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Volumn 175, Issue 5, 2005, Pages 2777-2782

Heat shock proteins as endogenous adjuvants in sterile and septic inflammation

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; LIGAND; TOLL LIKE RECEPTOR;

EID: 23844482773     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.175.5.2777     Document Type: Short Survey
Times cited : (190)

References (104)
  • 1
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa, F. 1996. Discovery of the heat shock response. Cell Stress Chaperones 1: 97-98.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 97-98
    • Ritossa, F.1
  • 2
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U., and M. Hayer-Hartl. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295: 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 3
    • 0025058568 scopus 로고
    • Induction and therapy of autoimmune diabetes in the non-obese diabetic (NOD/Lt) mouse by a 65-kDa heat shock protein
    • Elias, D., D, Markovits, T. Reshef, R. van der Zee, and I. R. Cohen. 1990. Induction and therapy of autoimmune diabetes in the non-obese diabetic (NOD/Lt) mouse by a 65-kDa heat shock protein. Proc. Natl. Acad. Sci. USA 87: 1576-1580.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1576-1580
    • Elias, D.1    Markovits, D.2    Reshef, T.3    Van Der Zee, R.4    Cohen, I.R.5
  • 4
    • 0033106415 scopus 로고    scopus 로고
    • T cell proliferative responses of type 1 diabetes patients and healthy individuals to human hsp60 and its peptides
    • Abulafia-Lapid, R., D. Elias, I. Raz, Y. Keren-Zur, H. Atlan, and I. R. Cohen. 1999. T cell proliferative responses of type 1 diabetes patients and healthy individuals to human hsp60 and its peptides. J. Autoimmun. 12: 121-129.
    • (1999) J. Autoimmun. , vol.12 , pp. 121-129
    • Abulafia-Lapid, R.1    Elias, D.2    Raz, I.3    Keren-Zur, Y.4    Atlan, H.5    Cohen, I.R.6
  • 5
    • 0038617504 scopus 로고    scopus 로고
    • T cells and autoantibodies co human HSP70 in type 1 diabetes in children
    • Abulafia-Lapid, R., D. Gillis, O. Yosef, H. Atlan, and I. R. Cohen. 2003. T cells and autoantibodies co human HSP70 in type 1 diabetes in children. J. Autoimmun. 20: 313-321.
    • (2003) J. Autoimmun. , vol.20 , pp. 313-321
    • Abulafia-Lapid, R.1    Gillis, D.2    Yosef, O.3    Atlan, H.4    Cohen, I.R.5
  • 6
    • 0024444150 scopus 로고
    • In vitro responses to a 65-kilodalton mycobacterial protein by synovial T cells from inflammatory arthritis patients
    • Gaston, J. S., P. F. Life, L. C. Bailey, and P. A. Bacon. 1989. In vitro responses to a 65-kilodalton mycobacterial protein by synovial T cells from inflammatory arthritis patients. J. Immunol. 143: 2494-2500.
    • (1989) J. Immunol. , vol.143 , pp. 2494-2500
    • Gaston, J.S.1    Life, P.F.2    Bailey, L.C.3    Bacon, P.A.4
  • 9
    • 0035253485 scopus 로고    scopus 로고
    • The human endoplasmic reticulum molecular chaperone BiP is an autoantigen for rheumatoid arthritis and prevents the induction of experimental arthritis
    • Corrigall, V. M., M. D. Bodman-Smith, M. S. Fife, B. Canas, L. K. Myers, P. Wooley, C. Soh, N. A. Staines, D. J. Pappin, S. E. Berlo, et al. 2001. The human endoplasmic reticulum molecular chaperone BiP is an autoantigen for rheumatoid arthritis and prevents the induction of experimental arthritis. J. Immunol. 166: 1492-1498.
    • (2001) J. Immunol. , vol.166 , pp. 1492-1498
    • Corrigall, V.M.1    Bodman-Smith, M.D.2    Fife, M.S.3    Canas, B.4    Myers, L.K.5    Wooley, P.6    Soh, C.7    Staines, N.A.8    Pappin, D.J.9    Berlo, S.E.10
  • 10
    • 0030897029 scopus 로고    scopus 로고
    • The role of heat shock protein, microbial and autoimmune agents in the aetiology of Behcet's disease
    • Lehner, T. 1997. The role of heat shock protein, microbial and autoimmune agents in the aetiology of Behcet's disease. Int. Rev. Immunol. 14: 21-32.
    • (1997) Int. Rev. Immunol. , vol.14 , pp. 21-32
    • Lehner, T.1
  • 11
    • 0026257154 scopus 로고
    • Heat shock proteins and systemic lupus erythematosus
    • Dhillon, V., D. Latchman, and D. Isenberg. 1991. Heat shock proteins and systemic lupus erythematosus. Lupus 1: 3-8.
    • (1991) Lupus , vol.1 , pp. 3-8
    • Dhillon, V.1    Latchman, D.2    Isenberg, D.3
  • 12
    • 0037105543 scopus 로고    scopus 로고
    • Inhibition of adjuvant arthritis by a DNA vaccine encoding human heat shock protein 60
    • Quintana, F. J., P. Carmi, F. Mor, and I. R. Cohen. 2002. Inhibition of adjuvant arthritis by a DNA vaccine encoding human heat shock protein 60. J. Immunol. 169: 3422-3428.
    • (2002) J. Immunol. , vol.169 , pp. 3422-3428
    • Quintana, F.J.1    Carmi, P.2    Mor, F.3    Cohen, I.R.4
  • 13
    • 0141920623 scopus 로고    scopus 로고
    • DNA fragments of human HSP60 vaccinate against adjuvant arthritis: Identification of a regulatory HSP60 peptide
    • Quintana, F. J., P. Carmi, F. Mor, and I. R. Cohen. 2003. DNA fragments of human HSP60 vaccinate against adjuvant arthritis: identification of a regulatory HSP60 peptide. J. Immunol. 171: 3533-3541.
    • (2003) J. Immunol. , vol.171 , pp. 3533-3541
    • Quintana, F.J.1    Carmi, P.2    Mor, F.3    Cohen, I.R.4
  • 14
    • 8444238954 scopus 로고    scopus 로고
    • Inhibition of adjuvant-induced arthritis by DNA vaccination with the 70-kd or the 90-kd human heat-shock protein: Immune cross-regulation with the 60-kd heat-shock protein
    • Quintana, F. J., P. Carmi, F. Mor, and I. R. Cohen. 2004. Inhibition of adjuvant-induced arthritis by DNA vaccination with the 70-kd or the 90-kd human heat-shock protein: immune cross-regulation with the 60-kd heat-shock protein. Arthritis Rheum. 50: 3712-3720.
    • (2004) Arthritis Rheum. , vol.50 , pp. 3712-3720
    • Quintana, F.J.1    Carmi, P.2    Mor, F.3    Cohen, I.R.4
  • 17
    • 0037097641 scopus 로고    scopus 로고
    • Resistance to adjuvant arthritis is due to protective antibodies against heat shock protein surface epitopes and the induction of IL-10 secretion
    • Ulmansky, R., C. J. Cohen, F. Szafer, E. Moallem, Z. G. Fridlender, Y. Kashi, and Y. Naparstek. 2002. Resistance to adjuvant arthritis is due to protective antibodies against heat shock protein surface epitopes and the induction of IL-10 secretion. J. Immunol. 168: 6463-6469.
    • (2002) J. Immunol. , vol.168 , pp. 6463-6469
    • Ulmansky, R.1    Cohen, C.J.2    Szafer, F.3    Moallem, E.4    Fridlender, Z.G.5    Kashi, Y.6    Naparstek, Y.7
  • 18
    • 0026322837 scopus 로고
    • Vaccination against autoimmune mouse diabetes with a T cell epitope of ehe human 65-kDa heat shock protein
    • Elias, D., T. Reshef, O. S. Bitk, R. van der Zee, M. D. Walker, and I. R. Cohen. 1991. Vaccination against autoimmune mouse diabetes with a T cell epitope of ehe human 65-kDa heat shock protein. Proc. Natl. Acad. Sci. USA 88: 3088-3091.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3088-3091
    • Elias, D.1    Reshef, T.2    Bitk, O.S.3    Van Der Zee, R.4    Walker, M.D.5    Cohen, I.R.6
  • 19
    • 0037111430 scopus 로고    scopus 로고
    • DNA vaccination with heat shock protein 60 inhibits cyclophosphamide- accelerated diabetes
    • Quintana, F. J., P. Carmi, and I. R. Cohen. 2002. DNA vaccination with heat shock protein 60 inhibits cyclophosphamide-accelerated diabetes. J. Immunol. 169: 6030-6035.
    • (2002) J. Immunol. , vol.169 , pp. 6030-6035
    • Quintana, F.J.1    Carmi, P.2    Cohen, I.R.3
  • 20
    • 0035944844 scopus 로고    scopus 로고
    • Cell function in new-onset type 1 diabetes and immunomodulation with a heat-shock protein peptide (DiaPep277): A randomised, double-blind, phase II trial
    • Raz, I., D. Elias, A. Avron, M. Tamir, M. Metzget, and I. R. Cohen. 2001. β Cell function in new-onset type 1 diabetes and immunomodulation with a heat-shock protein peptide (DiaPep277): a randomised, double-blind, phase II trial. Lancet 358: 1749-1753.
    • (2001) Lancet , vol.358 , pp. 1749-1753
    • Raz, I.1    Elias, D.2    Avron, A.3    Tamir, M.4    Metzget, M.5    Cohen, I.R.6
  • 21
    • 0345164329 scopus 로고    scopus 로고
    • + CTL effector cells in mice by immunization with a stress protein-influenza virus nucleoprotein fusion molecule
    • + CTL effector cells in mice by immunization with a stress protein-influenza virus nucleoprotein fusion molecule. Vaccine 17: 373-383.
    • (1999) Vaccine , vol.17 , pp. 373-383
    • Anthony, L.S.1    Wu, H.2    Sweet, H.3    Tutnnir, C.4    Boux, L.J.5    Mizzen, L.A.6
  • 22
    • 0030775140 scopus 로고    scopus 로고
    • Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity
    • Blachere, N. E., Z. Li, R. Y. Chandawarkar, R. Suto, N. S. Jaikaria, S. Basu, H. Udono, and P. K. Srivastava. 1997. Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity. J. Exp. Med. 186: 1315-1322.
    • (1997) J. Exp. Med. , vol.186 , pp. 1315-1322
    • Blachere, N.E.1    Li, Z.2    Chandawarkar, R.Y.3    Suto, R.4    Jaikaria, N.S.5    Basu, S.6    Udono, H.7    Srivastava, P.K.8
  • 23
    • 0036512171 scopus 로고    scopus 로고
    • Roles of heat-shock proteins in innate and adaptive immunity
    • Srivastava, P. 2002. Roles of heat-shock proteins in innate and adaptive immunity. Nat. Rev. Immunol. 2: 185-194.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 185-194
    • Srivastava, P.1
  • 24
    • 0036839577 scopus 로고    scopus 로고
    • Endogenous ligands of Toll-like receptors: Implications for regulating inflammatory and immune responses
    • Beg, A. A. 2002. Endogenous ligands of Toll-like receptors: implications for regulating inflammatory and immune responses. Trends Immunol. 23: 509-512.
    • (2002) Trends Immunol. , vol.23 , pp. 509-512
    • Beg, A.A.1
  • 25
    • 21244489948 scopus 로고    scopus 로고
    • Heat shock protein 60 activates cytokine-associated negative regulator SOCS3 in T cells: Effects on signaling, chemotaxis, and inflammation
    • Zanin-Zhorov, A., G. Tal, S. Shivtiel, M. Cohen, T. Lapidot, G. Nussbaum, R. Margalit, I. R. Cohen, and O. Lider. 2005. Heat shock protein 60 activates cytokine-associated negative regulator SOCS3 in T cells: effects on signaling, chemotaxis, and inflammation. J. Immunol. 175: 276-285.
    • (2005) J. Immunol. , vol.175 , pp. 276-285
    • Zanin-Zhorov, A.1    Tal, G.2    Shivtiel, S.3    Cohen, M.4    Lapidot, T.5    Nussbaum, G.6    Margalit, R.7    Cohen, I.R.8    Lider, O.9
  • 26
    • 14844347311 scopus 로고    scopus 로고
    • Heat shock protein 60 inhibits Th1-mediated hepatitis model via innate regulation of Th1/Th2 transcription factors and cytokines
    • Zanin-Zhorov, A., R. Bruck, G. Tal, S. Oren, H. Aeed, R. Hershkoviz, I. R. Cohen, and O. Lider. 2005. Heat shock protein 60 inhibits Th1-mediated hepatitis model via innate regulation of Th1/Th2 transcription factors and cytokines. J. Immunol. 174:3227-3236.
    • (2005) J. Immunol. , vol.174 , pp. 3227-3236
    • Zanin-Zhorov, A.1    Bruck, R.2    Tal, G.3    Oren, S.4    Aeed, H.5    Hershkoviz, R.6    Cohen, I.R.7    Lider, O.8
  • 27
    • 0043205830 scopus 로고    scopus 로고
    • T cells respond to heat shock protein 60 via TLR2: Activation of adhesion and inhibition of chemokine receptors
    • Zanin-Zhorov, A., G. Nussbaum, S. Franicza, I. R. Cohen, and O. Lider. 2003. T cells respond to heat shock protein 60 via TLR2: activation of adhesion and inhibition of chemokine receptors. FASEB J. 17: 1567-1569.
    • (2003) FASEB J. , vol.17 , pp. 1567-1569
    • Zanin-Zhorov, A.1    Nussbaum, G.2    Franicza, S.3    Cohen, I.R.4    Lider, O.5
  • 29
    • 0033382112 scopus 로고    scopus 로고
    • Immunostimulatory properties of the Leishmania infantum heat shock proteins HSP70 and HSP83
    • Rico, A. I., S. O. Angel, C. Alonso, and J. M. Requena. 1999. Immunostimulatory properties of the Leishmania infantum heat shock proteins HSP70 and HSP83. Mol. Immunol. 36: 1131-1139.
    • (1999) Mol. Immunol. , vol.36 , pp. 1131-1139
    • Rico, A.I.1    Angel, S.O.2    Alonso, C.3    Requena, J.M.4
  • 30
    • 0036819236 scopus 로고    scopus 로고
    • The heat shock proteins, Hsp70 and Hsp83, of Leishmania infantum are mitogens for mouse B cells
    • Rico, A. I., N. Girones, M. Fresno, C. Alonso, and J. M. Requena. 2002. The heat shock proteins, Hsp70 and Hsp83, of Leishmania infantum are mitogens for mouse B cells. Cell Stress Chaperones 7: 339-346.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 339-346
    • Rico, A.I.1    Girones, N.2    Fresno, M.3    Alonso, C.4    Requena, J.M.5
  • 31
    • 0037928705 scopus 로고    scopus 로고
    • Recombinant human heat shock protein 60 does not induce the release of tumor necrosis factor α from murine macrophages
    • Gao, B., and M. F. Tsan. 2003. Recombinant human heat shock protein 60 does not induce the release of tumor necrosis factor α from murine macrophages. J. Biol. Chem. 278: 22523-22529.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22523-22529
    • Gao, B.1    Tsan, M.F.2
  • 32
    • 0037414787 scopus 로고    scopus 로고
    • Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor α release by murine macrophages
    • Gao, B., and M. F. Tsan. 2003. Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor α release by murine macrophages. J. Biol. Chem. 278: 174-179.
    • (2003) J. Biol. Chem. , vol.278 , pp. 174-179
    • Gao, B.1    Tsan, M.F.2
  • 33
    • 1942516288 scopus 로고    scopus 로고
    • Induction of cytokines by heat shock proteins and endotoxin in murine macrophages
    • Gao, B., and M. F. Tsan. 2004. Induction of cytokines by heat shock proteins and endotoxin in murine macrophages. Biochem. Biophys. Res. Commun. 317: 1149-1154.
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 1149-1154
    • Gao, B.1    Tsan, M.F.2
  • 34
    • 0037066502 scopus 로고    scopus 로고
    • Decoding the patterns of self and nonself by the innate immune system
    • Medzhitov, R., and C. A. Janeway, Jr. 2002. Decoding the patterns of self and nonself by the innate immune system. Science 296: 298-300.
    • (2002) Science , vol.296 , pp. 298-300
    • Medzhitov, R.1    Janeway Jr., C.A.2
  • 35
    • 0033559496 scopus 로고    scopus 로고
    • Human 60-kDa heat-shock protein: A danger signal to the innate immune system
    • Chen, W., U. Syldath, K. Bellmann, V. Burkart, and H. Kolb. 1999. Human 60-kDa heat-shock protein: a danger signal to the innate immune system. J. Immunol. 162:3212-3219.
    • (1999) J. Immunol. , vol.162 , pp. 3212-3219
    • Chen, W.1    Syldath, U.2    Bellmann, K.3    Burkart, V.4    Kolb, H.5
  • 36
    • 0033747044 scopus 로고    scopus 로고
    • Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway
    • Basu, S., R. J. Binder, R. Suto, K. M. Anderson, and P. K. Srivastava. 2000. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway. Int. Immunol. 12: 1539-1546.
    • (2000) Int. Immunol. , vol.12 , pp. 1539-1546
    • Basu, S.1    Binder, R.J.2    Suto, R.3    Anderson, K.M.4    Srivastava, P.K.5
  • 38
    • 4544337512 scopus 로고    scopus 로고
    • Porphyromonas gingivalis lipopolysaccharide contains multiple lipid A species that functionally interact with both Toll-like receptors 2 and 4
    • Darveau, R. P., T. T. Pham, K. Lemley, R. A. Reife, B. W. Bainbridge, S. R. Coats, W. N. Howald, S. S. Way, and A. M. Hajjar. 2004. Porphyromonas gingivalis lipopolysaccharide contains multiple lipid A species that functionally interact with both Toll-like receptors 2 and 4. Infect. Immun. 72: 5041-5051.
    • (2004) Infect. Immun. , vol.72 , pp. 5041-5051
    • Darveau, R.P.1    Pham, T.T.2    Lemley, K.3    Reife, R.A.4    Bainbridge, B.W.5    Coats, S.R.6    Howald, W.N.7    Way, S.S.8    Hajjar, A.M.9
  • 39
    • 0033120081 scopus 로고    scopus 로고
    • Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: Evidence for TLR4 as the Lps gene product
    • Hoshino, K., O. Takeuchi, T. Kawai, H. Sanjo, T. Ogawa, Y. Takeda, K. Takeda, and S. Akira. 1999. Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product. J. Immunol. 162: 3749-3752.
    • (1999) J. Immunol. , vol.162 , pp. 3749-3752
    • Hoshino, K.1    Takeuchi, O.2    Kawai, T.3    Sanjo, H.4    Ogawa, T.5    Takeda, Y.6    Takeda, K.7    Akira, S.8
  • 41
    • 0037087398 scopus 로고    scopus 로고
    • Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs
    • Panjwani, N. N., L. Popova, and P. K. Srivastava. 2002. Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs. J. Immunol. 168: 2997-3003.
    • (2002) J. Immunol. , vol.168 , pp. 2997-3003
    • Panjwani, N.N.1    Popova, L.2    Srivastava, P.K.3
  • 42
    • 13444271569 scopus 로고    scopus 로고
    • Photodynamic therapy-induced cell surface expression and release of heat shock proteins; relevance for tumor response
    • Korbelik, M., J. Sun, and I. Cecic. 2005. Photodynamic therapy-induced cell surface expression and release of heat shock proteins; relevance for tumor response. Cancer Res. 65: 1018-1026.
    • (2005) Cancer Res. , vol.65 , pp. 1018-1026
    • Korbelik, M.1    Sun, J.2    Cecic, I.3
  • 44
    • 1642536402 scopus 로고    scopus 로고
    • The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells
    • Gastpar, R., C. Gross, L. Rossbacher, J. Ellwart, J. Riegger, and G. Multhoff. 2004. The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells. J. Immunol. 172: 972-980.
    • (2004) J. Immunol. , vol.172 , pp. 972-980
    • Gastpar, R.1    Gross, C.2    Rossbacher, L.3    Ellwart, J.4    Riegger, J.5    Multhoff, G.6
  • 45
    • 1842785206 scopus 로고    scopus 로고
    • A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation
    • Reits, E., J. Neijssen, C. Herberts, W. Benckhuijsen, L. Janssen, J. W. Drijfhout, and J. Neefjes. 2004. A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation. Immunity 20: 495-506.
    • (2004) Immunity , vol.20 , pp. 495-506
    • Reits, E.1    Neijssen, J.2    Herberts, C.3    Benckhuijsen, W.4    Janssen, L.5    Drijfhout, J.W.6    Neefjes, J.7
  • 47
    • 0033103513 scopus 로고    scopus 로고
    • Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- And peptide-specific immunity
    • Basu, S., and P. K. Srivastava. 1999. Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity. J. Exp. Med. 189:797-802.
    • (1999) J. Exp. Med. , vol.189 , pp. 797-802
    • Basu, S.1    Srivastava, P.K.2
  • 49
    • 0037328719 scopus 로고    scopus 로고
    • Heat shock protein 70 associations with myelin basic protein and proteolipid protein in multiple sclerosis brains
    • Cwiklinska, H., M. P. Mycko, O. Luvsannorov, B. Walkowiak, C. F. Brosnan, C. S. Raine, and K. W. Selmaj. 2003. Heat shock protein 70 associations with myelin basic protein and proteolipid protein in multiple sclerosis brains. Int. Immunol. 15: 241-249.
    • (2003) Int. Immunol. , vol.15 , pp. 241-249
    • Cwiklinska, H.1    Mycko, M.P.2    Luvsannorov, O.3    Walkowiak, B.4    Brosnan, C.F.5    Raine, C.S.6    Selmaj, K.W.7
  • 50
    • 0035697592 scopus 로고    scopus 로고
    • Effect of Hsp70-peptide complexes generated in vivo on modulation EAE
    • Galazka, G., A. Walczak, T. Betkowicz, and K. Selmaj. 2001. Effect of Hsp70-peptide complexes generated in vivo on modulation EAE. Adv. Exp. Med. Biol 495: 227-230.
    • (2001) Adv. Exp. Med. Biol , vol.495 , pp. 227-230
    • Galazka, G.1    Walczak, A.2    Betkowicz, T.3    Selmaj, K.4
  • 52
    • 0344585492 scopus 로고    scopus 로고
    • Aberrant extracellular and dendritic cell (DC) surface expression of heat shock protein (hsp)70 in the rheumatoid joint: Possible mechanisms of hsp/DC-mediated cross-priming
    • Martin, C. A., S. E. Carsons, R. Kowalewski, D. Bernstein, M. Valentino, and F. Santiago-Schwarz. 2003. Aberrant extracellular and dendritic cell (DC) surface expression of heat shock protein (hsp)70 in the rheumatoid joint: possible mechanisms of hsp/DC-mediated cross-priming. J. Immunol. 171: 5736-5742.
    • (2003) J. Immunol. , vol.171 , pp. 5736-5742
    • Martin, C.A.1    Carsons, S.E.2    Kowalewski, R.3    Bernstein, D.4    Valentino, M.5    Santiago-Schwarz, F.6
  • 53
    • 0345299172 scopus 로고    scopus 로고
    • The dual nature of specific immunological activity of tumor-derived gp96 preparations
    • Chandawarkar, R. Y., M, S. Wagh, and P. K. Srivastava. 1999. The dual nature of specific immunological activity of tumor-derived gp96 preparations. J. Exp. Med. 189: 1437-1442.
    • (1999) J. Exp. Med. , vol.189 , pp. 1437-1442
    • Chandawarkar, R.Y.1    Wagh, M.S.2    Srivastava, P.K.3
  • 54
    • 1842854683 scopus 로고    scopus 로고
    • Immune modulation with high-dose heat-shock protein gp96: Therapy of murine autoimmune diabetes and encephalomyelitis
    • Chandawarkar, R. Y., M. S. Wagh, J. T. Kovalchin, and P. Srivastava. 2004. Immune modulation with high-dose heat-shock protein gp96: therapy of murine autoimmune diabetes and encephalomyelitis. Int. Immunol. 16: 615-624.
    • (2004) Int. Immunol. , vol.16 , pp. 615-624
    • Chandawarkar, R.Y.1    Wagh, M.S.2    Kovalchin, J.T.3    Srivastava, P.4
  • 56
    • 0033838826 scopus 로고    scopus 로고
    • Immunotherapy of a human papillomavirus (HPV) type 16 E7-expressing tumour by administration of fusion protein comprising Mycobacterium bovis bacille Calmette-Guerin (BCG) hsp65 and HPV16 E7
    • Chu, N. R., H. B. Wu, T. Wu, L. J. Boux, M. I. Siegel, and L. A. Mizzen. 2000. Immunotherapy of a human papillomavirus (HPV) type 16 E7-expressing tumour by administration of fusion protein comprising Mycobacterium bovis bacille Calmette-Guerin (BCG) hsp65 and HPV16 E7. Clin. Exp. Immunol. 121: 216-225.
    • (2000) Clin. Exp. Immunol. , vol.121 , pp. 216-225
    • Chu, N.R.1    Wu, H.B.2    Wu, T.3    Boux, L.J.4    Siegel, M.I.5    Mizzen, L.A.6
  • 57
    • 0036219195 scopus 로고    scopus 로고
    • CpG motifs in bacterial DNA and their immune effects
    • Krieg, A. M. 2002. CpG motifs in bacterial DNA and their immune effects. Annu. Rev. Immunol. 20: 709-760.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 709-760
    • Krieg, A.M.1
  • 59
    • 0034868066 scopus 로고    scopus 로고
    • Role of the heat shock protein 90 in immune response stimulation by bacterial DNA and synthetic oligonucleotides
    • Zhu, F. G., and D. S. Pisetsky. 2001. Role of the heat shock protein 90 in immune response stimulation by bacterial DNA and synthetic oligonucleotides. Infect. Immun. 69: 5546-5552.
    • (2001) Infect. Immun. , vol.69 , pp. 5546-5552
    • Zhu, F.G.1    Pisetsky, D.S.2
  • 61
    • 0042357122 scopus 로고    scopus 로고
    • GRP94/gp96 elicits ERK activation in murine macrophages: A role for endotoxin contamination in NF-κB activation and nitric oxide production
    • Reed, R. C., B. Berwin, J. P. Baker, and C. V. Nicchitta. 2003. GRP94/gp96 elicits ERK activation in murine macrophages: a role for endotoxin contamination in NF-κB activation and nitric oxide production. J. Biol. Chem. 278: 31853-31860.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31853-31860
    • Reed, R.C.1    Berwin, B.2    Baker, J.P.3    Nicchitta, C.V.4
  • 63
    • 4344697308 scopus 로고    scopus 로고
    • Heat-shock protein 70 and heat-shock protein 90 associate with Toll-like receptor 4 in response to bacterial lipopolysaccharide
    • Triantafilou, M., and K. Triantafilou. 2004. Heat-shock protein 70 and heat-shock protein 90 associate with Toll-like receptor 4 in response to bacterial lipopolysaccharide. Biochem. Soc. Trans. 32: 636-639.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 636-639
    • Triantafilou, M.1    Triantafilou, K.2
  • 64
    • 0344012568 scopus 로고    scopus 로고
    • Stress-induced extracellular Hsp72 is a functionally significant danger signal to the immune system
    • Campisi, J., T. H. Leem, and M. Fleshner. 2003. Stress-induced extracellular Hsp72 is a functionally significant danger signal to the immune system. Cell Stress Chaperones 8: 272-286.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 272-286
    • Campisi, J.1    Leem, T.H.2    Fleshner, M.3
  • 65
    • 15244363969 scopus 로고    scopus 로고
    • Tregs in T cell vaccination: Exploring the regulation of regulation
    • Cohen, I. R., F. J. Quintana, and A. Mimran. 2004. Tregs in T cell vaccination: exploring the regulation of regulation. J. Clin. Invest. 114: 1227-1232.
    • (2004) J. Clin. Invest. , vol.114 , pp. 1227-1232
    • Cohen, I.R.1    Quintana, F.J.2    Mimran, A.3
  • 66
    • 0037065909 scopus 로고    scopus 로고
    • Inflammatory response after open heart surgery: Release of heat-shock protein 70 and signaling through Toll-like receptor-4
    • Dybdahl, B., A. Wahba, E. Lien, T. H. Flo, A. Waage, N. Qureshi, O. F. Sellevold, T. Espevik, and A. Sundan. 2002. Inflammatory response after open heart surgery: release of heat-shock protein 70 and signaling through Toll-like receptor-4. Circulation 105: 685-690.
    • (2002) Circulation , vol.105 , pp. 685-690
    • Dybdahl, B.1    Wahba, A.2    Lien, E.3    Flo, T.H.4    Waage, A.5    Qureshi, N.6    Sellevold, O.F.7    Espevik, T.8    Sundan, A.9
  • 67
    • 0032995051 scopus 로고    scopus 로고
    • Myocardial injury leads to a release of heat shock protein (hsp) 60 and a suppression of the anti-hsp65 immune response
    • Schett, G., B. Metzler, R. Kleindienst, A. Amberger, H. Recheis, Q. Xu, and G. Wick. 1999. Myocardial injury leads to a release of heat shock protein (hsp) 60 and a suppression of the anti-hsp65 immune response. Cardiovasc. Res. 42: 685-695.
    • (1999) Cardiovasc. Res. , vol.42 , pp. 685-695
    • Schett, G.1    Metzler, B.2    Kleindienst, R.3    Amberger, A.4    Recheis, H.5    Xu, Q.6    Wick, G.7
  • 69
    • 20744436655 scopus 로고    scopus 로고
    • Exosome-dependent trafficking of HSP70: A novel secretory pathway for cellular stress proteins
    • Lancaster, G. I., and M. A. Febbraio. 2005. Exosome-dependent trafficking of HSP70: A novel secretory pathway for cellular stress proteins. J. Biol. Chem. 280: 23349-23355.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23349-23355
    • Lancaster, G.I.1    Febbraio, M.A.2
  • 70
    • 0346734122 scopus 로고    scopus 로고
    • Cell surface expression of an endoplasmic reticulum resident heat shock protein gp96 triggers MyD88-dependent systemic autoimmune diseases
    • Liu, B., J. Dai, H. Zheng, D. Stoilova, S. Sun, and Z. Li. 2003. Cell surface expression of an endoplasmic reticulum resident heat shock protein gp96 triggers MyD88-dependent systemic autoimmune diseases. Proc. Natl. Acad. Sci. USA 100: 15824-15829.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15824-15829
    • Liu, B.1    Dai, J.2    Zheng, H.3    Stoilova, D.4    Sun, S.5    Li, Z.6
  • 71
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira, S., and K. Takeda. 2004. Toll-like receptor signalling. Nat. Rev. Immunol. 4: 499-511.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 72
    • 0347122087 scopus 로고    scopus 로고
    • Hsp70 promotes antigen-presenting cell function and converts T cell tolerance to autoimmunity in vivo
    • Millar, D. G., K. M. Garza, B. Odermatt, A. R. Elford, N. Ono, Z. Li, and P. S. Ohashi. 2003. Hsp70 promotes antigen-presenting cell function and converts T cell tolerance to autoimmunity in vivo. Nat. Med. 9: 1469-1476.
    • (2003) Nat. Med. , vol.9 , pp. 1469-1476
    • Millar, D.G.1    Garza, K.M.2    Odermatt, B.3    Elford, A.R.4    Ono, N.5    Li, Z.6    Ohashi, P.S.7
  • 73
    • 0038500959 scopus 로고    scopus 로고
    • Toll-Like receptor ligand links innate and adaptive immune responses by the production of heat-shock proteins
    • Kumaraguru, U., C. D. Pack, and B. T. Rouse. 2003. Toll-Like receptor ligand links innate and adaptive immune responses by the production of heat-shock proteins. J. Leukocyte Biol. 73:574-583.
    • (2003) J. Leukocyte Biol. , vol.73 , pp. 574-583
    • Kumaraguru, U.1    Pack, C.D.2    Rouse, B.T.3
  • 74
    • 0031029997 scopus 로고    scopus 로고
    • Increase of heat-shock protein and induction of γ/δ T cells in peritoneal exudate of mice after injection of live Fusobacterium nucleatum
    • Saito, K., H. Katsuragi, M. Mikami, C. Kato, M. Miyamaru, and K. Nagaso. 1997. Increase of heat-shock protein and induction of γ/δ T cells in peritoneal exudate of mice after injection of live Fusobacterium nucleatum. Immunology 90: 229-235.
    • (1997) Immunology , vol.90 , pp. 229-235
    • Saito, K.1    Katsuragi, H.2    Mikami, M.3    Kato, C.4    Miyamaru, M.5    Nagaso, K.6
  • 75
    • 0029873545 scopus 로고    scopus 로고
    • Induction of heat shock proteins and their possible roles in macrophages during activation by macrophage colony-stimulating factor
    • Teshima, S., K. Rokutan, M. Takahashi, T. Nikawa, and K. Kishi. 1996. Induction of heat shock proteins and their possible roles in macrophages during activation by macrophage colony-stimulating factor. Biochem. J. 315(Pt 2): 497-504.
    • (1996) Biochem. J. , vol.315 , Issue.PART 2 , pp. 497-504
    • Teshima, S.1    Rokutan, K.2    Takahashi, M.3    Nikawa, T.4    Kishi, K.5
  • 76
    • 0035903158 scopus 로고    scopus 로고
    • Endocytosed HSP60s use Toll-like receptor 2 (TLR2) and TLR4 to activate the Toll/interleukin-1 receptor signaling pathway in innate immune cells
    • Vabulas, R. M., P. Ahmad-Nejad, C. da Costa, T. Miethke, C. J. Kirschning, H. Hacker, and H. Wagner. 2001. Endocytosed HSP60s use Toll-like receptor 2 (TLR2) and TLR4 to activate the Toll/interleukin-1 receptor signaling pathway in innate immune cells. J. Biol. Chem. 276: 31332-31339.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31332-31339
    • Vabulas, R.M.1    Ahmad-Nejad, P.2    Da Costa, C.3    Miethke, T.4    Kirschning, C.J.5    Hacker, H.6    Wagner, H.7
  • 77
    • 0035871626 scopus 로고    scopus 로고
    • Induction of cross-tolerance by lipopolysaccharide and highly purified lipoteichoic acid via different Toll-like receptors independent of paracrine mediators
    • Lehner, M, D., S. Morath, K. S. Michelsen, R. R. Schumann, and T. Hartung. 2001. Induction of cross-tolerance by lipopolysaccharide and highly purified lipoteichoic acid via different Toll-like receptors independent of paracrine mediators. J. Immunol. 166: 5161-5167.
    • (2001) J. Immunol. , vol.166 , pp. 5161-5167
    • Lehner, M.D.1    Morath, S.2    Michelsen, K.S.3    Schumann, R.R.4    Hartung, T.5
  • 78
    • 0034671772 scopus 로고    scopus 로고
    • Synergy and cross-tolerance between Toll-like receptor (TLR)2- and TLR4-mediated signaling pathways
    • Sato, S., F. Nomura, T. Kawai, O. Takeuchi, P. F. Muhlradt, K. Takeda, and S. Akira. 2000. Synergy and cross-tolerance between Toll-like receptor (TLR)2- and TLR4-mediated signaling pathways. J. Immunol. 165: 7096-7101.
    • (2000) J. Immunol. , vol.165 , pp. 7096-7101
    • Sato, S.1    Nomura, F.2    Kawai, T.3    Takeuchi, O.4    Muhlradt, P.F.5    Takeda, K.6    Akira, S.7
  • 79
    • 0036892865 scopus 로고    scopus 로고
    • Counteracting interactions between lipopolysaccharide molecules with differential activation of toll-like receptors
    • Hajishengallis, G., M. Martin, R. E. Schifferle, and R. J. Genco. 2002. Counteracting interactions between lipopolysaccharide molecules with differential activation of toll-like receptors. Infect. Immun. 70: 6658-6664.
    • (2002) Infect. Immun. , vol.70 , pp. 6658-6664
    • Hajishengallis, G.1    Martin, M.2    Schifferle, R.E.3    Genco, R.J.4
  • 80
    • 0035500281 scopus 로고    scopus 로고
    • Differential induction of endotoxin tolerance by lipopolysaccharides derived from Porphyromonas gingivalis and Escherichia coli
    • Martin, M., J. Katz, S. N. Vogel, and S. M. Michalek. 2001. Differential induction of endotoxin tolerance by lipopolysaccharides derived from Porphyromonas gingivalis and Escherichia coli. J. Immunol. 167: 5278-5285.
    • (2001) J. Immunol. , vol.167 , pp. 5278-5285
    • Martin, M.1    Katz, J.2    Vogel, S.N.3    Michalek, S.M.4
  • 81
    • 0037218547 scopus 로고    scopus 로고
    • Induction of in vitro reprogramming by Toll-like receptor (TLR)2 and TLR4 agonists in murine macrophages: Effects of TLR "homotolerance" versus "heterotolerance" on NF-κB signaling pathway components
    • Dobrovolskaia, M. A., A. E. Medvedev, K. E. Thomas, N. Cuesta, V. Toshchakov, T. Ren, M. J. Cody, S. M. Michalek, N. R. Rice, and S. N. Vogel. 2003. Induction of in vitro reprogramming by Toll-like receptor (TLR)2 and TLR4 agonists in murine macrophages: effects of TLR "homotolerance" versus "heterotolerance" on NF-κB signaling pathway components. J. Immunol. 170: 508-519.
    • (2003) J. Immunol. , vol.170 , pp. 508-519
    • Dobrovolskaia, M.A.1    Medvedev, A.E.2    Thomas, K.E.3    Cuesta, N.4    Toshchakov, V.5    Ren, T.6    Cody, M.J.7    Michalek, S.M.8    Rice, N.R.9    Vogel, S.N.10
  • 82
    • 0042265135 scopus 로고    scopus 로고
    • Toll-like receptor 2- and 6-mediated stimulation by macrophage-activating lipopeptide 2 induces lipopolysaccharide (LPS) cross tolerance in mice, which results in protection from tumor necrosis factor α but in only partial protection from lethal LPS doses
    • Deiters, U., M. Gumenscheimer, C. Galanos, and P. F. Muhlradt. 2003. Toll-like receptor 2- and 6-mediated stimulation by macrophage-activating lipopeptide 2 induces lipopolysaccharide (LPS) cross tolerance in mice, which results in protection from tumor necrosis factor α but in only partial protection from lethal LPS doses. Infect. Immun. 71: 4456-4462.
    • (2003) Infect. Immun. , vol.71 , pp. 4456-4462
    • Deiters, U.1    Gumenscheimer, M.2    Galanos, C.3    Muhlradt, P.F.4
  • 83
    • 2442652487 scopus 로고    scopus 로고
    • HSP60 and CpG-DNA-oligonucleotides differentially regulate LPS-tolerance of hepatic Kupffer cells
    • Schuchmann, M., F. Hermann, J. Herkel, R. van der Zee, P. R. Galle, and A. W. Lohse. 2004. HSP60 and CpG-DNA-oligonucleotides differentially regulate LPS-tolerance of hepatic Kupffer cells. Immunol. Lett. 93: 199-204.
    • (2004) Immunol. Lett. , vol.93 , pp. 199-204
    • Schuchmann, M.1    Hermann, F.2    Herkel, J.3    Van Der Zee, R.4    Galle, P.R.5    Lohse, A.W.6
  • 84
    • 3442878145 scopus 로고    scopus 로고
    • HSP60 induces self-tolerance to repeated HSP60 stimulation and cross-tolerance to other pro-inflammatory stimuli
    • Kilmartin, B., and D. J. Reen. 2004. HSP60 induces self-tolerance to repeated HSP60 stimulation and cross-tolerance to other pro-inflammatory stimuli. Eur. J. Immunol. 34: 2041-2051.
    • (2004) Eur. J. Immunol. , vol.34 , pp. 2041-2051
    • Kilmartin, B.1    Reen, D.J.2
  • 85
    • 0037136537 scopus 로고    scopus 로고
    • The effect of infections on susceptibility to autoimmune and allergic diseases
    • Bach, J. F. 2002. The effect of infections on susceptibility to autoimmune and allergic diseases. N. Engl. J. Med. 347: 911-920.
    • (2002) N. Engl. J. Med. , vol.347 , pp. 911-920
    • Bach, J.F.1
  • 88
    • 0034210823 scopus 로고    scopus 로고
    • Discrimination and dialogue in the immune system
    • Cohen, I. R. 2000. Discrimination and dialogue in the immune system. Semin. Immunol. 12:215-219.
    • (2000) Semin. Immunol. , vol.12 , pp. 215-219
    • Cohen, I.R.1
  • 89
    • 0034112239 scopus 로고    scopus 로고
    • Autoimmunity can benefit self-maintenance
    • Schwartz, M., and I. R. Cohen. 2000. Autoimmunity can benefit self-maintenance. Immunol. Today 21: 265-268.
    • (2000) Immunol. Today , vol.21 , pp. 265-268
    • Schwartz, M.1    Cohen, I.R.2
  • 90
    • 5144227227 scopus 로고    scopus 로고
    • Functional immunomics: Microarray analysis of IgG autoantibody repertoires predicts the future response of mice to induced diabetes
    • Quintana, F. J., P. H. Hagedorn, G. Elizur, Y. Merbl, E. Domany, and I. R. Cohen. 2004. Functional immunomics: microarray analysis of IgG autoantibody repertoires predicts the future response of mice to induced diabetes. Proc. Natl. Acad. Sci. USA 101(Suppl. 2): 14615-14621.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.SUPPL. 2 , pp. 14615-14621
    • Quintana, F.J.1    Hagedorn, P.H.2    Elizur, G.3    Merbl, Y.4    Domany, E.5    Cohen, I.R.6
  • 91
    • 0036180102 scopus 로고    scopus 로고
    • Self-heat shock protein 60 induces tumour necrosis factor α in monocyte-derived macrophage: Possible role in chronic inflammatory periodontal disease
    • Ueki, K., K. Tabeta, H. Yoshie, and K. Yamazaki. 2002. Self-heat shock protein 60 induces tumour necrosis factor α in monocyte-derived macrophage: possible role in chronic inflammatory periodontal disease. Clin. Exp. Immunol. 127: 72-77.
    • (2002) Clin. Exp. Immunol. , vol.127 , pp. 72-77
    • Ueki, K.1    Tabeta, K.2    Yoshie, H.3    Yamazaki, K.4
  • 92
    • 0034650427 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex
    • Ohashi, K., V. Burkart, S. Flohe, and H. Kolb. 2000. Cutting edge: heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex. J. Immunol. 164:558-561.
    • (2000) J. Immunol. , vol.164 , pp. 558-561
    • Ohashi, K.1    Burkart, V.2    Flohe, S.3    Kolb, H.4
  • 93
    • 0036467447 scopus 로고    scopus 로고
    • Chlamydial heat shock protein 60 activates macrophages and endothelial cells through Toll-like receptor 4 and MD2 in a MyD88-dependent pathway
    • Bulut, Y., E. Faure, L. Thomas, H. Karahashi, K. S. Michelsen, O. Equils, S. G. Morrison, R. P. Morrison, and M. Arditi. 2002. Chlamydial heat shock protein 60 activates macrophages and endothelial cells through Toll-like receptor 4 and MD2 in a MyD88-dependent pathway. J. Immunol. 168: 1435-1440.
    • (2002) J. Immunol. , vol.168 , pp. 1435-1440
    • Bulut, Y.1    Faure, E.2    Thomas, L.3    Karahashi, H.4    Michelsen, K.S.5    Equils, O.6    Morrison, S.G.7    Morrison, R.P.8    Arditi, M.9
  • 94
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu, S., R. J. Binder, T. Ramalingam, and P. K. Srivastava. 2001. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 14: 303-313.
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 95
    • 0037177825 scopus 로고    scopus 로고
    • Novel signal transduction pathway utilized by extracellular HSP70: Role of Toll-like receptor (TLR)2 and TLR4
    • Asea, A., M. Rehli, E. Kabingu, J. A. Boch, O. Bare, P. E. Auron, M. A. Stevenson, and S. K. Calderwood. 2002. Novel signal transduction pathway utilized by extracellular HSP70: role of Toll-like receptor (TLR)2 and TLR4. J. Biol. Chem. 277: 15028-15034.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15028-15034
    • Asea, A.1    Rehli, M.2    Kabingu, E.3    Boch, J.A.4    Bare, O.5    Auron, P.E.6    Stevenson, M.A.7    Calderwood, S.K.8
  • 98
    • 0346849665 scopus 로고    scopus 로고
    • CD40, but not CD40L, is required for the optimal priming of T cells and control of aerosol M. tuberculosis infection
    • Lazarevic, V., A. J. Myers, C. A. Scanga, and J. L. Flynn. 2003. CD40, but not CD40L, is required for the optimal priming of T cells and control of aerosol M. tuberculosis infection. Immunity 19: 823-835.
    • (2003) Immunity , vol.19 , pp. 823-835
    • Lazarevic, V.1    Myers, A.J.2    Scanga, C.A.3    Flynn, J.L.4
  • 99
    • 0037144808 scopus 로고    scopus 로고
    • CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes
    • Becker, T., F. U. Hartl, and F. Wieland. 2002. CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. J. Cell Biol. 158: 1277-1285.
    • (2002) J. Cell Biol. , vol.158 , pp. 1277-1285
    • Becker, T.1    Hartl, F.U.2    Wieland, F.3
  • 100
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea, A., S. K. Kraeft, E. A. Kurt-Jones, M. A. Stevenson, L. B. Chen, R. W. Finberg, G. C. Koo, and S. K. Calderwood. 2000. HSP70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine. Nat. Med. 6: 435-442.
    • (2000) Nat. Med. , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6    Koo, G.C.7    Calderwood, S.K.8
  • 101
    • 0033975855 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells
    • Kol, A., A. H. Lichtman, R. W. Finberg, P. Libby, and E. A. Kurt-Jones. 2000. Cutting edge: heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells. J. Immunol. 164: 13-17.
    • (2000) J. Immunol. , vol.164 , pp. 13-17
    • Kol, A.1    Lichtman, A.H.2    Finberg, R.W.3    Libby, P.4    Kurt-Jones, E.A.5
  • 102
    • 0037298742 scopus 로고    scopus 로고
    • Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94
    • Gross, C., D. Hansch, R. Gastpar, and G. Multhoff. 2003. Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94. Biol. Chem. 384: 267-279.
    • (2003) Biol. Chem. , vol.384 , pp. 267-279
    • Gross, C.1    Hansch, D.2    Gastpar, R.3    Multhoff, G.4
  • 103
    • 0345305789 scopus 로고    scopus 로고
    • Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells
    • Berwin, B., J. P. Hart, S. Rice, C. Gass, S. V. Pizzo, S. R. Post, and C. V. Nicchitta. 2003. Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells. EMBO J. 22: 6127-6136.
    • (2003) EMBO J. , vol.22 , pp. 6127-6136
    • Berwin, B.1    Hart, J.P.2    Rice, S.3    Gass, C.4    Pizzo, S.V.5    Post, S.R.6    Nicchitta, C.V.7


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