. J. Biol. Chem. 277: 8279-8289.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8279-8289
    • Schibli, D.J.1    Hunter, H.N.2    Aseyev, V.3    Starner, T.D.4    Wiencek, J.M.5    McCray Jr., P.B.6    Tack, B.F.7    Vogel, H.J.8
  • 22
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and S. H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.