메뉴 건너뛰기




Volumn 53, Issue 1, 2009, Pages 256-260

Antifungal activities of human beta-defensins HBD-1 to HBD-3 and their C-terminal analogs Phd1 to Phd3

Author keywords

[No Author keywords available]

Indexed keywords

BETA DEFENSIN; BETA DEFENSIN 1; BETA DEFENSIN 2; BETA DEFENSIN 3; PROTEIN PHD1; PROTEIN PHD2; PROTEIN PHD3; UNCLASSIFIED DRUG;

EID: 59749096989     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00470-08     Document Type: Article
Times cited : (85)

References (36)
  • 2
    • 0032169557 scopus 로고    scopus 로고
    • Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung
    • Bals, R., X. Wang, Z. Wu, T. Freeman, V. Bafna, M. Zasloff, and J. M. Wilson. 1998. Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung. J. Clin. Investig. 102:874-880.
    • (1998) J. Clin. Investig , vol.102 , pp. 874-880
    • Bals, R.1    Wang, X.2    Wu, Z.3    Freeman, T.4    Bafna, V.5    Zasloff, M.6    Wilson, J.M.7
  • 3
    • 33749525670 scopus 로고    scopus 로고
    • Human beta-defensin-3: A promising antimicrobial peptide
    • Batoni, G., G. Maisetta, S. Esin, and M. Campa. 2006. Human beta-defensin-3: a promising antimicrobial peptide. Mini Rev. Med. Chem. 6:1063-1073.
    • (2006) Mini Rev. Med. Chem , vol.6 , pp. 1063-1073
    • Batoni, G.1    Maisetta, G.2    Esin, S.3    Campa, M.4
  • 6
    • 0034929327 scopus 로고    scopus 로고
    • Defensin antimicrobial peptide in the oral cavity
    • Dale, B. A., and S. Krisanaprakornkit. 2001. Defensin antimicrobial peptide in the oral cavity. J. Oral Pathol. Med. 30:321-327.
    • (2001) J. Oral Pathol. Med , vol.30 , pp. 321-327
    • Dale, B.A.1    Krisanaprakornkit, S.2
  • 8
    • 3242778563 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of vertebrates
    • Ganz, T. 2004. Defensins: antimicrobial peptides of vertebrates. C. R. Biol. 327:539-549.
    • (2004) C. R. Biol , vol.327 , pp. 539-549
    • Ganz, T.1
  • 9
    • 0030949875 scopus 로고    scopus 로고
    • Human β-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • Goldman, M. J., G. M. Anderson, E. D. Stolzenberg, U. P. Kari, M. Zasloff, and J. M. Wilson. 1997. Human β-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88:553-560.
    • (1997) Cell , vol.88 , pp. 553-560
    • Goldman, M.J.1    Anderson, G.M.2    Stolzenberg, E.D.3    Kari, U.P.4    Zasloff, M.5    Wilson, J.M.6
  • 11
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic
    • Harder, J., J. Bartels, E. Christophers, and J. M. Schröder. 2001. Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic. J. Biol. Chem. 276:5707-5713.
    • (2001) J. Biol. Chem , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schröder, J.M.4
  • 13
    • 33645820597 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of β-defensins, multi-functional peptides of the immune system
    • Kluver, E., K. Adermann, and A. Schulz. 2006. Synthesis and structure-activity relationship of β-defensins, multi-functional peptides of the immune system. J. Pept. Sci. 12:243-257.
    • (2006) J. Pept. Sci , vol.12 , pp. 243-257
    • Kluver, E.1    Adermann, K.2    Schulz, A.3
  • 14
    • 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
  • 15
    • 0042072743 scopus 로고    scopus 로고
    • Single disulfide and linear analogues corresponding to the carboxy-terminal segment of bovine β-defensin-2: Effects of introducing the beta hairpin nucleating sequence D-Pro-Gly on antibacterial activity and biophysical properties
    • Krishnakumari, V., A. Sharadadevi, S. Singh, and R. Nagaraj. 2003. Single disulfide and linear analogues corresponding to the carboxy-terminal segment of bovine β-defensin-2: effects of introducing the beta hairpin nucleating sequence D-Pro-Gly on antibacterial activity and biophysical properties. Biochemistry 42:9307-9315.
    • (2003) Biochemistry , vol.42 , pp. 9307-9315
    • Krishnakumari, V.1    Sharadadevi, A.2    Singh, S.3    Nagaraj, R.4
  • 16
    • 33750083071 scopus 로고    scopus 로고
    • Antibacterial activities of synthetic peptides corresponding to the carboxy-terminal region of human beta-defensins 1-3
    • Krishnakumari, V., S. Singh, and R. Nagaraj. 2006. Antibacterial activities of synthetic peptides corresponding to the carboxy-terminal region of human beta-defensins 1-3. Peptides 27:2607-2613.
    • (2006) Peptides , vol.27 , pp. 2607-2613
    • Krishnakumari, V.1    Singh, S.2    Nagaraj, R.3
  • 17
    • 4444246692 scopus 로고    scopus 로고
    • Primate defensins
    • Lehrer, R. I. 2004. Primate defensins. Nat. Rev. Microbiol. 2:727-738.
    • (2004) Nat. Rev. Microbiol , vol.2 , pp. 727-738
    • Lehrer, R.I.1
  • 18
    • 0036467390 scopus 로고    scopus 로고
    • Defensins of vertebrate animals
    • Lehrer, R. I., and T. Ganz. 2002. Defensins of vertebrate animals. Curr. Opin. Immunol. 14:96-102.
    • (2002) Curr. Opin. Immunol , vol.14 , pp. 96-102
    • Lehrer, R.I.1    Ganz, T.2
  • 19
    • 0023945703 scopus 로고
    • Modulation of the in vitro candidacidal activity of human neutrophil defensins by target cell metabolism and divalent cations
    • Lehrer, R. I., T. Ganz, D. Szklarek, and M. E. Selsted. 1988. Modulation of the in vitro candidacidal activity of human neutrophil defensins by target cell metabolism and divalent cations. J. Clin. Investig. 81:1829-1835.
    • (1988) J. Clin. Investig , vol.81 , pp. 1829-1835
    • Lehrer, R.I.1    Ganz, T.2    Szklarek, D.3    Selsted, M.E.4
  • 21
    • 0036171208 scopus 로고    scopus 로고
    • Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs: Structural and disulfide bridge requirements for activity
    • Mandal, M., M. V. Jagannadham, and R. Nagaraj. 2002. Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs: structural and disulfide bridge requirements for activity. Peptides 23:413-418.
    • (2002) Peptides , vol.23 , pp. 413-418
    • Mandal, M.1    Jagannadham, M.V.2    Nagaraj, R.3
  • 22
    • 0036196119 scopus 로고    scopus 로고
    • Antibacterial activities and conformations of synthetic alpha-defensin HNP-1 and analogs with one, two and three disulfide bridges
    • Mandal, M., and R. Nagaraj. 2002. Antibacterial activities and conformations of synthetic alpha-defensin HNP-1 and analogs with one, two and three disulfide bridges. J. Pept. Res. 59:95-104.
    • (2002) J. Pept. Res , vol.59 , pp. 95-104
    • Mandal, M.1    Nagaraj, R.2
  • 23
    • 0344483901 scopus 로고    scopus 로고
    • Mathews, M., H. P. Jia, J. M. Guthmiller, G. Losh, S. Graham, G. K. Johnson, B. F. Tack, and P. B. McCray, Jr. 1999. Production of beta-defensin antimicrobial peptides by the oral mucosa and salivary glands. Infect. Immun. 67:2740-2745.
    • Mathews, M., H. P. Jia, J. M. Guthmiller, G. Losh, S. Graham, G. K. Johnson, B. F. Tack, and P. B. McCray, Jr. 1999. Production of beta-defensin antimicrobial peptides by the oral mucosa and salivary glands. Infect. Immun. 67:2740-2745.
  • 24
    • 0142218765 scopus 로고    scopus 로고
    • Roles of antimicrobial peptides such as defensins in innate and adaptive immunity
    • Oppenheim, J. J., A. Biragyn, L. W. Kwak, and D. Yang. 2003. Roles of antimicrobial peptides such as defensins in innate and adaptive immunity. Ann. Rheum. Dis. 62:17-21.
    • (2003) Ann. Rheum. Dis , vol.62 , pp. 17-21
    • Oppenheim, J.J.1    Biragyn, A.2    Kwak, L.W.3    Yang, D.4
  • 26
    • 36248983841 scopus 로고    scopus 로고
    • Human defensins: Synthesis and structural properties
    • Pazgier, M., X. Li, W. Lu, and J. Lubkowski. 2007. Human defensins: synthesis and structural properties. Curr. Pharm. Des. 13:3096-3118.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 3096-3118
    • Pazgier, M.1    Li, X.2    Lu, W.3    Lubkowski, J.4
  • 27
    • 0034441731 scopus 로고    scopus 로고
    • Expression of the antimicrobial peptide, human beta-defensin-1, in duct cells of minor salivary glands and detection in saliva
    • Sahasrabudhe, K. S., J. R. Kimball, T. H. Morton, A. Weinberg, and B. A. Dale. 2000. Expression of the antimicrobial peptide, human beta-defensin-1, in duct cells of minor salivary glands and detection in saliva. J. Dent. Res. 79:1669-1674.
    • (2000) J. Dent. Res , vol.79 , pp. 1669-1674
    • Sahasrabudhe, K.S.1    Kimball, J.R.2    Morton, T.H.3    Weinberg, A.4    Dale, B.A.5
  • 30
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • Selsted, M., and A. J. Ouellette. 2005. Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 6:551-557.
    • (2005) Nat. Immunol , vol.6 , pp. 551-557
    • Selsted, M.1    Ouellette, A.J.2
  • 31
    • 0032751756 scopus 로고    scopus 로고
    • Permeabilization of fungal membranes by plant defensins inhibits fungal growth
    • Thevissen, K., F. R. Terras, and W. F. Broekaert. 1999. Permeabilization of fungal membranes by plant defensins inhibits fungal growth. Appl. Environ. Microbiol. 65:5451-5458.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 5451-5458
    • Thevissen, K.1    Terras, F.R.2    Broekaert, W.F.3
  • 32
    • 27644584146 scopus 로고    scopus 로고
    • Antibacterial activity of human neutrophil defensin HNP-1 analogs without cysteines
    • Varkey, J., and R. Nagaraj. 2005. Antibacterial activity of human neutrophil defensin HNP-1 analogs without cysteines. Antimicrob. Agents Chemother. 49:4561-4566.
    • (2005) Antimicrob. Agents Chemother , vol.49 , pp. 4561-4566
    • Varkey, J.1    Nagaraj, R.2
  • 33
    • 33845968880 scopus 로고    scopus 로고
    • Human beta-defensins kill Candida albicans in an energy-dependent and salt-sensitive manner without causing membrane disruption
    • Vylkova, S., N. Nayyar, W. Li, and M. Edgerton. 2007. Human beta-defensins kill Candida albicans in an energy-dependent and salt-sensitive manner without causing membrane disruption. Antimicrob. Agents Chemother. 51:154-161.
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 154-161
    • Vylkova, S.1    Nayyar, N.2    Li, W.3    Edgerton, M.4
  • 36
    • 34547120485 scopus 로고    scopus 로고
    • Toward understanding the cationicity of defensins: Arg and Lys versus their noncoded analogs
    • Zou, G., E. de Leeuw, C. Li, M. Pazgier, C. Li, P. Zeng, W.-Y. Lu, J. Lubkowski, and W. Lu. 2007. Toward understanding the cationicity of defensins: Arg and Lys versus their noncoded analogs. J. Biol. Chem. 282:19653-19665.
    • (2007) J. Biol. Chem , vol.282 , pp. 19653-19665
    • Zou, G.1    de Leeuw, E.2    Li, C.3    Pazgier, M.4    Li, C.5    Zeng, P.6    Lu, W.-Y.7    Lubkowski, J.8    Lu, W.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.