메뉴 건너뛰기




Volumn 113, Issue 2, 2009, Pages 328-337

Staphylococcal SSL5 inhibits leukocyte activation by chemokines and anaphylatoxins

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ANAPHYLATOXIN; BACTERIAL ANTIGEN; CALCIUM; CHEMOATTRACTANT; CHEMOKINE; CHEMOKINE RECEPTOR CCR1; CHEMOKINE RECEPTOR CCR2; CHEMOKINE RECEPTOR CXCR1; CHEMOKINE RECEPTOR CXCR2; CHEMOKINE RECEPTOR CXCR4; COMPLEMENT COMPONENT C3A; COMPLEMENT COMPONENT C5A; COMPLEMENT COMPONENT C5A RECEPTOR; CXCL1 CHEMOKINE; FORMYLMETHIONYLLEUCYLPHENYLALANINE; G PROTEIN COUPLED RECEPTOR; GLYCOSAMINOGLYCAN; INTERLEUKIN 8; LEUKOTRIENE RECEPTOR; MACROPHAGE INFLAMMATORY PROTEIN 1ALPHA; MONOCYTE CHEMOTACTIC PROTEIN 1; P SELECTIN GLYCOPROTEIN LIGAND 1; RANTES; SIALYL LEWIS X ANTIGEN; STAPHYLOCOCCAL SUPERANTIGEN LIKE 5 PROTEIN; STROMAL CELL DERIVED FACTOR 1; SUPERANTIGEN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CHEMOKINE RECEPTOR; EXOTOXIN; GALACTOSYL (1,4) FUCOPYRANOSYL (1,3) N ACETYLGLUCOSAMINE; GALACTOSYL-(1,4)-FUCOPYRANOSYL-(1,3)-N-ACETYLGLUCOSAMINE; IMMUNOLOGIC FACTOR; MEMBRANE PROTEIN; P SELECTIN LIGAND PROTEIN; P-SELECTIN LIGAND PROTEIN; TRISACCHARIDE; VIRULENCE FACTOR;

EID: 58849119618     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2008-04-153882     Document Type: Article
Times cited : (71)

References (47)
  • 2
    • 12544256911 scopus 로고    scopus 로고
    • Residues 10-18 within the C5a receptor N terminus compose a binding domain for chemotaxis inhibitory protein of Staphylococcus aureus
    • Postma B, Kleibeuker W, Poppelier MJ, et al. Residues 10-18 within the C5a receptor N terminus compose a binding domain for chemotaxis inhibitory protein of Staphylococcus aureus. J Biol Chem. 2005;280:2020-2027.
    • (2005) J Biol Chem , vol.280 , pp. 2020-2027
    • Postma, B.1    Kleibeuker, W.2    Poppelier, M.J.3
  • 3
    • 2442695297 scopus 로고    scopus 로고
    • Chemotaxis inhibitory protein of Staphylococcus aureus binds specifically to the C5a and formylated peptide receptor
    • Postma B, Poppelier MJ, van Galen JC, et al. Chemotaxis inhibitory protein of Staphylococcus aureus binds specifically to the C5a and formylated peptide receptor. J Immunol. 2004;172: 6994-7001.
    • (2004) J Immunol , vol.172 , pp. 6994-7001
    • Postma, B.1    Poppelier, M.J.2    van Galen, J.C.3
  • 4
    • 26844507589 scopus 로고    scopus 로고
    • The structure of the C5a receptor-blocking domain of chemotaxis inhibitory protein of Staphylococcus aureus is related to a group of immune evasive molecules
    • Haas PJ, de Haas CJ, Poppelier MJ, et al.The structure of the C5a receptor-blocking domain of chemotaxis inhibitory protein of Staphylococcus aureus is related to a group of immune evasive molecules. J Mol Biol. 2005;353:859-872.
    • (2005) J Mol Biol , vol.353 , pp. 859-872
    • Haas, P.J.1    de Haas, C.J.2    Poppelier, M.J.3
  • 5
    • 34948844450 scopus 로고    scopus 로고
    • Staphylococcal complement evasion by various convertase-blocking molecules
    • Jongerius I, Kohl J, Pandey MK, et al. Staphylococcal complement evasion by various convertase-blocking molecules. J Exp Med. 2007;204: 2461-2471.
    • (2007) J Exp Med , vol.204 , pp. 2461-2471
    • Jongerius, I.1    Kohl, J.2    Pandey, M.K.3
  • 6
    • 0037200073 scopus 로고    scopus 로고
    • The Three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome
    • Arcus VL, Langley R, Proft T, Fraser JD, Baker EN. The Three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome. J Biol Chem. 2002;277:32274-32281.
    • (2002) J Biol Chem , vol.277 , pp. 32274-32281
    • Arcus, V.L.1    Langley, R.2    Proft, T.3    Fraser, J.D.4    Baker, E.N.5
  • 7
    • 14044268137 scopus 로고    scopus 로고
    • The staphylococcal superantigenlike protein 7 binds IgAand complement C5 and inhibits IgA-Fc alpha RI binding and serum killing of bacteria
    • Langley R, Wines B, Willoughby N, Basu I, Proft T, Fraser JD. The staphylococcal superantigenlike protein 7 binds IgAand complement C5 and inhibits IgA-Fc alpha RI binding and serum killing of bacteria. J Immunol. 2005;174:2926-2933.
    • (2005) J Immunol , vol.174 , pp. 2926-2933
    • Langley, R.1    Wines, B.2    Willoughby, N.3    Basu, I.4    Proft, T.5    Fraser, J.D.6
  • 8
    • 33947590100 scopus 로고    scopus 로고
    • Staphylococcal superantigen-like 5 binds PSGL-1 and inhibits P-selectin-mediated neutrophil rolling
    • Bestebroer J, Poppelier MJ, Ulfman LH, et al. Staphylococcal superantigen-like 5 binds PSGL-1 and inhibits P-selectin-mediated neutrophil rolling. Blood. 2007;109:2936-2943.
    • (2007) Blood , vol.109 , pp. 2936-2943
    • Bestebroer, J.1    Poppelier, M.J.2    Ulfman, L.H.3
  • 9
    • 36249026299 scopus 로고    scopus 로고
    • Crystal structures of the staphylococcal toxin SSL5 in complex with sialyl Lewis X reveal a conserved binding site that shares common features with viral and bacterial sialic acid binding proteins
    • Baker HM, Basu I, Chung MC, Caradoc-DaviesT Fraser JD, Baker EN. Crystal structures of the staphylococcal toxin SSL5 in complex with sialyl Lewis X reveal a conserved binding site that shares common features with viral and bacterial sialic acid binding proteins. J Mol Biol. 2007;374: 1298-1308.
    • (2007) J Mol Biol , vol.374 , pp. 1298-1308
    • Baker, H.M.1    Basu, I.2    Chung, M.C.3    Caradoc-DaviesT Fraser, J.D.4    Baker, E.N.5
  • 10
    • 36248995861 scopus 로고    scopus 로고
    • The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition
    • Chung MC, Wines BD, Baker H, Langley RJ, Baker EN, Fraser JD. The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition. Mol Microbiol. 2007;66:1342-1355.
    • (2007) Mol Microbiol , vol.66 , pp. 1342-1355
    • Chung, M.C.1    Wines, B.D.2    Baker, H.3    Langley, R.J.4    Baker, E.N.5    Fraser, J.D.6
  • 11
    • 34247855761 scopus 로고    scopus 로고
    • Chemokine: Receptor structure, interactions, and antagonism
    • Allen SJ, Crown SE, Handel TM. Chemokine: receptor structure, interactions, and antagonism. Annu Rev Immunol. 2007;25:787-820.
    • (2007) Annu Rev Immunol , vol.25 , pp. 787-820
    • Allen, S.J.1    Crown, S.E.2    Handel, T.M.3
  • 12
    • 33748142935 scopus 로고    scopus 로고
    • ELR+ CXC chemokines and their receptors (CXC chemokine receptor 1 and CXC chemokine receptor 2) as new therapeutic targets
    • Bizzarri C, BeccariAR, Bertini R, CavicchiaMR, Giorgini S, Allegretti M. ELR+ CXC chemokines and their receptors (CXC chemokine receptor 1 and CXC chemokine receptor 2) as new therapeutic targets. Pharmacol Ther. 2006;112:139-149.
    • (2006) Pharmacol Ther , vol.112 , pp. 139-149
    • Bizzarri, C.1    Beccari, A.R.2    Bertini, R.3    Cavicchia, M.R.4    Giorgini, S.5    Allegretti, M.6
  • 13
    • 53449101060 scopus 로고    scopus 로고
    • Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: A novel mechanism for enzyme auto-regulation
    • Marx PF, Brondijk TH, Plug T, et al. Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme auto-regulation. Blood. 2008;112:2803-2809.
    • (2008) Blood , vol.112 , pp. 2803-2809
    • Marx, P.F.1    Brondijk, T.H.2    Plug, T.3
  • 14
    • 0015822275 scopus 로고
    • Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria
    • Jaffe EA, Nachman RL, Becker CG, Minick CR. Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria. J Clin Invest. 1973;52:2745-2756.
    • (1973) J Clin Invest , vol.52 , pp. 2745-2756
    • Jaffe, E.A.1    Nachman, R.L.2    Becker, C.G.3    Minick, C.R.4
  • 15
    • 0018908635 scopus 로고
    • Chemotactically responsive and nonresposive forms of a continuous human monocyte cell line
    • Fischer DG, Pike MC, Koren HS, Snyderman R. Chemotactically responsive and nonresposive forms of a continuous human monocyte cell line. J Immunol. 1980;125:463-465.
    • (1980) J Immunol , vol.125 , pp. 463-465
    • Fischer, D.G.1    Pike, M.C.2    Koren, H.S.3    Snyderman, R.4
  • 16
    • 0030893029 scopus 로고    scopus 로고
    • Undifferentiated U937 cells transfected with chemoattractant receptors: A model system to investigate chemotactic mechanisms and receptor structure/function relationships
    • Kew RR, Peng T, DiMartino SJ, et al. Undifferentiated U937 cells transfected with chemoattractant receptors: a model system to investigate chemotactic mechanisms and receptor structure/function relationships. J Leukoc Biol. 1997;61:329-337.
    • (1997) J Leukoc Biol , vol.61 , pp. 329-337
    • Kew, R.R.1    Peng, T.2    DiMartino, S.J.3
  • 17
    • 33751565688 scopus 로고    scopus 로고
    • A new staphylococcal anti-inflammatory protein that antagonizes the formyl peptide receptor-like 1
    • Prat C, Bestebroer J, de Haas CJ, van Strijp JA, van Kessel KP. A new staphylococcal anti-inflammatory protein that antagonizes the formyl peptide receptor-like 1. J Immunol. 2006;177:8017-8026.
    • (2006) J Immunol , vol.177 , pp. 8017-8026
    • Prat, C.1    Bestebroer, J.2    de Haas, C.J.3    van Strijp, J.A.4    van Kessel, K.P.5
  • 18
    • 6344272749 scopus 로고    scopus 로고
    • N-terminal residues of the chemotaxis inhibitory protein of Staphylococcus aureus are essential for blocking formylated peptide receptor but not C5a receptor
    • Haas PJ, de Haas CJ, Kleibeuker W, et al. N-terminal residues of the chemotaxis inhibitory protein of Staphylococcus aureus are essential for blocking formylated peptide receptor but not C5a receptor. J Immunol. 2004;173:5704-5711.
    • (2004) J Immunol , vol.173 , pp. 5704-5711
    • Haas, P.J.1    de Haas, C.J.2    Kleibeuker, W.3
  • 19
    • 2942538021 scopus 로고    scopus 로고
    • N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins
    • Wang J, Babcock GJ, Choe H, Farzan M, Sodroski J, Gabuzda D. N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins. Virology. 2004;324:140-150.
    • (2004) Virology , vol.324 , pp. 140-150
    • Wang, J.1    Babcock, G.J.2    Choe, H.3    Farzan, M.4    Sodroski, J.5    Gabuzda, D.6
  • 20
    • 0035803466 scopus 로고    scopus 로고
    • Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines
    • Bannert N, Craig S, Farzan M, et al. Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines. J Exp Med. 2001;194:1661-1673.
    • (2001) J Exp Med , vol.194 , pp. 1661-1673
    • Bannert, N.1    Craig, S.2    Farzan, M.3
  • 21
    • 33644828187 scopus 로고    scopus 로고
    • A novel peptide CXCR ligand derived from extracellular matrix degradation during airway inflammation
    • Weathington NM, van Houwelingen AH, Noerager BD, et al. A novel peptide CXCR ligand derived from extracellular matrix degradation during airway inflammation. Nat Med. 2006;12:317-323.
    • (2006) Nat Med , vol.12 , pp. 317-323
    • Weathington, N.M.1    van Houwelingen, A.H.2    Noerager, B.D.3
  • 22
    • 2342512869 scopus 로고    scopus 로고
    • Comparative analysis of high-affinity ligand binding and G protein coupling of the human CXCR1 chemokine receptor and of a CXCR1-Galpha fusion protein after heterologous production in baculovirus-infected insect cells
    • Maeda Y, Kuroki R, Haase W, Michel H, Reilander H. Comparative analysis of high-affinity ligand binding and G protein coupling of the human CXCR1 chemokine receptor and of a CXCR1-Galpha fusion protein after heterologous production in baculovirus-infected insect cells. Eur J Biochem. 2004;271:1677-1689.
    • (2004) Eur J Biochem , vol.271 , pp. 1677-1689
    • Maeda, Y.1    Kuroki, R.2    Haase, W.3    Michel, H.4    Reilander, H.5
  • 23
    • 0034662235 scopus 로고    scopus 로고
    • Identification of distinct surface-expressed and intracellular CXC-chemokine receptor 2 glycoforms in neutrophils: N-glycosylation is essential for maintenance of receptor surface expression
    • Ludwig A, Ehlert JE, Flad HD, Brandt E. Identification of distinct surface-expressed and intracellular CXC-chemokine receptor 2 glycoforms in neutrophils: N-glycosylation is essential for maintenance of receptor surface expression. J Immunol. 2000;165:1044-1052.
    • (2000) J Immunol , vol.165 , pp. 1044-1052
    • Ludwig, A.1    Ehlert, J.E.2    Flad, H.D.3    Brandt, E.4
  • 24
    • 0034327691 scopus 로고    scopus 로고
    • Monocyte chemotactic protein-1 receptor CCR2B is a glycoprotein that has tyrosine sulfation in a conserved extracellular N-terminal region
    • Preobrazhensky AA, Dragan S, Kawano T, et al. Monocyte chemotactic protein-1 receptor CCR2B is a glycoprotein that has tyrosine sulfation in a conserved extracellular N-terminal region. J Immunol. 2000;165:5295-5303.
    • (2000) J Immunol , vol.165 , pp. 5295-5303
    • Preobrazhensky, A.A.1    Dragan, S.2    Kawano, T.3
  • 25
    • 0141621071 scopus 로고    scopus 로고
    • Sulfation of tyrosine 174 in the human C3a receptor is essential for binding of C3a anaphylatoxin
    • Gao J, Choe H, Bota D, Wright PL, Gerard C, Gerard NP. Sulfation of tyrosine 174 in the human C3a receptor is essential for binding of C3a anaphylatoxin. J Biol Chem. 2003;278:37902-37908.
    • (2003) J Biol Chem , vol.278 , pp. 37902-37908
    • Gao, J.1    Choe, H.2    Bota, D.3    Wright, P.L.4    Gerard, C.5    Gerard, N.P.6
  • 26
    • 0027724659 scopus 로고
    • Evidence that the extracellular N-terminal domain of C5aR contains amino-acid residues crucial for C5a binding
    • Mery L, Boulay F. Evidence that the extracellular N-terminal domain of C5aR contains amino-acid residues crucial for C5a binding. Eur J Haematol. 1993;51:282-287.
    • (1993) Eur J Haematol , vol.51 , pp. 282-287
    • Mery, L.1    Boulay, F.2
  • 27
    • 0037436330 scopus 로고    scopus 로고
    • Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor
    • Wenzel-Seifert K, Seifert R. Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor. Biochem Biophys Res Commun. 2003;301:693-698.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 693-698
    • Wenzel-Seifert, K.1    Seifert, R.2
  • 28
    • 0034599741 scopus 로고    scopus 로고
    • Activation of lipoxin A(4) receptors by aspirin-triggered lipoxins and select peptides evokes ligand-specific responses in inflammation
    • Chiang N, Fierro IM, Gronert K, Serhan CN. Activation of lipoxin A(4) receptors by aspirin-triggered lipoxins and select peptides evokes ligand-specific responses in inflammation. J Exp Med. 2000;191:1197-1208.
    • (2000) J Exp Med , vol.191 , pp. 1197-1208
    • Chiang, N.1    Fierro, I.M.2    Gronert, K.3    Serhan, C.N.4
  • 30
    • 33646478846 scopus 로고    scopus 로고
    • Residues from transmembrane helices 3 and 5 participate in leukotriene B4 binding to BLT1
    • Sabirsh A, Bywater RP, Bristulf J, Owman C, Haeggstrom JZ. Residues from transmembrane helices 3 and 5 participate in leukotriene B4 binding to BLT1. Biochemistry. 2006;45:5733-5744.
    • (2006) Biochemistry , vol.45 , pp. 5733-5744
    • Sabirsh, A.1    Bywater, R.P.2    Bristulf, J.3    Owman, C.4    Haeggstrom, J.Z.5
  • 32
    • 0030956418 scopus 로고    scopus 로고
    • Alanine exchanges of polar amino acids in the transmembrane domains of a platelet-activating factor receptor generate both constitutively active and inactive mutants
    • Ishii I, Izumi T, Tsukamoto H, Umeyama H, Ui M, Shimizu T. Alanine exchanges of polar amino acids in the transmembrane domains of a platelet-activating factor receptor generate both constitutively active and inactive mutants. J Biol Chem. 1997;272:7846-7854.
    • (1997) J Biol Chem , vol.272 , pp. 7846-7854
    • Ishii, I.1    Izumi, T.2    Tsukamoto, H.3    Umeyama, H.4    Ui, M.5    Shimizu, T.6
  • 33
  • 34
    • 0034671926 scopus 로고    scopus 로고
    • Characterization of the binding site on the formyl peptide receptor using three receptor mutants and analogs of Met-Leu-Phe and Met-Met-Trp-Leu-Leu
    • Mills JS, Miettinen HM, Cummings D, Jesaitis AJ. Characterization of the binding site on the formyl peptide receptor using three receptor mutants and analogs of Met-Leu-Phe and Met-Met-Trp-Leu-Leu. J Biol Chem. 2000;275:39012-39017.
    • (2000) J Biol Chem , vol.275 , pp. 39012-39017
    • Mills, J.S.1    Miettinen, H.M.2    Cummings, D.3    Jesaitis, A.J.4
  • 35
    • 0027184065 scopus 로고
    • Multiple domains of the N-formyl peptide receptor are required for high-affinity ligand binding. Construction and analysis of chimeric N-formyl peptide receptors
    • Quehenberger O, Prossnitz ER, Cavanagh SL, Cochrane CG, Ye RD. Multiple domains of the N-formyl peptide receptor are required for high-affinity ligand binding. Construction and analysis of chimeric N-formyl peptide receptors. J Biol Chem. 1993;268:18167-18175.
    • (1993) J Biol Chem , vol.268 , pp. 18167-18175
    • Quehenberger, O.1    Prossnitz, E.R.2    Cavanagh, S.L.3    Cochrane, C.G.4    Ye, R.D.5
  • 36
    • 13444251075 scopus 로고    scopus 로고
    • Identification of functional domains in the formyl peptide receptor-like 1 for agonist-induced cell chemotaxis
    • Le Y, Ye RD, Gong W, Li J, Iribarren P, Wang JM. Identification of functional domains in the formyl peptide receptor-like 1 for agonist-induced cell chemotaxis. FEBS J. 2005;272:769-778.
    • (2005) FEBS J , vol.272 , pp. 769-778
    • Le, Y.1    Ye, R.D.2    Gong, W.3    Li, J.4    Iribarren, P.5    Wang, J.M.6
  • 37
    • 33845708770 scopus 로고    scopus 로고
    • ATP release guides neutrophil chemotaxis via P2Y2 and A3 receptors
    • Chen Y, Corriden R, Inoue Y, et al. ATP release guides neutrophil chemotaxis via P2Y2 and A3 receptors. Science. 2006;314:1792-1795.
    • (2006) Science , vol.314 , pp. 1792-1795
    • Chen, Y.1    Corriden, R.2    Inoue, Y.3
  • 38
    • 33846011082 scopus 로고    scopus 로고
    • Random mutagenesis of the complement factor 5a (C5a) receptor N terminus provides a structural constraint for C5a docking
    • Hagemann IS, Narzinski KD, Floyd DH, Baranski TJ. Random mutagenesis of the complement factor 5a (C5a) receptor N terminus provides a structural constraint for C5a docking. J Biol Chem. 2006;281:36783-36792.
    • (2006) J Biol Chem , vol.281 , pp. 36783-36792
    • Hagemann, I.S.1    Narzinski, K.D.2    Floyd, D.H.3    Baranski, T.J.4
  • 39
    • 0028844558 scopus 로고
    • The role of N-glycosylation for functional expression of the human platelet-activating factor receptor. Glycosylation is required for efficient membrane trafficking
    • Garcia RC, Cundell DR, Tuomanen EI, Kolakowski LF Jr, Gerard C, Gerard NP. The role of N-glycosylation for functional expression of the human platelet-activating factor receptor. Glycosylation is required for efficient membrane trafficking. J Biol Chem. 1995;270:25178-25184.
    • (1995) J Biol Chem , vol.270 , pp. 25178-25184
    • Garcia, R.C.1    Cundell, D.R.2    Tuomanen, E.I.3    Kolakowski Jr, L.F.4    Gerard, C.5    Gerard, N.P.6
  • 40
    • 0012805136 scopus 로고    scopus 로고
    • Recombinant P-selectin glycoprotein ligand-1 directly inhibits leukocyte rolling by all 3 selectins in vivo: Complete inhibition of rolling is not required for anti-inflammatory effect
    • Hicks AE, Nolan SL, Ridger VC, Hellewell PG, Norman KE. Recombinant P-selectin glycoprotein ligand-1 directly inhibits leukocyte rolling by all 3 selectins in vivo: complete inhibition of rolling is not required for anti-inflammatory effect. Blood. 2003;101:3249-3256.
    • (2003) Blood , vol.101 , pp. 3249-3256
    • Hicks, A.E.1    Nolan, S.L.2    Ridger, V.C.3    Hellewell, P.G.4    Norman, K.E.5
  • 41
    • 34247261581 scopus 로고    scopus 로고
    • Interaction of the selectin ligand PSGL-1 with chemokines CCL21 and CCL19 facilitates efficient homing of T cells to secondary lymphoid organs
    • Veerman KM, Williams MJ, Uchimura K, et al. Interaction of the selectin ligand PSGL-1 with chemokines CCL21 and CCL19 facilitates efficient homing of T cells to secondary lymphoid organs. Nat Immunol. 2007;8:532-539.
    • (2007) Nat Immunol , vol.8 , pp. 532-539
    • Veerman, K.M.1    Williams, M.J.2    Uchimura, K.3
  • 42
    • 10644292431 scopus 로고    scopus 로고
    • Human P-selectin glycoprotein ligand-1 (PSGL-1) interacts with the skin-associated chemokine CCL27 via sulfated tyrosines at the PSGL-1 amino terminus
    • Hirata T, Furukawa Y, Yang BG, et al. Human P-selectin glycoprotein ligand-1 (PSGL-1) interacts with the skin-associated chemokine CCL27 via sulfated tyrosines at the PSGL-1 amino terminus. J Biol Chem. 2004;279:51775-51782.
    • (2004) J Biol Chem , vol.279 , pp. 51775-51782
    • Hirata, T.1    Furukawa, Y.2    Yang, B.G.3
  • 43
    • 0037271850 scopus 로고    scopus 로고
    • Viral mimicry of cytokines, chemokines and their receptors
    • Alcami A. Viral mimicry of cytokines, chemokines and their receptors. Nat Rev Immunol. 2003;3:36-50.
    • (2003) Nat Rev Immunol , vol.3 , pp. 36-50
    • Alcami, A.1
  • 44
    • 0038218002 scopus 로고    scopus 로고
    • Subversion of the chemokine world by microbial pathogens
    • Liston A, McColl S. Subversion of the chemokine world by microbial pathogens. Bioessays. 2003; 25:478-488.
    • (2003) Bioessays , vol.25 , pp. 478-488
    • Liston, A.1    McColl, S.2
  • 45
  • 46
    • 0037621716 scopus 로고    scopus 로고
    • Proteoglycans are potent modulators of the biological responses of eosinophils to chemokines
    • Culley FJ, Fadlon EJ, Kirchem A, Williams TJ, Jose PJ, Pease JE. Proteoglycans are potent modulators of the biological responses of eosinophils to chemokines. Eur J Immunol. 2003;33: 1302-1310.
    • (2003) Eur J Immunol , vol.33 , pp. 1302-1310
    • Culley, F.J.1    Fadlon, E.J.2    Kirchem, A.3    Williams, T.J.4    Jose, P.J.5    Pease, J.E.6
  • 47
    • 33746039699 scopus 로고    scopus 로고
    • Chemoattractants, extracellular proteases, and the integrated host defense response
    • Zabel BA, Zuniga L, Ohyama T, et al. Chemoattractants, extracellular proteases, and the integrated host defense response. Exp Hematol. 2006;34:1021-1032.
    • (2006) Exp Hematol , vol.34 , pp. 1021-1032
    • Zabel, B.A.1    Zuniga, L.2    Ohyama, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.