메뉴 건너뛰기




Volumn 102, Issue 2, 2003, Pages 689-697

Defect in neutrophil killing and increased susceptibility to infection with nonpathogenic gram-positive bacteria in peptidoglycan recognition protein-S (PGRP-S)-deficient mice

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN 6; PROTEIN S; TUMOR NECROSIS FACTOR ALPHA;

EID: 0038826813     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2002-12-3853     Document Type: Article
Times cited : (159)

References (54)
  • 2
    • 0034680145 scopus 로고    scopus 로고
    • Toll-like receptors in the induction of the innate immune responses
    • Aderem A, Ulevitch RJ. Toll-like receptors in the induction of the innate immune responses. Nature. 2000;406:782-787.
    • (2000) Nature , vol.406 , pp. 782-787
    • Aderem, A.1    Ulevitch, R.J.2
  • 4
    • 0032544089 scopus 로고    scopus 로고
    • A peptidoglycan recognition protein in innate immunity conserved from insects to mammals
    • Kang D, Liu G, Lundstrom A, Gelius E, Steiner H. A peptidoglycan recognition protein in innate immunity conserved from insects to mammals. Proc Natl Acad Sci U S A. 1998;95:10078-10082.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 10078-10082
    • Kang, D.1    Liu, G.2    Lundstrom, A.3    Gelius, E.4    Steiner, H.5
  • 5
  • 6
    • 0035860732 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins: A novel family of four human innate immunity pattern recognition molecules
    • Liu C, Xu Z, Gupta D, Dziarski R. Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules. J Biol Chem. 2001;276:34686-34694.
    • (2001) J Biol Chem , vol.276 , pp. 34686-34694
    • Liu, C.1    Xu, Z.2    Gupta, D.3    Dziarski, R.4
  • 7
    • 0029884417 scopus 로고    scopus 로고
    • Purification of peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori
    • Yoshida H, Kinoshita K, Ashida M. Purification of peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori. J Biol Chem. 1996;271:13854-13860.
    • (1996) J Biol Chem , vol.271 , pp. 13854-13860
    • Yoshida, H.1    Kinoshita, K.2    Ashida, M.3
  • 8
    • 0000926038 scopus 로고    scopus 로고
    • Recent advances in research on the insect prophenoloxidase cascade
    • Brey PT, Hultmark D, eds. London, England: Chapman & Hall
    • Ashida M, Brey PT. Recent advances in research on the insect prophenoloxidase cascade. In: Brey PT, Hultmark D, eds. Molecular Mechanisms of Immune Responses in Insects. London, England: Chapman & Hall; 1997:135-172.
    • (1997) Molecular Mechanisms of Immune Responses in Insects , pp. 135-172
    • Ashida, M.1    Brey, P.T.2
  • 9
    • 0035856990 scopus 로고    scopus 로고
    • Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein
    • Michel T, Reichhart J-M, Hoffmann JA, Royet J. Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein. Nature. 2001;414:756-759.
    • (2001) Nature , vol.414 , pp. 756-759
    • Michel, T.1    Reichhart, J.-M.2    Hoffmann, J.A.3    Royet, J.4
  • 10
    • 0037061450 scopus 로고    scopus 로고
    • The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein
    • Gottar M, Gobert V, Michel T, et al. The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein. Nature. 2002;416:640-644.
    • (2002) Nature , vol.416 , pp. 640-644
    • Gottar, M.1    Gobert, V.2    Michel, T.3
  • 11
    • 0037066464 scopus 로고    scopus 로고
    • Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila
    • Choe K-M, Werner T, Stoven S, Hultmark D, Anderson KV. Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila. Science. 2002;296:359-362.
    • (2002) Science , vol.296 , pp. 359-362
    • Choe, K.-M.1    Werner, T.2    Stoven, S.3    Hultmark, D.4    Anderson, K.V.5
  • 12
    • 0037061482 scopus 로고    scopus 로고
    • Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli
    • Ramet M, Manfruelli P, Pearson A, Mathey-Prevot B, Ezekowitz RAB. Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature. 2002;416:644-648.
    • (2002) Nature , vol.416 , pp. 644-648
    • Ramet, M.1    Manfruelli, P.2    Pearson, A.3    Mathey-Prevot, B.4    Ezekowitz, R.A.B.5
  • 13
    • 0037108754 scopus 로고    scopus 로고
    • Overexpression of a pattern-recognition receptor, peptidoglycan-recognition protein-LE, activates imd/ relish-mediated antibacterial defense and the prophenoloxidase cascade in Drosophila larvae
    • Takehana A, Katsuyama T, Yano T, et al. Overexpression of a pattern-recognition receptor, peptidoglycan-recognition protein-LE, activates imd/ relish-mediated antibacterial defense and the prophenoloxidase cascade in Drosophila larvae. Proc Natl Acad Sci U S A. 2002;99:13705-13710.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13705-13710
    • Takehana, A.1    Katsuyama, T.2    Yano, T.3
  • 14
    • 0034637543 scopus 로고    scopus 로고
    • Mammalian peptidoglycan recognition protein binds peptidoglycan with high affinity, is expressed in neutrophils, and inhibits bacterial growth
    • Liu C, Gelius E, Liu G, Steiner H, Dziarski R. Mammalian peptidoglycan recognition protein binds peptidoglycan with high affinity, is expressed in neutrophils, and inhibits bacterial growth. J Biol Chem. 2000;275:24490-24499.
    • (2000) J Biol Chem , vol.275 , pp. 24490-24499
    • Liu, C.1    Gelius, E.2    Liu, G.3    Steiner, H.4    Dziarski, R.5
  • 15
    • 0021866578 scopus 로고
    • Soluble peptidoglycan fragments stimulate antibacterial protein by fat body from larvae of Manduca sexta
    • Dunn PE, Dai W, Kanost MR, Geng CX. Soluble peptidoglycan fragments stimulate antibacterial protein by fat body from larvae of Manduca sexta. Dev Comp Immunol. 1985;9:559-568.
    • (1985) Dev Comp Immunol , vol.9 , pp. 559-568
    • Dunn, P.E.1    Dai, W.2    Kanost, M.R.3    Geng, C.X.4
  • 16
    • 0032714015 scopus 로고    scopus 로고
    • Interactions of CD14 with components of Gram-positive bacteria
    • Dziarski R, Ulmer AJ, Gupta D. Interactions of CD14 with components of Gram-positive bacteria. Chem Immunol. 2000;74:83-107.
    • (2000) Chem Immunol , vol.74 , pp. 83-107
    • Dziarski, R.1    Ulmer, A.J.2    Gupta, D.3
  • 17
    • 0003014798 scopus 로고    scopus 로고
    • Interactions of bacterial lipopolysaccharide and peptidoglycan with mammalian CD14
    • Doyle RJ, ed. New York, NY: Kluwer Academic/Plenum
    • Dziarski R, Ulmer AJ, Gupta D. Interactions of bacterial lipopolysaccharide and peptidoglycan with mammalian CD14. In: Doyle RJ, ed. Glycomicrobiology. New York, NY: Kluwer Academic/ Plenum; 2000:145-186.
    • (2000) Glycomicrobiology , pp. 145-186
    • Dziarski, R.1    Ulmer, A.J.2    Gupta, D.3
  • 18
    • 0037530328 scopus 로고    scopus 로고
    • The bacterial cell: Peptidoglycan
    • Sussman M, ed. Molecular Medical Microbiology. London, England: Academic Press
    • Doyle RJ, Dziarski R. The bacterial cell: peptidoglycan. In: Sussman M, ed. Molecular Medical Microbiology. London, England: Academic Press; 2001:137-153.
    • (2001) , pp. 137-153
    • Doyle, R.J.1    Dziarski, R.2
  • 19
    • 0029048442 scopus 로고
    • Peptidoglycan induces transcription and secretion of TNF-α and activation of Lyn, extracellular signal-regulated kinase, and Rsk signal transduction proteins in mouse macrophages
    • Gupta D, Jin Y, Dziarski R. Peptidoglycan induces transcription and secretion of TNF-α and activation of Lyn, extracellular signal-regulated kinase, and Rsk signal transduction proteins in mouse macrophages. J Immunol. 1995;155:2620-2630.
    • (1995) J Immunol , vol.155 , pp. 2620-2630
    • Gupta, D.1    Jin, Y.2    Dziarski, R.3
  • 20
    • 0034617074 scopus 로고    scopus 로고
    • Chemokines are the main pro-inflammatory mediators in human monocytes activated by Staphylococcus aureus, peptidoglycan, and endotoxin
    • Wang Z-M, Liu C, Dziarski R. Chemokines are the main pro-inflammatory mediators in human monocytes activated by Staphylococcus aureus, peptidoglycan, and endotoxin. J Biol Chem. 2000;275:20260-20267.
    • (2000) J Biol Chem , vol.275 , pp. 20260-20267
    • Wang, Z.-M.1    Liu, C.2    Dziarski, R.3
  • 21
    • 0019141043 scopus 로고
    • Polyclonal activation of immunoglobulin secretion in B lymphocytes induced by staphylococcal peptidoglycan
    • Dziarski R. Polyclonal activation of immunoglobulin secretion in B lymphocytes induced by staphylococcal peptidoglycan. J Immunol. 1980;125:2478-2483.
    • (1980) J Immunol , vol.125 , pp. 2478-2483
    • Dziarski, R.1
  • 22
    • 0028114530 scopus 로고
    • Soluble peptidoglycan-induced monokine production can be blocked by anti-CD14 monoclonal antibodies and by lipid A partial structures
    • Weidemann B, Brade H, Rietschel ET, et al. Soluble peptidoglycan-induced monokine production can be blocked by anti-CD14 monoclonal antibodies and by lipid A partial structures. Infect Immun. 1994;62:4709-4715.
    • (1994) Infect Immun , vol.62 , pp. 4709-4715
    • Weidemann, B.1    Brade, H.2    Rietschel, E.T.3
  • 23
    • 0029814185 scopus 로고    scopus 로고
    • CD14 is a cell-activating receptor for bacterial peptidoglycan
    • Gupta D, Kirkland TN, Viriyakosol S, Dziarski R. CD14 is a cell-activating receptor for bacterial peptidoglycan. J Biol Chem. 1996;27:23310-23316.
    • (1996) J Biol Chem , vol.27 , pp. 23310-23316
    • Gupta, D.1    Kirkland, T.N.2    Viriyakosol, S.3    Dziarski, R.4
  • 24
    • 0032502682 scopus 로고    scopus 로고
    • Binding of bacterial peptidoglycan to CD14
    • Dziarski R, Tapping RI, Tobias P. Binding of bacterial peptidoglycan to CD14. J Biol Chem. 1998;273:8680-8690.
    • (1998) J Biol Chem , vol.273 , pp. 8680-8690
    • Dziarski, R.1    Tapping, R.I.2    Tobias, P.3
  • 25
    • 0033580949 scopus 로고    scopus 로고
    • Peptidoglycan- and lipoteichoic acid-induced cell activation is mediated by Toll-like receptor 2
    • Schwandner R, Dziarski R, Wesche H, Rothe M, Kirschning CJ. Peptidoglycan- and lipoteichoic acid-induced cell activation is mediated by Toll-like receptor 2. J Biol Chem. 1999;274:17406-17409.
    • (1999) J Biol Chem , vol.274 , pp. 17406-17409
    • Schwandner, R.1    Dziarski, R.2    Wesche, H.3    Rothe, M.4    Kirschning, C.J.5
  • 26
    • 0033168728 scopus 로고    scopus 로고
    • Recognition of Grampositive bacterial cell wall components by the innate immune system occurs via Toll-like receptor 2
    • Yoshimura A, Lien E, Ingalls RR, Tuomanen E, Dziarski R, Golenbock D. Recognition of Grampositive bacterial cell wall components by the innate immune system occurs via Toll-like receptor 2. J Immunol. 1999;163:1-5.
    • (1999) J Immunol , vol.163 , pp. 1-5
    • Yoshimura, A.1    Lien, E.2    Ingalls, R.R.3    Tuomanen, E.4    Dziarski, R.5    Golenbock, D.6
  • 27
    • 0033213590 scopus 로고    scopus 로고
    • Differential roles of TLR2 and TLR4 in recognition of Gram-negative and Gram-positive bacterial cell wall components
    • Takeuchi O, Hoshino K, Kawai T, et al. Differential roles of TLR2 and TLR4 in recognition of Gram-negative and Gram-positive bacterial cell wall components. Immunity. 1999;11:443-451.
    • (1999) Immunity , vol.11 , pp. 443-451
    • Takeuchi, O.1    Hoshino, K.2    Kawai, T.3
  • 28
    • 0037205436 scopus 로고    scopus 로고
    • Isolation, characterization, and antimicrobial properties of bovine oligosaccharide-binding protein
    • Tydell CC, Yount N, Tran D, Yuan J, Selsted ME. Isolation, characterization, and antimicrobial properties of bovine oligosaccharide-binding protein. J Biol Chem. 2002;277:19658-19664.
    • (2002) J Biol Chem , vol.277 , pp. 19658-19664
    • Tydell, C.C.1    Yount, N.2    Tran, D.3    Yuan, J.4    Selsted, M.E.5
  • 29
    • 0033059762 scopus 로고    scopus 로고
    • Construction of gene targeting vectors from XKOS genomic libraries
    • Wattler S, Kelly M, Nehls M. Construction of gene targeting vectors from XKOS genomic libraries. Biotechniques. 1999;26:1150-1160.
    • (1999) Biotechniques , vol.26 , pp. 1150-1160
    • Wattler, S.1    Kelly, M.2    Nehls, M.3
  • 30
    • 0029081511 scopus 로고
    • The importance of a lipopolysaccharide-initiated, cytokine-mediated host defense mechanism in mice against extraintestinally invasive Escherichia coli
    • Cross A, Asher L, Seguin M, et al. The importance of a lipopolysaccharide-initiated, cytokine-mediated host defense mechanism in mice against extraintestinally invasive Escherichia coli. J Clin Invest. 1995;96:676-689.
    • (1995) J Clin Invest , vol.96 , pp. 676-689
    • Cross, A.1    Asher, L.2    Seguin, M.3
  • 31
    • 0028085885 scopus 로고
    • Measurement of nonopsonic phagocytic killing by human and mouse phagocytes
    • Rest RF, Speert DP. Measurement of nonopsonic phagocytic killing by human and mouse phagocytes. Meth Enzymol. 1994;236:91-108.
    • (1994) Meth Enzymol , vol.236 , pp. 91-108
    • Rest, R.F.1    Speert, D.P.2
  • 32
    • 0001905297 scopus 로고    scopus 로고
    • Measurement of bacterial ingestion and killing by macrophages
    • Coligan JH, et al, eds. New York, NY: John Wiley & Sons; 1994:14.6.1-14.6.
    • Campbell PA, Canono BP, Drevets DA. Measurement of bacterial ingestion and killing by macrophages. In: Coligan JH, et al, eds. Current Protocols in Immunology. New York, NY: John Wiley & Sons; 1994:14.6.1-14.6.13.
    • Current Protocols in Immunology , pp. 13
    • Campbell, P.A.1    Canono, B.P.2    Drevets, D.A.3
  • 33
    • 0028265107 scopus 로고
    • Isolation and characterization of gelatinase granules from human neutrophils
    • Kjeldsen LH, Sengelov H, Lollike H, Nielsen MH, Borregaard N. Isolation and characterization of gelatinase granules from human neutrophils. Blood. 1994;83:1640-1649.
    • (1994) Blood , vol.83 , pp. 1640-1649
    • Kjeldsen, L.H.1    Sengelov, H.2    Lollike, H.3    Nielsen, M.H.4    Borregaard, N.5
  • 34
    • 0030997435 scopus 로고
    • Granules of the human neutrophilic polymorphonuclear leukocyte
    • Borregaard N, Cowland JB. Granules of the human neutrophilic polymorphonuclear leukocyte. Blood. 1977;89:3503-3521.
    • (1977) Blood , vol.89 , pp. 3503-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 35
    • 0006780884 scopus 로고    scopus 로고
    • Neutrophilic leukocytes
    • Lee GR, et al, eds. Baltimore, MD: Williams & Wilkins
    • Skubitz KM. Neutrophilic leukocytes. In: Lee GR, et al, eds. Wintrobe's Clinical Hematology. Baltimore, MD: Williams & Wilkins; 1999:300-350.
    • (1999) Wintrobe's Clinical Hematology , pp. 300-350
    • Skubitz, K.M.1
  • 36
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • Hampton MB, Kettle AJ, Winterbourn CC. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood. 1998;92:3007-3017.
    • (1998) Blood , vol.92 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 37
    • 0002328868 scopus 로고    scopus 로고
    • Granulocytic phagocytes
    • Mandell GL, Bennett JE, Dolin R, eds. Vol 1. Philadelphia, PA: Churchill Livingstone
    • Nauseef WM, Clark RA. Granulocytic phagocytes. In: Mandell GL, Bennett JE, Dolin R, eds. Principles and Practice of Infectious Diseases. Vol 1. Philadelphia, PA: Churchill Livingstone; 2000:89-112.
    • (2000) Principles and Practice of Infectious Diseases , pp. 89-112
    • Nauseef, W.M.1    Clark, R.A.2
  • 38
    • 0036198121 scopus 로고    scopus 로고
    • Antimicrobial polypeptides in host defense of the respiratory tract
    • Ganz T. Antimicrobial polypeptides in host defense of the respiratory tract. J Clin Invest. 2002;109:693-697.
    • (2002) J Clin Invest , vol.109 , pp. 693-697
    • Ganz, T.1
  • 40
    • 0017834531 scopus 로고
    • Oxygen-dependent microbial killing by phagocytes
    • Babior BM. Oxygen-dependent microbial killing by phagocytes. N Engl J Med. 1978;298:659-668.
    • (1978) N Engl J Med , vol.298 , pp. 659-668
    • Babior, B.M.1
  • 41
    • 0025976579 scopus 로고
    • Molecular basis of chronic granulomatous disease
    • Smith RM, Curnutte JT. Molecular basis of chronic granulomatous disease. N Engl J Med. 1991;77:673-686.
    • (1991) N Engl J Med , vol.77 , pp. 673-686
    • Smith, R.M.1    Curnutte, J.T.2
  • 42
    • 0015975763 scopus 로고
    • Bactericidal activity of aerobic and anaerobic polymorphonuclear neutrophils
    • Mandell GL. Bactericidal activity of aerobic and anaerobic polymorphonuclear neutrophils. Infect Immun. 1974;9:337-341.
    • (1974) Infect Immun , vol.9 , pp. 337-341
    • Mandell, G.L.1
  • 45
    • 0030816504 scopus 로고    scopus 로고
    • Redundant contribution of myeloperoxidase-dependent systems to neutrophil-mediated killing of Escherichia coli
    • Rosen H, Michel BR. Redundant contribution of myeloperoxidase-dependent systems to neutrophil-mediated killing of Escherichia coli. Infect Immun. 1997;65:4173-4178.
    • (1997) Infect Immun , vol.65 , pp. 4173-4178
    • Rosen, H.1    Michel, B.R.2
  • 46
    • 0027514011 scopus 로고
    • Purification, primary structure, and antimicrobial activities of β-defensins, a new family of antimicrobial peptides from bovine neutrophils
    • Selsted ME, Tang Y-Q, Morris WL, et al. Purification, primary structure, and antimicrobial activities of β-defensins, a new family of antimicrobial peptides from bovine neutrophils. J Biol Chem. 1993;268:6641-6648.
    • (1993) J Biol Chem , vol.268 , pp. 6641-6648
    • Selsted, M.E.1    Tang, Y.-Q.2    Morris, W.L.3
  • 48
    • 0037470091 scopus 로고    scopus 로고
    • A scavenger function for a Drosophila peptidoglycan recognition protein
    • Mellroth P, Karlsson J, Steiner H. A scavenger function for a Drosophila peptidoglycan recognition protein. J Biol Chem. 2003;278:7059-7064.
    • (2003) J Biol Chem , vol.278 , pp. 7059-7064
    • Mellroth, P.1    Karlsson, J.2    Steiner, H.3
  • 49
    • 0035253732 scopus 로고    scopus 로고
    • MD-2 enables Toll-like receptor-2 (TLR2)-mediated responses to LPS and enhances TLR2-mediated responses to Gram-positive and Gram-negative bacteria and their cell wall components
    • Dziarski R, Wang Q, Miyake K, Kirschning CJ, Gupta D. MD-2 enables Toll-like receptor-2 (TLR2)-mediated responses to LPS and enhances TLR2-mediated responses to Gram-positive and Gram-negative bacteria and their cell wall components. J Immunol. 2001;166:1938-1944.
    • (2001) J Immunol , vol.166 , pp. 1938-1944
    • Dziarski, R.1    Wang, Q.2    Miyake, K.3    Kirschning, C.J.4    Gupta, D.5
  • 50
    • 0036167107 scopus 로고    scopus 로고
    • Drosophila innate immunity: An evolutionary perspective
    • Hoffmann JA, Reichhart J-M. Drosophila innate immunity: an evolutionary perspective. Nat Immunol. 2002;3:121-126.
    • (2002) Nat Immunol , vol.3 , pp. 121-126
    • Hoffmann, J.A.1    Reichhart, J.-M.2
  • 51
    • 0034007076 scopus 로고    scopus 로고
    • Physical contact between lipopolysaccharide and Toll-like receptor 4 revealed by genetic complementation
    • Poltorak A, Ricciardi-Castagnoli P, Citterio S, Beutler B. Physical contact between lipopolysaccharide and Toll-like receptor 4 revealed by genetic complementation. Proc Natl Acad Sci U S A. 2000;97:2163-2167.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 2163-2167
    • Poltorak, A.1    Ricciardi-Castagnoli, P.2    Citterio, S.3    Beutler, B.4
  • 52
    • 0034002247 scopus 로고    scopus 로고
    • Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide
    • Lien E, Means TK, Heine H, et al. Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide. J Clin Invest. 2000;105:497-504.
    • (2000) J Clin Invest , vol.105 , pp. 497-504
    • Lien, E.1    Means, T.K.2    Heine, H.3
  • 53
    • 0037025399 scopus 로고    scopus 로고
    • The extracellular Toll-like receptor 2 domain directly binds peptidoglycan derived from Staphylococcus aureus
    • Iwaki D, Mitsuzawa H, Murakami S, et al. The extracellular Toll-like receptor 2 domain directly binds peptidoglycan derived from Staphylococcus aureus. J Biol Chem. 2002;277:24315-24320.
    • (2002) J Biol Chem , vol.277 , pp. 24315-24320
    • Iwaki, D.1    Mitsuzawa, H.2    Murakami, S.3
  • 54
    • 0035877718 scopus 로고    scopus 로고
    • Lipopolysaccharide is in close proximity to each of the proteins in its membrane receptor complex: Transfer from CD14 to TLR4 and MD-2
    • da Silva Correia J, Soldau K, Christen U, Tobias PS, Ulevitch RJ. Lipopolysaccharide is in close proximity to each of the proteins in its membrane receptor complex: transfer from CD14 to TLR4 and MD-2. J Biol Chem. 2001;276:21129-21135.
    • (2001) J Biol Chem , vol.276 , pp. 21129-21135
    • Da Silva Correia, J.1    Soldau, K.2    Christen, U.3    Tobias, P.S.4    Ulevitch, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.