메뉴 건너뛰기




Volumn 31, Issue 12, 2007, Pages 1278-1296

Canine cathelicidin (K9CATH): Gene cloning, expression, and biochemical activity of a novel pro-myeloid antimicrobial peptide

Author keywords

Antimicrobial peptide; Carnivore; Cathelicidin; Dog; Gene

Indexed keywords

CATHELICIDIN; K9CATH; LIPOPOLYSACCHARIDE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 35648949904     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2007.03.007     Document Type: Article
Times cited : (58)

References (64)
  • 1
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. J Leukoc Biol 75 (2004) 39-48
    • (2004) J Leukoc Biol , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 2
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: basic facts and emerging concepts
    • Boman H.G. Antibacterial peptides: basic facts and emerging concepts. J Intern Med 254 (2003) 197-215
    • (2003) J Intern Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 3
    • 13844322065 scopus 로고    scopus 로고
    • The cathelicidins-structure, function and evolution
    • Tomasinsig L., and Zanetti M. The cathelicidins-structure, function and evolution. Curr Protein Pept Sci 6 (2005) 23-34
    • (2005) Curr Protein Pept Sci , vol.6 , pp. 23-34
    • Tomasinsig, L.1    Zanetti, M.2
  • 4
    • 0036379140 scopus 로고    scopus 로고
    • Cathelicidins, essential gene-encoded mammalian antibiotics
    • Zaiou M., and Gallo R. Cathelicidins, essential gene-encoded mammalian antibiotics. J Mol Med 80 (2002) 549-561
    • (2002) J Mol Med , vol.80 , pp. 549-561
    • Zaiou, M.1    Gallo, R.2
  • 5
    • 0038364156 scopus 로고    scopus 로고
    • Cathelicidins-a family of multifunctional antimicrobial peptides
    • Bals R., and Wilson J.M. Cathelicidins-a family of multifunctional antimicrobial peptides. Cell Mol Life Sci 60 (2003) 711-720
    • (2003) Cell Mol Life Sci , vol.60 , pp. 711-720
    • Bals, R.1    Wilson, J.M.2
  • 6
    • 0027472180 scopus 로고
    • The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics
    • Zanetti M., Del Sal G., Storici P., et al. The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics. J Biol Chem 268 (1993) 522-526
    • (1993) J Biol Chem , vol.268 , pp. 522-526
    • Zanetti, M.1    Del Sal, G.2    Storici, P.3
  • 7
    • 0037960231 scopus 로고    scopus 로고
    • Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence
    • Zaiou M., Nizet V., and Gallo R.L. Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence. J Invest Dermatol 120 (2003) 810-816
    • (2003) J Invest Dermatol , vol.120 , pp. 810-816
    • Zaiou, M.1    Nizet, V.2    Gallo, R.L.3
  • 8
    • 0034332193 scopus 로고    scopus 로고
    • The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations
    • Agerberth B., Charo J., Werr J., et al. The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations. Blood 96 (2000) 3086-3093
    • (2000) Blood , vol.96 , pp. 3086-3093
    • Agerberth, B.1    Charo, J.2    Werr, J.3
  • 9
    • 0028087018 scopus 로고
    • A novel granulocyte-derived peptide with lipopolysaccharide-neutralizing activity
    • Larrick J.W., Hirata M., Zheng H., et al. A novel granulocyte-derived peptide with lipopolysaccharide-neutralizing activity. J Immunol 152 (1994) 231-240
    • (1994) J Immunol , vol.152 , pp. 231-240
    • Larrick, J.W.1    Hirata, M.2    Zheng, H.3
  • 10
    • 0142200897 scopus 로고    scopus 로고
    • Epithelial cell-derived antibacterial peptides human beta-defensins and cathelicidin: multifunctional activities on mast cells
    • Niyonsaba F., Hirata M., Ogawa H., et al. Epithelial cell-derived antibacterial peptides human beta-defensins and cathelicidin: multifunctional activities on mast cells. Curr Drug Targets Inflamm Allergy 2 (2003) 224-231
    • (2003) Curr Drug Targets Inflamm Allergy , vol.2 , pp. 224-231
    • Niyonsaba, F.1    Hirata, M.2    Ogawa, H.3
  • 11
    • 0036240209 scopus 로고    scopus 로고
    • A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis
    • Niyonsaba F., Iwabuchi K., Someya A., et al. A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis. Immunology 106 (2002) 20-26
    • (2002) Immunology , vol.106 , pp. 20-26
    • Niyonsaba, F.1    Iwabuchi, K.2    Someya, A.3
  • 12
    • 0033863168 scopus 로고    scopus 로고
    • Structural features and biological activities of the cathelicidin-derived antimicrobial peptides
    • Gennaro R., and Zanetti M. Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers 55 (2000) 31-49
    • (2000) Biopolymers , vol.55 , pp. 31-49
    • Gennaro, R.1    Zanetti, M.2
  • 13
    • 0034806944 scopus 로고    scopus 로고
    • RL-37, an alpha-helical antimicrobial peptide of the rhesus monkey
    • Zhao C., Nguyen T., Boo L.M., et al. RL-37, an alpha-helical antimicrobial peptide of the rhesus monkey. Antimicrob Agents Chemother 45 (2001) 2695-2702
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 2695-2702
    • Zhao, C.1    Nguyen, T.2    Boo, L.M.3
  • 14
    • 0035106913 scopus 로고    scopus 로고
    • Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules
    • Bals R., Lang C., Weiner D.J., et al. Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules. Clin Diagn Lab Immunol 8 (2001) 370-375
    • (2001) Clin Diagn Lab Immunol , vol.8 , pp. 370-375
    • Bals, R.1    Lang, C.2    Weiner, D.J.3
  • 15
    • 0032482980 scopus 로고    scopus 로고
    • The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface
    • Bals R., Wang X., Zasloff M., et al. The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface. Proc Natl Acad Sci USA 95 (1998) 9541-9546
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9541-9546
    • Bals, R.1    Wang, X.2    Zasloff, M.3
  • 16
    • 0029961492 scopus 로고    scopus 로고
    • Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities
    • Skerlavaj B., Gennaro R., Bagella L., et al. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J Biol Chem 271 (1996) 28375-28381
    • (1996) J Biol Chem , vol.271 , pp. 28375-28381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.3
  • 17
    • 0030728214 scopus 로고    scopus 로고
    • Structural organization of the bovine cathelicidin gene family and identification of a novel member
    • Scocchi M., Wang S., and Zanetti M. Structural organization of the bovine cathelicidin gene family and identification of a novel member. FEBS Lett 417 (1997) 311-315
    • (1997) FEBS Lett , vol.417 , pp. 311-315
    • Scocchi, M.1    Wang, S.2    Zanetti, M.3
  • 18
    • 0032808386 scopus 로고    scopus 로고
    • Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytes
    • Shamova O., Brogden K.A., Zhao C., et al. Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytes. Infect Immun 67 (1999) 4106-4111
    • (1999) Infect Immun , vol.67 , pp. 4106-4111
    • Shamova, O.1    Brogden, K.A.2    Zhao, C.3
  • 19
    • 0028834275 scopus 로고
    • cDNA sequences of three sheep myeloid cathelicidins
    • Bagella L., Scocchi M., and Zanetti M. cDNA sequences of three sheep myeloid cathelicidins. FEBS Lett 376 (1995) 225-228
    • (1995) FEBS Lett , vol.376 , pp. 225-228
    • Bagella, L.1    Scocchi, M.2    Zanetti, M.3
  • 20
    • 0028244635 scopus 로고
    • Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells
    • Zanetti M., Storici P., Tossi A., et al. Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells. J Biol Chem 269 (1994) 7855-7858
    • (1994) J Biol Chem , vol.269 , pp. 7855-7858
    • Zanetti, M.1    Storici, P.2    Tossi, A.3
  • 21
    • 0030926012 scopus 로고    scopus 로고
    • Synthesis and antibacterial action of cecropin and proline-arginine-rich peptides from pig intestine
    • Vunnam S., Juvvadi P., and Merrifield R.B. Synthesis and antibacterial action of cecropin and proline-arginine-rich peptides from pig intestine. J Pept Res 49 (1997) 59-66
    • (1997) J Pept Res , vol.49 , pp. 59-66
    • Vunnam, S.1    Juvvadi, P.2    Merrifield, R.B.3
  • 22
    • 0032878239 scopus 로고    scopus 로고
    • Novel cathelicidins in horse leukocytes(1)
    • Scocchi M., Bontempo D., Boscolo S., et al. Novel cathelicidins in horse leukocytes(1). FEBS Lett 457 (1999) 459-464
    • (1999) FEBS Lett , vol.457 , pp. 459-464
    • Scocchi, M.1    Bontempo, D.2    Boscolo, S.3
  • 23
    • 0035115442 scopus 로고    scopus 로고
    • Structural and functional analysis of horse cathelicidin peptides
    • Skerlavaj B., Scocchi M., Gennaro R., et al. Structural and functional analysis of horse cathelicidin peptides. Antimicrob Agents Chemother 45 (2001) 715-722
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 715-722
    • Skerlavaj, B.1    Scocchi, M.2    Gennaro, R.3
  • 24
    • 0034832028 scopus 로고    scopus 로고
    • Processing site and gene structure for the murine antimicrobial peptide CRAMP
    • Pestonjamasp V.K., Huttner K.H., and Gallo R.L. Processing site and gene structure for the murine antimicrobial peptide CRAMP. Peptides 22 (2001) 1643-1650
    • (2001) Peptides , vol.22 , pp. 1643-1650
    • Pestonjamasp, V.K.1    Huttner, K.H.2    Gallo, R.L.3
  • 25
    • 0344080624 scopus 로고    scopus 로고
    • Phylogeny, processing and expression of the rat cathelicidin rCRAMP: a model for innate antimicrobial peptides
    • Termen S., Tollin M., Olsson B., et al. Phylogeny, processing and expression of the rat cathelicidin rCRAMP: a model for innate antimicrobial peptides. Cell Mol Life Sci 60 (2003) 536-549
    • (2003) Cell Mol Life Sci , vol.60 , pp. 536-549
    • Termen, S.1    Tollin, M.2    Olsson, B.3
  • 26
    • 0035884820 scopus 로고    scopus 로고
    • Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells
    • Nagaoka I., Hirota S., Niyonsaba F., et al. Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells. J Immunol 167 (2001) 3329-3338
    • (2001) J Immunol , vol.167 , pp. 3329-3338
    • Nagaoka, I.1    Hirota, S.2    Niyonsaba, F.3
  • 27
    • 0027466916 scopus 로고
    • Antibacterial 15-kDa protein isoforms (p15s) are members of a novel family of leukocyte proteins
    • Levy O., Weiss J., Zarember K., et al. Antibacterial 15-kDa protein isoforms (p15s) are members of a novel family of leukocyte proteins. J Biol Chem 268 (1993) 6058-6063
    • (1993) J Biol Chem , vol.268 , pp. 6058-6063
    • Levy, O.1    Weiss, J.2    Zarember, K.3
  • 28
    • 22944458199 scopus 로고    scopus 로고
    • The role of cathelicidins in the innate host defenses of mammals
    • Zanetti M. The role of cathelicidins in the innate host defenses of mammals. Curr Issues Mol Biol 7 (2005) 179-196
    • (2005) Curr Issues Mol Biol , vol.7 , pp. 179-196
    • Zanetti, M.1
  • 29
    • 0033797218 scopus 로고    scopus 로고
    • Regulation of cathelicidin gene expression: induction by lipopolysaccharide, interleukin-6, retinoic acid, and Salmonella enterica serovar typhimurium infection
    • Wu H., Zhang G., Minton J.E., et al. Regulation of cathelicidin gene expression: induction by lipopolysaccharide, interleukin-6, retinoic acid, and Salmonella enterica serovar typhimurium infection. Infect Immun 68 (2000) 5552-5558
    • (2000) Infect Immun , vol.68 , pp. 5552-5558
    • Wu, H.1    Zhang, G.2    Minton, J.E.3
  • 30
    • 17644363748 scopus 로고    scopus 로고
    • Molecular cloning and characterization of three {beta}-defensins from canine testes
    • Sang Y., Ortega M.T., Blecha F., et al. Molecular cloning and characterization of three {beta}-defensins from canine testes. Infect Immun 73 (2005) 2611-2620
    • (2005) Infect Immun , vol.73 , pp. 2611-2620
    • Sang, Y.1    Ortega, M.T.2    Blecha, F.3
  • 31
    • 33746210214 scopus 로고    scopus 로고
    • Macrophages acquire neutrophil granules for antimicrobial activity against intracellular pathogens
    • Tan B.H., Meinken C., Bastian M., et al. Macrophages acquire neutrophil granules for antimicrobial activity against intracellular pathogens. J Immunol 177 (2006) 1864-1871
    • (2006) J Immunol , vol.177 , pp. 1864-1871
    • Tan, B.H.1    Meinken, C.2    Bastian, M.3
  • 32
    • 0025183708 scopus 로고
    • Basic local alignment search tool
    • Altschul S.F., Gish W., Miller W., et al. Basic local alignment search tool. J Mol Biol 215 (1990) 403-410
    • (1990) J Mol Biol , vol.215 , pp. 403-410
    • Altschul, S.F.1    Gish, W.2    Miller, W.3
  • 33
    • 0035823624 scopus 로고    scopus 로고
    • Essential role of the conformational flexibility of helices 1 and 5 on the lipid binding activity of apolipophorin-III
    • Soulages J.L., Arrese E.L., Chetty P.S., et al. Essential role of the conformational flexibility of helices 1 and 5 on the lipid binding activity of apolipophorin-III. J Biol Chem 276 (2001) 34162-34166
    • (2001) J Biol Chem , vol.276 , pp. 34162-34166
    • Soulages, J.L.1    Arrese, E.L.2    Chetty, P.S.3
  • 34
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen Y.H., Yang J.T., and Chau K.H. Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry 13 (1974) 3350-3359
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 35
    • 0029128705 scopus 로고
    • The solution structure of the active domain of CAP18-a lipopolysaccharide binding protein from rabbit leukocytes
    • Chen C., Brock R., Luh F., et al. The solution structure of the active domain of CAP18-a lipopolysaccharide binding protein from rabbit leukocytes. FEBS Lett 370 (1995) 46-52
    • (1995) FEBS Lett , vol.370 , pp. 46-52
    • Chen, C.1    Brock, R.2    Luh, F.3
  • 36
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl Acids Res 22 (1994) 4673-4680
    • (1994) Nucl Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 38
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L.J., Bryson K., and Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 16 (2000) 404-405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 39
    • 85190534384 scopus 로고    scopus 로고
    • Pfaller MA, Chaturvedi V, Espinel-Ingroff A, et al. Manual NCCLS. Reference method for broth dilution antifungal susceptibility testing of yeasts; approved standard-2nd ed. NCCLS document M27-A2 [ISBN 1-56238-469-4]. NCCLS, 940 West Valley Road, Suite 1400, Wayne, PA 19087-1898, USA. NCCLS 2002;22.
  • 40
    • 85190558166 scopus 로고    scopus 로고
    • Ferraro MJ, Wikler MA, Craig WA, et al. Manual NCCLS. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically; approved standard, 6th ed. NCCLS document M7-A6 [ISBN 1-56238-486-4]. NCCLS, 940 West Valley Road, Suite 1400, Wayne, PA 19087-1898 USA, 2003. NCCLS 2003;23.
  • 41
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner J., Cho Y., Dinh N.N., et al. Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob Agents Chemother 42 (1998) 2206-2214
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3
  • 42
    • 0036178436 scopus 로고    scopus 로고
    • SMAP-29 has two LPS-binding sites and a central hinge
    • Tack B.F., Sawai M.V., Kearney W.R., et al. SMAP-29 has two LPS-binding sites and a central hinge. Eur J Biochem 269 (2002) 1181-1189
    • (2002) Eur J Biochem , vol.269 , pp. 1181-1189
    • Tack, B.F.1    Sawai, M.V.2    Kearney, W.R.3
  • 43
    • 0033433992 scopus 로고    scopus 로고
    • SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytes
    • Skerlavaj B., Benincasa M., Risso A., et al. SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytes. FEBS Lett 463 (1999) 58-62
    • (1999) FEBS Lett , vol.463 , pp. 58-62
    • Skerlavaj, B.1    Benincasa, M.2    Risso, A.3
  • 44
    • 0036092782 scopus 로고    scopus 로고
    • Solution structure of a cathelicidin-derived antimicrobial peptide, CRAMP as determined by NMR spectroscopy
    • Yu K., Park K., Kang S.W., et al. Solution structure of a cathelicidin-derived antimicrobial peptide, CRAMP as determined by NMR spectroscopy. J Pept Res 60 (2002) 1-9
    • (2002) J Pept Res , vol.60 , pp. 1-9
    • Yu, K.1    Park, K.2    Kang, S.W.3
  • 45
    • 0032211616 scopus 로고    scopus 로고
    • Cytotoxicity and apoptosis mediated by two peptides of innate immunity
    • Risso A., Zanetti M., and Gennaro R. Cytotoxicity and apoptosis mediated by two peptides of innate immunity. Cell Immunol 189 (1998) 107-115
    • (1998) Cell Immunol , vol.189 , pp. 107-115
    • Risso, A.1    Zanetti, M.2    Gennaro, R.3
  • 46
    • 0036785559 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses
    • Scott M.G., Davidson D.J., Gold M.R., et al. The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses. J Immunol 169 (2002) 3883-3891
    • (2002) J Immunol , vol.169 , pp. 3883-3891
    • Scott, M.G.1    Davidson, D.J.2    Gold, M.R.3
  • 47
    • 0030484497 scopus 로고    scopus 로고
    • Six antimicrobial peptide genes of the cathelicidin family map to bovine chromosome 22q24 by fluorescence in situ hybridization
    • Castiglioni B., Scocchi M., Zanetti M., et al. Six antimicrobial peptide genes of the cathelicidin family map to bovine chromosome 22q24 by fluorescence in situ hybridization. Cytogenet Cell Genet 75 (1996) 240-242
    • (1996) Cytogenet Cell Genet , vol.75 , pp. 240-242
    • Castiglioni, B.1    Scocchi, M.2    Zanetti, M.3
  • 48
    • 0034184327 scopus 로고    scopus 로고
    • Porcine antimicrobial peptides: new prospects for ancient molecules of host defense
    • Zhang G., Ross C.R., and Blecha F. Porcine antimicrobial peptides: new prospects for ancient molecules of host defense. Vet Res 31 (2000) 277-296
    • (2000) Vet Res , vol.31 , pp. 277-296
    • Zhang, G.1    Ross, C.R.2    Blecha, F.3
  • 49
    • 1342282224 scopus 로고    scopus 로고
    • Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense
    • Murakami M., Lopez-Garcia B., Braff M., et al. Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense. J Immunol 172 (2004) 3070-3077
    • (2004) J Immunol , vol.172 , pp. 3070-3077
    • Murakami, M.1    Lopez-Garcia, B.2    Braff, M.3
  • 50
    • 0034809874 scopus 로고    scopus 로고
    • Structure-activity analysis of SMAP-29, a sheep leukocytes-derived antimicrobial peptide
    • Shin S.Y., Park E.J., Yang S.T., et al. Structure-activity analysis of SMAP-29, a sheep leukocytes-derived antimicrobial peptide. Biochem Biophys Res Commun 285 (2001) 1046-1051
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 1046-1051
    • Shin, S.Y.1    Park, E.J.2    Yang, S.T.3
  • 51
    • 0036891933 scopus 로고    scopus 로고
    • Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva
    • Murakami M., Ohtake T., Dorschner R.A., et al. Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva. J Dent Res 81 (2002) 845-850
    • (2002) J Dent Res , vol.81 , pp. 845-850
    • Murakami, M.1    Ohtake, T.2    Dorschner, R.A.3
  • 52
    • 11144242839 scopus 로고    scopus 로고
    • Protegrin structure-activity relationships: using homology models of synthetic sequences to determine structural characteristics important for activity
    • Ostberg N., and Kaznessis Y. Protegrin structure-activity relationships: using homology models of synthetic sequences to determine structural characteristics important for activity. Peptides 26 (2005) 197-206
    • (2005) Peptides , vol.26 , pp. 197-206
    • Ostberg, N.1    Kaznessis, Y.2
  • 53
    • 0036257411 scopus 로고    scopus 로고
    • Cathelicidin peptides as candidates for a novel class of antimicrobials
    • Zanetti M., Gennaro R., Skerlavaj B., et al. Cathelicidin peptides as candidates for a novel class of antimicrobials. Curr Pharm Des 8 (2002) 779-793
    • (2002) Curr Pharm Des , vol.8 , pp. 779-793
    • Zanetti, M.1    Gennaro, R.2    Skerlavaj, B.3
  • 54
    • 0036218636 scopus 로고    scopus 로고
    • Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity
    • Ramanathan B., Davis E.G., Ross C.R., et al. Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity. Microbes Infect 4 (2002) 361-372
    • (2002) Microbes Infect , vol.4 , pp. 361-372
    • Ramanathan, B.1    Davis, E.G.2    Ross, C.R.3
  • 55
    • 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
  • 56
    • 0023671957 scopus 로고
    • Transmission of Brucella canis by contact exposure
    • Carmichael L.E., and Joubert J.C. Transmission of Brucella canis by contact exposure. Cornell Vet 78 (1988) 63-73
    • (1988) Cornell Vet , vol.78 , pp. 63-73
    • Carmichael, L.E.1    Joubert, J.C.2
  • 57
    • 0019844768 scopus 로고
    • The genital Mycoplasma and Ureaplasma flora of healthy and diseased dogs
    • Doig P.A., Ruhnke H.L., and Bosu W.T. The genital Mycoplasma and Ureaplasma flora of healthy and diseased dogs. Can J Comp Med 45 (1981) 233-238
    • (1981) Can J Comp Med , vol.45 , pp. 233-238
    • Doig, P.A.1    Ruhnke, H.L.2    Bosu, W.T.3
  • 58
    • 0027453985 scopus 로고
    • Ureaplasma canigenitalium spp. nov., isolated from dogs
    • Harasawa R., Imada Y., Kotani H., et al. Ureaplasma canigenitalium spp. nov., isolated from dogs. Int J Syst Bacteriol 43 (1993) 640-644
    • (1993) Int J Syst Bacteriol , vol.43 , pp. 640-644
    • Harasawa, R.1    Imada, Y.2    Kotani, H.3
  • 59
    • 21344432145 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae downregulates expression of the human antimicrobial peptide LL-37
    • Bergman P., Johansson L., Asp V., et al. Neisseria gonorrhoeae downregulates expression of the human antimicrobial peptide LL-37. Cell Microbiol 7 (2005) 1009-1017
    • (2005) Cell Microbiol , vol.7 , pp. 1009-1017
    • Bergman, P.1    Johansson, L.2    Asp, V.3
  • 60
    • 22544486843 scopus 로고    scopus 로고
    • Cationic antimicrobial peptide resistance in Neisseria meningitidis
    • Tzeng Y.L., Ambrose K.D., Zughaier S., et al. Cationic antimicrobial peptide resistance in Neisseria meningitidis. J Bacteriol 187 (2005) 5387-5396
    • (2005) J Bacteriol , vol.187 , pp. 5387-5396
    • Tzeng, Y.L.1    Ambrose, K.D.2    Zughaier, S.3
  • 61
    • 2942582739 scopus 로고    scopus 로고
    • Reduction in the bactericidal activity of selected cathelicidin peptides by bovine calf serum or exogenous endotoxin
    • Bartlett K.H., McCray Jr. P.B., and Thorne P.S. Reduction in the bactericidal activity of selected cathelicidin peptides by bovine calf serum or exogenous endotoxin. Int J Antimicrob Agents 23 (2004) 606-612
    • (2004) Int J Antimicrob Agents , vol.23 , pp. 606-612
    • Bartlett, K.H.1    McCray Jr., P.B.2    Thorne, P.S.3
  • 62
    • 21444456146 scopus 로고    scopus 로고
    • Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37
    • Ciornei C.D., Sigurdardottir T., Schmidtchen A., et al. Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37. Antimicrob Agents Chemother 49 (2005) 2845-2850
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2845-2850
    • Ciornei, C.D.1    Sigurdardottir, T.2    Schmidtchen, A.3
  • 63
    • 0034098916 scopus 로고    scopus 로고
    • Bactericidal activity of mammalian cathelicidin-derived peptides
    • Travis S.M., Anderson N.N., Forsyth W.R., et al. Bactericidal activity of mammalian cathelicidin-derived peptides. Infect Immun 68 (2000) 2748-2755
    • (2000) Infect Immun , vol.68 , pp. 2748-2755
    • Travis, S.M.1    Anderson, N.N.2    Forsyth, W.R.3
  • 64
    • 0034618590 scopus 로고    scopus 로고
    • CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity
    • Shin S.Y., Kang S.W., Lee D.G., et al. CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity. Biochem Biophys Res Commun 275 (2000) 904-909
    • (2000) Biochem Biophys Res Commun , vol.275 , pp. 904-909
    • Shin, S.Y.1    Kang, S.W.2    Lee, D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.