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Volumn 51, Issue 2, 2007, Pages 141-146

Recombinant expression, isotope labeling, refolding, and purification of an antimicrobial peptide, piscidin

Author keywords

Antimicrobial peptide; NMR; Piscidin; Recombinant

Indexed keywords

ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; FISH PROTEIN; HYBRID PROTEIN; MORONECIDIN PROTEIN, MORONE SAXATILIS; NITROGEN;

EID: 33751426612     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.07.010     Document Type: Article
Times cited : (40)

References (14)
  • 1
    • 0025818448 scopus 로고
    • Antibacterial peptides: key components needed in immunity
    • Boman H.G. Antibacterial peptides: key components needed in immunity. Cell 65 (1991) 205-207
    • (1991) Cell , vol.65 , pp. 205-207
    • Boman, H.G.1
  • 2
    • 0026511839 scopus 로고
    • Antibiotic peptides as mediators of innate immunity
    • Zasloff M. Antibiotic peptides as mediators of innate immunity. Curr. Opin. Immunol. 4 (1992) 3-7
    • (1992) Curr. Opin. Immunol. , vol.4 , pp. 3-7
    • Zasloff, M.1
  • 3
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman H.G. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13 (1995) 61-92
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 4
    • 0028920870 scopus 로고
    • Structure-activity studies on magainins and other host defense peptides
    • Maloy W.L., and Kari U.P. Structure-activity studies on magainins and other host defense peptides. Biopolymers 37 (1995) 105-122
    • (1995) Biopolymers , vol.37 , pp. 105-122
    • Maloy, W.L.1    Kari, U.P.2
  • 5
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: a new source of antibiotics
    • Hancock R.E., and Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16 (1998) 82-88
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 6
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic alpha-helical antimicrobial peptides
    • Oren Z., and Shai Y. Mode of action of linear amphipathic alpha-helical antimicrobial peptides. Biopolymers 47 (1998) 451-463
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 8
    • 0033168860 scopus 로고    scopus 로고
    • Antibiotic peptides from higher eukaryotes: biology and applications
    • Ganz T., and Lehrer R.I. Antibiotic peptides from higher eukaryotes: biology and applications. Mol. Med. Today 5 (1999) 292-297
    • (1999) Mol. Med. Today , vol.5 , pp. 292-297
    • Ganz, T.1    Lehrer, R.I.2
  • 9
    • 0035890996 scopus 로고    scopus 로고
    • Peptide antibiotics in mast cells of fish
    • Silphaduang U., and Noga E.J. Peptide antibiotics in mast cells of fish. Nature 414 (2002) 268-269
    • (2002) Nature , vol.414 , pp. 268-269
    • Silphaduang, U.1    Noga, E.J.2
  • 10
    • 0037388453 scopus 로고    scopus 로고
    • Comparison of the conformation and electrostatic surface properties of magainin peptides bound to sodium dodecyl sulfate and dodecylphosphocholine micelles
    • Hicks R.P., Mones E., Kim H., Koser B.W., Nichols D.A., and Bhattacharjee A.K. Comparison of the conformation and electrostatic surface properties of magainin peptides bound to sodium dodecyl sulfate and dodecylphosphocholine micelles. Biopolymers 68 (2003) 459-470
    • (2003) Biopolymers , vol.68 , pp. 459-470
    • Hicks, R.P.1    Mones, E.2    Kim, H.3    Koser, B.W.4    Nichols, D.A.5    Bhattacharjee, A.K.6
  • 11
    • 0018795594 scopus 로고
    • Lipid-protein interactions: NMR study of melittin and its binding to lysophosphatidylcholine
    • De Bony J., Dufourcq J., and Clin B. Lipid-protein interactions: NMR study of melittin and its binding to lysophosphatidylcholine. Biochim. Biophys. Acta 552 (1979) 531-534
    • (1979) Biochim. Biophys. Acta , vol.552 , pp. 531-534
    • De Bony, J.1    Dufourcq, J.2    Clin, B.3
  • 14
    • 1642287434 scopus 로고    scopus 로고
    • Prevention of aggregation after refolding by balanced stabilization-destabilization: production of the Arabidopsis thaliana protein APG8a (At4g21980) for NMR structure determination
    • Chae Y.K., Im H., Zhao Q., Doelling J.H., Vierstra R.D., and Markley J.L. Prevention of aggregation after refolding by balanced stabilization-destabilization: production of the Arabidopsis thaliana protein APG8a (At4g21980) for NMR structure determination. Protein. Expr. Purif. 34 (2005) 280-283
    • (2005) Protein. Expr. Purif. , vol.34 , pp. 280-283
    • Chae, Y.K.1    Im, H.2    Zhao, Q.3    Doelling, J.H.4    Vierstra, R.D.5    Markley, J.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.