Showing results 5 to 8 of 8
Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions Park, CB; Kim, HS; Kim, Sun-Chang, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.244, no.1, pp.253 - 257, 1998-03 |
Not only the nature of peptide but also the characteristics of cell membrane determine the antimicrobial mechanism of a peptide. Liang, JF; Kim, Sun-Chang, INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS, v.53, no.5, pp.518 - 522, 1999-05 |
Structural and functional implications of a proline residue in the antimicrobial peptide gaegurin Suh, JY; Lee, YT; Park, CB; Lee, KH; Kim, Sun-Chang; Choi, BS, EUROPEAN JOURNAL OF BIOCHEMISTRY, v.266, no.2, pp.665 - 674, 1999-12 |
Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II Park, CB; Yi, Gwan-Su; Matsuzaki, K; Kim, MS; Kim, Sun-Chang, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.97, no.15, pp.8245 - 8250, 2000-07 |
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