메뉴 건너뛰기




Volumn 39, Issue 4, 2012, Pages 344-351

Expression of tandem repeat cecropin B in chlamydomonas reinhardtii and its antibacterial effect

Author keywords

Antimicrobial peptide; Bait algae; Chlamydomonas reinhardtii; Tandem Cecropin B

Indexed keywords

ALGAE; BACILLUS SUBTILIS; CHLAMYDOMONAS REINHARDTII; ESCHERICHIA COLI; MICROCOCCUS LUTEUS; NEGIBACTERIA; POSIBACTERIA;

EID: 84860849674     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: 10.3724/SP.J.1206.2010.00671     Document Type: Article
Times cited : (13)

References (16)
  • 1
    • 0025818448 scopus 로고
    • Antibacterial peptides: Key components needed in immunity
    • Boman H G. Antimicrobial peptides: key components needed in immunity. Cell, 1991, 65(2): 205-207 (Pubitemid 121006052)
    • (1991) Cell , vol.65 , Issue.2 , pp. 205-207
    • Boman, H.G.1
  • 3
    • 0018820115 scopus 로고
    • Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark D, Steiner H, Rasmuson T, et al. Insect immunity: Purification and properties of three inducible proteins from hemolymph of immunized pupae of Hyalaphora cecropia. Eur J Biochem, 1980, 106(1): 7-16 (Pubitemid 10057882)
    • (1980) European Journal of Biochemistry , vol.106 , Issue.1 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 5
    • 0037183527 scopus 로고    scopus 로고
    • Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity
    • DOI 10.1021/bi0256983
    • Tachi T, Epand R F, Epand R M, et al. Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity. Biochemistry, 2002, 41(34): 10723-10731 (Pubitemid 34913333)
    • (2002) Biochemistry , vol.41 , Issue.34 , pp. 10723-10731
    • Tachi, T.1    Epand, R.F.2    Epand, R.M.3    Matsuzaki, K.4
  • 6
    • 0023750396 scopus 로고
    • In vitro cytocidal effect of novel lytic peptides on plasmodium falciparum and trypanosoma cruzi
    • Jaynes J M, Burton C A, Barr S B, et al. In vitro cytocidal effect of novel lytic peptides on plasmodium falciparum and trypanosoma cruzi. FASEB J, 1988, 2(13): 2878-2883
    • (1988) FASEB J , vol.2 , Issue.13 , pp. 2878-2883
    • Jaynes, J.M.1    Burton, C.A.2    Barr, S.B.3
  • 7
    • 0034044911 scopus 로고    scopus 로고
    • In vitro characterization of the anticancer activity of membrane-active cationic peptides. 1. Peptide-mediated cytotoxicity and peptide-enhanced cytotoxic activity of doxorubicin against wild-type and p-glycoprotein over-expressing tumor cell lines
    • Johnstone S A, Gelmon K, Mayer L D, et al. In vitro characterization of the anticancer activity of membrane-active cationic peptides. I. Peptide-mediated cytotoxicity and peptideenhanced cytotoxic activity of doxorubicin against wild-type and p-glycoprotein over-expressing tumor cell lines. Anticancer Drug Des, 2000, 15(2): 151-160 (Pubitemid 30410474)
    • (2000) Anti-Cancer Drug Design , vol.15 , Issue.2 , pp. 151-160
    • Johnstone, S.A.1    Gelmon, K.2    Mayer, L.D.3    Hancock, R.E.4    Bally, M.B.5
  • 8
    • 20444406094 scopus 로고    scopus 로고
    • Sesquin, a potent defensin-like antifungal peotide frombeans with inhibitory activities toward tumor cells and HIV-1 reverse transcriptase
    • Wong J H, Ng T B. Sesquin, a potent defensin-like antifungal peotide frombeans with inhibitory activities toward tumor cells and HIV-1 reverse transcriptase. Peptides, 2005, 26(7): 1120-1126
    • (2005) Peptides , vol.26 , Issue.7 , pp. 1120-1126
    • Wong, J.H.1    Ng, T.B.2
  • 9
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • DOI 10.1016/j.peptides.2003.08.023
    • Powers J P, Hancock R E. The relationship between peptide structure and antibacterial activity. Peptides, 2003, 24 (11): 1681-1691 (Pubitemid 38198075)
    • (2003) Peptides , vol.24 , Issue.11 , pp. 1681-1691
    • Powers, J.-P.S.1    Hancock, R.E.W.2
  • 10
    • 60649118336 scopus 로고    scopus 로고
    • Transgenic microalgae as a non-antibiotic bactericide producer to defend against bacterial pathogen infection in the fish digestive tract
    • Li S S, Tsai H J. Transgenic microalgae as a non-antibiotic bactericide producer to defend against bacterial pathogen infection in the fish digestive tract. Fish & Shellfish Immunology, 2009, 26(2): 316-325
    • (2009) Fish & Shellfish Immunology , vol.26 , Issue.2 , pp. 316-325
    • Li, S.S.1    Tsai, H.J.2
  • 11
    • 33845919888 scopus 로고    scopus 로고
    • Chlamydomonas reinhardtii: A protein expression system for pharmaceutical and biotechnological proteins
    • DOI 10.1385/MB:34:2:213, PII MB342213
    • Griesbeck C, Kobl I, Heitzer M. Chlamydomonas reinhardtii: a protein expression system for pharmaceutical and biotechnological proteins. Mol Biotechnol, 2006, 34(2): 213-223 (Pubitemid 46030395)
    • (2006) Molecular Biotechnology , vol.34 , Issue.2 , pp. 213-223
    • Griesbeck, C.1    Kobl, I.2    Heitzer, M.3
  • 12
    • 0342680049 scopus 로고    scopus 로고
    • The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas
    • DOI 10.1046/j.1365-313X.2000.00652.x
    • Schroda M, Blocker D, Beck C F. The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas. Plant J. 2000, 21(2): 121-131 (Pubitemid 30121306)
    • (2000) Plant Journal , vol.21 , Issue.2 , pp. 121-131
    • Schroda, M.1    Blocker, D.2    Beck, C.F.3
  • 13
    • 0036690768 scopus 로고    scopus 로고
    • Sequence elements within an HSP70 promoter counteract transcriptional transgene silencing in Chlamydomonas
    • DOI 10.1046/j.1365-313X.2002.01371.x
    • Schroda M, Beck C F, Vallon O. Sequence elements within an HSP70 promoter counteract transcriptional transgene silencing in Chlamydomonas. Plant J. 2002, 31(4): 445-455 (Pubitemid 34989852)
    • (2002) Plant Journal , vol.31 , Issue.4 , pp. 445-455
    • Schroda, M.1    Beck, C.F.2    Vallon, O.3
  • 15
    • 0141650651 scopus 로고    scopus 로고
    • Production of the active antifungal Pisum sativum defensin 1 (Psd1) in Pichia pastoris: Overcoming the inefficiency of the STE13 protease
    • DOI 10.1016/S1046-5928(03)00136-0
    • Cabral K M, Almeida M S, Valente A P, et al. Production of the active antifungal pisum sativum defensin I in Pichia pastoris: Overcoming the inefficiency of the STE13 protease. Protein Expression Purification, 2003, 31(1): 115-122 (Pubitemid 37207649)
    • (2003) Protein Expression and Purification , vol.31 , Issue.1 , pp. 115-122
    • Cabral, K.M.S.1    Almeida, M.S.2    Valente, A.P.3    Almeida, F.C.L.4    Kurtenbach, E.5
  • 16
    • 33646858133 scopus 로고    scopus 로고
    • Expression of the antimicrobial peptides in plants to control phytopathogenic bacteria and fungi
    • DOI 10.1007/s00299-005-0102-5
    • Oard S V, Enright F M. Expression of the antimicrobial peptides in plants to control phytopathogenic bacteria and fungi. Plant Cell Report, 2006, 25(6): 561-572 (Pubitemid 43787385)
    • (2006) Plant Cell Reports , vol.25 , Issue.6 , pp. 561-572
    • Oard, S.V.1    Enright, F.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.