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Volumn 16, Issue 9, 2010, Pages 1024-1039

Antimicrobial peptides present in mammalian skin and gut are multifunctional defence molecules

Author keywords

Antimicrobial peptides; Atopic dermatitis; Crohn's disease; Gut; Inflammation; Innate immunity; Psoriasis; Skin

Indexed keywords

ALPHA DEFENSIN; BETA DEFENSIN; BETA DEFENSIN 1; BETA DEFENSIN 2; BETA DEFENSIN 3; BETA DEFENSIN 4; BETA DEFENSIN 5; CALCITONIN GENE RELATED PEPTIDE; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CHROMOGRANIN A; DEFENSIN; DERMCIDIN; GAMMA INTERFERON; INTERLEUKIN 13; INTERLEUKIN 4; INTERLEUKIN 5; LACTOFERRIN; LECTIN; LYSOZYME; MACROPHAGE INFLAMMATORY PROTEIN 3ALPHA; NEUROPEPTIDE; PHOSPHOLIPASE A2; POLYPEPTIDE ANTIBIOTIC AGENT; PSORIASIN; RIBONUCLEASE A; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 7; TUMOR NECROSIS FACTOR ALPHA; UNINDEXED DRUG; VASOACTIVE INTESTINAL POLYPEPTIDE;

EID: 77950272369     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161210790963823     Document Type: Review
Times cited : (40)

References (225)
  • 1
    • 1642545489 scopus 로고    scopus 로고
    • Antimicrobial peptides: From invertebrates to vertebrates
    • Bulet P, Stocklin R, Menin L. Antimicrobial peptides: from invertebrates to vertebrates. Immunol Rev 2004; 198: 169-184
    • (2004) Immunol Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 3
    • 44049091618 scopus 로고    scopus 로고
    • Hidden weapons of microbial destruction in plant genomes
    • Manners JM. Hidden weapons of microbial destruction in plant genomes. Genome Biol 2007; 8: 225.
    • (2007) Genome Biol , vol.8 , pp. 225
    • Manners, J.M.1
  • 4
    • 0018820115 scopus 로고
    • Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark D, Steiner H, Rasmuson T, Boman HG. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur J Biochem 1980; 106: 7-16.
    • (1980) Eur J Biochem , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 5
    • 0020562530 scopus 로고
    • Antibacterial activity of microbicidal cationic proteins 1 and 2, natural peptide antibiotics of rabbit lung macrophages
    • Lehrer RI, Selsted ME, Szklarek D, Fleischmann J. Antibacterial activity of microbicidal cationic proteins 1 and 2, natural peptide antibiotics of rabbit lung macrophages. Infect Immun 1983; 42: 10-14
    • (1983) Infect Immun , vol.42 , pp. 10-14
    • Lehrer, R.I.1    Selsted, M.E.2    Szklarek, D.3    Fleischmann, J.4
  • 6
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci USA 1987; 84: 5449-5453
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 7
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. J Leukoc Biol 2004; 75: 39-48.
    • (2004) J Leukoc Biol , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 8
    • 0036606951 scopus 로고    scopus 로고
    • Mammalian defensins in immunity: More than just microbicidal
    • Yang D, Biragyn A, Kwak LW, Oppenheim JJ. Mammalian defensins in immunity: more than just microbicidal. Trends Immunol 2002; 23: 291-296
    • (2002) Trends Immunol , vol.23 , pp. 291-296
    • Yang, D.1    Biragyn, A.2    Kwak, L.W.3    Oppenheim, J.J.4
  • 10
    • 53149136247 scopus 로고    scopus 로고
    • Distribution of mucins and antimicrobial substances lysozyme and lactoferrin in the laryngeal subglottic region
    • Kutta H, Willer A, Steven P, Brauer L, Tsokos M, Paulsen F. Distribution of mucins and antimicrobial substances lysozyme and lactoferrin in the laryngeal subglottic region. J Anat 2008; 213: 473-481
    • (2008) J Anat , vol.213 , pp. 473-481
    • Kutta, H.1    Willer, A.2    Steven, P.3    Brauer, L.4    Tsokos, M.5    Paulsen, F.6
  • 11
    • 0030175070 scopus 로고    scopus 로고
    • Azurocidin, a natural antibiotic from human neutrophils: Expression, antimicrobial activity, and secretion
    • Almeida RP, Vanet A, Witko-Sarsat V, Melchior M, McCabe D, Gabay JE. Azurocidin, a natural antibiotic from human neutrophils: expression, antimicrobial activity, and secretion. Protein Exp Purif 1996; 7: 355-366
    • (1996) Protein Exp Purif , vol.7 , pp. 355-366
    • Almeida, R.P.1    Vanet, A.2    Witko-Sarsat, V.3    Melchior, M.4    McCabe, D.5    Gabay, J.E.6
  • 12
    • 0027407534 scopus 로고
    • Antibiotic peptides and serine protease homologs in human polymorphonuclear leukocytes: Defensins and azurocidin
    • Gabay JE, Almeida RP. Antibiotic peptides and serine protease homologs in human polymorphonuclear leukocytes: defensins and azurocidin. Curr Opin Immunol 1993; 5: 97-102.
    • (1993) Curr Opin Immunol , vol.5 , pp. 97-102
    • Gabay, J.E.1    Almeida, R.P.2
  • 13
    • 85047685350 scopus 로고    scopus 로고
    • Using antimicrobial host defense peptides as anti-infective and immunomodulatory agents
    • Kruse T, Kristensen HH. Using antimicrobial host defense peptides as anti-infective and immunomodulatory agents. Exp Rev Anti Infect Ther 2008; 6: 887-895
    • (2008) Exp Rev Anti Infect Ther , vol.6 , pp. 887-895
    • Kruse, T.1    Kristensen, H.H.2
  • 14
    • 0347755460 scopus 로고    scopus 로고
    • APD: The antimicrobial peptide database
    • Wang Z, Wang G. APD: the antimicrobial peptide database. Nucleic Acids Res 2004; 32: D590-2.
    • (2004) Nucleic Acids Res , vol.32
    • Wang, Z.1    Wang, G.2
  • 18
    • 20644432642 scopus 로고    scopus 로고
    • The nervous system and innate immunity: The neuropeptide connection
    • Brogden KA, Guthmiller JM, Salzet M, Zasloff M. The nervous system and innate immunity: the neuropeptide connection. Nat Immunol 2005; 6: 558-564
    • (2005) Nat Immunol , vol.6 , pp. 558-564
    • Brogden, K.A.1    Guthmiller, J.M.2    Salzet, M.3    Zasloff, M.4
  • 19
    • 0036835140 scopus 로고    scopus 로고
    • Cellular distribution of anionic antimicrobial peptide in normal lung and during acute pulmonary inflammation
    • Fales-Williams AJ, Brogden KA, Huffman E, Gallup JM, Ackermann MR. Cellular distribution of anionic antimicrobial peptide in normal lung and during acute pulmonary inflammation. Vet Pathol 2002; 39: 706-711
    • (2002) Vet Pathol , vol.39 , pp. 706-711
    • Fales-Williams, A.J.1    Brogden, K.A.2    Huffman, E.3    Gallup, J.M.4    Ackermann, M.R.5
  • 21
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • Durr UH, Sudheendra US, Ramamoorthy A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim Biophys Acta 2006; 1758: 1408-1425
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1408-1425
    • Durr, U.H.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 22
    • 58149263244 scopus 로고    scopus 로고
    • The roles of cathelicidin LL-37 in immune defences and novel clinical applications
    • Nijnik A, Hancock RE. The roles of cathelicidin LL-37 in immune defences and novel clinical applications. Curr Opin Hematol 2009; 16: 41-47
    • (2009) Curr Opin Hematol , vol.16 , pp. 41-47
    • Nijnik, A.1    Hancock, R.E.2
  • 23
    • 33847151791 scopus 로고    scopus 로고
    • Cation-pi interactions stabilize the structure of the antimicrobial peptide indolicidin near membranes: Molecular dynamics simulations
    • Khandelia H, Kaznessis YN. Cation-pi interactions stabilize the structure of the antimicrobial peptide indolicidin near membranes: molecular dynamics simulations. J Phys Chem B 2007; 111: 242-250
    • (2007) J Phys Chem B , vol.111 , pp. 242-250
    • Khandelia, H.1    Kaznessis, Y.N.2
  • 24
    • 0031920773 scopus 로고    scopus 로고
    • Structure and property of model peptides of proline/argininerich region in bactenecin 5
    • Niidome T, Mihara H, Oka M, Hayashi T, Saiki T, Yoshida K, et al. Structure and property of model peptides of proline/argininerich region in bactenecin 5. J Pept Res 1998; 51: 337-345
    • (1998) J Pept Res , vol.51 , pp. 337-345
    • Niidome, T.1    Mihara, H.2    Oka, M.3    Hayashi, T.4    Saiki, T.5    Yoshida, K.6
  • 25
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 2005; 3: 238-250
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 26
    • 4744347696 scopus 로고    scopus 로고
    • A cascade of 24 histatins (histatin 3 fragments) in human saliva. Suggestions for a pre-secretory sequential cleavage pathway
    • Castagnola M, Inzitari R, Rossetti DV, Olmi C, Cabras T, Piras V, et al. A cascade of 24 histatins (histatin 3 fragments) in human saliva. Suggestions for a pre-secretory sequential cleavage pathway. J Biol Chem 2004; 279: 41436-41443
    • (2004) J Biol Chem , vol.279 , pp. 41436-41443
    • Castagnola, M.1    Inzitari, R.2    Rossetti, D.V.3    Olmi, C.4    Cabras, T.5    Piras, V.6
  • 27
    • 0023888810 scopus 로고
    • Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans
    • Oppenheim FG, Xu T, McMillian FM, Levitz SM, Diamond RD, Offner GD, et al. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J Biol Chem 1988; 263: 7472-7477
    • (1988) J Biol Chem , vol.263 , pp. 7472-7477
    • Oppenheim, F.G.1    Xu, T.2    McMillian, F.M.3    Levitz, S.M.4    Diamond, R.D.5    Offner, G.D.6
  • 28
    • 0025733707 scopus 로고
    • Anticandidal activity of major human salivary histatins
    • Xu T, Levitz SM, Diamond RD, Oppenheim FG. Anticandidal activity of major human salivary histatins. Infect Immun 1991; 59: 2549-2554
    • (1991) Infect Immun , vol.59 , pp. 2549-2554
    • Xu, T.1    Levitz, S.M.2    Diamond, R.D.3    Oppenheim, F.G.4
  • 29
    • 33745698864 scopus 로고    scopus 로고
    • Defensins in innate antiviral immunity
    • Klotman ME, Chang TL. Defensins in innate antiviral immunity. Nat Rev Immunol 2006; 6: 447-456
    • (2006) Nat Rev Immunol , vol.6 , pp. 447-456
    • Klotman, M.E.1    Chang, T.L.2
  • 30
    • 11144242839 scopus 로고    scopus 로고
    • Protegrin structure-activity relationships: Using homology models of synthetic sequences to determine structural characteristics important for activity
    • Ostberg N, Kaznessis Y. Protegrin structure-activity relationships: using homology models of synthetic sequences to determine structural characteristics important for activity. Peptides 2005; 26: 197-206.
    • (2005) Peptides , vol.26 , pp. 197-206
    • Ostberg, N.1    Kaznessis, Y.2
  • 31
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy W, Takase M, Wakabayashi H, Kawase K, Tomita M. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J Appl Bacteriol 1992; 73: 472-479
    • (1992) J Appl Bacteriol , vol.73 , pp. 472-479
    • Bellamy, W.1    Takase, M.2    Wakabayashi, H.3    Kawase, K.4    Tomita, M.5
  • 32
    • 0037725162 scopus 로고    scopus 로고
    • Potassium efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane
    • Mosc
    • Viejo-Diaz M, Andres MT, Perez-Gil J, Sanchez M, Fierro JF. Potassium efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane. Biochemistry (Mosc) 2003; 68: 217-227
    • (2003) Biochemistry , vol.68 , pp. 217-227
    • Viejo-Diaz, M.1    Andres, M.T.2    Perez-Gil, J.3    Sanchez, M.4    Fierro, J.F.5
  • 33
    • 33845972609 scopus 로고    scopus 로고
    • Composition effect on peptide interaction with lipids and bacteria: Variants of C3a peptide CNY21
    • Ringstad L, Andersson Nordahl E, Schmidtchen A, Malmsten M. Composition effect on peptide interaction with lipids and bacteria: variants of C3a peptide CNY21. Biophys J 2007; 92: 87-98.
    • (2007) Biophys J , vol.92 , pp. 87-98
    • Ringstad, L.1    Andersson Nordahl, E.2    Schmidtchen, A.3    Malmsten, M.4
  • 35
    • 0036893696 scopus 로고    scopus 로고
    • Antimicrobial peptides from human platelets
    • Tang YQ, Yeaman MR, Selsted ME. Antimicrobial peptides from human platelets. Infect Immun 2002; 70: 6524-6533
    • (2002) Infect Immun , vol.70 , pp. 6524-6533
    • Tang, Y.Q.1    Yeaman, M.R.2    Selsted, M.E.3
  • 37
    • 0038468340 scopus 로고    scopus 로고
    • Antimicrobial chromogranins and proenkephalin-A-derived peptides: Antibacterial and antifungal activities of chromogranins and proenkephalin-A-derived peptides
    • Metz-Boutigue MH, Goumon Y, Strub JM, Lugardon K, Aunis D. Antimicrobial chromogranins and proenkephalin-A-derived peptides: Antibacterial and antifungal activities of chromogranins and proenkephalin-A-derived peptides. Ann NY Acad Sci 2003; 992: 168-178
    • (2003) Ann NY Acad Sci , vol.992 , pp. 168-178
    • Metz-Boutigue, M.H.1    Goumon, Y.2    Strub, J.M.3    Lugardon, K.4    Aunis, D.5
  • 38
    • 34748844591 scopus 로고    scopus 로고
    • Antimicrobial peptides: Natural effectors of the innate immune system
    • Radek K, Gallo R. Antimicrobial peptides: natural effectors of the innate immune system. Semin Immunopathol 2007; 29: 27-43.
    • (2007) Semin Immunopathol , vol.29 , pp. 27-43
    • Radek, K.1    Gallo, R.2
  • 40
    • 33751549487 scopus 로고    scopus 로고
    • Paneth cells: Leukocyte-like mediators of innate immunity in the intestine
    • Keshav S. Paneth cells: leukocyte-like mediators of innate immunity in the intestine. J Leukoc Biol 2006; 80: 500-508
    • (2006) J Leukoc Biol , vol.80 , pp. 500-508
    • Keshav, S.1
  • 41
    • 33645051715 scopus 로고    scopus 로고
    • Antimicrobial skin peptides and proteins
    • Schroder JM, Harder J. Antimicrobial skin peptides and proteins. Cell Mol Life Sci 2006; 63: 469-486
    • (2006) Cell Mol Life Sci , vol.63 , pp. 469-486
    • Schroder, J.M.1    Harder, J.2
  • 42
    • 34247117757 scopus 로고    scopus 로고
    • Cationic host defence peptides: Innate immune regulatory peptides as a novel approach for treating infections
    • Mookherjee N, Hancock RE. Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections. Cell Mol Life Sci 2007; 64: 922-933
    • (2007) Cell Mol Life Sci , vol.64 , pp. 922-933
    • Mookherjee, N.1    Hancock, R.E.2
  • 44
    • 0032491406 scopus 로고    scopus 로고
    • Characterization of antibacterial COOH-terminal proenkephalin-A-derived peptides (PEAP) in infectious fluids. Importance of enkelytin, the antibacterial PEAP209-237 secreted by stimulated chromaffin cells
    • Goumon Y, Lugardon K, Kieffer B, Lefevre JF, Van Dorsselaer A, Aunis D, et al. Characterization of antibacterial COOH-terminal proenkephalin-A-derived peptides (PEAP) in infectious fluids. Importance of enkelytin, the antibacterial PEAP209-237 secreted by stimulated chromaffin cells. J Biol Chem 1998; 273: 29847-29856
    • (1998) J Biol Chem , vol.273 , pp. 29847-29856
    • Goumon, Y.1    Lugardon, K.2    Kieffer, B.3    Lefevre, J.F.4    Van Dorsselaer, A.5    Aunis, D.6
  • 45
    • 0034646659 scopus 로고    scopus 로고
    • Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin a
    • Lugardon K, Raffner R, Goumon Y, Corti A, Delmas A, Bulet P, et al. Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. J Biol Chem 2000; 275: 10745-10753
    • (2000) J Biol Chem , vol.275 , pp. 10745-10753
    • Lugardon, K.1    Raffner, R.2    Goumon, Y.3    Corti, A.4    Delmas, A.5    Bulet, P.6
  • 46
    • 85047690831 scopus 로고
    • Processing of chromogranin B in bovine adrenal medulla. Identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity
    • Strub JM, Garcia-Sablone P, Lonning K, Taupenot L, Hubert P, Van Dorsselaer A, et al. Processing of chromogranin B in bovine adrenal medulla. Identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity. Eur J Biochem 1995; 229: 356-368
    • (1995) Eur J Biochem , vol.229 , pp. 356-368
    • Strub, J.M.1    Garcia-Sablone, P.2    Lonning, K.3    Taupenot, L.4    Hubert, P.5    Van Dorsselaer, A.6
  • 47
    • 0346366980 scopus 로고    scopus 로고
    • Activation of Toll-like receptor 2 on human tracheobronchial epithelial cells induces the antimicrobial peptide human beta defensin-2
    • Hertz CJ, Wu Q, Porter EM, Zhang YJ, Weismuller KH, Godowski PJ, et al. Activation of Toll-like receptor 2 on human tracheobronchial epithelial cells induces the antimicrobial peptide human beta defensin-2. J Immunol 2003; 171: 6820-6826
    • (2003) J Immunol , vol.171 , pp. 6820-6826
    • Hertz, C.J.1    Wu, Q.2    Porter, E.M.3    Zhang, Y.J.4    Weismuller, K.H.5    Godowski, P.J.6
  • 48
    • 0037218616 scopus 로고    scopus 로고
    • By IL-1 signaling, monocyte-derived cells dramatically enhance the epidermal antimicrobial response to lipopolysaccharide
    • Liu L, Roberts AA, Ganz T. By IL-1 signaling, monocyte-derived cells dramatically enhance the epidermal antimicrobial response to lipopolysaccharide. J Immunol 2003; 170: 575-580
    • (2003) J Immunol , vol.170 , pp. 575-580
    • Liu, L.1    Roberts, A.A.2    Ganz, T.3
  • 49
    • 6344225825 scopus 로고    scopus 로고
    • β-defensin-2 expression is regulated by TLR signaling in intestinal epithelial cells
    • Vora P, Youdim A, Thomas LS, Fukata M, Tesfay SY, Lukasek K, et al. β-defensin-2 expression is regulated by TLR signaling in intestinal epithelial cells. J Immunol 2004; 173: 5398-5405
    • (2004) J Immunol , vol.173 , pp. 5398-5405
    • Vora, P.1    Youdim, A.2    Thomas, L.S.3    Fukata, M.4    Tesfay, S.Y.5    Lukasek, K.6
  • 50
    • 0242332115 scopus 로고    scopus 로고
    • Bifidobacterium cell wall proteins induced β-defensin 2 mRNA expression in human intestinal epithelial cells
    • Sichuan Da Xue Xue Bao Yi Xue Ban
    • Wang G, Feng Y, Wang Y, Huang N, Wu Q, Wang B. Bifidobacterium cell wall proteins induced β-defensin 2 mRNA expression in human intestinal epithelial cells. Sichuan Da Xue Xue Bao Yi Xue Ban 2003; 34: 622-624
    • (2003) Sichuan Da Xue Xue Bao Yi Xue Ban , vol.34 , pp. 622-624
    • Wang, G.1    Feng, Y.2    Wang, Y.3    Huang, N.4    Wu, Q.5    Wang, B.6
  • 53
    • 33744965671 scopus 로고    scopus 로고
    • Nucleotide-binding oligomerization domain-1 and epidermal growth factor receptor: Critical regulators of beta-defensins during Helicobacter pylori infection
    • Boughan PK, Argent RH, Body-Malapel M, Park JH, Ewings KE, Bowie AG, et al. Nucleotide-binding oligomerization domain-1 and epidermal growth factor receptor: critical regulators of beta-defensins during Helicobacter pylori infection. J Biol Chem 2006; 281: 11637-11648
    • (2006) J Biol Chem , vol.281 , pp. 11637-11648
    • Boughan, P.K.1    Argent, R.H.2    Body-Malapel, M.3    Park, J.H.4    Ewings, K.E.5    Bowie, A.G.6
  • 54
    • 0035399769 scopus 로고    scopus 로고
    • Toll receptors in innate immunity
    • Imler JL, Hoffmann JA. Toll receptors in innate immunity. Trends Cell Biol 2001; 11: 304-311
    • (2001) Trends Cell Biol , vol.11 , pp. 304-311
    • Imler, J.L.1    Hoffmann, J.A.2
  • 55
    • 65649108429 scopus 로고    scopus 로고
    • The critical role of Toll-like receptor signaling pathways in the induction and progression of autoimmune diseases
    • Li M, Zhou Y, Feng G, Su SB. The critical role of Toll-like receptor signaling pathways in the induction and progression of autoimmune diseases. Curr Mol Med 2009; 9: 365-374
    • (2009) Curr Mol Med , vol.9 , pp. 365-374
    • Li, M.1    Zhou, Y.2    Feng, G.3    Su, S.B.4
  • 56
    • 5444262511 scopus 로고    scopus 로고
    • Toll-like receptor control of the adaptive immune responses
    • Iwasaki A, Medzhitov R. Toll-like receptor control of the adaptive immune responses. Nat Immunol 2004; 5: 987-995
    • (2004) Nat Immunol , vol.5 , pp. 987-995
    • Iwasaki, A.1    Medzhitov, R.2
  • 57
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S, Uematsu S, Takeuchi O. Pathogen recognition and innate immunity. Cell 2006; 124: 783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 58
    • 52649119389 scopus 로고    scopus 로고
    • Innate immune responses in murine pleural mesothelial cells: Toll-like receptor-2 dependent induction of β-defensin-2 by staphylococcal peptidoglycan
    • Hussain T, Nasreen N, Lai Y, Bellew BF, Antony VB, Mohammed KA. Innate immune responses in murine pleural mesothelial cells: Toll-like receptor-2 dependent induction of β-defensin-2 by staphylococcal peptidoglycan. Am J Physiol Lung Cell Mol Physiol 2008; 295: L461-70.
    • (2008) Am J Physiol Lung Cell Mol Physiol , vol.295
    • Hussain, T.1    Nasreen, N.2    Lai, Y.3    Bellew, B.F.4    Antony, V.B.5    Mohammed, K.A.6
  • 60
    • 67649083645 scopus 로고    scopus 로고
    • The antimicrobial peptide HBD-2 and the Toll-like receptors-2 and -4 are induced in synovial membranes in case of septic arthritis
    • Varoga D, Klostermeier E, Paulsen F, Wruck C, Lippross S, Brandenburg LO, et al. The antimicrobial peptide HBD-2 and the Toll-like receptors-2 and -4 are induced in synovial membranes in case of septic arthritis. Virchows Arch 2009; 454: 685-694
    • (2009) Virchows Arch , vol.454 , pp. 685-694
    • Varoga, D.1    Klostermeier, E.2    Paulsen, F.3    Wruck, C.4    Lippross, S.5    Brandenburg, L.O.6
  • 61
    • 67349197815 scopus 로고    scopus 로고
    • Human β-defensin-2 and psoriasin are overexpressed in lesions of acne inversa
    • Schlapbach C, Yawalkar N, Hunger RE. Human β-defensin-2 and psoriasin are overexpressed in lesions of acne inversa. J Am Acad Dermatol 2009; 61: 58-65.
    • (2009) J Am Acad Dermatol , vol.61 , pp. 58-65
    • Schlapbach, C.1    Yawalkar, N.2    Hunger, R.E.3
  • 62
    • 59949092583 scopus 로고    scopus 로고
    • The antimicrobial protein psoriasin (S100A7) is upregulated in atopic dermatitis and after experimental skin barrier disruption
    • Glaser R, Meyer-Hoffert U, Harder J, Cordes J, Wittersheim M, Kobliakova J, et al. The antimicrobial protein psoriasin (S100A7) is upregulated in atopic dermatitis and after experimental skin barrier disruption. J Invest Dermatol 2009; 129: 641-649
    • (2009) J Invest Dermatol , vol.129 , pp. 641-649
    • Glaser, R.1    Meyer-Hoffert, U.2    Harder, J.3    Cordes, J.4    Wittersheim, M.5    Kobliakova, J.6
  • 63
    • 16644382075 scopus 로고    scopus 로고
    • RIG-I: Critical regulator for virus-induced innate immunity
    • Yoneyama M, Fujita T. RIG-I: critical regulator for virus-induced innate immunity. Tanpakushitsu Kakusan Koso 2004; 49: 2571-2578
    • (2004) Tanpakushitsu Kakusan Koso , vol.49 , pp. 2571-2578
    • Yoneyama, M.1    Fujita, T.2
  • 64
    • 35348932070 scopus 로고    scopus 로고
    • Intracellular NOD-like receptors in host defense and disease
    • Kanneganti TD, Lamkanfi M, Nunez G. Intracellular NOD-like receptors in host defense and disease. Immunity 2007; 27: 549-559
    • (2007) Immunity , vol.27 , pp. 549-559
    • Kanneganti, T.D.1    Lamkanfi, M.2    Nunez, G.3
  • 65
    • 37349070287 scopus 로고    scopus 로고
    • The Paneth cell alpha-defensin deficiency of ileal Crohn's disease is linked to Wnt/Tcf-4
    • Wehkamp J, Wang G, Kubler I, Nuding S, Gregorieff A, Schnabel A, et al. The Paneth cell alpha-defensin deficiency of ileal Crohn's disease is linked to Wnt/Tcf-4. J Immunol 2007; 179: 3109-3118
    • (2007) J Immunol , vol.179 , pp. 3109-3118
    • Wehkamp, J.1    Wang, G.2    Kubler, I.3    Nuding, S.4    Gregorieff, A.5    Schnabel, A.6
  • 66
    • 48349087831 scopus 로고    scopus 로고
    • Antimicrobial peptides and the skin immune defense system
    • Schauber J, Gallo RL. Antimicrobial peptides and the skin immune defense system. J Allergy Clin Immunol 2008; 122: 261-266
    • (2008) J Allergy Clin Immunol , vol.122 , pp. 261-266
    • Schauber, J.1    Gallo, R.L.2
  • 67
    • 0034998495 scopus 로고    scopus 로고
    • Induction of human beta-defensin-2 expression in human astrocytes by lipopolysaccharide and cytokines
    • Hao HN, Zhao J, Lotoczky G, Grever WE, Lyman WD. Induction of human beta-defensin-2 expression in human astrocytes by lipopolysaccharide and cytokines. J Neurochem 2001; 77: 1027-1035
    • (2001) J Neurochem , vol.77 , pp. 1027-1035
    • Hao, H.N.1    Zhao, J.2    Lotoczky, G.3    Grever, W.E.4    Lyman, W.D.5
  • 68
    • 50849111787 scopus 로고    scopus 로고
    • Natural immunity first line defense. New treatment against infections and autoimmune diseases in sight
    • Bergman P, Gudmundsson GH, Agerberth B. Natural immunity first line defense. New treatment against infections and autoimmune diseases in sight. Lakartidningen 2008; 105: 2254-2259
    • (2008) Lakartidningen , vol.105 , pp. 2254-2259
    • Bergman, P.1    Gudmundsson, G.H.2    Agerberth, B.3
  • 69
    • 0027144508 scopus 로고
    • Bactenecin, a leukocytic antimicrobial peptide, is cytotoxic to neuronal and glial cells
    • Radermacher SW, Schoop VM, Schluesener HJ. Bactenecin, a leukocytic antimicrobial peptide, is cytotoxic to neuronal and glial cells. J Neurosci Res 1993; 36: 657-662
    • (1993) J Neurosci Res , vol.36 , pp. 657-662
    • Radermacher, S.W.1    Schoop, V.M.2    Schluesener, H.J.3
  • 70
    • 49049122099 scopus 로고    scopus 로고
    • Microbial challenge promotes the regenerative process of the injured central nervous system of the medicinal leech by inducing the synthesis of antimicrobial peptides in neurons and microglia
    • Schikorski D, Cuvillier-Hot V, Leippe M, Boidin-Wichlacz C, Slomianny C, Macagno E, et al. Microbial challenge promotes the regenerative process of the injured central nervous system of the medicinal leech by inducing the synthesis of antimicrobial peptides in neurons and microglia. J Immunol 2008; 181: 1083-1095
    • (2008) J Immunol , vol.181 , pp. 1083-1095
    • Schikorski, D.1    Cuvillier-Hot, V.2    Leippe, M.3    Boidin-Wichlacz, C.4    Slomianny, C.5    Macagno, E.6
  • 72
    • 42649142893 scopus 로고    scopus 로고
    • The role of the multifunctional peptide LL-37 in host defense
    • Kai-Larsen Y, Agerberth B. The role of the multifunctional peptide LL-37 in host defense. Front Biosci 2008; 13: 3760-3767
    • (2008) Front Biosci , vol.13 , pp. 3760-3767
    • Kai-Larsen, Y.1    Agerberth, B.2
  • 73
    • 0033569408 scopus 로고    scopus 로고
    • β-defensins: Linking innate and adaptive immunity through dendritic and T cell CCR6
    • Yang D, Chertov O, Bykovskaia SN, Chen Q, Buffo MJ, Shogan J, et al. β-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
  • 74
    • 0033566011 scopus 로고    scopus 로고
    • Neutrophil defensins induce histamine secretion from mast cells: Mechanisms of action
    • Befus AD, Mowat C, Gilchrist M, Hu J, Solomon S, Bateman A. Neutrophil defensins induce histamine secretion from mast cells: mechanisms of action. J Immunol 1999; 163: 947-953
    • (1999) J Immunol , vol.163 , pp. 947-953
    • Befus, A.D.1    Mowat, C.2    Gilchrist, M.3    Hu, J.4    Solomon, S.5    Bateman, A.6
  • 75
    • 49449114876 scopus 로고    scopus 로고
    • Antibacterial chemokines - Actors in both innate and adaptive immunity
    • Eliasson M, Egesten A. Antibacterial chemokines - actors in both innate and adaptive immunity. Contrib Microbiol 2008; 15: 101-117
    • (2008) Contrib Microbiol , vol.15 , pp. 101-117
    • Eliasson, M.1    Egesten, A.2
  • 76
    • 0033003889 scopus 로고    scopus 로고
    • Elafin (elastase-specific inhibitor) has antimicrobial activity against gram-positive and gram-negative respiratory pathogens
    • Simpson AJ, Maxwell AI, Govan JR, Haslett C, Sallenave JM. Elafin (elastase-specific inhibitor) has antimicrobial activity against gram-positive and gram-negative respiratory pathogens. FEBS Lett 1999; 452: 309-313
    • (1999) FEBS Lett , vol.452 , pp. 309-313
    • Simpson, A.J.1    Maxwell, A.I.2    Govan, J.R.3    Haslett, C.4    Sallenave, J.M.5
  • 77
    • 19744361985 scopus 로고    scopus 로고
    • Antimicrobial activity of murine lung cells against Staphylococcus aureus is increased in vitro and in vivo after elafin gene transfer
    • McMichael JW, Maxwell AI, Hayashi K, Taylor K, Wallace WA, Govan JR, et al. Antimicrobial activity of murine lung cells against Staphylococcus aureus is increased in vitro and in vivo after elafin gene transfer. Infect Immun 2005; 73: 3609-3617
    • (2005) Infect Immun , vol.73 , pp. 3609-3617
    • McMichael, J.W.1    Maxwell, A.I.2    Hayashi, K.3    Taylor, K.4    Wallace, W.A.5    Govan, J.R.6
  • 78
    • 18244405296 scopus 로고    scopus 로고
    • The antimicrobial antiproteinase elafin binds to lipopolysaccharide and modulates macrophage responses
    • McMichael JW, Roghanian A, Jiang L, Ramage R, Sallenave JM. The antimicrobial antiproteinase elafin binds to lipopolysaccharide and modulates macrophage responses. Am J Respir Cell Mol Biol 2005; 32: 443-452
    • (2005) Am J Respir Cell Mol Biol , vol.32 , pp. 443-452
    • McMichael, J.W.1    Roghanian, A.2    Jiang, L.3    Ramage, R.4    Sallenave, J.M.5
  • 79
    • 36848998523 scopus 로고    scopus 로고
    • Beyond inflammation: Airway epithelial cells are at the interface of innate and adaptive immunity
    • Kato A, Schleimer RP. Beyond inflammation: airway epithelial cells are at the interface of innate and adaptive immunity. Curr Opin Immunol 2007; 19: 711-720
    • (2007) Curr Opin Immunol , vol.19 , pp. 711-720
    • Kato, A.1    Schleimer, R.P.2
  • 80
    • 34548457793 scopus 로고    scopus 로고
    • NOD2 and defensins: Translating innate to adaptive immunity in Crohn's disease
    • Peyrin-Biroulet L, Chamaillard M. NOD2 and defensins: translating innate to adaptive immunity in Crohn's disease. J Endotoxin Res 2007; 13: 135-139
    • (2007) J Endotoxin Res , vol.13 , pp. 135-139
    • Peyrin-Biroulet, L.1    Chamaillard, M.2
  • 81
    • 34748850100 scopus 로고    scopus 로고
    • The skin barrier as an innate immune element
    • Elias PM. The skin barrier as an innate immune element. Semin Immunopathol 2007; 29: 3-14.
    • (2007) Semin Immunopathol , vol.29 , pp. 3-14
    • Elias, P.M.1
  • 82
    • 0015105597 scopus 로고
    • Isolation and characterization of human skin lysozyme
    • Ogawa H, Miyazaki H, Kimura M. Isolation and characterization of human skin lysozyme. J Invest Dermatol 1971; 57: 111-116
    • (1971) J Invest Dermatol , vol.57 , pp. 111-116
    • Ogawa, H.1    Miyazaki, H.2    Kimura, M.3
  • 85
    • 0027232811 scopus 로고
    • Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy W, Wakabayashi H, Takase M, Kawase K, Shimamura S, Tomita M. Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin. Med Microbiol Immunol 1993; 182: 97-105.
    • (1993) Med Microbiol Immunol , vol.182 , pp. 97-105
    • Bellamy, W.1    Wakabayashi, H.2    Takase, M.3    Kawase, K.4    Shimamura, S.5    Tomita, M.6
  • 86
    • 28444462150 scopus 로고    scopus 로고
    • Lactoferrin: A modulator of immune and inflammatory responses
    • Legrand D, Elass E, Carpentier M, Mazurier J. Lactoferrin: a modulator of immune and inflammatory responses. Cell Mol Life Sci 2005; 62: 2549-2559
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2549-2559
    • Legrand, D.1    Elass, E.2    Carpentier, M.3    Mazurier, J.4
  • 87
    • 20444427567 scopus 로고    scopus 로고
    • Modulation of expression of superantigens by human transferrin and lactoferrin: A novel mechanism in host-Streptococcus interactions
    • Kansal RG, Aziz RK, Kotb M. Modulation of expression of superantigens by human transferrin and lactoferrin: a novel mechanism in host-Streptococcus interactions. J Infect Dis 2005; 191: 2121-2129
    • (2005) J Infect Dis , vol.191 , pp. 2121-2129
    • Kansal, R.G.1    Aziz, R.K.2    Kotb, M.3
  • 89
    • 33646830838 scopus 로고    scopus 로고
    • Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L
    • Baechle D, Flad T, Cansier A, Steffen H, Schittek B, Tolson J, et al. Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L. J Biol Chem 2006; 281: 5406-5415
    • (2006) J Biol Chem , vol.281 , pp. 5406-5415
    • Baechle, D.1    Flad, T.2    Cansier, A.3    Steffen, H.4    Schittek, B.5    Tolson, J.6
  • 90
    • 33846079739 scopus 로고    scopus 로고
    • The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci
    • Lai Y, Villaruz AE, Li M, Cha DJ, Sturdevant DE, Otto M. The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci. Mol Microbiol 2007; 63: 497-506.
    • (2007) Mol Microbiol , vol.63 , pp. 497-506
    • Lai, Y.1    Villaruz, A.E.2    Li, M.3    Cha, D.J.4    Sturdevant, D.E.5    Otto, M.6
  • 91
    • 33644662743 scopus 로고    scopus 로고
    • Generation of multiple stable dermcidin-derived antimicrobial peptides in sweat of different body sites
    • Rieg S, Seeber S, Steffen H, Humeny A, Kalbacher H, Stevanovic S, et al. Generation of multiple stable dermcidin-derived antimicrobial peptides in sweat of different body sites. J Invest Dermatol 2006; 126: 354-365
    • (2006) J Invest Dermatol , vol.126 , pp. 354-365
    • Rieg, S.1    Seeber, S.2    Steffen, H.3    Humeny, A.4    Kalbacher, H.5    Stevanovic, S.6
  • 92
    • 33746886670 scopus 로고    scopus 로고
    • Naturally processed dermcidin-derived peptides do not permeabilize bacterial membranes and kill microorganisms irrespective of their charge
    • Steffen H, Rieg S, Wiedemann I, Kalbacher H, Deeg M, Sahl HG, et al. Naturally processed dermcidin-derived peptides do not permeabilize bacterial membranes and kill microorganisms irrespective of their charge. Antimicrob Agents Chemother 2006; 50: 2608-2620
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 2608-2620
    • Steffen, H.1    Rieg, S.2    Wiedemann, I.3    Kalbacher, H.4    Deeg, M.5    Sahl, H.G.6
  • 93
    • 34547172207 scopus 로고    scopus 로고
    • Proteomic analysis of human cervico-vaginal fluid
    • Shaw JL, Smith CR, Diamandis EP. Proteomic analysis of human cervico-vaginal fluid. J Proteome Res 2007; 6: 2859-2865
    • (2007) J Proteome Res , vol.6 , pp. 2859-2865
    • Shaw, J.L.1    Smith, C.R.2    Diamandis, E.P.3
  • 95
    • 33845351359 scopus 로고    scopus 로고
    • The RNase a superfamily: Generation of diversity and innate host defense
    • Dyer KD, Rosenberg HF. The RNase a superfamily: generation of diversity and innate host defense. Mol Divers 2006; 10: 585-597
    • (2006) Mol Divers , vol.10 , pp. 585-597
    • Dyer, K.D.1    Rosenberg, H.F.2
  • 96
    • 0024385410 scopus 로고
    • Antibacterial properties of eosinophil major basic protein and eosinophil cationic protein
    • Lehrer RI, Szklarek D, Barton A, Ganz T, Hamann KJ, Gleich GJ. Antibacterial properties of eosinophil major basic protein and eosinophil cationic protein. J Immunol 1989; 142: 4428-4434
    • (1989) J Immunol , vol.142 , pp. 4428-4434
    • Lehrer, R.I.1    Szklarek, D.2    Barton, A.3    Ganz, T.4    Hamann, K.J.5    Gleich, G.J.6
  • 97
    • 0037195896 scopus 로고    scopus 로고
    • RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin
    • Harder J, Schroder JM. RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin. J Biol Chem 2002; 277: 46779-46784
    • (2002) J Biol Chem , vol.277 , pp. 46779-46784
    • Harder, J.1    Schroder, J.M.2
  • 98
    • 70349745535 scopus 로고    scopus 로고
    • Degradation by stratum corneum proteases prevents endogenous RNase inhibitor from blocking antimicrobial activities of RNase 5 and RNase 7
    • Abtin A, Eckhart L, Mildner M, Ghannadan M, Harder J, Schroder JM, et al. Degradation by stratum corneum proteases prevents endogenous RNase inhibitor from blocking antimicrobial activities of RNase 5 and RNase 7. J Invest Dermatol 2009; 129: 2193-2201
    • (2009) J Invest Dermatol , vol.129 , pp. 2193-2201
    • Abtin, A.1    Eckhart, L.2    Mildner, M.3    Ghannadan, M.4    Harder, J.5    Schroder, J.M.6
  • 99
    • 0030610328 scopus 로고    scopus 로고
    • Immunohistochemical localization of the Ca2+ binding S100 proteins in normal human skin and melanocytic lesions
    • Boni R, Burg G, Doguoglu A, Ilg EC, Schafer BW, Muller B, et al. Immunohistochemical localization of the Ca2+ binding S100 proteins in normal human skin and melanocytic lesions. Br J Dermatol 1997; 137: 39-43.
    • (1997) Br J Dermatol , vol.137 , pp. 39-43
    • Boni, R.1    Burg, G.2    Doguoglu, A.3    Ilg, E.C.4    Schafer, B.W.5    Muller, B.6
  • 100
    • 0037406261 scopus 로고    scopus 로고
    • S100 protein subcellular localization during epidermal differentiation and psoriasis
    • Broome AM, Ryan D, Eckert RL. S100 protein subcellular localization during epidermal differentiation and psoriasis. J Histochem Cytochem 2003; 51: 675-685
    • (2003) J Histochem Cytochem , vol.51 , pp. 675-685
    • Broome, A.M.1    Ryan, D.2    Eckert, R.L.3
  • 101
    • 0028224044 scopus 로고
    • Immunohistochemical localization of calcium-binding proteins in the human cutaneous sensory corpuscles
    • Del Valle ME, Vazquez E, Represa J, Malinovsky L, Vega JA. Immunohistochemical localization of calcium-binding proteins in the human cutaneous sensory corpuscles. Neurosci Lett 1994; 168: 247-250
    • (1994) Neurosci Lett , vol.168 , pp. 247-250
    • Del Valle, M.E.1    Vazquez, E.2    Represa, J.3    Malinovsky, L.4    Vega, J.A.5
  • 103
    • 15444380167 scopus 로고    scopus 로고
    • Expression patterns of S100A7 (psoriasin) and S100A9 (calgranulin-B) in keratinocyte differentiation
    • Martinsson H, Yhr M, Enerback C. Expression patterns of S100A7 (psoriasin) and S100A9 (calgranulin-B) in keratinocyte differentiation. Exp Dermatol 2005; 14: 161-168
    • (2005) Exp Dermatol , vol.14 , pp. 161-168
    • Martinsson, H.1    Yhr, M.2    Enerback, C.3
  • 105
    • 44849110924 scopus 로고    scopus 로고
    • Microbicidal protein psoriasin is a multifunctional modulator of neutrophil activation
    • Zheng Y, Niyonsaba F, Ushio H, Ikeda S, Nagaoka I, Okumura K, et al. Microbicidal protein psoriasin is a multifunctional modulator of neutrophil activation. Immunology 2008; 124: 357-367
    • (2008) Immunology , vol.124 , pp. 357-367
    • Zheng, Y.1    Niyonsaba, F.2    Ushio, H.3    Ikeda, S.4    Nagaoka, I.5    Okumura, K.6
  • 106
    • 0037388020 scopus 로고    scopus 로고
    • In human epidermis, beta-defensin 2 is packaged in lamellar bodies
    • Oren A, Ganz T, Liu L, Meerloo T. In human epidermis, beta-defensin 2 is packaged in lamellar bodies. Exp Mol Pathol 2003; 74: 180-182
    • (2003) Exp Mol Pathol , vol.74 , pp. 180-182
    • Oren, A.1    Ganz, T.2    Liu, L.3    Meerloo, T.4
  • 107
    • 3442893805 scopus 로고    scopus 로고
    • Human β-defensin-2 expression is increased in chronic wounds
    • Butmarc J, Yufit T, Carson P, Falanga V. Human β-defensin-2 expression is increased in chronic wounds. Wound Repair Regen 2004; 12: 439-443
    • (2004) Wound Repair Regen , vol.12 , pp. 439-443
    • Butmarc, J.1    Yufit, T.2    Carson, P.3    Falanga, V.4
  • 109
    • 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 1998; 95: 9541-9546
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9541-9546
    • Bals, R.1    Wang, X.2    Zasloff, M.3    Wilson, J.M.4
  • 110
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz T. Defensins: antimicrobial peptides of innate immunity. Nat Rev Immunol 2003; 3: 710-720
    • (2003) Nat Rev Immunol , vol.3 , pp. 710-720
    • Ganz, T.1
  • 111
    • 47049124548 scopus 로고    scopus 로고
    • IL-12, IL-23, and IL-27 enhance human beta-defensin-2 production in human keratinocytes
    • Kanda N, Watanabe S. IL-12, IL-23, and IL-27 enhance human beta-defensin-2 production in human keratinocytes. Eur J Immunol 2008; 38: 1287-1296
    • (2008) Eur J Immunol , vol.38 , pp. 1287-1296
    • Kanda, N.1    Watanabe, S.2
  • 112
    • 17044367481 scopus 로고    scopus 로고
    • Differential regulation of β-defensin expression in human skin by microbial stimuli
    • Sorensen OE, Thapa DR, Rosenthal A, Liu L, Roberts AA, Ganz T. Differential regulation of β-defensin expression in human skin by microbial stimuli. J Immunol 2005; 174: 4870-4879
    • (2005) J Immunol , vol.174 , pp. 4870-4879
    • Sorensen, O.E.1    Thapa, D.R.2    Rosenthal, A.3    Liu, L.4    Roberts, A.A.5    Ganz, T.6
  • 113
    • 0034946112 scopus 로고    scopus 로고
    • Expression of the peptide antibiotics human beta defensin-1 and human beta defensin-2 in normal human skin
    • Ali RS, Falconer A, Ikram M, Bissett CE, Cerio R, Quinn AG. Expression of the peptide antibiotics human beta defensin-1 and human beta defensin-2 in normal human skin. J Invest Dermatol 2001; 117: 106-111
    • (2001) J Invest Dermatol , vol.117 , pp. 106-111
    • Ali, R.S.1    Falconer, A.2    Ikram, M.3    Bissett, C.E.4    Cerio, R.5    Quinn, A.G.6
  • 114
    • 4143097141 scopus 로고    scopus 로고
    • Differential gene induction of human β-defensins (hBD-1, -2, -3, and -4) in keratinocytes is inhibited by retinoic acid
    • Harder J, Meyer-Hoffert U, Wehkamp K, Schwichtenberg L, Schroder JM. Differential gene induction of human β-defensins (hBD-1, -2, -3, and -4) in keratinocytes is inhibited by retinoic acid. J Invest Dermatol 2004; 123: 522-529
    • (2004) J Invest Dermatol , vol.123 , pp. 522-529
    • Harder, J.1    Meyer-Hoffert, U.2    Wehkamp, K.3    Schwichtenberg, L.4    Schroder, J.M.5
  • 115
    • 43149084824 scopus 로고    scopus 로고
    • Isolation and short-term culture of primary keratinocytes, hair follicle populations and dermal cells from newborn mice and keratinocytes from adult mice for in vitro analysis and for grafting to immunodeficient mice
    • Lichti U, Anders J, Yuspa SH. Isolation and short-term culture of primary keratinocytes, hair follicle populations and dermal cells from newborn mice and keratinocytes from adult mice for in vitro analysis and for grafting to immunodeficient mice. Nat Prot 2008; 3: 799-810.
    • (2008) Nat Prot , vol.3 , pp. 799-810
    • Lichti, U.1    Anders, J.2    Yuspa, S.H.3
  • 116
    • 33745849146 scopus 로고    scopus 로고
    • Injury-induced innate immune response in human skin mediated by transactivation of the epidermal growth factor receptor
    • Sorensen OE, Thapa DR, Roupe KM, Valore EV, Sjobring U, Roberts AA, et al. Injury-induced innate immune response in human skin mediated by transactivation of the epidermal growth factor receptor. J Clin Invest 2006; 116: 1878-1885
    • (2006) J Clin Invest , vol.116 , pp. 1878-1885
    • Sorensen, O.E.1    Thapa, D.R.2    Roupe, K.M.3    Valore, E.V.4    Sjobring, U.5    Roberts, A.A.6
  • 117
    • 0001475281 scopus 로고    scopus 로고
    • Identification of a novel, multifunctional β-defensin (human β-defensin 3) with specific antimicrobial activity. Its interaction with plasma membranes of Xenopus oocytes and the induction of macrophage chemoattraction
    • Garcia JR, Jaumann F, Schulz S, Krause A, Rodriguez-Jimenez J, Forssmann U, et al. Identification of a novel, multifunctional β-defensin (human β-defensin 3) with specific antimicrobial activity. Its interaction with plasma membranes of Xenopus oocytes and the induction of macrophage chemoattraction. Cell Tissue Res 2001; 306: 257-264
    • (2001) Cell Tissue Res , vol.306 , pp. 257-264
    • Garcia, J.R.1    Jaumann, F.2    Schulz, S.3    Krause, A.4    Rodriguez-Jimenez, J.5    Forssmann, U.6
  • 118
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human β -defensin-3, a novel human inducible peptide antibiotic
    • Harder J, Bartels J, Christophers E, Schroder JM. Isolation and characterization of human β -defensin-3, a novel human inducible peptide antibiotic. J Biol Chem 2001; 276: 5707-5713
    • (2001) J Biol Chem , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schroder, J.M.4
  • 119
    • 33847040438 scopus 로고    scopus 로고
    • Antimicrobial peptides human β-defensins stimulate epidermal keratinocyte migration, proliferation and production of proinflammatory cytokines and chemokines
    • Niyonsaba F, Ushio H, Nakano N, Ng W, Sayama K, Hashimoto K, et al. Antimicrobial peptides human β-defensins stimulate epidermal keratinocyte migration, proliferation and production of proinflammatory cytokines and chemokines. J Invest Dermatol 2007; 127: 594-604.
    • (2007) J Invest Dermatol , vol.127 , pp. 594-604
    • Niyonsaba, F.1    Ushio, H.2    Nakano, N.3    Ng, W.4    Sayama, K.5    Hashimoto, K.6
  • 120
    • 33645284772 scopus 로고    scopus 로고
    • Neural regulation of innate immunity: A coordinated nonspecific host response to pathogens
    • Sternberg EM. Neural regulation of innate immunity: a coordinated nonspecific host response to pathogens. Nat Rev Immunol 2006; 6: 318-328
    • (2006) Nat Rev Immunol , vol.6 , pp. 318-328
    • Sternberg, E.M.1
  • 122
    • 34247373134 scopus 로고    scopus 로고
    • Current considerations about Merkel cells
    • Lucarz A, Brand G. Current considerations about Merkel cells. Eur J Cell Biol 2007; 86: 243-251
    • (2007) Eur J Cell Biol , vol.86 , pp. 243-251
    • Lucarz, A.1    Brand, G.2
  • 123
    • 0024822597 scopus 로고
    • Immunohistochemical analysis of chromogranin a and multiple peptides in the mammalian Merkel cell: Further evidence for its paraneuronal function?
    • Hartschuh W, Weihe E, Yanaihara N. Immunohistochemical analysis of chromogranin A and multiple peptides in the mammalian Merkel cell: further evidence for its paraneuronal function? Arch Histol Cytol 1989; 52 (Suppl): 423-431
    • (1989) Arch Histol Cytol , vol.52 , Issue.SUPPL. , pp. 423-431
    • Hartschuh, W.1    Weihe, E.2    Yanaihara, N.3
  • 124
    • 0024444679 scopus 로고
    • Chromogranin a in the mammalian Merkel cell: Cellular and subcellular distribution
    • Hartschuh W, Weihe E, Egner U. Chromogranin A in the mammalian Merkel cell: cellular and subcellular distribution. J Invest Dermatol 1989; 93: 641-648
    • (1989) J Invest Dermatol , vol.93 , pp. 641-648
    • Hartschuh, W.1    Weihe, E.2    Egner, U.3
  • 126
    • 34548061243 scopus 로고    scopus 로고
    • Neuropeptide processing and its impact on melanocortin pathways
    • Pritchard LE, White A. Neuropeptide processing and its impact on melanocortin pathways. Endocrinology 2007; 148: 4201-4207
    • (2007) Endocrinology , vol.148 , pp. 4201-4207
    • Pritchard, L.E.1    White, A.2
  • 128
    • 0025065115 scopus 로고
    • Alpha-MSH peptides inhibit acute inflammation and contact sensitivity
    • Hiltz ME, Lipton JM. Alpha-MSH peptides inhibit acute inflammation and contact sensitivity. Peptides 1990; 11: 979-982
    • (1990) Peptides , vol.11 , pp. 979-982
    • Hiltz, M.E.1    Lipton, J.M.2
  • 129
    • 0035282828 scopus 로고    scopus 로고
    • Effects of melanocortin peptides on lipopolysaccharide/interferon- γ-induced NF-κB DNA binding and nitric oxide production in macrophage-like RAW 264.7 cells: Evidence for dual mechanisms of action
    • Mandrika I, Muceniece R, Wikberg JE. Effects of melanocortin peptides on lipopolysaccharide/interferon-γ-induced NF-κB DNA binding and nitric oxide production in macrophage-like RAW 264.7 cells: evidence for dual mechanisms of action. Biochem Pharmacol 2001; 61: 613-621
    • (2001) Biochem Pharmacol , vol.61 , pp. 613-621
    • Mandrika, I.1    Muceniece, R.2    Wikberg, J.E.3
  • 130
    • 0025849694 scopus 로고
    • α-melanocyte-stimulating hormone reduces interleukin-1 β effects on rat stomach preparations possibly through interference with a type I receptor
    • Mugridge KG, Perretti M, Ghiara P, Parente L. α-melanocyte- stimulating hormone reduces interleukin-1 β effects on rat stomach preparations possibly through interference with a type I receptor. Eur J Pharmacol 1991; 197: 151-155
    • (1991) Eur J Pharmacol , vol.197 , pp. 151-155
    • Mugridge, K.G.1    Perretti, M.2    Ghiara, P.3    Parente, L.4
  • 131
    • 0025210523 scopus 로고
    • α-melanocyte stimulating hormone message and inhibitory sequences: Comparative structure-activity studies on melanocytes
    • Sawyer TK, Staples DJ, Castrucci AM, Hadley ME, al-Obeidi FA, Cody WL, et al. α-melanocyte stimulating hormone message and inhibitory sequences: comparative structure-activity studies on melanocytes. Peptides 1990; 11: 351-357
    • (1990) Peptides , vol.11 , pp. 351-357
    • Sawyer, T.K.1    Staples, D.J.2    Castrucci, A.M.3    Hadley, M.E.4    Al-Obeidi, F.A.5    Cody, W.L.6
  • 132
    • 38549120838 scopus 로고    scopus 로고
    • The endocrine role for chromogranin A: A prohormone for peptides with regulatory properties
    • Helle KB, Corti A, Metz-Boutigue MH, Tota B. The endocrine role for chromogranin A: a prohormone for peptides with regulatory properties. Cell Mol Life Sci 2007; 64: 2863-2886
    • (2007) Cell Mol Life Sci , vol.64 , pp. 2863-2886
    • Helle, K.B.1    Corti, A.2    Metz-Boutigue, M.H.3    Tota, B.4
  • 133
    • 0035929558 scopus 로고    scopus 로고
    • Structural and biological characterization of chromofungin, the antifungal chromogranin A-(47-66)-derived peptide
    • Lugardon K, Chasserot-Golaz S, Kieffer AE, Maget-Dana R, Nullans G, Kieffer B, et al. Structural and biological characterization of chromofungin, the antifungal chromogranin A-(47-66)-derived peptide. J Biol Chem 2001; 276: 35875-35882
    • (2001) J Biol Chem , vol.276 , pp. 35875-35882
    • Lugardon, K.1    Chasserot-Golaz, S.2    Kieffer, A.E.3    Maget-Dana, R.4    Nullans, G.5    Kieffer, B.6
  • 134
    • 0037727654 scopus 로고    scopus 로고
    • Catestatin (CgA344-364) stimulates rat mast cell release of histamine in a manner comparable to mastoparan and other cationic charged neuropeptides
    • Kruger PG, Mahata SK, Helle KB. Catestatin (CgA344-364) stimulates rat mast cell release of histamine in a manner comparable to mastoparan and other cationic charged neuropeptides. Regul Pept 2003; 114: 29-35.
    • (2003) Regul Pept , vol.114 , pp. 29-35
    • Kruger, P.G.1    Mahata, S.K.2    Helle, K.B.3
  • 136
    • 38549098276 scopus 로고    scopus 로고
    • Antimicrobial peptides in human skin disease
    • Yamasaki K, Gallo RL. Antimicrobial peptides in human skin disease. Eur J Dermatol 2008; 18: 11-21.
    • (2008) Eur J Dermatol , vol.18 , pp. 11-21
    • Yamasaki, K.1    Gallo, R.L.2
  • 139
    • 0026741044 scopus 로고
    • Non-immunological defence mechanisms of the gut
    • Sarker SA, Gyr K. Non-immunological defence mechanisms of the gut. Gut 1992; 33: 987-993
    • (1992) Gut , vol.33 , pp. 987-993
    • Sarker, S.A.1    Gyr, K.2
  • 140
    • 20744443283 scopus 로고    scopus 로고
    • Innate defenses of the intestinal epithelial barrier
    • Muller CA, Autenrieth IB, Peschel A. Innate defenses of the intestinal epithelial barrier. Cell Mol Life Sci 2005; 62: 1297-1307
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1297-1307
    • Muller, C.A.1    Autenrieth, I.B.2    Peschel, A.3
  • 141
    • 0016664344 scopus 로고
    • The distribution of muramidase (lysozyme) in human tissues
    • Mason DY, Taylor CR. The distribution of muramidase (lysozyme) in human tissues. J Clin Pathol 1975; 28: 124-132
    • (1975) J Clin Pathol , vol.28 , pp. 124-132
    • Mason, D.Y.1    Taylor, C.R.2
  • 142
    • 0023908145 scopus 로고
    • Immunohistochemical observations of lysozyme in the Paneth cells of specific-pathogen-free and germ-free mice
    • Satoh Y, Ishikawa K, Tanaka H, Oomori Y, Ono K. Immunohistochemical observations of lysozyme in the Paneth cells of specific-pathogen-free and germ-free mice. Acta Histochem 1988; 83: 185-188
    • (1988) Acta Histochem , vol.83 , pp. 185-188
    • Satoh, Y.1    Ishikawa, K.2    Tanaka, H.3    Oomori, Y.4    Ono, K.5
  • 143
    • 28844435745 scopus 로고    scopus 로고
    • Lactoferrin accelerates reconstitution of the humoral and cellular immune response during chemotherapy-induced immunosuppression and bone marrow transplant in mice
    • Artym J, Zimecki M, Kuryszko J, Kruzel ML. Lactoferrin accelerates reconstitution of the humoral and cellular immune response during chemotherapy-induced immunosuppression and bone marrow transplant in mice. Stem Cells Dev 2005; 14: 548-555
    • (2005) Stem Cells Dev , vol.14 , pp. 548-555
    • Artym, J.1    Zimecki, M.2    Kuryszko, J.3    Kruzel, M.L.4
  • 144
    • 0033258176 scopus 로고    scopus 로고
    • Adherence and invasion-two pathogenicity factors in bacterial and fungal pathogens
    • Muller FM, Morschhauser J, Kohler G, Oelschlaeger TA, Ziebuhr W, Hacker J. Adherence and invasion-two pathogenicity factors in bacterial and fungal pathogens. Mycoses 1999; 42 (Suppl 1): 39-42.
    • (1999) Mycoses , vol.42 , Issue.SUPPL. 1 , pp. 39-42
    • Muller, F.M.1    Morschhauser, J.2    Kohler, G.3    Oelschlaeger, T.A.4    Ziebuhr, W.5    Hacker, J.6
  • 145
    • 0033615737 scopus 로고    scopus 로고
    • On the diversity of secreted phospholipases A(2). Cloning, tissue distribution, and functional expression of two novel mouse group II enzymes
    • Valentin E, Ghomashchi F, Gelb MH, Lazdunski M, Lambeau G. On the diversity of secreted phospholipases A(2). Cloning, tissue distribution, and functional expression of two novel mouse group II enzymes. J Biol Chem 1999; 274: 31195-31202
    • (1999) J Biol Chem , vol.274 , pp. 31195-31202
    • Valentin, E.1    Ghomashchi, F.2    Gelb, M.H.3    Lazdunski, M.4    Lambeau, G.5
  • 146
    • 52149122500 scopus 로고    scopus 로고
    • Pathophysiology of LPS-induced gastrointestinal injury in the rat: Role of secretory phospholipase A2
    • Zayat M, Lichtenberger LM, Dial EJ. Pathophysiology of LPS-induced gastrointestinal injury in the rat: role of secretory phospholipase A2. Shock 2008; 30: 206-211
    • (2008) Shock , vol.30 , pp. 206-211
    • Zayat, M.1    Lichtenberger, L.M.2    Dial, E.J.3
  • 147
    • 0023746603 scopus 로고
    • Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils
    • Romeo D, Skerlavaj B, Bolognesi M, Gennaro R. Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J Biol Chem 1988; 263: 9573-9575
    • (1988) J Biol Chem , vol.263 , pp. 9573-9575
    • Romeo, D.1    Skerlavaj, B.2    Bolognesi, M.3    Gennaro, R.4
  • 148
    • 0036151109 scopus 로고    scopus 로고
    • Cell differentiation is a key determinant of cathelicidin LL-37/human cationic antimicrobial protein 18 expression by human colon epithelium
    • Hase K, Eckmann L, Leopard JD, Varki N, Kagnoff MF. Cell differentiation is a key determinant of cathelicidin LL-37/human cationic antimicrobial protein 18 expression by human colon epithelium. Infect Immun 2002; 70: 953-963
    • (2002) Infect Immun , vol.70 , pp. 953-963
    • Hase, K.1    Eckmann, L.2    Leopard, J.D.3    Varki, N.4    Kagnoff, M.F.5
  • 150
    • 1542564787 scopus 로고    scopus 로고
    • The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization
    • Davidson DJ, Currie AJ, Reid GS, Bowdish DM, MacDonald KL, Ma RC, et al. The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization. J Immunol 2004; 172: 1146-1156
    • (2004) J Immunol , vol.172 , pp. 1146-1156
    • Davidson, D.J.1    Currie, A.J.2    Reid, G.S.3    Bowdish, D.M.4    MacDonald, K.L.5    Ma, R.C.6
  • 151
    • 38849088077 scopus 로고    scopus 로고
    • Host defense peptide LL-37, in synergy with inflammatory mediator IL-1β, augments immune responses by multiple pathways
    • Yu J, Mookherjee N, Wee K, Bowdish DM, Pistolic J, Li Y, et al. Host defense peptide LL-37, in synergy with inflammatory mediator IL-1β, augments immune responses by multiple pathways. J Immunol 2007; 179: 7684-7691
    • (2007) J Immunol , vol.179 , pp. 7684-7691
    • Yu, J.1    Mookherjee, N.2    Wee, K.3    Bowdish, D.M.4    Pistolic, J.5    Li, Y.6
  • 152
    • 30044433704 scopus 로고    scopus 로고
    • Modulation of the TLR-mediated inflammatory response by the endogenous human host defense peptide LL-37
    • Mookherjee N, Brown KL, Bowdish DM, Doria S, Falsafi R, Hokamp K, et al. Modulation of the TLR-mediated inflammatory response by the endogenous human host defense peptide LL-37. J Immunol 2006; 176: 2455-2464
    • (2006) J Immunol , vol.176 , pp. 2455-2464
    • Mookherjee, N.1    Brown, K.L.2    Bowdish, D.M.3    Doria, S.4    Falsafi, R.5    Hokamp, K.6
  • 153
    • 0037340434 scopus 로고    scopus 로고
    • Angiogenins: A new class of microbicidal proteins involved in innate immunity
    • Hooper LV, Stappenbeck TS, Hong CV, Gordon JI. Angiogenins: a new class of microbicidal proteins involved in innate immunity. Nat Immunol 2003; 4: 269-273
    • (2003) Nat Immunol , vol.4 , pp. 269-273
    • Hooper, L.V.1    Stappenbeck, T.S.2    Hong, C.V.3    Gordon, J.I.4
  • 154
    • 0026794004 scopus 로고
    • Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase a superfamily
    • Saxena SK, Rybak SM, Davey RT, Jr., Youle RJ, Ackerman EJ. Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily. J Biol Chem 1992; 267: 21982-21986
    • (1992) J Biol Chem , vol.267 , pp. 21982-21986
    • Saxena, S.K.1    Rybak, S.M.2    Davey Jr., R.T.3    Youle, R.J.4    Ackerman, E.J.5
  • 155
    • 0036840337 scopus 로고    scopus 로고
    • Expression of the regenerating gene family in inflammatory bowel disease mucosa: Reg Iα upregulation, processing, and antiapoptotic activity
    • Dieckgraefe BK, Crimmins DL, Landt V, Houchen C, Anant S, Porche-Sorbet R, et al. Expression of the regenerating gene family in inflammatory bowel disease mucosa: Reg Iα upregulation, processing, and antiapoptotic activity. J Investig Med 2002; 50: 421-434
    • (2002) J Investig Med , vol.50 , pp. 421-434
    • Dieckgraefe, B.K.1    Crimmins, D.L.2    Landt, V.3    Houchen, C.4    Anant, S.5    Porche-Sorbet, R.6
  • 157
    • 0034704102 scopus 로고    scopus 로고
    • Germ-free and colonized mice generate the same products from enteric prodefensins
    • Putsep K, Axelsson LG, Boman A, Midtvedt T, Normark S, Boman HG, et al. Germ-free and colonized mice generate the same products from enteric prodefensins. J Biol Chem 2000; 275: 40478-40482
    • (2000) J Biol Chem , vol.275 , pp. 40478-40482
    • Putsep, K.1    Axelsson, L.G.2    Boman, A.3    Midtvedt, T.4    Normark, S.5    Boman, H.G.6
  • 159
    • 4444246183 scopus 로고    scopus 로고
    • Increased diversity of intestinal antimicrobial peptides by covalent dimer formation
    • Hornef MW, Putsep K, Karlsson J, Refai E, Andersson M. Increased diversity of intestinal antimicrobial peptides by covalent dimer formation. Nat Immunol 2004; 5: 836-843
    • (2004) Nat Immunol , vol.5 , pp. 836-843
    • Hornef, M.W.1    Putsep, K.2    Karlsson, J.3    Refai, E.4    Andersson, M.5
  • 160
    • 0032734313 scopus 로고    scopus 로고
    • Expression and regulation of the human β-defensins hBD-1 and hBD-2 in intestinal epithelium
    • O'Neil DA, Porter EM, Elewaut D, Anderson GM, Eckmann L, Ganz T, et al. Expression and regulation of the human β-defensins hBD-1 and hBD-2 in intestinal epithelium. J Immunol 1999; 163: 6718-6724
    • (1999) J Immunol , vol.163 , pp. 6718-6724
    • O'Neil, D.A.1    Porter, E.M.2    Elewaut, D.3    Anderson, G.M.4    Eckmann, L.5    Ganz, T.6
  • 161
    • 33644540149 scopus 로고    scopus 로고
    • Albumin and amino acids upregulate the expression of human β-defensin 1
    • Sherman H, Chapnik N, Froy O. Albumin and amino acids upregulate the expression of human β-defensin 1. Mol Immunol 2006; 43: 1617-1623
    • (2006) Mol Immunol , vol.43 , pp. 1617-1623
    • Sherman, H.1    Chapnik, N.2    Froy, O.3
  • 162
    • 2142653566 scopus 로고    scopus 로고
    • Differential regulation of β-defensin gene expression during Cryptosporidium parvum infection
    • Zaalouk TK, Bajaj-Elliott M, George JT, McDonald V. Differential regulation of β-defensin gene expression during Cryptosporidium parvum infection. Infect Immun 2004; 72: 2772-2779
    • (2004) Infect Immun , vol.72 , pp. 2772-2779
    • Zaalouk, T.K.1    Bajaj-Elliott, M.2    George, J.T.3    McDonald, V.4
  • 163
    • 33846653740 scopus 로고    scopus 로고
    • Innate immune defenses in the intestinal tract
    • Dann SM, Eckmann L. Innate immune defenses in the intestinal tract. Curr Opin Gastroenterol 2007; 23: 115-120
    • (2007) Curr Opin Gastroenterol , vol.23 , pp. 115-120
    • Dann, S.M.1    Eckmann, L.2
  • 164
    • 3542990948 scopus 로고    scopus 로고
    • β-Defensin-3 and -4 in intestinal epithelial cells display increased mRNA expression in ulcerative colitis
    • Fahlgren A, Hammarstrom S, Danielsson A, Hammarstrom ML. β-Defensin-3 and -4 in intestinal epithelial cells display increased mRNA expression in ulcerative colitis. Clin Exp Immunol 2004; 137: 379-385
    • (2004) Clin Exp Immunol , vol.137 , pp. 379-385
    • Fahlgren, A.1    Hammarstrom, S.2    Danielsson, A.3    Hammarstrom, M.L.4
  • 165
    • 0031006408 scopus 로고    scopus 로고
    • Prognosis and management of Crohn's disease in the over-55 age group
    • Walmsley RS, Gillen CD, Allan RN. Prognosis and management of Crohn's disease in the over-55 age group. Postgrad Med J 1997; 73: 225-229
    • (1997) Postgrad Med J , vol.73 , pp. 225-229
    • Walmsley, R.S.1    Gillen, C.D.2    Allan, R.N.3
  • 166
    • 67650222193 scopus 로고    scopus 로고
    • KRJ-I and BON cell lines: Defining an appropriate enterochromaffin cell neuroendocrine tumor model
    • Siddique ZL, Drozdov I, Floch J, Gustafsson BI, Stunes K, Pfragner R, et al. KRJ-I and BON cell lines: defining an appropriate enterochromaffin cell neuroendocrine tumor model. Neuroendocrinology 2009; 89: 458-470
    • (2009) Neuroendocrinology , vol.89 , pp. 458-470
    • Siddique, Z.L.1    Drozdov, I.2    Floch, J.3    Gustafsson, B.I.4    Stunes, K.5    Pfragner, R.6
  • 167
    • 40949090110 scopus 로고    scopus 로고
    • Distinct morphology of serotonin-containing enterochromaffin (EC) cells in the rat distal colon
    • Kuramoto H, Kadowaki M, Sakamoto H, Yuasa K, Todo A, Shirai R. Distinct morphology of serotonin-containing enterochromaffin (EC) cells in the rat distal colon. Arch Histol Cytol 2007; 70: 235-241
    • (2007) Arch Histol Cytol , vol.70 , pp. 235-241
    • Kuramoto, H.1    Kadowaki, M.2    Sakamoto, H.3    Yuasa, K.4    Todo, A.5    Shirai, R.6
  • 168
    • 48449088875 scopus 로고    scopus 로고
    • The role of serotonin in intestinal luminal sensing and secretion
    • Oxford
    • Hansen MB, Witte AB. The role of serotonin in intestinal luminal sensing and secretion. Acta Physiol (Oxford) 2008; 193: 311-323
    • (2008) Acta Physiol , vol.193 , pp. 311-323
    • Hansen, M.B.1    Witte, A.B.2
  • 169
    • 3042554997 scopus 로고    scopus 로고
    • Expression of the endocytic proteins dynamin and amphiphysin in rat gastric enterochromaffin-like cells
    • Zanner R, Gratzl M, Prinz C. Expression of the endocytic proteins dynamin and amphiphysin in rat gastric enterochromaffin-like cells. J Cell Sci 2004; 117: 2369-2376
    • (2004) J Cell Sci , vol.117 , pp. 2369-2376
    • Zanner, R.1    Gratzl, M.2    Prinz, C.3
  • 170
    • 0017176922 scopus 로고
    • Enterochromaffin cells as the endocrine source of gastrointestinal substance P
    • Heitz P, Polak JM, Timson DM, Pearse AG. Enterochromaffin cells as the endocrine source of gastrointestinal substance P. Histochemistry 1976; 49: 343-347
    • (1976) Histochemistry , vol.49 , pp. 343-347
    • Heitz, P.1    Polak, J.M.2    Timson, D.M.3    Pearse, A.G.4
  • 171
    • 0025923006 scopus 로고
    • Immunoreactivities for chromogranin a and B, and secretogranin II in the guinea pig entero-endocrine system: Cellular distributions and intercellular heterogeneities
    • Cetin Y, Grube D. Immunoreactivities for chromogranin A and B, and secretogranin II in the guinea pig entero-endocrine system: cellular distributions and intercellular heterogeneities. Cell Tissue Res 1991; 264: 231-241
    • (1991) Cell Tissue Res , vol.264 , pp. 231-241
    • Cetin, Y.1    Grube, D.2
  • 172
    • 0017097854 scopus 로고
    • Melatonin and enterochromaffine cells
    • Raikhlin NT, Kvetnoy IM. Melatonin and enterochromaffine cells. Acta Histochem 1976; 55: 19-24.
    • (1976) Acta Histochem , vol.55 , pp. 19-24
    • Raikhlin, N.T.1    Kvetnoy, I.M.2
  • 173
    • 0035207186 scopus 로고    scopus 로고
    • D-glucose releases 5-hydroxytryptamine from human BON cells as a model of enterochromaffin cells
    • Kim M, Cooke HJ, Javed NH, Carey HV, Christofi F, Raybould HE. D-glucose releases 5-hydroxytryptamine from human BON cells as a model of enterochromaffin cells. Gastroenterology 2001; 121: 1400-1406
    • (2001) Gastroenterology , vol.121 , pp. 1400-1406
    • Kim, M.1    Cooke, H.J.2    Javed, N.H.3    Carey, H.V.4    Christofi, F.5    Raybould, H.E.6
  • 174
    • 34247631654 scopus 로고    scopus 로고
    • Enterochromaffin cells of the human gut: Sensors for spices and odorants
    • Braun T, Voland P, Kunz L, Prinz C, Gratzl M. Enterochromaffin cells of the human gut: sensors for spices and odorants. Gastroenterology 2007; 132: 1890-1901
    • (2007) Gastroenterology , vol.132 , pp. 1890-1901
    • Braun, T.1    Voland, P.2    Kunz, L.3    Prinz, C.4    Gratzl, M.5
  • 177
    • 84887212359 scopus 로고    scopus 로고
    • Two chromogranin A-derived peptides induce calcium entry in human
    • Zhang D, Shooshtarizadeh P, Laventie BJ, Colin DA, Chich JF, Vidic J, et al. Two chromogranin A-derived peptides induce calcium entry in human neutrophils by calmodulin-regulated calcium independent phospholipase A2. PLoS One 2009; 4: e4501.
    • (2009) PLoS One , vol.4
    • Zhang, D.1    Shooshtarizadeh, P.2    Laventie, B.J.3    Colin, D.A.4    Chich, J.F.5    Vidic, J.6
  • 178
    • 3142570441 scopus 로고    scopus 로고
    • A role for chromogranin a (4-16), a vasostatin-derived peptide, on human colonic motility. An in vitro study
    • Ghia JE, Crenner F, Rohr S, Meyer C, Metz-Boutigue MH, Aunis D, et al. A role for chromogranin A (4-16), a vasostatin-derived peptide, on human colonic motility. An in vitro study. Regul Pept 2004; 121: 31-39
    • (2004) Regul Pept , vol.121 , pp. 31-39
    • Ghia, J.E.1    Crenner, F.2    Rohr, S.3    Meyer, C.4    Metz-Boutigue, M.H.5    Aunis, D.6
  • 179
    • 19644400927 scopus 로고    scopus 로고
    • Effect of acetic acid or trypsin application on rat colonic motility in vitro and modulation by two synthetic fragments of chromogranin a
    • Ghia JE, Pradaud I, Crenner F, Metz-Boutigue MH, Aunis D, Angel F. Effect of acetic acid or trypsin application on rat colonic motility in vitro and modulation by two synthetic fragments of chromogranin A. Regul Pept 2005; 124: 27-35.
    • (2005) Regul Pept , vol.124 , pp. 27-35
    • Ghia, J.E.1    Pradaud, I.2    Crenner, F.3    Metz-Boutigue, M.H.4    Aunis, D.5    Angel, F.6
  • 181
    • 20844454920 scopus 로고    scopus 로고
    • Nucleotide-binding oligomerization domain-2 modulates specific TLR pathways for the induction of cytokine release
    • Netea MG, Ferwerda G, de Jong DJ, Jansen T, Jacobs L, Kramer M, et al. Nucleotide-binding oligomerization domain-2 modulates specific TLR pathways for the induction of cytokine release. J Immunol 2005; 174: 6518-6523
    • (2005) J Immunol , vol.174 , pp. 6518-6523
    • Netea, M.G.1    Ferwerda, G.2    De Jong, D.J.3    Jansen, T.4    Jacobs, L.5    Kramer, M.6
  • 182
    • 35348940762 scopus 로고    scopus 로고
    • Defensins and Paneth cells in inflammatory bowel disease
    • Shi J. Defensins and Paneth cells in inflammatory bowel disease. Inflamm Bowel Dis 2007; 13: 1284-1292
    • (2007) Inflamm Bowel Dis , vol.13 , pp. 1284-1292
    • Shi, J.1
  • 184
    • 7244257312 scopus 로고    scopus 로고
    • NOD2 (CARD15) mutations in Crohn's disease are associated with diminished mucosal α-defensin expression
    • Wehkamp J, Harder J, Weichenthal M, Schwab M, Schaffeler E, Schlee M, et al. NOD2 (CARD15) mutations in Crohn's disease are associated with diminished mucosal α-defensin expression. Gut 2004; 53: 1658-1664
    • (2004) Gut , vol.53 , pp. 1658-1664
    • Wehkamp, J.1    Harder, J.2    Weichenthal, M.3    Schwab, M.4    Schaffeler, E.5    Schlee, M.6
  • 185
    • 0014447697 scopus 로고
    • The Paneth cell in health and disease
    • Lewin K. The Paneth cell in health and disease. Ann R Coll Surg Engl 1969; 44: 23-37.
    • (1969) Ann R Coll Surg Engl , vol.44 , pp. 23-37
    • Lewin, K.1
  • 187
    • 10744222688 scopus 로고    scopus 로고
    • Expression of NOD2 in Paneth cells: A possible link to Crohn's ileitis
    • Ogura Y, Lala S, Xin W, Smith E, Dowds TA, Chen FF, et al. Expression of NOD2 in Paneth cells: a possible link to Crohn's ileitis. Gut 2003; 52: 1591-1597
    • (2003) Gut , vol.52 , pp. 1591-1597
    • Ogura, Y.1    Lala, S.2    Xin, W.3    Smith, E.4    Dowds, T.A.5    Chen, F.F.6
  • 193
    • 0018358644 scopus 로고
    • Seminalplasmin - An antimicrobial protein from bovine seminal plasma which acts in E. coli by specific inhibition of rRNA synthesis
    • Reddy ES, Bhargava PM. Seminalplasmin - an antimicrobial protein from bovine seminal plasma which acts in E. coli by specific inhibition of rRNA synthesis. Nature 1979; 279: 725-728
    • (1979) Nature , vol.279 , pp. 725-728
    • Reddy, E.S.1    Bhargava, P.M.2
  • 195
    • 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, Merluzzi L, Risso A, Zanetti M. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J Biol Chem 1996; 271: 28375-28381
    • (1996) J Biol Chem , vol.271 , pp. 28375-28381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.3    Merluzzi, L.4    Risso, A.5    Zanetti, M.6
  • 196
    • 0029584314 scopus 로고
    • Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide
    • Mahoney MM, Lee AY, Brezinski-Caliguri DJ, Huttner KM. Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide. FEBS Lett 1995; 377: 519-522
    • (1995) FEBS Lett , vol.377 , pp. 519-522
    • Mahoney, M.M.1    Lee, A.Y.2    Brezinski-Caliguri, D.J.3    Huttner, K.M.4
  • 197
    • 0036231767 scopus 로고    scopus 로고
    • Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides
    • Sawai MV, Waring AJ, Kearney WR, McCray PB, Jr, Forsyth WR, Lehrer RI, et al. Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides. Protein Eng 2002; 15: 225-232
    • (2002) Protein Eng , vol.15 , pp. 225-232
    • Sawai, M.V.1    Waring, A.J.2    Kearney, W.R.3    McCray Jr., P.B.4    Forsyth, W.R.5    Lehrer, R.I.6
  • 198
    • 0028244635 scopus 로고
    • Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells
    • Zanetti M, Storici P, Tossi A, Scocchi M, Gennaro R. Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells. J Biol Chem 1994; 269: 7855-7858
    • (1994) J Biol Chem , vol.269 , pp. 7855-7858
    • Zanetti, M.1    Storici, P.2    Tossi, A.3    Scocchi, M.4    Gennaro, R.5
  • 200
    • 0024460671 scopus 로고
    • Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils
    • Gennaro R, Skerlavaj B, Romeo D. Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils. Infect Immun 1989; 57: 3142-3146
    • (1989) Infect Immun , vol.57 , pp. 3142-3146
    • Gennaro, R.1    Skerlavaj, B.2    Romeo, D.3
  • 201
    • 0029129210 scopus 로고
    • Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: Comparative mapping of the locus for the human peptide antibiotic FALL-39
    • Gudmundsson GH, Magnusson KP, Chowdhary BP, Johansson M, Andersson L, Boman HG. Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39. Proc Natl Acad Sci USA 1995; 92: 7085-7089
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7085-7089
    • Gudmundsson, G.H.1    Magnusson, Kp.2    Chowdhary, B.P.3    Johansson, M.4    Andersson, L.5    Boman, H.G.6
  • 203
    • 0022623229 scopus 로고
    • The primary structure and functional characterization of the neutral histidine-rich polypeptide from human parotid secretion
    • Oppenheim FG, Yang YC, Diamond RD, Hyslop D, Offner GD, Troxler RF. The primary structure and functional characterization of the neutral histidine-rich polypeptide from human parotid secretion. J Biol Chem 1986; 261: 1177-1182
    • (1986) J Biol Chem , vol.261 , pp. 1177-1182
    • Oppenheim, F.G.1    Yang, Y.C.2    Diamond, R.D.3    Hyslop, D.4    Offner, G.D.5    Troxler, R.F.6
  • 204
  • 205
    • 0026778020 scopus 로고
    • Bactericidal activities of rat defensins and synthetic rabbit defensins on Staphylococci, Klebsiella pneumoniae (Chedid, 277, and 8N3), Pseudomonas aeruginosa (mucoid and nonmucoid strains), Salmonella typhimurium (Ra, Rc, Rd, and Re of LPS mutants) and Escherichia coli
    • Kohashi O, Ono T, Ohki K, Soejima T, Moriya T, Umeda A, et al. Bactericidal activities of rat defensins and synthetic rabbit defensins on Staphylococci, Klebsiella pneumoniae (Chedid, 277, and 8N3), Pseudomonas aeruginosa (mucoid and nonmucoid strains), Salmonella typhimurium (Ra, Rc, Rd, and Re of LPS mutants) and Escherichia coli. Microbiol Immunol 1992; 36: 369-380
    • (1992) Microbiol Immunol , vol.36 , pp. 369-380
    • Kohashi, O.1    Ono, T.2    Ohki, K.3    Soejima, T.4    Moriya, T.5    Umeda, A.6
  • 206
    • 54149114782 scopus 로고    scopus 로고
    • Cloning and identification of a novel sperm binding protein, HEL-75, with antibacterial activity and expressed in the human epididymis
    • Lin YQ, Li JY, Wang HY, Liu J, Zhang CL, Wang WT, et al. Cloning and identification of a novel sperm binding protein, HEL-75, with antibacterial activity and expressed in the human epididymis. Hum Reprod 2008; 23: 2086-2094
    • (2008) Hum Reprod , vol.23 , pp. 2086-2094
    • Lin, Y.Q.1    Li, J.Y.2    Wang, H.Y.3    Liu, J.4    Zhang, C.L.5    Wang, W.T.6
  • 207
    • 4444383056 scopus 로고    scopus 로고
    • SPAG11/isoform HE2C, an atypical anionic β-defensin-like peptide
    • von Horsten HH, Schafer B, Kirchhoff C. SPAG11/isoform HE2C, an atypical anionic β-defensin-like peptide. Peptides 2004; 25: 1223-1233
    • (2004) Peptides , vol.25 , pp. 1223-1233
    • Von Horsten, H.H.1    Schafer, B.2    Kirchhoff, C.3
  • 209
    • 0027443966 scopus 로고
    • A novel cDNA sequence encoding a pig leukocyte antimicrobial peptide with a cathelin-like pro-sequence
    • Storici P, Zanetti M. A novel cDNA sequence encoding a pig leukocyte antimicrobial peptide with a cathelin-like pro-sequence. Biochem Biophys Res Commun 1993; 196: 1363-1368
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 1363-1368
    • Storici, P.1    Zanetti, M.2
  • 210
    • 0034607350 scopus 로고    scopus 로고
    • Synthesis, microbicidal activity, and solution structure of the dodecapeptide from bovine neutrophils
    • Raj PA, Karunakaran T, Sukumaran DK. Synthesis, microbicidal activity, and solution structure of the dodecapeptide from bovine neutrophils. Biopolymers 2000; 53: 281-292
    • (2000) Biopolymers , vol.53 , pp. 281-292
    • Raj, P.A.1    Karunakaran, T.2    Sukumaran, D.K.3
  • 211
    • 0028980267 scopus 로고
    • Casocidin-I: A casein-α s2 derived peptide exhibits antibacterial activity
    • Zucht HD, Raida M, Adermann K, Magert HJ, Forssmann WG. Casocidin-I: a casein-α s2 derived peptide exhibits antibacterial activity. FEBS Lett 1995; 372: 185-188
    • (1995) FEBS Lett , vol.372 , pp. 185-188
    • Zucht, H.D.1    Raida, M.2    Adermann, K.3    Magert, H.J.4    Forssmann, W.G.5
  • 212
    • 0033022708 scopus 로고    scopus 로고
    • Isolation and identification of three bactericidal domains in the bovine alpha-lactalbumin molecule
    • Pellegrini A, Thomas U, Bramaz N, Hunziker P, von Fellenberg R. Isolation and identification of three bactericidal domains in the bovine alpha-lactalbumin molecule. Biochim Biophys Acta 1999; 1426: 439-448
    • (1999) Biochim Biophys Acta , vol.1426 , pp. 439-448
    • Pellegrini, A.1    Thomas, U.2    Bramaz, N.3    Hunziker, P.4    Von Fellenberg, R.5
  • 214
    • 0037390719 scopus 로고    scopus 로고
    • The N- and C-terminal fragments of ubiquitin are important for the antimicrobial activities
    • Kieffer AE, Goumon Y, Ruh O, Chasserot-Golaz S, Nullans G, Gasnier C, et al. The N- and C-terminal fragments of ubiquitin are important for the antimicrobial activities. FASEB J 2003; 17: 776-778
    • (2003) FASEB J , vol.17 , pp. 776-778
    • Kieffer, A.E.1    Goumon, Y.2    Ruh, O.3    Chasserot-Golaz, S.4    Nullans, G.5    Gasnier, C.6
  • 215
    • 33846036096 scopus 로고    scopus 로고
    • The worldwide Protein Data Bank (wwPDB): Ensuring a single, uniform archive of PDB data
    • Berman H, Henrick K, Nakamura H, Markley JL. The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data. Nucleic Acids Res 2007; 35: D301-3.
    • (2007) Nucleic Acids Res , vol.35
    • Berman, H.1    Henrick, K.2    Nakamura, H.3    Markley, J.L.4
  • 216
    • 0034719121 scopus 로고    scopus 로고
    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
    • Rozek A, Friedrich CL, Hancock RE. Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry 2000; 39: 15765-15774
    • (2000) Biochemistry , vol.39 , pp. 15765-15774
    • Rozek, A.1    Friedrich, C.L.2    Hancock, R.E.3
  • 217
    • 57749088664 scopus 로고    scopus 로고
    • Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles
    • Wang G. Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J Biol Chem 2008; 283: 32637-32643
    • (2008) J Biol Chem , vol.283 , pp. 32637-32643
    • Wang, G.1
  • 218
    • 0035188391 scopus 로고    scopus 로고
    • Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity
    • Bauer F, Schweimer K, Kluver E, Conejo-Garcia JR, Forssmann WG, Rosch P, et al. Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity. Protein Sci 2001; 10: 2470-2479
    • (2001) Protein Sci , vol.10 , pp. 2470-2479
    • Bauer, F.1    Schweimer, K.2    Kluver, E.3    Conejo-Garcia, J.R.4    Forssmann, W.G.5    Rosch, P.6
  • 219
    • 0037020241 scopus 로고    scopus 로고
    • The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis
    • Hunter HN, Fulton DB, Ganz T, Vogel HJ. The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. J Biol Chem 2002; 277: 37597-37603
    • (2002) J Biol Chem , vol.277 , pp. 37597-37603
    • Hunter, H.N.1    Fulton, D.B.2    Ganz, T.3    Vogel, H.J.4
  • 220
    • 0033043122 scopus 로고    scopus 로고
    • Zinc-binding site of an S100 protein revealed. Two crystal structures of Ca2+-bound human psoriasin (S100A7) in the Zn2+-loaded and Zn2+-free states
    • Brodersen DE, Nyborg J, Kjeldgaard M. Zinc-binding site of an S100 protein revealed. Two crystal structures of Ca2+-bound human psoriasin (S100A7) in the Zn2+-loaded and Zn2+-free states. Biochemistry 1999; 38: 1695-1704
    • (1999) Biochemistry , vol.38 , pp. 1695-1704
    • Brodersen, D.E.1    Nyborg, J.2    Kjeldgaard, M.3
  • 221
    • 23044463641 scopus 로고    scopus 로고
    • Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent
    • Hunter HN, Demcoe AR, Jenssen H, Gutteberg TJ, Vogel HJ. Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent. Antimicrob Agents Chemother 2005; 49: 3387-3395
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 3387-3395
    • Hunter, H.N.1    Demcoe, A.R.2    Jenssen, H.3    Gutteberg, T.J.4    Vogel, H.J.5
  • 222
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey W, Dalke A, Schulten K. VMD: visual molecular dynamics. J Mol Graph 1996; 14: 27-8, 33-38
    • (1996) J Mol Graph , vol.14 , Issue.27-28 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 223
    • 47149104071 scopus 로고    scopus 로고
    • The blockade of IL-6 signaling in rational drug design
    • Adachi Y, Yoshio-Hoshino N, Nishimoto N. The blockade of IL-6 signaling in rational drug design. Curr Pharm Des 2008; 14(12): 1217-1224
    • (2008) Curr Pharm Des , vol.14 , Issue.12 , pp. 1217-1224
    • Adachi, Y.1    Yoshio-Hoshino, N.2    Nishimoto, N.3
  • 225
    • 68449091371 scopus 로고    scopus 로고
    • Recent understanding of leukocytapheresis (LCAP) for the treatment of inflammatory bowel disease
    • Mitsuyama K, Yamasaki H, Kuwaki K, Takedatsu H, Sata M. Recent understanding of leukocytapheresis (LCAP) for the treatment of inflammatory bowel disease. Curr Pharm Des 2009; 15(18): 2110-2119
    • (2009) Curr Pharm Des , vol.15 , Issue.18 , pp. 2110-2119
    • Mitsuyama, K.1    Yamasaki, H.2    Kuwaki, K.3    Takedatsu, H.4    Sata, M.5


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