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Volumn 50, Issue 4, 2006, Pages 1522-1524

The antimicrobial peptide polyphemusin localizes to the cytoplasm of Escherichia coli following treatment

Author keywords

[No Author keywords available]

Indexed keywords

4',6 DIAMIDINO 2 PHENYLINDOLE; BACTERIAL DNA; BIOTIN; POLYPEPTIDE ANTIBIOTIC AGENT; POLYPHEMUSIN I; TRITON X 100; UNCLASSIFIED DRUG;

EID: 33645780418     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.50.4.1522-1524.2006     Document Type: Article
Times cited : (46)

References (10)
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  • 5
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    • Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes
    • Powers, J. P., A. Tan, A. Ramamoorthy, and R. E. W. Hancock. 2005. Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes. Biochemistry 44:15504-15513.
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  • 7
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    • Wu, M., and R. E. W. Hancock. 1999. Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane. J. Biol. Chem. 274:29-35.
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  • 8
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    • Binding of tachyplesin I to DNA revealed by footprinting analysis: Significant contribution of secondary structure to DNA binding and implication for biological action
    • Yonezawa, A., J. Kuwahara, N. Fujii, and Y. Sugiura. 1992. Binding of tachyplesin I to DNA revealed by footprinting analysis: significant contribution of secondary structure to DNA binding and implication for biological action. Biochemistry 31:2998-3004.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.