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Volumn 172, Issue 2, 2004, Pages 1203-1212

Identification of a Novel FcγRIIIaα-Associated Molecule That Contains Significant Homology to Porcine Cathelin

Author keywords

[No Author keywords available]

Indexed keywords

CATHELICIDIN; CATHELIN; FC RECEPTOR; MONOCLONAL ANTIBODY;

EID: 1642536410     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.172.2.1203     Document Type: Article
Times cited : (13)

References (58)
  • 3
    • 0027204803 scopus 로고
    • Human IgG Fc receptor heterogeneity: Molecular aspects and clinical implications
    • Van de Winkel, J. G. J., and P. J. A. Capel. 1993. Human IgG Fc receptor heterogeneity: molecular aspects and clinical implications. Immunol. Today 14:215.
    • (1993) Immunol. Today , vol.14 , pp. 215
    • Van De Winkel, J.G.J.1    Capel, P.J.A.2
  • 4
    • 0027289163 scopus 로고
    • Expression of the Fc receptor for IgG (FcRI1/CDw32) by human circulating T and B lymphocytes
    • Mantzioris, B., M. Berger, W. Sewell, and H. Zola. 1993. Expression of the Fc receptor for IgG (FcRI1/CDw32) by human circulating T and B lymphocytes. J. Immunol. 150:5175.
    • (1993) J. Immunol. , vol.150 , pp. 5175
    • Mantzioris, B.1    Berger, M.2    Sewell, W.3    Zola, H.4
  • 5
    • 0024151944 scopus 로고
    • Structure and function of human and murine receptors for IgG
    • Unkeless, J. C., E. Scigliano, and V. H. Freedman. 1988. Structure and function of human and murine receptors for IgG. Annu. Rey. Immunol. 6:251.
    • (1988) Annu. Rey. Immunol. , vol.6 , pp. 251
    • Unkeless, J.C.1    Scigliano, E.2    Freedman, V.H.3
  • 8
    • 0027238292 scopus 로고
    • Lymphocyte Fc receptors: The special case of T cells
    • Sandor, M., and R. G. Lynch. 1993. Lymphocyte Fc receptors: the special case of T cells. Immunol. Today 14:227.
    • (1993) Immunol. Today , vol.14 , pp. 227
    • Sandor, M.1    Lynch, R.G.2
  • 9
    • 0023792164 scopus 로고
    • Functional and biochemical analysis of CD16 antigen on natural killer cells and granulocytes
    • Lanier, L. L., J. J. Ruitenberg, and J. H. Phillips. 1988. Functional and biochemical analysis of CD16 antigen on natural killer cells and granulocytes. J. Immunol. 141:3478.
    • (1988) J. Immunol. , vol.141 , pp. 3478
    • Lanier, L.L.1    Ruitenberg, J.J.2    Phillips, J.H.3
  • 10
    • 0024342834 scopus 로고
    • Alternative membrane forms of FcγRIII (CD16) on human natural killer cells and neutrophils: Cell type-specific expression of two genes that differ in single nucleotide substitutions
    • Ravetch, J. V., and B. Perussia. 1989. Alternative membrane forms of FcγRIII (CD16) on human natural killer cells and neutrophils: cell type-specific expression of two genes that differ in single nucleotide substitutions. J. Exp. Med. 170:481.
    • (1989) J. Exp. Med. , vol.170 , pp. 481
    • Ravetch, J.V.1    Perussia, B.2
  • 11
    • 0024811801 scopus 로고
    • A single amino acid in the glycosyl phosphatidylinositol attachment domain determines the membrane topology of FcγRIII
    • Kurosaki. T., and J. V. Ravelch. 1989. A single amino acid in the glycosyl phosphatidylinositol attachment domain determines the membrane topology of FcγRIII. Nature 342:805.
    • (1989) Nature , vol.342 , pp. 805
    • Kurosaki, T.1    Ravelch, J.V.2
  • 12
    • 0024841156 scopus 로고
    • Membrane anchoring of a human IgG Fc receptor (CD16) determined by a single amino acid
    • Lanier, L. L., S. Cwirla, G. Yu, R. Testi, and J. H. Phillips. 1989. Membrane anchoring of a human IgG Fc receptor (CD16) determined by a single amino acid. Science 246:1611.
    • (1989) Science , vol.246 , pp. 1611
    • Lanier, L.L.1    Cwirla, S.2    Yu, G.3    Testi, R.4    Phillips, J.H.5
  • 13
    • 0024421452 scopus 로고
    • Human FcγRIII(CD16): Isoforms with distinct allelic expression, extracellular domains, and membrane linkages on polymorphonuclear and natural killer cells
    • Edberg, J. C., P. B. Redecha, J. E. Salmon and R. P. Kimberly. 1989. Human FcγRIII(CD16): isoforms with distinct allelic expression, extracellular domains, and membrane linkages on polymorphonuclear and natural killer cells. J. Immunol. 143:1642.
    • (1989) J. Immunol. , vol.143 , pp. 1642
    • Edberg, J.C.1    Redecha, P.B.2    Salmon, J.E.3    Kimberly, R.P.4
  • 14
    • 0024346084 scopus 로고
    • Different membrane anchors of FcγRIII (CD16) on K/NK-lymphocytes and neutrophils: Protein-vs lipid-anchor
    • Ueda, E., T. Kinoshita, J. Nojima, K. Inoue, and T. Kitani. 1989. Different membrane anchors of FcγRIII (CD16) on K/NK-lymphocytes and neutrophils: protein-vs lipid-anchor. J. Immunol. 143:1274.
    • (1989) J. Immunol. , vol.143 , pp. 1274
    • Ueda, E.1    Kinoshita, T.2    Nojima, J.3    Inoue, K.4    Kitani, T.5
  • 15
    • 0025128539 scopus 로고
    • The Fc-receptor III of cultured human monocytes: Structural similarity with FcRIII of natural killer cells and role in the extracellular lysis of sensitized erythrocytes
    • Klaassen, R. J. L., W. H. Ouwehand, T. W. J. Huizinga, C. P. Engelfriet, and A. E. G. K. Von Dem Borne. 1990. The Fc-receptor III of cultured human monocytes: structural similarity with FcRIII of natural killer cells and role in the extracellular lysis of sensitized erythrocytes. J. Immunol. 144:599.
    • (1990) J. Immunol. , vol.144 , pp. 599
    • Klaassen, R.J.L.1    Ouwehand, W.H.2    Huizinga, T.W.J.3    Engelfriet, C.P.4    Von Dem Borne, A.E.G.K.5
  • 16
    • 0024370739 scopus 로고
    • Natural killer cell and granulocyte Fcγ receptor III (CD16) differ in membrane anchor and signal transduction
    • Selvaraj, P., O. Carpén, M. L. Hibbs, and T. A. Springer. 1989. Natural killer cell and granulocyte Fcγ receptor III (CD16) differ in membrane anchor and signal transduction. J. Immunol. 143:3283.
    • (1989) J. Immunol. , vol.143 , pp. 3283
    • Selvaraj, P.1    Carpén, O.2    Hibbs, M.L.3    Springer, T.A.4
  • 18
    • 0026075422 scopus 로고
    • Rat CD16 is defined by a family of class III Fcγ receptors requiring co-expression of heteroprotein subunits
    • Farber, D. L., and D. W. Sears. 1991. Rat CD16 is defined by a family of class III Fcγ receptors requiring co-expression of heteroprotein subunits. J. Immunol. 146:4352.
    • (1991) J. Immunol. , vol.146 , pp. 4352
    • Farber, D.L.1    Sears, D.W.2
  • 19
    • 0026015285 scopus 로고
    • Characterization of the family of dimers associated with Fc receptors (FcεR1 and FcγRIII)
    • Letourneur, O., I. Kennedy, A. Brini, J. Ortaldo, J. O'Shea, and J. Kinet. 1991. Characterization of the family of dimers associated with Fc receptors (FcεR1 and FcγRIII). J. Immunol. 147:2652.
    • (1991) J. Immunol. , vol.147 , pp. 2652
    • Letourneur, O.1    Kennedy, I.2    Brini, A.3    Ortaldo, J.4    O'Shea, J.5    Kinet, J.6
  • 20
    • 0026327771 scopus 로고
    • Structural similarity between Fc receptors and T cell receptors: Expression of the γ-subunit of FcεR1 in human T cells, natural killer cells and thymocytes
    • Vivier, E., N. Rochet, J. P. Kochan, D. H. Presky, S. F. Schlossman, and P. Anderson. 1991. Structural similarity between Fc receptors and T cell receptors: expression of the γ-subunit of FcεR1 in human T cells, natural killer cells and thymocytes. I. Enhan Immunol. 147:4263.
    • (1991) I. Enhan Immunol. , vol.147 , pp. 4263
    • Vivier, E.1    Rochet, N.2    Kochan, J.P.3    Presky, D.H.4    Schlossman, S.F.5    Anderson, P.6
  • 21
    • 0024451644 scopus 로고
    • CD3-negative natural killer cells express TCR as part of a novel molecular complex
    • Anderson, P., M. Caligiuri, J. Ritz, and S. F. Schlossman. 1989. CD3-negative natural killer cells express TCR as part of a novel molecular complex. Nature 341:159.
    • (1989) Nature , vol.341 , pp. 159
    • Anderson, P.1    Caligiuri, M.2    Ritz, J.3    Schlossman, S.F.4
  • 22
    • 0024822508 scopus 로고
    • Co-association of CD3ζ with a receptor (CD16) for IgG Fc on human natural killer cells
    • Lanier, L. L., G. Yu, and J. H. Phillips. 1989. Co-association of CD3ζ with a receptor (CD16) for IgG Fc on human natural killer cells. Nature 342:803.
    • (1989) Nature , vol.342 , pp. 803
    • Lanier, L.L.1    Yu, G.2    Phillips, J.H.3
  • 23
    • 0025237245 scopus 로고
    • Fcγ receptor type III (CD16) is included in the ζ NK receptor complex expressed by human natural killer cells
    • Anderson, P., M. Caligiuri, C. O'Brien, T. Manley, J. Ritz, and S. F. Schlossman. 1990. Fcγ receptor type III (CD16) is included in the ζ NK receptor complex expressed by human natural killer cells. Proc. Natl. Acad. Sci. USA 87:2274.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2274
    • Anderson, P.1    Caligiuri, M.2    O'Brien, C.3    Manley, T.4    Ritz, J.5    Schlossman, S.F.6
  • 24
    • 0025735616 scopus 로고
    • A subunit common to an IgG Fc receptor and the T-cell receptor mediates assembly through different interactions
    • Kurosaki, T., I. Gander, and J. V. Ravetch. 1991. A subunit common to an IgG Fc receptor and the T-cell receptor mediates assembly through different interactions. Proc. Natl. Acad. Sci. USA 88:3837.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3837
    • Kurosaki, T.1    Gander, I.2    Ravetch, J.V.3
  • 25
    • 0026542308 scopus 로고
    • The β subunit of the FcχRI is associated with the FcγRIII on mast cells
    • Kurosaki, T., I. Gander, U. Wirthmueller, and J. V. Ravetch. 1992. The β subunit of the FcχRI is associated with the FcγRIII on mast cells. J. Exp. Med. 175:447.
    • (1992) J. Exp. Med. , vol.175 , pp. 447
    • Kurosaki, T.1    Gander, I.2    Wirthmueller, U.3    Ravetch, J.V.4
  • 26
    • 0027991163 scopus 로고
    • Molecular cloning and identification of the porcine cytolytic trigger molecule G7 as an FcγRIIIα (CDI6) homologue
    • Halloran, P. J., S. E. Sweeney, C. M. Strohmeier, and Y. B. Kim. 1994. Molecular cloning and identification of the porcine cytolytic trigger molecule G7 as an FcγRIIIα (CDI6) homologue. J. Immunol. 153:2631.
    • (1994) J. Immunol. , vol.153 , pp. 2631
    • Halloran, P.J.1    Sweeney, S.E.2    Strohmeier, C.M.3    Kim, Y.B.4
  • 27
    • 0025093501 scopus 로고
    • Characterization of a monoclonal antibody enhancing porcine natural killer cell activity (PNK-E)
    • Johnson, B. D., and Y. B. Kim. 1990. Characterization of a monoclonal antibody enhancing porcine natural killer cell activity (PNK-E). Cell. Immunol. 125:107.
    • (1990) Cell. Immunol. , vol.125 , pp. 107
    • Johnson, B.D.1    Kim, Y.B.2
  • 28
    • 0025851601 scopus 로고
    • Further characterization of PNK-E: A monoclonal antibody enhancing porcine natural killer cell activity
    • Johnson, B. D., W. G. Wierda, and Y. B. Kim. 1991. Further characterization of PNK-E: a monoclonal antibody enhancing porcine natural killer cell activity. Cell. Immunol. 134:378.
    • (1991) Cell. Immunol. , vol.134 , pp. 378
    • Johnson, B.D.1    Wierda, W.G.2    Kim, Y.B.3
  • 29
    • 0027140285 scopus 로고
    • Induction of porcine granulocyte-mediated tumor cytotoxicity by two distinct monoclonal antibodies against lytic trigger molecules (PNK-E/G7)
    • Wierda, W. G., B. D. Johnson. M. E. Date. and Y. B. Kim. 1993. Induction of porcine granulocyte-mediated tumor cytotoxicity by two distinct monoclonal antibodies against lytic trigger molecules (PNK-E/G7). J. Immunol. 151:7117.
    • (1993) J. Immunol. , vol.151 , pp. 7117
    • Wierda, W.G.1    Johnson, B.D.2    Date, M.E.3    Kim, Y.B.4
  • 30
    • 0027408731 scopus 로고
    • Two distinct porcine natural killer lytic trigger molecules as PNK-E/G7 molecular complex
    • Wierda, W. G., B. D. Johnson, M. D. Dato. and Y. B. Kim. 1993. Two distinct porcine natural killer lytic trigger molecules as PNK-E/G7 molecular complex. Cell. Immunol. 146:270.
    • (1993) Cell. Immunol. , vol.146 , pp. 270
    • Wierda, W.G.1    Johnson, B.D.2    Dato, M.D.3    Kim, Y.B.4
  • 31
    • 0028104468 scopus 로고
    • Biochemical characterization of the porcine FcγRIIIα homologue G7
    • Halloran, P. J., S. E. Sweeney, and Y. B. Kim. 1994. Biochemical characterization of the porcine FcγRIIIα homologue G7. Cell. Immunol. 158:400.
    • (1994) Cell. Immunol. , vol.158 , pp. 400
    • Halloran, P.J.1    Sweeney, S.E.2    Kim, Y.B.3
  • 32
    • 0030601362 scopus 로고    scopus 로고
    • Identification of a unique porcine FcγRIIIAα molecular complex
    • Sweeney, S. E., P. J. Halloran, and Y. B. Kim. 1996. Identification of a unique porcine FcγRIIIAα molecular complex. Cell. Immunol. 172:92.
    • (1996) Cell. Immunol. , vol.172 , pp. 92
    • Sweeney, S.E.1    Halloran, P.J.2    Kim, Y.B.3
  • 33
    • 0027133441 scopus 로고
    • Pig leukocyte cysteine proteinase inhibitor (PLCPI), a new member of the stefin family
    • Lenarcic, B., A. Ritonja, and I. Dolenc. 1993. Pig leukocyte cysteine proteinase inhibitor (PLCPI), a new member of the stefin family. FEBS Lett. 336:289.
    • (1993) FEBS Lett. , vol.336 , pp. 289
    • Lenarcic, B.1    Ritonja, A.2    Dolenc, I.3
  • 34
    • 0018960376 scopus 로고
    • Natural killing (NK) and antibody-dependent cellular cytotoxicity (ADCC) in specific pathogen-free (SPF) miniature swine and germfree piglets. I. Comparison of NK and ADCC
    • Kim, Y. B., N. D. Huh, H. S. Koren, and D. B. Amos. 1980. Natural killing (NK) and antibody-dependent cellular cytotoxicity (ADCC) in specific pathogen-free (SPF) miniature swine and germfree piglets. I. Comparison of NK and ADCC. J. Immunol. 125:755.
    • (1980) J. Immunol. , vol.125 , pp. 755
    • Kim, Y.B.1    Huh, N.D.2    Koren, H.S.3    Amos, D.B.4
  • 35
    • 0019787646 scopus 로고
    • Development of alveolar macrophages in specific pathogen-free and germ-free Minnesota miniature swine
    • Rothlein, R., R. Gallily, and Y. B. Kim. 1981. Development of alveolar macrophages in specific pathogen-free and germ-free Minnesota miniature swine. J. Reticuloendothel. Soc. 30:483.
    • (1981) J. Reticuloendothel. Soc. , vol.30 , pp. 483
    • Rothlein, R.1    Gallily, R.2    Kim, Y.B.3
  • 36
    • 0026580898 scopus 로고
    • Internal protein sequence analysis: Enzymatic digestion for less than 10 μg of protein bound to polyvinylidene difluoride or nitrocellulose membranes
    • Fernandez, J., M. DeMott, D. Atherton, and S. C. Mische. 1992. Internal protein sequence analysis: enzymatic digestion for less than 10 μg of protein bound to polyvinylidene difluoride or nitrocellulose membranes. Anal. Biochem. 201:255.
    • (1992) Anal. Biochem. , vol.201 , pp. 255
    • Fernandez, J.1    DeMott, M.2    Atherton, D.3    Mische, S.C.4
  • 37
    • 0014529897 scopus 로고
    • An enzymic method for the trace iodination of immunoglobulins and other proteins
    • Marchalonis, J. J. 1969. An enzymic method for the trace iodination of immunoglobulins and other proteins. Biochem. J. 113:299.
    • (1969) Biochem. J. , vol.113 , pp. 299
    • Marchalonis, J.J.1
  • 38
    • 0018176340 scopus 로고
    • A rapid, novel method for the solid-phase derivatization of IgG antibodies for immune-affinity chromatography
    • Gersten, M. M., and J. J. Marchalonis. 1978. A rapid, novel method for the solid-phase derivatization of IgG antibodies for immune-affinity chromatography. J. Immunol. Methods 24:305.
    • (1978) J. Immunol. Methods , vol.24 , pp. 305
    • Gersten, M.M.1    Marchalonis, J.J.2
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 40
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti, M., R. Gennaro, and D. Romeo. 1995. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374:1.
    • (1995) FEBS Lett. , vol.374 , pp. 1
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 41
    • 0030012702 scopus 로고    scopus 로고
    • Antibiotic proteins of polymorphonuclear leukocytes
    • Levy, O. 1996. Antibiotic proteins of polymorphonuclear leukocytes. Eur. J. Haematol. 56:263.
    • (1996) Eur. J. Haematol. , vol.56 , pp. 263
    • Levy, O.1
  • 42
    • 0029051685 scopus 로고
    • Defensins and other endogenous peptide antibiotics of vertebrates
    • Martin, E., T. Ganz, and R. I. Lehrer. 1995. Defensins and other endogenous peptide antibiotics of vertebrates. J Leukocyte Biol. 58:128.
    • (1995) J Leukocyte Biol. , vol.58 , pp. 128
    • Martin, E.1    Ganz, T.2    Lehrer, R.I.3
  • 43
    • 0036467390 scopus 로고    scopus 로고
    • Defensins of vertebrate animals
    • Lehrer, R., and T. Ganz. 2002. Defensins of vertebrate animals. Curr. Opin. Immunol. 14:96.
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 96
    • Lehrer, R.1    Ganz, T.2
  • 44
    • 0029015666 scopus 로고
    • The structure of porcine protegrin genes
    • Zhao, C., T. Ganz, and R. I. Lehrer. 1995. The structure of porcine protegrin genes. FEBS Lett. 368:197.
    • (1995) FEBS Lett. , vol.368 , pp. 197
    • Zhao, C.1    Ganz, T.2    Lehrer, R.I.3
  • 46
    • 0028092047 scopus 로고
    • Syndecans, cell surface haparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide form wounds
    • Gallo, R. L., M. Ono, and T. Povsic. 1994. Syndecans, cell surface haparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide form wounds. Proc. Natl. Acad. Sci. USA 91:11035.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11035
    • Gallo, R.L.1    Ono, M.2    Povsic, T.3
  • 47
    • 0028244635 scopus 로고
    • Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells
    • Zanetti, M., P. Storici, A. Tossi, M. Scocchi, and R. Gennaro. 1994. Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells. J. Biol. Chem. 269:7855.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7855
    • Zanetti, M.1    Storici, P.2    Tossi, A.3    Scocchi, M.4    Gennaro, R.5
  • 49
    • 0025953533 scopus 로고
    • Stimulus-induced maturation of probactenecins, precursors of neutrophil antimicrobial polypeptides
    • Zanetti, M., L. Litteri, G. Griffiths, R. Gennaro, and D. Romeo. 1991. Stimulus-induced maturation of probactenecins, precursors of neutrophil antimicrobial polypeptides. J. Immunol. 146:4295.
    • (1991) J. Immunol. , vol.146 , pp. 4295
    • Zanetti, M.1    Litteri, L.2    Griffiths, G.3    Gennaro, R.4    Romeo, D.5
  • 50
    • 0029007198 scopus 로고
    • hCAP-18, a cathelin/probactenecin-like protein of human neutrophil specific granules
    • Cowland, J., A. Johnsen, and N. Borregaard. 1995. hCAP-18, a cathelin/probactenecin-like protein of human neutrophil specific granules. FEBS Lett. 368:173.
    • (1995) FEBS Lett. , vol.368 , pp. 173
    • Cowland, J.1    Johnsen, A.2    Borregaard, N.3
  • 51
    • 0028969853 scopus 로고
    • Extracellular accumulation of potently microbicidal bactericidal/permeability-increasing protein and p15s in an evolving sterile rabbit peritoneal inflammatory exudate
    • Weinrauch, Y., A. Foreman, and C. Shu. 1995. Extracellular accumulation of potently microbicidal bactericidal/permeability-increasing protein and p15s in an evolving sterile rabbit peritoneal inflammatory exudate. J. Clin. Invest. 95:1916.
    • (1995) J. Clin. Invest. , vol.95 , pp. 1916
    • Weinrauch, Y.1    Foreman, A.2    Shu, C.3
  • 52
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sorenson, O., P. Follin, A. Johnson, J. Calafat, G. Tjabringa, P. Hiemstra, and N. Borregaard. 2001. Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 97:3951.
    • (2001) Blood , vol.97 , pp. 3951
    • Sorenson, O.1    Follin, P.2    Johnson, A.3    Calafat, J.4    Tjabringa, G.5    Hiemstra, P.6    Borregaard, N.7
  • 53
    • 0033664277 scopus 로고    scopus 로고
    • Leukocyte antimicrobial peptides: Multifunctional effector molecules of innate immunity
    • Risso, A. 2000. Leukocyte antimicrobial peptides: multifunctional effector molecules of innate immunity. J. Leukocyte Biol. 68:785.
    • (2000) J. Leukocyte Biol. , vol.68 , pp. 785
    • Risso, A.1
  • 56
    • 0037087422 scopus 로고    scopus 로고
    • Antimicrobial peptides initiate IL-IB posttranslational processing: A novel role beyond innate immunity
    • Perregaux, D., K. Bhavsar, L. Contillo, J. Shi, and C. Gabel. 2002. Antimicrobial peptides initiate IL-IB posttranslational processing: a novel role beyond innate immunity. J. Immunol. 168:3024.
    • (2002) J. Immunol. , vol.168 , pp. 3024
    • Perregaux, D.1    Bhavsar, K.2    Contillo, L.3    Shi, J.4    Gabel, C.5
  • 57
    • 0036772907 scopus 로고    scopus 로고
    • Structure of the cathelicidin motif of protegrin-3 precursor: Structural insights into the activation mechanism of an antimicrobial protein
    • Sanchez, J.-F., F. Hoh, M.-P. Strub, A. Aumelas, and C. Dumas. 2002. Structure of the cathelicidin motif of protegrin-3 precursor: structural insights into the activation mechanism of an antimicrobial protein. Structure 10:1363.
    • (2002) Structure , vol.10 , pp. 1363
    • Sanchez, J.-F.1    Hoh, F.2    Strub, M.-P.3    Aumelas, A.4    Dumas, C.5


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