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Volumn 120, Issue 5, 2003, Pages 810-816

Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence

Author keywords

Infection; Innate immunity; Protease; Skin; Staphylococcus

Indexed keywords

CATHELICIDIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CATHELIN; PROTEIN HCAP18; UNCLASSIFIED DRUG;

EID: 0037960231     PISSN: 0022202X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1523-1747.2003.12132.x     Document Type: Article
Times cited : (226)

References (54)
  • 1
    • 0023189459 scopus 로고
    • Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C and chicken cystatin
    • Abrahamson M, Ritonja A, Brown MA, Grubb A, Machleidt W, Barrett AJ: Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C and chicken cystatin. J Biol Chem 262:9688-9694, 1987
    • (1987) J Biol Chem , vol.262 , pp. 9688-9694
    • Abrahamson, M.1    Ritonja, A.2    Brown, M.A.3    Grubb, A.4    Machleidt, W.5    Barrett, A.J.6
  • 2
    • 0030053568 scopus 로고    scopus 로고
    • A cysteine protease inhibitor stored in the large granules of horseshoe crab hemocytes: Purification, characterization, cDNA cloning and tissue localization
    • Agarwala KL, Kawabata S, Hirata M, Miyagi M, Tsunasawa S, Iwanaga S: A cysteine protease inhibitor stored in the large granules of horseshoe crab hemocytes: Purification, characterization, cDNA cloning and tissue localization. J Biochem (Tokyo) 119:85-94, 1996
    • (1996) J Biochem (Tokyo) , vol.119 , pp. 85-94
    • Agarwala, K.L.1    Kawabata, S.2    Hirata, M.3    Miyagi, M.4    Tsunasawa, S.5    Iwanaga, S.6
  • 4
    • 0033787069 scopus 로고    scopus 로고
    • Secretory leukocyte protease inhibitor mediates non-redundant functions necessary for normal wound healing
    • Ashcroft GS, Lei K, Jin W, et al: Secretory leukocyte protease inhibitor mediates non-redundant functions necessary for normal wound healing. Nat Med 6:1147-1153, 2000
    • (2000) Nat Med , vol.6 , pp. 1147-1153
    • Ashcroft, G.S.1    Lei, K.2    Jin, W.3
  • 5
    • 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, Wilson JM: 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 95:9541-9546, 1998
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9541-9546
    • Bals, R.1    Wang, X.2    Zasloff, M.3    Wilson, J.M.4
  • 6
    • 0033560645 scopus 로고    scopus 로고
    • Transfer of a cathelicidin peptide antibiotic gene restores bacterial killing in a cystic fibrosis xenograft model
    • Bals R, Weiner DJ, Meegalla RL, Wilson JM: Transfer of a cathelicidin peptide antibiotic gene restores bacterial killing in a cystic fibrosis xenograft model. J Clin Invest 103:1113-1117, 1999a
    • (1999) J Clin Invest , vol.103 , pp. 1113-1117
    • Bals, R.1    Weiner, D.J.2    Meegalla, R.L.3    Wilson, J.M.4
  • 7
    • 0032708355 scopus 로고    scopus 로고
    • Augmentation of innate host defense by expression of a cathelicidin antimicrobial peptide
    • Bals R, Weiner DJ, Moscioni AD, Meegalla RL, Wilson JM: Augmentation of innate host defense by expression of a cathelicidin antimicrobial peptide. Infect Immun 67:6084-6089, 1999b
    • (1999) Infect Immun , vol.67 , pp. 6084-6089
    • Bals, R.1    Weiner, D.J.2    Moscioni, A.D.3    Meegalla, R.L.4    Wilson, J.M.5
  • 8
    • 0024546648 scopus 로고
    • Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor
    • Bjorck L, Akesson P, Bohus M,Trojnar J, Abrahamson M, Olafsson I, Grubb A: Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor. Nature 337:385-386, 1989
    • (1989) Nature , vol.337 , pp. 385-386
    • Bjorck, L.1    Akesson, P.2    Bohus, M.3    Trojnar, J.4    Abrahamson, M.5    Olafsson, I.6    Grubb, A.7
  • 10
    • 0033962266 scopus 로고    scopus 로고
    • Innate immunity and the normal microflora
    • Boman HG: Innate immunity and the normal microflora. Immunol Rev 173:5-16, 2000
    • (2000) Immunol Rev , vol.173 , pp. 5-16
    • Boman, H.G.1
  • 11
    • 0035163451 scopus 로고    scopus 로고
    • Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds
    • Cole AM, Shi J, Ceccarelli A, Kim YH, Park A, Ganz T: Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds. Blood 97:297-304, 2001
    • (2001) Blood , vol.97 , pp. 297-304
    • Cole, A.M.1    Shi, J.2    Ceccarelli, A.3    Kim, Y.H.4    Park, A.5    Ganz, T.6
  • 12
    • 0034946907 scopus 로고    scopus 로고
    • Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus
    • Dorschner RA, Pestonjamasp VK, Tamakuwala S, et al: Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus. J Invest Dermatol 117:91-97, 2001
    • (2001) J Invest Dermatol , vol.117 , pp. 91-97
    • Dorschner, R.A.1    Pestonjamasp, V.K.2    Tamakuwala, S.3
  • 13
    • 9444225012 scopus 로고    scopus 로고
    • Mode of action of the antimicrobial peptide indolicidin
    • Falla TJ, Karunaratne DN, Hancock RE: Mode of action of the antimicrobial peptide indolicidin. J Biol Chem 271:19298-19303, 1996
    • (1996) J Biol Chem , vol.271 , pp. 19298-19303
    • Falla, T.J.1    Karunaratne, D.N.2    Hancock, R.E.3
  • 14
    • 0030956070 scopus 로고    scopus 로고
    • The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders
    • Frohm M, Agerberth B, Ahangari G, Stahle-Backdahl M, Liden S, Wigzell H, Gudmundsson GH: The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J Biol Chem 272:15258-15263, 1997
    • (1997) J Biol Chem , vol.272 , pp. 15258-15263
    • Frohm, M.1    Agerberth, B.2    Ahangari, G.3    Stahle-Backdahl, M.4    Liden, S.5    Wigzell, H.6    Gudmundsson, G.H.7
  • 15
    • 0028092047 scopus 로고
    • Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds
    • Gallo RL, Ono M, Povsic T, Page C, Eriksson E, Klagsbrun M, Bernfield M: Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proc Natl Acad Sci USA 91:11035-11039, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11035-11039
    • Gallo, R.L.1    Ono, M.2    Povsic, T.3    Page, C.4    Eriksson, E.5    Klagsbrun, M.6    Bernfield, M.7
  • 16
    • 0031009432 scopus 로고    scopus 로고
    • Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse
    • Gallo RL, Kim KJ, Bernfield M, Kozak CA, Zanetti M, Merluzzi L, Gennaro R: Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse. J Biol Chem 272:13088-13093, 1997
    • (1997) J Biol Chem , vol.272 , pp. 13088-13093
    • Gallo, R.L.1    Kim, K.J.2    Bernfield, M.3    Kozak, C.A.4    Zanetti, M.5    Merluzzi, L.6    Gennaro, R.7
  • 17
    • 0031046654 scopus 로고    scopus 로고
    • Antimicrobial peptides of leukocytes
    • Ganz T, Lehrer RI: Antimicrobial peptides of leukocytes. Curr Opin Hematol 4:53-58, 1997
    • (1997) Curr Opin Hematol , vol.4 , pp. 53-58
    • Ganz, T.1    Lehrer, R.I.2
  • 18
    • 0033863168 scopus 로고    scopus 로고
    • Structural features and biological activities of the cathelicidin-derived antimicrobial peptides
    • Gennaro R, Zanetti M: Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers 55:31-49, 2000
    • (2000) Biopolymers , vol.55 , pp. 31-49
    • Gennaro, R.1    Zanetti, M.2
  • 19
    • 0031725844 scopus 로고    scopus 로고
    • Biological characterization of a novel mammalian antimicrobial peptide
    • Gennaro R, Scocchi M, Merluzzi L, Zanetti M: Biological characterization of a novel mammalian antimicrobial peptide. Biochim Biophys Acta 1425:361-368, 1998
    • (1998) Biochim Biophys Acta , vol.1425 , pp. 361-368
    • Gennaro, R.1    Scocchi, M.2    Merluzzi, L.3    Zanetti, M.4
  • 20
    • 0029893253 scopus 로고    scopus 로고
    • The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes
    • Gudmundsson GH, Agerberth B, Odeberg J, Bergman T, Olsson B, Salcedo R: The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur J Biochem 238:325-332, 1996
    • (1996) Eur J Biochem , vol.238 , pp. 325-332
    • Gudmundsson, G.H.1    Agerberth, B.2    Odeberg, J.3    Bergman, T.4    Olsson, B.5    Salcedo, R.6
  • 21
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock RE: Peptide antibiotics. Lancet 349:418-422, 1997
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.1
  • 24
    • 0035126317 scopus 로고    scopus 로고
    • Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator
    • Islam D, Bandholtz L, Nilsson J, Wigzell H, Christensson B, Agerberth B, Gudmundsson G: Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator. Nat Med 7:180-185, 2001
    • (2001) Nat Med , vol.7 , pp. 180-185
    • Islam, D.1    Bandholtz, L.2    Nilsson, J.3    Wigzell, H.4    Christensson, B.5    Agerberth, B.6    Gudmundsson, G.7
  • 25
    • 0035055831 scopus 로고    scopus 로고
    • Specific antibodies to Porphyromonas gingivalis Lys-gingipain by DNA vaccination inhibit bacterial binding to hemoglobin and protect mice from infection
    • Kuboniwa M, Amano A, Shizukuishi S, Nakagawa I, Hamada S: Specific antibodies to Porphyromonas gingivalis Lys-gingipain by DNA vaccination inhibit bacterial binding to hemoglobin and protect mice from infection. Infect Immun 69:2972-2979, 2001
    • (2001) Infect Immun , vol.69 , pp. 2972-2979
    • Kuboniwa, M.1    Amano, A.2    Shizukuishi, S.3    Nakagawa, I.4    Hamada, S.5
  • 26
    • 0033042528 scopus 로고    scopus 로고
    • Extracellular cysteine protease produced by Streptococcus pyogenes participates in the pathogenesis of invasive skin infection and dissemination in mice
    • Lukomski S, Montgomery CA, Rurangirwa J, Geske RS, Barrish JP, Adams GJ, Musser JM: Extracellular cysteine protease produced by Streptococcus pyogenes participates in the pathogenesis of invasive skin infection and dissemination in mice. Infect Immun 67:1779-1788, 1999
    • (1999) Infect Immun , vol.67 , pp. 1779-1788
    • Lukomski, S.1    Montgomery, C.A.2    Rurangirwa, J.3    Geske, R.S.4    Barrish, J.P.5    Adams, G.J.6    Musser, J.M.7
  • 28
    • 0036450262 scopus 로고    scopus 로고
    • Cathelicidin antimicrobial peptide expression in sweat, an innate defense system for the skin
    • Murakami M, Othake T, Dorshner R, Shittek B, Garbe C, Gallo RL: Cathelicidin antimicrobial peptide expression in sweat, an innate defense system for the skin. J Invest Dermatol, 119:1090-1095, 2002
    • (2002) J Invest Dermatol , vol.119 , pp. 1090-1095
    • Murakami, M.1    Othake, T.2    Dorshner, R.3    Shittek, B.4    Garbe, C.5    Gallo, R.L.6
  • 29
    • 0035936156 scopus 로고    scopus 로고
    • Innate antimicrobial peptide protects the skin from invasive bacterial infection
    • Nizet V, Ohtake T, Lauth X, et al: Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature 414:454-457, 2001
    • (2001) Nature , vol.414 , pp. 454-457
    • Nizet, V.1    Ohtake, T.2    Lauth, X.3
  • 30
    • 0037057645 scopus 로고    scopus 로고
    • Endogenous antimicrobial peptides and skin infections in atopic dermatitis
    • Ong PY, Ohtake T, Brandt C, et al: Endogenous antimicrobial peptides and skin infections in atopic dermatitis. N Engl J Med 347:1151-1160, 2002
    • (2002) N Engl J Med , vol.347 , pp. 1151-1160
    • Ong, P.Y.1    Ohtake, T.2    Brandt, C.3
  • 31
    • 0037007214 scopus 로고    scopus 로고
    • IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G
    • von Pawel-Rammingen U, Johansson BP, Bjorck L: IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G. Embo J 21:1607-1615, 2002
    • (2002) Embo J , vol.21 , pp. 1607-1615
    • Von Pawel-Rammingen, U.1    Johansson, B.P.2    Bjorck, L.3
  • 32
    • 0036218636 scopus 로고    scopus 로고
    • Cathelicidins: Microbicidal activity, mechanisms of action, and roles in innate immunity
    • Ramanathan B, Davis EG, Ross CR, Blecha F: Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity. Microbes Infect 4:361-372, 2002
    • (2002) Microbes Infect , vol.4 , pp. 361-372
    • Ramanathan, B.1    Davis, E.G.2    Ross, C.R.3    Blecha, F.4
  • 34
    • 0024349857 scopus 로고
    • Primary structure of a new cysteine proteinase inhibitor from pig leucocytes
    • Ritonja A, Kopitar M, Jerala R, Turk V: Primary structure of a new cysteine proteinase inhibitor from pig leucocytes. FEBS Lett 285:211-214, 1989
    • (1989) FEBS Lett , vol.285 , pp. 211-214
    • Ritonja, A.1    Kopitar, M.2    Jerala, R.3    Turk, V.4
  • 36
    • 0036772907 scopus 로고    scopus 로고
    • Structure of the cathelicidin motif of the protegrin-3 precursor: Structural insights into the activation mechanism of an antimicrobial protein
    • Sanchez JF, Hoh F, Strub MP, Aumelas A, Dumas C: Structure of the cathelicidin motif of the protegrin-3 precursor: structural insights into the activation mechanism of an antimicrobial protein. Structure 10:1363-1370, 2002a
    • (2002) Structure , vol.10 , pp. 1363-1370
    • Sanchez, J.F.1    Hoh, F.2    Strub, M.P.3    Aumelas, A.4    Dumas, C.5
  • 37
    • 0037039376 scopus 로고    scopus 로고
    • Overexpression and structural study of the cathelicidin motif of the protegrin-3 precursor
    • Sanchez JF, Wojcik F, Yang YS, et al: Overexpression and structural study of the cathelicidin motif of the protegrin-3 precursor. Biochemistry 41:21-30, 2002b
    • (2002) Biochemistry , vol.41 , pp. 21-30
    • Sanchez, J.F.1    Wojcik, F.2    Yang, Y.S.3
  • 38
    • 0036528903 scopus 로고    scopus 로고
    • Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection
    • Schaller-Bals S, Schulze A, Bals R: Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection. Am J Respir Crit Care Med 165:992-995, 2002
    • (2002) Am J Respir Crit Care Med , vol.165 , pp. 992-995
    • Schaller-Bals, S.1    Schulze, A.2    Bals, R.3
  • 39
    • 0030728214 scopus 로고    scopus 로고
    • Structural organization of the bovine cathelicidin gene family and identification of a novel member
    • Scocchi M, Wang S, Zanetti M: Structural organization of the bovine cathelicidin gene family and identification of a novel member. FEBS Lett 417:311-315, 1997
    • (1997) FEBS Lett , vol.417 , pp. 311-315
    • Scocchi, M.1    Wang, S.2    Zanetti, M.3
  • 40
    • 0030880531 scopus 로고    scopus 로고
    • The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils
    • Sorensen O, Arnljots K, Cowland JB, Bainton DF, Borregaard N: The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils. Blood 90:2796-2803, 1997
    • (1997) Blood , vol.90 , pp. 2796-2803
    • Sorensen, O.1    Arnljots, K.2    Cowland, J.B.3    Bainton, D.F.4    Borregaard, N.5
  • 41
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL- 37 by extracellular cleavage with proteinase 3
    • Sorensen OE, Follin P, Johnsen AH, Calafat J, Tjabringa GS, Hiemstra PS, Borregaard N: Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 97:3951-3395, 2001
    • (2001) Blood , vol.97 , pp. 3951-3395
    • Sorensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5    Hiemstra, P.S.6    Borregaard, N.7
  • 42
    • 0030623934 scopus 로고    scopus 로고
    • Designer assays for antimicrobial peptides. Disputing the one-size- fits-all' theory
    • Steinberg DA, Lehrer RI: Designer assays for antimicrobial peptides. Disputing the one-size- fits-all' theory. Meth Mol Biol 78:169-186, 1997
    • (1997) Meth Mol Biol , vol.78 , pp. 169-186
    • Steinberg, D.A.1    Lehrer, R.I.2
  • 43
    • 0030057777 scopus 로고    scopus 로고
    • Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides
    • Storici P, Tossi A, Lenarcic B, Romeo D: Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides. Eur J Biochem 238:769-776, 1996
    • (1996) Eur J Biochem , vol.238 , pp. 769-776
    • Storici, P.1    Tossi, A.2    Lenarcic, B.3    Romeo, D.4
  • 44
    • 0027973629 scopus 로고
    • Inhibition of growth and cysteine proteinase activity of Staphylococcus aureus V8 by phosphorylated cystatin α in skin cornified envelope
    • Takahashi M, Tezuka T, Katunuma N: Inhibition of growth and cysteine proteinase activity of Staphylococcus aureus V8 by phosphorylated cystatin α in skin cornified envelope. FEBS Lett 335:275-278, 1994
    • (1994) FEBS Lett , vol.335 , pp. 275-278
    • Takahashi, M.1    Tezuka, T.2    Katunuma, N.3
  • 45
    • 0031686776 scopus 로고    scopus 로고
    • Lehrer R1: Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner J, Cho Y, Dinh NN, Waring AJ, Lehrer R1: Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob Agents Chemother 42:2206-2214, 1998
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4
  • 46
    • 0029978338 scopus 로고    scopus 로고
    • Intramolecular inhibition of human defensin HNP- 1 by its propiece
    • Valore EV, Martin E, Harwig SS, Ganz T: Intramolecular inhibition of human defensin HNP-1 by its propiece. J Clin Invest 97:1624-1629, 1996
    • (1996) J Clin Invest , vol.97 , pp. 1624-1629
    • Valore, E.V.1    Martin, E.2    Harwig, S.S.3    Ganz, T.4
  • 47
    • 0027528409 scopus 로고
    • Chemotactic and protease-inhibiting activities of antibiotic peptide precursors
    • Verbanac D, Zanetti M, Romeo D: Chemotactic and protease-inhibiting activities of antibiotic peptide precursors. FEBS Lett 317:255-258, 1993
    • (1993) FEBS Lett , vol.317 , pp. 255-258
    • Verbanac, D.1    Zanetti, M.2    Romeo, D.3
  • 49
    • 0036379140 scopus 로고    scopus 로고
    • Cathelicidins, essential gene-encoded mammalian antibiotics
    • Zaiou M, Gallo RL: Cathelicidins, essential gene-encoded mammalian antibiotics. J Mol Med 80:549-561, 2002
    • (2002) J Mol Med , vol.80 , pp. 549-561
    • Zaiou, M.1    Gallo, R.L.2
  • 50
    • 0025081012 scopus 로고
    • Bactenecins, defense polypeptides of bovine neutrophils, are generated from precursor molecules stored in the large granules
    • Zanetti M, Litteri L, Gennaro R, Horstmann H, Romeo D: Bactenecins, defense polypeptides of bovine neutrophils, are generated from precursor molecules stored in the large granules. J Cell Biol 111:1363-1371, 1990
    • (1990) J Cell Biol , vol.111 , pp. 1363-1371
    • Zanetti, M.1    Litteri, L.2    Gennaro, R.3    Horstmann, H.4    Romeo, D.5
  • 51
    • 0025953533 scopus 로고
    • Stimulus-induced maturation of probactenecins, precursors of neutrophil antimicrobial polypeptides
    • Zanetti M, Litteri L, Griffiths G, Gennaro R, Romeo D: Stimulus-induced maturation of probactenecins, precursors of neutrophil antimicrobial polypeptides. J Immunol 146:4295-4300, 1991
    • (1991) J Immunol , vol.146 , pp. 4295-4300
    • Zanetti, M.1    Litteri, L.2    Griffiths, G.3    Gennaro, R.4    Romeo, D.5
  • 52
    • 0036149798 scopus 로고    scopus 로고
    • Host defense functions of proteolytically processed and parent (unprocessed) cathelicidins of rabbit granulocytes
    • Zarember KA, Katz SS, Tack BF, Doukhan L, Weiss J, Elsbach P: Host defense functions of proteolytically processed and parent (unprocessed) cathelicidins of rabbit granulocytes. Infect Immun 70:569-576, 2002
    • (2002) Infect Immun , vol.70 , pp. 569-576
    • Zarember, K.A.1    Katz, S.S.2    Tack, B.F.3    Doukhan, L.4    Weiss, J.5    Elsbach, P.6
  • 53
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M: Antimicrobial peptides of multicellular organisms. Nature 415:389-395, 2002
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 54
    • 0034243942 scopus 로고    scopus 로고
    • Entamoeba histolytica cysteine proteinases with interleukin-1 β converting enzyme (ICE) activity cause intestinal inflammation and tissue damage in amoebiasis
    • Zhang Z, Wang L, Seydel KB, Li E, Ankri S, Mirelman D, Stanley SL Jr: Entamoeba histolytica cysteine proteinases with interleukin-1 β converting enzyme (ICE) activity cause intestinal inflammation and tissue damage in amoebiasis. Mol Microbiol 37:542-548, 2000
    • (2000) Mol Microbiol , vol.37 , pp. 542-548
    • Zhang, Z.1    Wang, L.2    Seydel, K.B.3    Li, E.4    Ankri, S.5    Mirelman, D.6    Stanley S.L., Jr.7


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