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Volumn 11, Issue 8, 2011, Pages 565-

Are heat shock proteins DAMPs?

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HIGH MOBILITY GROUP B1 PROTEIN; SCAVENGER RECEPTOR A; SCAVENGER RECEPTOR A1; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; UNCLASSIFIED DRUG;

EID: 79960768302     PISSN: 14741733     EISSN: 14741741     Source Type: Journal    
DOI: 10.1038/nri2873-c2     Document Type: Letter
Times cited : (5)

References (9)
  • 1
    • 78649526394 scopus 로고    scopus 로고
    • Sterile inflammation: Sensing and reacting to damage
    • Chen, G. Y. & Nuñez. G. Sterile inflammation: sensing and reacting to damage. Nature Rev. Immunol. 10, 826-837 (2010).
    • (2010) Nature Rev. Immunol. , vol.10 , pp. 826-837
    • Chen, G.Y.1    Nuñez, G.2
  • 2
    • 79960810171 scopus 로고    scopus 로고
    • Heat shock proteins are no DAMPs rather 'DAMPERs'
    • 25 Jul doi:10.1038/nri2873-c1
    • Broere, F., van der Zee, R. & van Eden, W. Heat shock proteins are no DAMPs, rather 'DAMPERs'. Nature Rev. Immunol. 25 Jul 2011 (doi:10.1038/nri2873- c1).
    • (2011) Nature Rev. Immunol.
    • Broere, F.1    Van Der Zee, R.2    Van Eden, W.3
  • 3
    • 12444290815 scopus 로고    scopus 로고
    • Heat shock protein 60: Specific binding of lipopolysaccharide
    • Habich, C. et al. Heat shock protein 60: specific binding of lipopolysaccharide. J. Immunol. 174, 1298-1305 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 1298-1305
    • Habich, C.1
  • 4
    • 33747339222 scopus 로고    scopus 로고
    • Interaction of TLR2 and TLR4 ligands with the N-terminal domain of Gp96 amplifies innate and adaptive immune responses
    • Warger, T. et al. Interaction of TLR2 and TLR4 ligands with the N-terminal domain of Gp96 amplifies innate and adaptive immune responses. J. Biol. Chem. 281, 22545-22553 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 22545-22553
    • Warger, T.1
  • 5
    • 33947510303 scopus 로고    scopus 로고
    • Synergistic and differential modulation of immune responses by Hsp60 and lipopolysaccharide
    • Osterloh, A., Kalinke, U., Weiss, S., Fleischer, B. & Breloer, M. Synergistic and differential modulation of immune responses by Hsp60 and lipopolysaccharide. J. Biol. Chem. 282, 4669-4680 (2006).
    • (2006) J. Biol. Chem. , vol.282 , pp. 4669-4680
    • Osterloh, A.1    Kalinke, U.2    Weiss, S.3    Fleischer, B.4    Breloer, M.5
  • 7
    • 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
    • DOI 10.1074/jbc.M208742200
    • Gao, B & Tsan, M. F. 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). (Pubitemid 36043559)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 174-179
    • Gao, B.1    Tsan, M.-F.2
  • 8
    • 0036467388 scopus 로고    scopus 로고
    • Roles of heat-shock proteins in antigen presentation and cross-presentation
    • DOI 10.1016/S0952-7915(01)00297-7
    • Li, Z., Menoret, A. & Srivastava, P. Roles of heat-shock proteins in antigen presentation and cross-presentation. Curr. Opin. Immunol. 14, 45-51 (2002). (Pubitemid 34085106)
    • (2002) Current Opinion in Immunology , vol.14 , Issue.1 , pp. 45-51
    • Li, Z.1    Menoret, A.2    Srivastava, P.3
  • 9
    • 0037040541 scopus 로고    scopus 로고
    • Protein folding. Molecular chaperones in the cytosol: From nascent chain to folded protein
    • DOI 10.1126/science.1068408
    • Hartl, F. U. & Hayer-Hartl, M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858 (2002). (Pubitemid 34214115)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.