메뉴 건너뛰기




Volumn 40, Issue 1, 2010, Pages 186-196

The antimicrobial activity of CCL28 is dependent on C-terminal positively-charged amino acids

Author keywords

Antimicrobial peptide; CCL28; Chemokines; Innate immunity

Indexed keywords

BETA CHEMOKINE; CHEMOKINE; CHEMOKINE CCL28; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; AMINO ACID; CCL28 PROTEIN, MOUSE;

EID: 74249102743     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.200939819     Document Type: Article
Times cited : (43)

References (49)
  • 1
    • 34247855761 scopus 로고    scopus 로고
    • Chemokine: Receptor structure, interactions, and antagonism
    • Allen, S. J., Crown, S. E. and Handel, T. M., Chemokine: receptor structure, interactions, and antagonism. Annu. Rev. Immunol. 2007. 25: 787-820.
    • (2007) Annu. Rev. Immunol , vol.25 , pp. 787-820
    • Allen, S.J.1    Crown, S.E.2    Handel, T.M.3
  • 2
    • 0030001675 scopus 로고    scopus 로고
    • Lymphocyte homing and homeostasis
    • Butcher, E. C. and Picker, L. J., Lymphocyte homing and homeostasis. Science 1996. 272: 60-66.
    • (1996) Science , vol.272 , pp. 60-66
    • Butcher, E.C.1    Picker, L.J.2
  • 3
    • 27744531173 scopus 로고    scopus 로고
    • Chemokines: Key players in innate and adaptive immunity
    • Esche, C., Stellato, C. and Beck, L. A., Chemokines: key players in innate and adaptive immunity. J. Invest. Dermatol. 2005. 125: 615-628.
    • (2005) J. Invest. Dermatol , vol.125 , pp. 615-628
    • Esche, C.1    Stellato, C.2    Beck, L.A.3
  • 4
    • 0035523289 scopus 로고    scopus 로고
    • Role of chemokines in the pathogenesis of asthma
    • Lukacs, N. W., Role of chemokines in the pathogenesis of asthma. Nat. Rev. Immunol. 2001. 1: 108-116.
    • (2001) Nat. Rev. Immunol , vol.1 , pp. 108-116
    • Lukacs, N.W.1
  • 5
    • 46249102418 scopus 로고    scopus 로고
    • The human CXC chemokine granulocyte chemotactic protein 2 (GCP-2)/CXCL6 possesses membrane-disrupting properties and is antibacterial
    • Linge, H. M., Collin, M., Nordenfelt, P., Morgelin, M., Malmsten, M. and Egesten, A., The human CXC chemokine granulocyte chemotactic protein 2 (GCP-2)/CXCL6 possesses membrane-disrupting properties and is antibacterial. Antimicrob. Agents Chemother. 2008. 52: 2599-2607.
    • (2008) Antimicrob. Agents Chemother , vol.52 , pp. 2599-2607
    • Linge, H.M.1    Collin, M.2    Nordenfelt, P.3    Morgelin, M.4    Malmsten, M.5    Egesten, A.6
  • 8
    • 0346665751 scopus 로고    scopus 로고
    • A common mucosal chemokine (mucosae-associated epithelial chemokine/CCL28) selectively attracts IgA plasmablasts
    • Lazarus, N. H., Kunkel, E. J., Johnston, B., Wilson, E., Youngman, K. R. and Butcher, E. C., A common mucosal chemokine (mucosae-associated epithelial chemokine/CCL28) selectively attracts IgA plasmablasts. J. Immunol. 2003. 170: 3799-3805.
    • (2003) J. Immunol , vol.170 , pp. 3799-3805
    • Lazarus, N.H.1    Kunkel, E.J.2    Johnston, B.3    Wilson, E.4    Youngman, K.R.5    Butcher, E.C.6
  • 9
    • 4644227215 scopus 로고    scopus 로고
    • CCL28 controls immunoglobulin (Ig)A plasma cell accumulation in the lactating mammary gland and IgA antibody transfer to the neonate
    • Wilson, E. and Butcher, E. C., CCL28 controls immunoglobulin (Ig)A plasma cell accumulation in the lactating mammary gland and IgA antibody transfer to the neonate. J. Exp. Med. 2004. 200: 805-809.
    • (2004) J. Exp. Med , vol.200 , pp. 805-809
    • Wilson, E.1    Butcher, E.C.2
  • 10
    • 0037310861 scopus 로고    scopus 로고
    • CCL28 has dual roles in mucosal immunity as a chemokine with broad-spectrum antimicrobial activity
    • Hieshima, K., Ohtani, H., Shibano, M., Izawa, D., Nakayama, T., Kawasaki, Y., Shiba, F. et al., CCL28 has dual roles in mucosal immunity as a chemokine with broad-spectrum antimicrobial activity. J. Immunol. 2003. 170: 1452-1461.
    • (2003) J. Immunol , vol.170 , pp. 1452-1461
    • Hieshima, K.1    Ohtani, H.2    Shibano, M.3    Izawa, D.4    Nakayama, T.5    Kawasaki, Y.6    Shiba, F.7
  • 11
    • 0037417311 scopus 로고    scopus 로고
    • Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin
    • Salzman, N. H., Ghosh, D., Huttner, K. M., Paterson, Y. and Bevins, C. L., Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin. Nature 2003. 422: 522-526.
    • (2003) Nature , vol.422 , pp. 522-526
    • Salzman, N.H.1    Ghosh, D.2    Huttner, K.M.3    Paterson, Y.4    Bevins, C.L.5
  • 12
    • 0033214433 scopus 로고    scopus 로고
    • Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense
    • Wilson, C. L., Ouellette, A. J., Satchell, D. P., Ayabe, T., Lopez-Boado, Y. S., Stratman, J. L., Hultgren, et al., Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense. Science 1999. 286: 113-117.
    • (1999) Science , vol.286 , pp. 113-117
    • Wilson, C.L.1    Ouellette, A.J.2    Satchell, D.P.3    Ayabe, T.4    Lopez-Boado, Y.S.5    Stratman, J.L.6    Hultgren7
  • 13
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic alpha helical antimicrobial peptides
    • Giangaspero, A., Sandri, L. and Tossi, A., Amphipathic alpha helical antimicrobial peptides. Eur. J. Biochem. 2001. 268: 5589-5600.
    • (2001) Eur. J. Biochem , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 14
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H. W., Action of antimicrobial peptides: two-state model. Biochemistry 2000. 39: 8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 15
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai, Y., Mode of action of membrane active antimicrobial peptides. Biopolymers 2002. 66: 236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 17
    • 33847298627 scopus 로고    scopus 로고
    • Studies of the biological properties of human beta-defensin 1
    • Pazgier, M., Prahl, A., Hoover, D. M. and Lubkowski, J., Studies of the biological properties of human beta-defensin 1. J. Biol. Chem. 2007. 282: 1819-1829.
    • (2007) J. Biol. Chem , vol.282 , pp. 1819-1829
    • Pazgier, M.1    Prahl, A.2    Hoover, D.M.3    Lubkowski, J.4
  • 18
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers, J. P. and Hancock, R. E., The relationship between peptide structure and antibacterial activity. Peptides 2003. 24: 1681-1691.
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 19
    • 12144289841 scopus 로고    scopus 로고
    • Structure-activity determinants in paneth cell alpha-defensins: Loss-of-function in mouse cryptdin-4 by charge-reversal at arginine residue positions
    • Tanabe, H., Qu, X., Weeks, C. S., Cummings, J. E., Kolusheva, S., Walsh, K. B., Jelinek, R. et al., Structure-activity determinants in paneth cell alpha-defensins: loss-of-function in mouse cryptdin-4 by charge-reversal at arginine residue positions. J. Biol. Chem. 2004. 279: 11976-11983.
    • (2004) J. Biol. Chem , vol.279 , pp. 11976-11983
    • Tanabe, H.1    Qu, X.2    Weeks, C.S.3    Cummings, J.E.4    Kolusheva, S.5    Walsh, K.B.6    Jelinek, R.7
  • 20
    • 39149127361 scopus 로고    scopus 로고
    • Structure-activity relationships in beta-defensin peptides
    • Taylor, K., Barran, P. E. and Dorin, J. R., Structure-activity relationships in beta-defensin peptides. Biopolymers 2008. 90: 1-7.
    • (2008) Biopolymers , vol.90 , pp. 1-7
    • Taylor, K.1    Barran, P.E.2    Dorin, J.R.3
  • 21
    • 43749116000 scopus 로고    scopus 로고
    • Analysis and separation of residues important for the chemoattractant and antimicrobial activities of beta-defensin 3
    • Taylor, K., Clarke, D. J., McCullough, B., Chin, W., Seo, E., Yang, D., Oppenheim, J. et al., Analysis and separation of residues important for the chemoattractant and antimicrobial activities of beta-defensin 3. J. Biol. Chem. 2008. 283: 6631-6639.
    • (2008) J. Biol. Chem , vol.283 , pp. 6631-6639
    • Taylor, K.1    Clarke, D.J.2    McCullough, B.3    Chin, W.4    Seo, E.5    Yang, D.6    Oppenheim, J.7
  • 22
    • 30044432598 scopus 로고    scopus 로고
    • Why is the Arg5-Glu13 salt bridge conserved in mammalian alpha-defensins?
    • Wu, Z., Li, X., de Leeuw, E., Ericksen, B. and Lu, W., Why is the Arg5-Glu13 salt bridge conserved in mammalian alpha-defensins? J. Biol. Chem. 2005. 280: 43039-43047.
    • (2005) J. Biol. Chem , vol.280 , pp. 43039-43047
    • Wu, Z.1    Li, X.2    de Leeuw, E.3    Ericksen, B.4    Lu, W.5
  • 23
    • 25444478690 scopus 로고    scopus 로고
    • Reconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids
    • Xie, C., Prahl, A., Ericksen, B., Wu, Z., Zeng, P., Li, X., Lu, W. Y. et al., Reconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids. J. Biol. Chem. 2005. 280: 32921-32929.
    • (2005) J. Biol. Chem , vol.280 , pp. 32921-32929
    • Xie, C.1    Prahl, A.2    Ericksen, B.3    Wu, Z.4    Zeng, P.5    Li, X.6    Lu, W.Y.7
  • 24
    • 34547120485 scopus 로고    scopus 로고
    • Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs
    • Zou, G., de Leeuw, E., Li, C., Pazgier, M., Li, C., Zeng, P., Lu, W. Y. et al., Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs. J. Biol. Chem. 2007. 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
  • 25
    • 7944221827 scopus 로고    scopus 로고
    • heparin-derived disaccharides allows the rational design of chemokine inhibitors
    • The X-ray structure of RANTES
    • Shaw, J. P., Johnson, Z., Borlat, F., Zwahlen, C., Kungl, A., Roulin, K., Harrenga, A. et al., The X-ray structure of RANTES: heparin-derived disaccharides allows the rational design of chemokine inhibitors. Structure 2004. 12: 2081-2093.
    • (2004) Structure , vol.12 , pp. 2081-2093
    • Shaw, J.P.1    Johnson, Z.2    Borlat, F.3    Zwahlen, C.4    Kungl, A.5    Roulin, K.6    Harrenga, A.7
  • 26
    • 0034176108 scopus 로고    scopus 로고
    • Cutting edge: The orphan chemokine receptor G protein-coupled receptor-2 (GPR-2, CCR10) binds the skinassociated chemokine CCL27 (CTACK/ALP/ILC)
    • Homey, B., Wang, W., Soto, H., Buchanan, M. E., Wiesenborn, A., Catron, D., Muller, A. et al., Cutting edge: the orphan chemokine receptor G protein-coupled receptor-2 (GPR-2, CCR10) binds the skinassociated chemokine CCL27 (CTACK/ALP/ILC). J. Immunol. 2000. 164: 3465-3470.
    • (2000) J. Immunol , vol.164 , pp. 3465-3470
    • Homey, B.1    Wang, W.2    Soto, H.3    Buchanan, M.E.4    Wiesenborn, A.5    Catron, D.6    Muller, A.7
  • 27
    • 40549102762 scopus 로고    scopus 로고
    • Human macrophage inflammatory protein 3alpha: Protein and peptide nuclear magnetic resonance solution structures, dimerization, dynamics, and anti-infective properties
    • Chan, D. I., Hunter, H. N., Tack, B. F. and Vogel, H. J., Human macrophage inflammatory protein 3alpha: protein and peptide nuclear magnetic resonance solution structures, dimerization, dynamics, and anti-infective properties. Antimicrob. Agents Chemother. 2008. 52: 883-894.
    • (2008) Antimicrob. Agents Chemother , vol.52 , pp. 883-894
    • Chan, D.I.1    Hunter, H.N.2    Tack, B.F.3    Vogel, H.J.4
  • 28
    • 0032833999 scopus 로고    scopus 로고
    • Identification of residues in the monocyte chemotactic protein-1 that contact the MCP-1 receptor, CCR2
    • Hemmerich, S., Paavola, C., Bloom, A., Bhakta, S., Freedman, R., Grunberger, D., Krstenansky, J. et al., Identification of residues in the monocyte chemotactic protein-1 that contact the MCP-1 receptor, CCR2. Biochemistry 1999. 38: 13013-13025.
    • (1999) Biochemistry , vol.38 , pp. 13013-13025
    • Hemmerich, S.1    Paavola, C.2    Bloom, A.3    Bhakta, S.4    Freedman, R.5    Grunberger, D.6    Krstenansky, J.7
  • 29
    • 0037020263 scopus 로고    scopus 로고
    • The structure of human macrophage inflammatory protein-3alpha /CCL20. Linking antimicrobial and CC chemokine receptor-6-binding activities with human beta-defensins
    • Hoover, D. M., Boulegue, C., Yang, D., Oppenheim, J. J., Tucker, K., Lu, W. and Lubkowski, J., The structure of human macrophage inflammatory protein-3alpha /CCL20. Linking antimicrobial and CC chemokine receptor-6-binding activities with human beta-defensins. J. Biol. Chem. 2002. 277: 37647-37654.
    • (2002) J. Biol. Chem , vol.277 , pp. 37647-37654
    • Hoover, D.M.1    Boulegue, C.2    Yang, D.3    Oppenheim, J.J.4    Tucker, K.5    Lu, W.6    Lubkowski, J.7
  • 30
    • 1642393757 scopus 로고    scopus 로고
    • Determinants of high-affinity binding and receptor activation in the N-terminus of CCL-19 (MIP-3 beta)
    • Ott, T. R., Lio, F. M., Olshefski, D., Liu, X. J., Struthers, R. S. and Ling, N., Determinants of high-affinity binding and receptor activation in the N-terminus of CCL-19 (MIP-3 beta). Biochemistry 2004. 43: 3670-3678.
    • (2004) Biochemistry , vol.43 , pp. 3670-3678
    • Ott, T.R.1    Lio, F.M.2    Olshefski, D.3    Liu, X.J.4    Struthers, R.S.5    Ling, N.6
  • 31
    • 34547776727 scopus 로고    scopus 로고
    • Chemokine signaling specificity: Essential role for the N-terminal domain of chemokine receptors
    • Prado, G. N., Suetomi, K., Shumate, D., Maxwell, C., Ravindran, A., Rajarathnam, K. and Navarro, J., Chemokine signaling specificity: essential role for the N-terminal domain of chemokine receptors. Biochemistry 2007. 46: 8961-8968.
    • (2007) Biochemistry , vol.46 , pp. 8961-8968
    • Prado, G.N.1    Suetomi, K.2    Shumate, D.3    Maxwell, C.4    Ravindran, A.5    Rajarathnam, K.6    Navarro, J.7
  • 32
    • 33750929921 scopus 로고    scopus 로고
    • Structural basis of chemokine receptor function - a model for binding affinity and ligand selectivity
    • Rajagopalan, L. and Rajarathnam, K., Structural basis of chemokine receptor function - a model for binding affinity and ligand selectivity. Biosci. Rep. 2006. 26: 325-339.
    • (2006) Biosci. Rep , vol.26 , pp. 325-339
    • Rajagopalan, L.1    Rajarathnam, K.2
  • 33
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M., Antimicrobial peptides of multicellular organisms. Nature 2002. 415: 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 34
    • 33745298438 scopus 로고    scopus 로고
    • Epithelial inflammation is associated with CCL28 production and the recruitment of regulatory T cells expressing CCR10
    • Eksteen, B., Miles, A., Curbishley, S. M., Tselepis, C., Grant, A. J., Walker, L. S. and Adams, D. H., Epithelial inflammation is associated with CCL28 production and the recruitment of regulatory T cells expressing CCR10. J. Immunol. 2006. 177: 593-603.
    • (2006) J. Immunol , vol.177 , pp. 593-603
    • Eksteen, B.1    Miles, A.2    Curbishley, S.M.3    Tselepis, C.4    Grant, A.J.5    Walker, L.S.6    Adams, D.H.7
  • 35
    • 46449103038 scopus 로고    scopus 로고
    • CCL28 is increased in human Helicobacter pylori-induced gastritis and mediates recruitment of gastric immunoglobulin A-secreting cells
    • Hansson, M., Hermansson, M., Svensson, H., Elfvin, A., Hansson, L. E., Johnsson, E., Sjoling, A. and Quiding-Jarbrink, M., CCL28 is increased in human Helicobacter pylori-induced gastritis and mediates recruitment of gastric immunoglobulin A-secreting cells. Infect. Immun. 2008. 76: 3304-3311.
    • (2008) Infect. Immun , vol.76 , pp. 3304-3311
    • Hansson, M.1    Hermansson, M.2    Svensson, H.3    Elfvin, A.4    Hansson, L.E.5    Johnsson, E.6    Sjoling, A.7    Quiding-Jarbrink, M.8
  • 36
    • 0030038197 scopus 로고    scopus 로고
    • Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils
    • Chertov, O., Michiel, D. F., Xu, L., Wang, J. M., Tani, K., Murphy, W. J., Longo, D. L. et al., Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils. J. Biol. Chem. 1996. 271: 2935-2940.
    • (1996) J. Biol. Chem , vol.271 , pp. 2935-2940
    • Chertov, O.1    Michiel, D.F.2    Xu, L.3    Wang, J.M.4    Tani, K.5    Murphy, W.J.6    Longo, D.L.7
  • 37
    • 0033569408 scopus 로고    scopus 로고
    • Beta-defensins: Linking innate and adaptive immunity through dendritic and T cell CCR6
    • Yang, D., Chertov, O., Bykovskaia, S. N., Chen, Q., Buffo, M. J., Shogan, J., Anderson, M. et al., Beta-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6. Science 1999. 286: 525-528.
    • (1999) Science , vol.286 , pp. 525-528
    • Yang, D.1    Chertov, O.2    Bykovskaia, S.N.3    Chen, Q.4    Buffo, M.J.5    Shogan, J.6    Anderson, M.7
  • 38
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans - as exemplified by chemokines
    • Handel, T. M., Johnson, Z., Crown, S. E., Lau, E. K. and Proudfoot, A. E., Regulation of protein function by glycosaminoglycans - as exemplified by chemokines. Annu. Rev. Biochem. 2005. 74: 385-410.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Proudfoot, A.E.5
  • 39
    • 2542498611 scopus 로고    scopus 로고
    • Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: Implications for structure and function in vivo
    • Lau, E. K., Paavola, C. D., Johnson, Z., Gaudry, J. P., Geretti, E., Borlat, F., Kungl, A. J. et al., Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: implications for structure and function in vivo. J. Biol. Chem. 2004. 279: 22294-22305.
    • (2004) J. Biol. Chem , vol.279 , pp. 22294-22305
    • Lau, E.K.1    Paavola, C.D.2    Johnson, Z.3    Gaudry, J.P.4    Geretti, E.5    Borlat, F.6    Kungl, A.J.7
  • 40
    • 0037022280 scopus 로고    scopus 로고
    • Structural diversity of heparan sulfate binding domains in chemokines
    • Lortat-Jacob, H., Grosdidier, A. and Imberty, A., Structural diversity of heparan sulfate binding domains in chemokines. Proc. Natl. Acad. Sci. USA 2002. 99: 1229-1234.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1229-1234
    • Lortat-Jacob, H.1    Grosdidier, A.2    Imberty, A.3
  • 41
    • 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., Schulz-Maronde, S., Scheid, S., Meyer, B., Forssmann, W. G. and Adermann, K., Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity. Biochemistry 2005. 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
  • 42
    • 0033564890 scopus 로고    scopus 로고
    • Disulfide bridges in interleukin-8 probed using non-natural disulfide analogues: Dissociation of roles in structure from function
    • Rajarathnam, K., Sykes, B. D., Dewald, B., Baggiolini, M. and Clark-Lewis, I., Disulfide bridges in interleukin-8 probed using non-natural disulfide analogues: dissociation of roles in structure from function. Biochemistry 1999. 38: 7653-7658.
    • (1999) Biochemistry , vol.38 , pp. 7653-7658
    • Rajarathnam, K.1    Sykes, B.D.2    Dewald, B.3    Baggiolini, M.4    Clark-Lewis, I.5
  • 43
    • 33646891071 scopus 로고    scopus 로고
    • Deletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective binding
    • Ramamoorthy, A., Thennarasu, S., Tan, A., Gottipati, K., Sreekumar, S., Heyl, D. L., An, F. Y. and Shelburne, C. E., Deletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective binding. Biochemistry 2006. 45: 6529-6540.
    • (2006) Biochemistry , vol.45 , pp. 6529-6540
    • Ramamoorthy, A.1    Thennarasu, S.2    Tan, A.3    Gottipati, K.4    Sreekumar, S.5    Heyl, D.L.6    An, F.Y.7    Shelburne, C.E.8
  • 45
    • 33847037505 scopus 로고    scopus 로고
    • Structure and mechanism of action of the antimicrobial peptide piscidin
    • Campagna, S., Saint, N., Molle, G. and Aumelas, A., Structure and mechanism of action of the antimicrobial peptide piscidin. Biochemistry 2007. 46: 1771-1778.
    • (2007) Biochemistry , vol.46 , pp. 1771-1778
    • Campagna, S.1    Saint, N.2    Molle, G.3    Aumelas, A.4
  • 46
    • 35148876147 scopus 로고    scopus 로고
    • Study of the interaction of human defensins with cell membrane models: Relationships between structure and biological activity
    • Lourenzoni, M. R., Namba, A. M., Caseli, L., Degreve, L. and Zaniquelli, M. E., Study of the interaction of human defensins with cell membrane models: relationships between structure and biological activity. J. Phys. Chem. B 2007. 111: 11318-11329.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 11318-11329
    • Lourenzoni, M.R.1    Namba, A.M.2    Caseli, L.3    Degreve, L.4    Zaniquelli, M.E.5
  • 47
    • 33750820630 scopus 로고    scopus 로고
    • Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR
    • Mani, R., Cady, S. D., Tang, M., Waring, A. J., Lehrer, R. I. and Hong, M., Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR. Proc. Natl. Acad. Sci USA 2006. 103: 16242-16247.
    • (2006) Proc. Natl. Acad. Sci USA , vol.103 , pp. 16242-16247
    • Mani, R.1    Cady, S.D.2    Tang, M.3    Waring, A.J.4    Lehrer, R.I.5    Hong, M.6
  • 48
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus
    • Schibli, D. J., Hunter, H. N., Aseyev, V., Starner, T. D., Wiencek, J. M., McCray, P. B., Jr., Tack, B. F. and Vogel, H. J., The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. J. Biol. Chem. 2002. 277: 8279-8289.
    • (2002) J. Biol. Chem , vol.277 , pp. 8279-8289
    • Schibli, D.J.1    Hunter, H.N.2    Aseyev, V.3    Starner, T.D.4    Wiencek, J.M.5    McCray Jr., P.B.6    Tack, B.F.7    Vogel, H.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.