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Volumn 12, Issue 3, 2012, Pages 168-179

Accessory molecules for Toll-like receptors and their function

Author keywords

[No Author keywords available]

Indexed keywords

B LYMPHOCYTE RECEPTOR; CHAPERONE; DECTIN 1; DNA; HIGH MOBILITY GROUP B1 PROTEIN; PATTERN RECOGNITION RECEPTOR; PROTEIN MD 2; RNA; TOLL LIKE RECEPTOR; VITRONECTIN;

EID: 84862804952     PISSN: 14741733     EISSN: 14741741     Source Type: Journal    
DOI: 10.1038/nri3151     Document Type: Review
Times cited : (339)

References (103)
  • 1
    • 0031739939 scopus 로고    scopus 로고
    • Introduction: The role of innate immunity in the adaptive immune response
    • Janeway, C. A. Jr & Medzhitov, R. Introduction: the role of innate immunity in the adaptive immune response. Semin. Immunol. 10, 349-350 (1998).
    • (1998) Semin. Immunol. , vol.10 , pp. 349-350
    • Janeway Jr., C.A.1    Medzhitov, R.2
  • 2
    • 33845951211 scopus 로고    scopus 로고
    • DAMPs, PAMPs and alarmins: All we need to know about danger
    • Bianchi, M. E. DAMPs, PAMPs and alarmins: all we need to know about danger. J. Leukoc. Biol. 81, 1-5 (2007).
    • (2007) J. Leukoc. Biol. , vol.81 , pp. 1-5
    • Bianchi, M.E.1
  • 3
    • 79959447465 scopus 로고    scopus 로고
    • Structural biology of the Toll-like receptor family
    • Kang, J. Y. & Lee, J.-O. Structural biology of the Toll-like receptor family. Annu. Rev. Biochem. 80, 917-941 (2011).
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 917-941
    • Kang, J.Y.1    Lee, J.-O.2
  • 4
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: Update on Toll-like receptors
    • Kawai, T. & Akira, S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nature Immunol. 11, 373-384 (2010).
    • (2010) Nature Immunol. , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 5
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling
    • O'Neill, L. A. & Bowie, A. G. The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. Nature Rev. Immunol. 7, 353-364 (2007).
    • (2007) Nature Rev. Immunol. , vol.7 , pp. 353-364
    • O'Neill, L.A.1    Bowie, A.G.2
  • 6
    • 33847183077 scopus 로고    scopus 로고
    • Cooperation of Toll-like receptor signals in innate immune defence
    • Trinchieri, G. & Sher, A. Cooperation of Toll-like receptor signals in innate immune defence. Nature Rev. Immunol. 7, 179-190 (2007).
    • (2007) Nature Rev. Immunol. , vol.7 , pp. 179-190
    • Trinchieri, G.1    Sher, A.2
  • 7
    • 20644450804 scopus 로고    scopus 로고
    • Negative regulation of Toll-like receptor-mediated immune responses
    • Liew, F. Y., Xu, D., Brint, E. K. & O'Neill, L. A. Negative regulation of Toll-like receptor-mediated immune responses. Nature Rev. Immunol. 5, 446-458 (2005).
    • (2005) Nature Rev. Immunol. , vol.5 , pp. 446-458
    • Liew, F.Y.1    Xu, D.2    Brint, E.K.3    O'Neill, L.A.4
  • 8
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder, K. & Tschopp, J. The inflammasomes. Cell 140, 821-832 (2010).
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 9
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi, O. & Akira, S. Pattern recognition receptors and inflammation. Cell 140, 805-820 (2010).
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 10
    • 74549206702 scopus 로고    scopus 로고
    • How the noninflammasome NLRs function in the innate immune system
    • Ting, J. P., Duncan, J. A. & Lei, Y. How the noninflammasome NLRs function in the innate immune system. Science 327, 286-290 (2010).
    • (2010) Science , vol.327 , pp. 286-290
    • Ting, J.P.1    Duncan, J.A.2    Lei, Y.3
  • 11
    • 77649179433 scopus 로고    scopus 로고
    • NLRP3 inflammasome activation: The convergence of multiple signalling pathways on ROS production?
    • Tschopp, J. & Schroder, K. NLRP3 inflammasome activation: the convergence of multiple signalling pathways on ROS production? Nature Rev. Immunol. 10, 210-215 (2010).
    • (2010) Nature Rev. Immunol. , vol.10 , pp. 210-215
    • Tschopp, J.1    Schroder, K.2
  • 12
    • 0028965644 scopus 로고
    • Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin
    • Ulevitch, R. J. & Tobias, P. S. Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin. Annu. Rev. Immunol. 13, 437-457 (1995).
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 437-457
    • Ulevitch, R.J.1    Tobias, P.S.2
  • 13
    • 20644469429 scopus 로고    scopus 로고
    • CD14 is required for MyD88-independent LPS signaling
    • Jiang, Z. et al. CD14 is required for MyD88-independent LPS signaling. Nature Immunol. 6, 565-570 (2005).
    • (2005) Nature Immunol. , vol.6 , pp. 565-570
    • Jiang, Z.1
  • 14
    • 0032502682 scopus 로고    scopus 로고
    • Binding of bacterial peptidoglycan to CD14
    • Dziarski, R., Tapping, R. I. & Tobias, P. S. Binding of bacterial peptidoglycan to CD14. J. Biol. Chem. 273, 8680-8690 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 8680-8690
    • Dziarski, R.1    Tapping, R.I.2    Tobias, P.S.3
  • 15
    • 4043051517 scopus 로고    scopus 로고
    • Lipopolysaccharide binding protein binds to triacylated and diacylated lipopeptides and mediates innate immune responses
    • Schroder, N. W. et al. Lipopolysaccharide binding protein binds to triacylated and diacylated lipopeptides and mediates innate immune responses. J. Immunol. 173, 2683-2691 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 2683-2691
    • Schroder, N.W.1
  • 16
    • 0038182550 scopus 로고    scopus 로고
    • Lipoteichoic acid (LTA) of Streptococcus pneumoniae and Staphylococcus aureus activates immune cells via Toll-like receptor (TLR)-2, lipopolysaccharide-binding protein (LBP), and CD14, whereas TLR-4 and MD-2 are not involved
    • Schroder, N. W. et al. Lipoteichoic acid (LTA) of Streptococcus pneumoniae and Staphylococcus aureus activates immune cells via Toll-like receptor (TLR)-2, lipopolysaccharide-binding protein (LBP), and CD14, whereas TLR-4 and MD-2 are not involved. J. Biol. Chem. 278, 15587-15594 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 15587-15594
    • Schroder, N.W.1
  • 17
    • 0030685133 scopus 로고    scopus 로고
    • Lipopolysaccharide-binding protein is required to combat a murine Gram-negative bacterial infection
    • Jack, R. S. et al. Lipopolysaccharide-binding protein is required to combat a murine Gram-negative bacterial infection. Nature 389, 742-745 (1997).
    • (1997) Nature , vol.389 , pp. 742-745
    • Jack, R.S.1
  • 18
    • 0041429598 scopus 로고    scopus 로고
    • Recognition of pneumococcal peptidoglycan: An expanded, pivotal role for LPS binding protein
    • Weber, J. R. et al. Recognition of pneumococcal peptidoglycan: an expanded, pivotal role for LPS binding protein. Immunity 19, 269-279 (2003).
    • (2003) Immunity , vol.19 , pp. 269-279
    • Weber, J.R.1
  • 19
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu, R. et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J. Exp. Med. 189, 1777-1782 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 1777-1782
    • Shimazu, R.1
  • 20
    • 0036301797 scopus 로고    scopus 로고
    • Essential role of MD-2 in LPS responsiveness and TLR4 distribution
    • Nagai, Y. et al. Essential role of MD-2 in LPS responsiveness and TLR4 distribution. Nature Immunol. 3, 667-672 (2002).
    • (2002) Nature Immunol. , vol.3 , pp. 667-672
    • Nagai, Y.1
  • 21
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • This paper is the first description of the crystal structure of a TLR in complex with its ligand and an accessory molecule
    • Park, B. S. et al. The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 458, 1191-1195 (2009). This paper is the first description of the crystal structure of a TLR in complex with its ligand and an accessory molecule.
    • (2009) Nature , vol.458 , pp. 1191-1195
    • Park, B.S.1
  • 22
    • 0028911434 scopus 로고
    • The CD36, CLA-1 (CD36L1), and LIMPII (CD36L2) gene family: Cellular distribution, chromosomal location, and genetic evolution
    • Calvo, D., Dopazo, J. & Vega, M. A. The CD36, CLA-1 (CD36L1), and LIMPII (CD36L2) gene family: cellular distribution, chromosomal location, and genetic evolution. Genomics 25, 100-106 (1995).
    • (1995) Genomics , vol.25 , pp. 100-106
    • Calvo, D.1    Dopazo, J.2    Vega, M.A.3
  • 23
    • 33750070631 scopus 로고    scopus 로고
    • Membrane sorting of Toll-like receptor (TLR)-2/6 and TLR2/1 heterodimers at the cell surface determines heterotypic associations with CD36 and intracellular targeting
    • Triantafilou, M. et al. Membrane sorting of Toll-like receptor (TLR)-2/6 and TLR2/1 heterodimers at the cell surface determines heterotypic associations with CD36 and intracellular targeting. J. Biol. Chem. 281, 31002-31011 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 31002-31011
    • Triantafilou, M.1
  • 24
    • 13444280215 scopus 로고    scopus 로고
    • CD36 is a sensor of diacylglycerides
    • Hoebe, K. et al. CD36 is a sensor of diacylglycerides. Nature 433, 523-527 (2005).
    • (2005) Nature , vol.433 , pp. 523-527
    • Hoebe, K.1
  • 25
    • 23744514918 scopus 로고    scopus 로고
    • Response to Staphylococcus aureus requires CD36-mediated phagocytosis triggered by the COOH-terminal cytoplasmic domain
    • Stuart, L. M. et al. Response to Staphylococcus aureus requires CD36-mediated phagocytosis triggered by the COOH-terminal cytoplasmic domain. J. Cell Biol. 170, 477-485 (2005).
    • (2005) J. Cell Biol. , vol.170 , pp. 477-485
    • Stuart, L.M.1
  • 26
    • 75649087741 scopus 로고    scopus 로고
    • CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer
    • Stewart, C. R. et al. CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer. Nature Immunol. 11, 155-161 (2010).
    • (2010) Nature Immunol. , vol.11 , pp. 155-161
    • Stewart, C.R.1
  • 27
    • 0029809772 scopus 로고    scopus 로고
    • CD36 is palmitoylated on both N-and C-terminal cytoplasmic tails
    • Tao, N., Wagner, S. J. & Lublin, D. M. CD36 is palmitoylated on both N-and C-terminal cytoplasmic tails. J. Biol. Chem. 271, 22315-22320 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 22315-22320
    • Tao, N.1    Wagner, S.J.2    Lublin, D.M.3
  • 28
    • 78649434143 scopus 로고    scopus 로고
    • CD14 is a coreceptor of Toll-like receptors 7 and 9
    • Baumann, C. L. et al. CD14 is a coreceptor of Toll-like receptors 7 and 9. J. Exp. Med. 207, 2689-2701 (2010).
    • (2010) J. Exp. Med. , vol.207 , pp. 2689-2701
    • Baumann, C.L.1
  • 29
    • 0027955127 scopus 로고
    • Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14
    • Hailman, E. et al. Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14. J. Exp. Med. 179, 269-277 (1994).
    • (1994) J. Exp. Med. , vol.179 , pp. 269-277
    • Hailman, E.1
  • 30
    • 32244432768 scopus 로고    scopus 로고
    • Double-stranded RNA-mediated TLR3 activation is enhanced by CD14
    • This paper provided the first concrete evidence that CD14 is important for endosomal TLRs in addition to surface TLRs
    • Lee, H. K., Dunzendorfer, S., Soldau, K. & Tobias, P. S. Double-stranded RNA-mediated TLR3 activation is enhanced by CD14. Immunity 24, 153-163 (2006). This paper provided the first concrete evidence that CD14 is important for endosomal TLRs in addition to surface TLRs.
    • (2006) Immunity , vol.24 , pp. 153-163
    • Lee, H.K.1    Dunzendorfer, S.2    Soldau, K.3    Tobias, P.S.4
  • 31
    • 33750601160 scopus 로고    scopus 로고
    • CD14 directly binds to triacylated lipopeptides and facilitates recognition of the lipopeptides by the receptor complex of Toll-like receptors 2 and 1 without binding to the complex
    • Nakata, T. et al. CD14 directly binds to triacylated lipopeptides and facilitates recognition of the lipopeptides by the receptor complex of Toll-like receptors 2 and 1 without binding to the complex. Cell. Microbiol. 8, 1899-1909 (2006).
    • (2006) Cell. Microbiol. , vol.8 , pp. 1899-1909
    • Nakata, T.1
  • 32
    • 15744396047 scopus 로고    scopus 로고
    • Crystal structure of CD14 and its implications for lipopolysaccharide signaling
    • Kim, J. I. et al. Crystal structure of CD14 and its implications for lipopolysaccharide signaling. J. Biol. Chem. 280, 11347-11351 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 11347-11351
    • Kim, J.I.1
  • 33
    • 0029919991 scopus 로고    scopus 로고
    • Resistance to endotoxin shock and reduced dissemination of Gram-negative bacteria in CD14-deficient mice
    • Haziot, A. et al. Resistance to endotoxin shock and reduced dissemination of Gram-negative bacteria in CD14-deficient mice. Immunity 4, 407-414 (1996).
    • (1996) Immunity , vol.4 , pp. 407-414
    • Haziot, A.1
  • 34
    • 81055129630 scopus 로고    scopus 로고
    • CD14 controls the LPS-induced endocytosis of Toll-like receptor 4
    • This was the first description of LPS-induced trafficking of TLR4 by CD14
    • Zanoni, I. et al. CD14 controls the LPS-induced endocytosis of Toll-like receptor 4. Cell 147, 868-880 (2011). This was the first description of LPS-induced trafficking of TLR4 by CD14.
    • (2011) Cell , vol.147 , pp. 868-880
    • Zanoni, I.1
  • 36
    • 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, P. S. & Ulevitch, R. J. 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. 276, 21129-21135 (2001).
    • (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
  • 37
    • 1642529500 scopus 로고    scopus 로고
    • Isolation of an endotoxin-MD-2 complex that produces Toll-like receptor 4-dependent cell activation at picomolar concentrations
    • Gioannini, T. L. et al. Isolation of an endotoxin-MD-2 complex that produces Toll-like receptor 4-dependent cell activation at picomolar concentrations. Proc. Natl Acad. Sci. USA 101, 4186-4191 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4186-4191
    • Gioannini, T.L.1
  • 38
    • 0345505220 scopus 로고    scopus 로고
    • Human cytomegalovirus activates inflammatory cytokine responses via CD14 and Toll-like receptor 2
    • Compton, T. et al. Human cytomegalovirus activates inflammatory cytokine responses via CD14 and Toll-like receptor 2. J. Virol. 77, 4588-4596 (2003).
    • (2003) J. Virol. , vol.77 , pp. 4588-4596
    • Compton, T.1
  • 39
    • 34247577195 scopus 로고    scopus 로고
    • Vesicular stomatitis virus glycoprotein G activates a specific antiviral Toll-like receptor 4-dependent pathway
    • Georgel, P. et al. Vesicular stomatitis virus glycoprotein G activates a specific antiviral Toll-like receptor 4-dependent pathway. Virology 362, 304-313 (2007).
    • (2007) Virology , vol.362 , pp. 304-313
    • Georgel, P.1
  • 40
    • 5944261457 scopus 로고    scopus 로고
    • Pattern recognition receptors TLR4 and CD14 mediate response to respiratory syncytial virus
    • Kurt-Jones, E. A. et al. Pattern recognition receptors TLR4 and CD14 mediate response to respiratory syncytial virus. Nature Immunol. 1, 398-401 (2000).
    • (2000) Nature Immunol. , vol.1 , pp. 398-401
    • Kurt-Jones, E.A.1
  • 41
    • 70349336164 scopus 로고    scopus 로고
    • TRIL, a functional component of the TLR4 signaling complex, highly expressed in brain
    • Carpenter, S. et al. TRIL, a functional component of the TLR4 signaling complex, highly expressed in brain. J. Immunol. 183, 3989-3995 (2009).
    • (2009) J. Immunol. , vol.183 , pp. 3989-3995
    • Carpenter, S.1
  • 42
    • 80055098606 scopus 로고    scopus 로고
    • Toll-like receptor 3 (TLR3) signaling requires TLR4 interactor with leucine-rich repeats (TRIL)
    • Carpenter, S., Wochal, P., Dunne, A. & O'Neill, L. A. Toll-like receptor 3 (TLR3) signaling requires TLR4 interactor with leucine-rich repeats (TRIL). J. Biol. Chem. 286, 38795-38804 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 38795-38804
    • Carpenter, S.1    Wochal, P.2    Dunne, A.3    O'Neill, L.A.4
  • 43
    • 46749083014 scopus 로고    scopus 로고
    • Proteinase 3 and neutrophil elastase enhance inflammation in mice by inactivating antiinflammatory progranulin
    • Kessenbrock, K. et al. Proteinase 3 and neutrophil elastase enhance inflammation in mice by inactivating antiinflammatory progranulin. J. Clin. Invest. 118, 2438-2447 (2008).
    • (2008) J. Clin. Invest. , vol.118 , pp. 2438-2447
    • Kessenbrock, K.1
  • 44
    • 0037074016 scopus 로고    scopus 로고
    • Conversion of proepithelin to epithelins: Roles of SLPI and elastase in host defense and wound repair
    • Zhu, J. et al. Conversion of proepithelin to epithelins: roles of SLPI and elastase in host defense and wound repair. Cell 111, 867-878 (2002).
    • (2002) Cell , vol.111 , pp. 867-878
    • Zhu, J.1
  • 45
    • 79954570242 scopus 로고    scopus 로고
    • Granulin is a soluble cofactor for Toll-like receptor 9 signaling
    • Here, granulin was shown to have an essential role in ligand delivery for TLR9 activation
    • Park, B. et al. Granulin is a soluble cofactor for Toll-like receptor 9 signaling. Immunity 34, 505-513 (2011). Here, granulin was shown to have an essential role in ligand delivery for TLR9 activation.
    • (2011) Immunity , vol.34 , pp. 505-513
    • Park, B.1
  • 46
    • 17144376810 scopus 로고    scopus 로고
    • High-mobility group box 1 protein (HMGB1): Nuclear weapon in the immune arsenal
    • Lotze, M. T. & Tracey, K. J. High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nature Rev. Immunol. 5, 331-342 (2005).
    • (2005) Nature Rev. Immunol. , vol.5 , pp. 331-342
    • Lotze, M.T.1    Tracey, K.J.2
  • 47
    • 79953066407 scopus 로고    scopus 로고
    • HMGB1 is a therapeutic target for sterile inflammation and infection
    • Andersson, U. & Tracey, K. J. HMGB1 is a therapeutic target for sterile inflammation and infection. Annu. Rev. Immunol. 29, 139-162 (2011).
    • (2011) Annu. Rev. Immunol. , vol.29 , pp. 139-162
    • Andersson, U.1    Tracey, K.J.2
  • 48
    • 34250837518 scopus 로고    scopus 로고
    • A novel role for HMGB1 in TLR9-mediated inflammatory responses to CpG-DNA
    • Ivanov, S. et al. A novel role for HMGB1 in TLR9-mediated inflammatory responses to CpG-DNA. Blood 110, 1970-1981 (2007).
    • (2007) Blood , vol.110 , pp. 1970-1981
    • Ivanov, S.1
  • 49
    • 34247236200 scopus 로고    scopus 로고
    • Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE
    • This work first reported a role for HMGB1 in delivering DNA to TLR9
    • Tian, J. et al. Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE. Nature Immunol. 8, 487-496 (2007). This work first reported a role for HMGB1 in delivering DNA to TLR9.
    • (2007) Nature Immunol. , vol.8 , pp. 487-496
    • Tian, J.1
  • 50
    • 59649126956 scopus 로고    scopus 로고
    • Induction of inflammatory and immune responses by HMGB1-nucleosome complexes: Implications for the pathogenesis of SLE
    • Urbonaviciute, V. et al. Induction of inflammatory and immune responses by HMGB1-nucleosome complexes: implications for the pathogenesis of SLE. J. Exp. Med. 205, 3007-3018 (2008).
    • (2008) J. Exp. Med. , vol.205 , pp. 3007-3018
    • Urbonaviciute, V.1
  • 51
    • 0037061453 scopus 로고    scopus 로고
    • Chromatin-IgG complexes activate B cells by dual engagement of IgM and Tolllike receptors
    • Leadbetter, E. A. et al. Chromatin-IgG complexes activate B cells by dual engagement of IgM and Tolllike receptors. Nature 416, 603-607 (2002).
    • (2002) Nature , vol.416 , pp. 603-607
    • Leadbetter, E.A.1
  • 52
    • 75749158495 scopus 로고    scopus 로고
    • RAGE-independent autoreactive B cell activation in response to chromatin and HMGB1/DNA immune complexes
    • Avalos, A. M. et al. RAGE-independent autoreactive B cell activation in response to chromatin and HMGB1/DNA immune complexes. Autoimmunity 43, 103-110 (2010).
    • (2010) Autoimmunity , vol.43 , pp. 103-110
    • Avalos, A.M.1
  • 53
    • 70449092388 scopus 로고    scopus 로고
    • HMGB proteins function as universal sentinels for nucleic-acid-mediated innate immune responses
    • Yanai, H. et al. HMGB proteins function as universal sentinels for nucleic-acid-mediated innate immune responses. Nature 462, 99-103 (2009).
    • (2009) Nature , vol.462 , pp. 99-103
    • Yanai, H.1
  • 54
    • 34948862264 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide
    • This paper demonstrated the role of LL37 in DNA delivery to TLR9 in pDCs
    • Lande, R. et al. Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide. Nature 449, 564-569 (2007). This paper demonstrated the role of LL37 in DNA delivery to TLR9 in pDCs.
    • (2007) Nature , vol.449 , pp. 564-569
    • Lande, R.1
  • 55
    • 48549088455 scopus 로고    scopus 로고
    • Antimicrobial peptides and self-DNA in autoimmune skin inflammation
    • Gilliet, M. & Lande, R. Antimicrobial peptides and self-DNA in autoimmune skin inflammation. Curr. Opin. Immunol. 20, 401-407 (2008).
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 401-407
    • Gilliet, M.1    Lande, R.2
  • 56
    • 0031574103 scopus 로고    scopus 로고
    • The cathelicidin family of antimicrobial peptide precursors: A component of the oxygen-independent defense mechanisms of neutrophils
    • Zanetti, M., Gennaro, R. & Romeo, D. The cathelicidin family of antimicrobial peptide precursors: a component of the oxygen-independent defense mechanisms of neutrophils. Ann. NY Acad. Sci. 832, 147-162 (1997).
    • (1997) Ann. NY Acad. Sci. , vol.832 , pp. 147-162
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 57
    • 69549135324 scopus 로고    scopus 로고
    • Self-RNA-antimicrobial peptide complexes activate human dendritic cells through TLR7 and TLR8
    • Ganguly, D. et al. Self-RNA-antimicrobial peptide complexes activate human dendritic cells through TLR7 and TLR8. J. Exp. Med. 206, 1983-1994 (2009).
    • (2009) J. Exp. Med. , vol.206 , pp. 1983-1994
    • Ganguly, D.1
  • 58
    • 33645239012 scopus 로고    scopus 로고
    • Roles of heat shock protein gp96 in the ER quality control: Redundant or unique function?
    • Yang, Y. & Li, Z. Roles of heat shock protein gp96 in the ER quality control: redundant or unique function? Mol. Cells 20, 173-182 (2005).
    • (2005) Mol. Cells , vol.20 , pp. 173-182
    • Yang, Y.1    Li, Z.2
  • 59
    • 51649117657 scopus 로고    scopus 로고
    • Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin
    • Liu, B. & Li, Z. Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin. Blood 112, 1223-1230 (2008).
    • (2008) Blood , vol.112 , pp. 1223-1230
    • Liu, B.1    Li, Z.2
  • 60
    • 0034795208 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
    • Randow, F. & Seed, B. Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. Nature Cell Biol. 3, 891-896 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 891-896
    • Randow, F.1    Seed, B.2
  • 61
    • 34948853214 scopus 로고    scopus 로고
    • GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion
    • Wanderling, S. et al. GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion. Mol. Biol. Cell 18, 3764-3775 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3764-3775
    • Wanderling, S.1
  • 62
    • 33847260278 scopus 로고    scopus 로고
    • Heat shock protein gp96 is a master chaperone for Toll-like receptors and is important in the innate function of macrophages
    • Yang, Y. et al. Heat shock protein gp96 is a master chaperone for Toll-like receptors and is important in the innate function of macrophages. Immunity 26, 215-226 (2007).
    • (2007) Immunity , vol.26 , pp. 215-226
    • Yang, Y.1
  • 63
    • 79959825676 scopus 로고    scopus 로고
    • Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex
    • Staron, M. et al. Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex. Blood 117, 7136-7144 (2011).
    • (2011) Blood , vol.117 , pp. 7136-7144
    • Staron, M.1
  • 64
    • 84857475033 scopus 로고    scopus 로고
    • Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone
    • This paper shows that GRP94 and PRAT4A work together to chaperone TLRs
    • Liu, B. et al. Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone. Nature Commun. 1, 79 (2010). This paper shows that GRP94 and PRAT4A work together to chaperone TLRs.
    • (2010) Nature Commun. , vol.1 , pp. 79
    • Liu, B.1
  • 65
    • 33746214788 scopus 로고    scopus 로고
    • A protein associated with Toll-like receptor 4 (PRAT4A) regulates cell surface expression of TLR4
    • Wakabayashi, Y. et al. A protein associated with Toll-like receptor 4 (PRAT4A) regulates cell surface expression of TLR4. J. Immunol. 177, 1772-1779 (2006).
    • (2006) J. Immunol. , vol.177 , pp. 1772-1779
    • Wakabayashi, Y.1
  • 66
    • 36549072863 scopus 로고    scopus 로고
    • A protein associated with Toll-like receptor (TLR) 4 (PRAT4A) is required for TLR-dependent immune responses
    • Takahashi, K. et al. A protein associated with Toll-like receptor (TLR) 4 (PRAT4A) is required for TLR-dependent immune responses. J. Exp. Med. 204, 2963-2976 (2007).
    • (2007) J. Exp. Med. , vol.204 , pp. 2963-2976
    • Takahashi, K.1
  • 67
    • 54949103603 scopus 로고    scopus 로고
    • A single base mutation in the PRAT4A gene reveals differential interaction of PRAT4A with Toll-like receptors
    • Kiyokawa, T. et al. A single base mutation in the PRAT4A gene reveals differential interaction of PRAT4A with Toll-like receptors. Int. Immunol. 20, 1407-1415 (2008).
    • (2008) Int. Immunol. , vol.20 , pp. 1407-1415
    • Kiyokawa, T.1
  • 68
    • 31344466165 scopus 로고    scopus 로고
    • The Unc93b1 mutation 3d disrupts exogenous antigen presentation and signaling via Toll-like receptors 3, 7 and 9
    • Tabeta, K. et al. The Unc93b1 mutation 3d disrupts exogenous antigen presentation and signaling via Toll-like receptors 3, 7 and 9. Nature Immunol. 7, 156-164 (2006).
    • (2006) Nature Immunol. , vol.7 , pp. 156-164
    • Tabeta, K.1
  • 69
    • 33750016788 scopus 로고    scopus 로고
    • Herpes simplex virus encephalitis in human UNC-93B deficiency
    • Casrouge, A. et al. Herpes simplex virus encephalitis in human UNC-93B deficiency. Science 314, 308-312 (2006).
    • (2006) Science , vol.314 , pp. 308-312
    • Casrouge, A.1
  • 70
    • 34247484007 scopus 로고    scopus 로고
    • The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling
    • Brinkmann, M. M. et al. The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling. J. Cell Biol. 177, 265-275 (2007).
    • (2007) J. Cell Biol. , vol.177 , pp. 265-275
    • Brinkmann, M.M.1
  • 71
    • 40749098665 scopus 로고    scopus 로고
    • UNC93B1 delivers nucleotide-sensing Toll-like receptors to endolysosomes
    • This paper provides evidence for the role of UNC93B1 in the trafficking of endosomal TLRs
    • Kim, Y. M., Brinkmann, M. M., Paquet, M. E. & Ploegh, H. L. UNC93B1 delivers nucleotide-sensing Toll-like receptors to endolysosomes. Nature 452, 234-238 (2008). This paper provides evidence for the role of UNC93B1 in the trafficking of endosomal TLRs.
    • (2008) Nature , vol.452 , pp. 234-238
    • Kim, Y.M.1    Brinkmann, M.M.2    Paquet, M.E.3    Ploegh, H.L.4
  • 72
    • 67449136127 scopus 로고    scopus 로고
    • Unc93B1 biases Toll-like receptor responses to nucleic acid in dendritic cells toward DNA-but against RNA-sensing
    • Fukui, R. et al. Unc93B1 biases Toll-like receptor responses to nucleic acid in dendritic cells toward DNA-but against RNA-sensing. J. Exp. Med. 206, 1339-1350 (2009).
    • (2009) J. Exp. Med. , vol.206 , pp. 1339-1350
    • Fukui, R.1
  • 73
    • 79960470158 scopus 로고    scopus 로고
    • Unc93B1 restricts systemic lethal inflammation by orchestrating Toll-like receptor 7 and 9 trafficking
    • Fukui, R. et al. Unc93B1 restricts systemic lethal inflammation by orchestrating Toll-like receptor 7 and 9 trafficking. Immunity 35, 69-81 (2011).
    • (2011) Immunity , vol.35 , pp. 69-81
    • Fukui, R.1
  • 74
    • 1342289622 scopus 로고    scopus 로고
    • Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network
    • Nakatsu, F. & Ohno, H. Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network. Cell Struct. Funct. 28, 419-429 (2003).
    • (2003) Cell Struct. Funct. , vol.28 , pp. 419-429
    • Nakatsu, F.1    Ohno, H.2
  • 75
    • 77956689533 scopus 로고    scopus 로고
    • Bifurcation of Toll-like receptor 9 signaling by adaptor protein 3
    • This study was the first to demonstrate that AP3 has a role in TLR9-dependent IFN responses
    • Sasai, M., Linehan, M. M. & Iwasaki, A. Bifurcation of Toll-like receptor 9 signaling by adaptor protein 3. Science 329, 1530-1534 (2010). This study was the first to demonstrate that AP3 has a role in TLR9-dependent IFN responses.
    • (2010) Science , vol.329 , pp. 1530-1534
    • Sasai, M.1    Linehan, M.M.2    Iwasaki, A.3
  • 76
    • 78649877815 scopus 로고    scopus 로고
    • Slc15a4, AP-3, and Hermansky-Pudlak syndrome proteins are required for Toll-like receptor signaling in plasmacytoid dendritic cells
    • Blasius, A. L. et al. Slc15a4, AP-3, and Hermansky-Pudlak syndrome proteins are required for Toll-like receptor signaling in plasmacytoid dendritic cells. Proc. Natl Acad. Sci. USA 107, 19973-19978 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 19973-19978
    • Blasius, A.L.1
  • 77
    • 33746884630 scopus 로고    scopus 로고
    • Properties regulating the nature of the plasmacytoid dendritic cell response to Toll-like receptor 9 activation
    • Guiducci, C. et al. Properties regulating the nature of the plasmacytoid dendritic cell response to Toll-like receptor 9 activation. J. Exp. Med. 203, 1999-2008 (2006).
    • (2006) J. Exp. Med. , vol.203 , pp. 1999-2008
    • Guiducci, C.1
  • 78
    • 17844380477 scopus 로고    scopus 로고
    • Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction
    • Honda, K. et al. Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction. Nature 434, 1035-1040 (2005).
    • (2005) Nature , vol.434 , pp. 1035-1040
    • Honda, K.1
  • 79
    • 57349191215 scopus 로고    scopus 로고
    • The ectodomain of Toll-like receptor 9 is cleaved to generate a functional receptor
    • Ewald, S. E. et al. The ectodomain of Toll-like receptor 9 is cleaved to generate a functional receptor. Nature 456, 658-662 (2008).
    • (2008) Nature , vol.456 , pp. 658-662
    • Ewald, S.E.1
  • 80
    • 56349114913 scopus 로고    scopus 로고
    • Proteolytic cleavage in an endolysosomal compartment is required for activation of Toll-like receptor 9
    • References 79 and 80 demonstrate the cleavage requirement for TLR9 activation by CpG DNA
    • Park, B. et al. Proteolytic cleavage in an endolysosomal compartment is required for activation of Toll-like receptor 9. Nature Immunol. 9, 1407-1414 (2008). References 79 and 80 demonstrate the cleavage requirement for TLR9 activation by CpG DNA.
    • (2008) Nature Immunol. , vol.9 , pp. 1407-1414
    • Park, B.1
  • 81
    • 38849127573 scopus 로고    scopus 로고
    • Cathepsin K-dependent Toll-like receptor 9 signaling revealed in experimental arthritis
    • Asagiri, M. et al. Cathepsin K-dependent Toll-like receptor 9 signaling revealed in experimental arthritis. Science 319, 624-627 (2008).
    • (2008) Science , vol.319 , pp. 624-627
    • Asagiri, M.1
  • 82
    • 38649126557 scopus 로고    scopus 로고
    • Cathepsins are required for Tolllike receptor 9 responses
    • Matsumoto, F. et al. Cathepsins are required for Tolllike receptor 9 responses. Biochem. Biophys. Res. Commun. 367, 693-699 (2008).
    • (2008) Biochem. Biophys. Res. Commun. , vol.367 , pp. 693-699
    • Matsumoto, F.1
  • 83
    • 70449477746 scopus 로고    scopus 로고
    • Critical role for asparagine endopeptidase in endocytic Toll-like receptor signaling in dendritic cells
    • This is the first demonstration of a role for AEP in TLR9 activation in primary DCs
    • Sepulveda, F. E. et al. Critical role for asparagine endopeptidase in endocytic Toll-like receptor signaling in dendritic cells. Immunity 31, 737-748 (2009). This is the first demonstration of a role for AEP in TLR9 activation in primary DCs.
    • (2009) Immunity , vol.31 , pp. 737-748
    • Sepulveda, F.E.1
  • 84
    • 79955743119 scopus 로고    scopus 로고
    • Nucleic acid recognition by Toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase
    • Ewald, S. E. et al. Nucleic acid recognition by Toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase. J. Exp. Med. 208, 643-651 (2011).
    • (2011) J. Exp. Med. , vol.208 , pp. 643-651
    • Ewald, S.E.1
  • 85
    • 79952762131 scopus 로고    scopus 로고
    • Antiviral protein Viperin promotes Toll-like receptor 7-and Toll-like receptor 9-mediated type I interferon production in plasmacytoid dendritic cells
    • Saitoh, T. et al. Antiviral protein Viperin promotes Toll-like receptor 7-and Toll-like receptor 9-mediated type I interferon production in plasmacytoid dendritic cells. Immunity 34, 352-363 (2011).
    • (2011) Immunity , vol.34 , pp. 352-363
    • Saitoh, T.1
  • 86
    • 45549098345 scopus 로고    scopus 로고
    • A Toll-like receptor 2-integrin β3 complex senses bacterial lipopeptides via vitronectin
    • Gerold, G. et al. A Toll-like receptor 2-integrin β3 complex senses bacterial lipopeptides via vitronectin. Nature Immunol. 9, 761-768 (2008).
    • (2008) Nature Immunol. , vol.9 , pp. 761-768
    • Gerold, G.1
  • 87
    • 33646908228 scopus 로고    scopus 로고
    • Phosphoinositidemediated adaptor recruitment controls Toll-like receptor signaling
    • Kagan, J. C. & Medzhitov, R. Phosphoinositidemediated adaptor recruitment controls Toll-like receptor signaling. Cell 125, 943-955 (2006).
    • (2006) Cell , vol.125 , pp. 943-955
    • Kagan, J.C.1    Medzhitov, R.2
  • 88
    • 0038558249 scopus 로고    scopus 로고
    • Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2
    • Gantner, B. N., Simmons, R. M., Canavera, S. J., Akira, S. & Underhill, D. M. Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2. J. Exp. Med. 197, 1107-1117 (2003).
    • (2003) J. Exp. Med. , vol.197 , pp. 1107-1117
    • Gantner, B.N.1    Simmons, R.M.2    Canavera, S.J.3    Akira, S.4    Underhill, D.M.5
  • 89
    • 21044436437 scopus 로고    scopus 로고
    • The radioprotective 105/MD-1 complex links TLR2 and TLR4/MD-2 in antibody response to microbial membranes
    • Nagai, Y. et al. The radioprotective 105/MD-1 complex links TLR2 and TLR4/MD-2 in antibody response to microbial membranes. J. Immunol. 174, 7043-7049 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 7043-7049
    • Nagai, Y.1
  • 90
    • 20644450101 scopus 로고    scopus 로고
    • Negative regulation of Toll-like receptor 4 signaling by the Toll-like receptor homolog RP105
    • Divanovic, S. et al. Negative regulation of Toll-like receptor 4 signaling by the Toll-like receptor homolog RP105. Nature Immunol. 6, 571-578 (2005).
    • (2005) Nature Immunol. , vol.6 , pp. 571-578
    • Divanovic, S.1
  • 91
    • 58249090959 scopus 로고    scopus 로고
    • RP105 facilitates macrophage activation by Mycobacterium tuberculosis lipoproteins
    • Blumenthal, A. et al. RP105 facilitates macrophage activation by Mycobacterium tuberculosis lipoproteins. Cell Host Microbe 5, 35-46 (2009).
    • (2009) Cell Host Microbe , vol.5 , pp. 35-46
    • Blumenthal, A.1
  • 92
    • 58749093255 scopus 로고    scopus 로고
    • Autoreactive B cells discriminate CpG-rich and CpG-poor DNA and this response is modulated by IFN-α
    • Uccellini, M. B. et al. Autoreactive B cells discriminate CpG-rich and CpG-poor DNA and this response is modulated by IFN-α. J. Immunol. 181, 5875-5884 (2008).
    • (2008) J. Immunol. , vol.181 , pp. 5875-5884
    • Uccellini, M.B.1
  • 93
    • 0347480224 scopus 로고    scopus 로고
    • Activation of autoreactive B cells by CpG dsDNA
    • Viglianti, G. A. et al. Activation of autoreactive B cells by CpG dsDNA. Immunity 19, 837-847 (2003).
    • (2003) Immunity , vol.19 , pp. 837-847
    • Viglianti, G.A.1
  • 94
    • 27744444832 scopus 로고    scopus 로고
    • RNA-associated autoantigens activate B cells by combined B cell antigen receptor/Toll-like receptor 7 engagement
    • Lau, C. M. et al. RNA-associated autoantigens activate B cells by combined B cell antigen receptor/Toll-like receptor 7 engagement. J. Exp. Med. 202, 1171-1177 (2005).
    • (2005) J. Exp. Med. , vol.202 , pp. 1171-1177
    • Lau, C.M.1
  • 95
    • 44649161194 scopus 로고    scopus 로고
    • The B cell receptor governs the subcellular location of Toll-like receptor 9 leading to hyperresponses to DNA-containing antigens
    • Chaturvedi, A., Dorward, D. & Pierce, S. K. The B cell receptor governs the subcellular location of Toll-like receptor 9 leading to hyperresponses to DNA-containing antigens. Immunity 28, 799-809 (2008).
    • (2008) Immunity , vol.28 , pp. 799-809
    • Chaturvedi, A.1    Dorward, D.2    Pierce, S.K.3
  • 96
    • 77953275701 scopus 로고    scopus 로고
    • Differential cytokine production and bystander activation of autoreactive B cells in response to CpG-A and CpG-B oligonucleotides
    • Avalos, A. M. et al. Differential cytokine production and bystander activation of autoreactive B cells in response to CpG-A and CpG-B oligonucleotides. J. Immunol. 183, 6262-6268 (2009).
    • (2009) J. Immunol. , vol.183 , pp. 6262-6268
    • Avalos, A.M.1
  • 97
    • 0028851635 scopus 로고
    • The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system
    • Hori, O. et al. The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system. J. Biol. Chem. 270, 25752-25761 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 25752-25761
    • Hori, O.1
  • 98
    • 27744453362 scopus 로고    scopus 로고
    • Understanding RAGE, the receptor for advanced glycation end products
    • Bierhaus, A. et al. Understanding RAGE, the receptor for advanced glycation end products. J. Mol. Med. 83, 876-886 (2005).
    • (2005) J. Mol. Med. , vol.83 , pp. 876-886
    • Bierhaus, A.1
  • 99
    • 0034737582 scopus 로고    scopus 로고
    • The binding of oxidized low density lipoprotein to mouse CD36 is mediated in part by oxidized phospholipids that are associated with both the lipid and protein moieties of the lipoprotein
    • Boullier, A. et al. The binding of oxidized low density lipoprotein to mouse CD36 is mediated in part by oxidized phospholipids that are associated with both the lipid and protein moieties of the lipoprotein. J. Biol. Chem. 275, 9163-9169 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 9163-9169
    • Boullier, A.1
  • 100
    • 0036141148 scopus 로고    scopus 로고
    • CD36, a class B scavenger receptor, is expressed on microglia in Alzheimer's disease brains and can mediate production of reactive oxygen species in response to (3-amyloid fibrils
    • Coraci, I. S. et al. CD36, a class B scavenger receptor, is expressed on microglia in Alzheimer's disease brains and can mediate production of reactive oxygen species in response to (3-amyloid fibrils. Am. J. Pathol. 160, 101-112 (2002).
    • (2002) Am. J. Pathol. , vol.160 , pp. 101-112
    • Coraci, I.S.1
  • 101
    • 70449580312 scopus 로고    scopus 로고
    • Soluble CD36 ectodomain binds negatively charged diacylglycerol ligands and acts as a co-receptor for TLR2
    • Jimenez-Dalmaroni, M. J. et al. Soluble CD36 ectodomain binds negatively charged diacylglycerol ligands and acts as a co-receptor for TLR2. PLoS ONE 4, e7411 (2009).
    • (2009) PLoS ONE , vol.4
    • Jimenez-Dalmaroni, M.J.1
  • 102
    • 0033565407 scopus 로고    scopus 로고
    • Signaling events induced by lipopolysaccharide-activated Toll-like receptor 2
    • Yang, R. B., Mark, M. R., Gurney, A. L. & Godowski, P. J. Signaling events induced by lipopolysaccharide-activated Toll-like receptor 2. J. Immunol. 163, 639-643 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 639-643
    • Yang, R.B.1    Mark, M.R.2    Gurney, A.L.3    Godowski, P.J.4
  • 103
    • 0034819316 scopus 로고    scopus 로고
    • Essential roles of CD14 and lipopolysaccharide-binding protein for activation of Tolllike receptor (TLR) 2 as well as TLR4 reconstitution of TLR2-and TLR4-activation by distinguishable ligands in LPS preparations
    • Muta, T & Takeshige, K. Essential roles of CD14 and lipopolysaccharide-binding protein for activation of Tolllike receptor (TLR) 2 as well as TLR4 reconstitution of TLR2-and TLR4-activation by distinguishable ligands in LPS preparations. Eur. J. Biochem. 268, 4580-4589 (2001).
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4580-4589
    • Muta, T.1    Takeshige, K.2


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