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Volumn 7, Issue 8, 2008, Pages 1185-1199

Heat-shock proteins as powerful weapons in vaccine development

Author keywords

Autoimmunity; Cancer; Chaperone; Gp96; Heat shock protein; HSP70; Immunotherapy; Infectious diseases; Vaccination strategies

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CALRETICULIN; CHAPERONE; GLYCOPROTEIN GP 96; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 10; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; OXYGEN REGULATED PROTEIN 150; VACCINE;

EID: 53849129597     PISSN: 14760584     EISSN: 17448395     Source Type: Journal    
DOI: 10.1586/14760584.7.8.1185     Document Type: Review
Times cited : (108)

References (95)
  • 1
    • 0022857444 scopus 로고
    • Heat shock and the heat shock proteins
    • Burdon RH. Heat shock and the heat shock proteins. Biochem. J. 240, 313-324 (1986).
    • (1986) Biochem. J , vol.240 , pp. 313-324
    • Burdon, R.H.1
  • 2
    • 0042235547 scopus 로고    scopus 로고
    • Heat shock proteins as regulators of the immune response
    • Describes the structure and synthesis of heat-shock proteins (HSPs) and their roles in eliciting innate and adaptive immunity, •
    • Pockley AG. Heat shock proteins as regulators of the immune response. Lancet 362(9382), 469-476 (2003). • Describes the structure and synthesis of heat-shock proteins (HSPs) and their roles in eliciting innate and adaptive immunity.
    • (2003) Lancet , vol.362 , Issue.9382 , pp. 469-476
    • Pockley, A.G.1
  • 3
    • 0031972072 scopus 로고    scopus 로고
    • Immune responses to stress proteins: Applications to infectious disease and cancer
    • Mizzen L. Immune responses to stress proteins: applications to infectious disease and cancer. Biotherapy 10, 173-189 (1998).
    • (1998) Biotherapy , vol.10 , pp. 173-189
    • Mizzen, L.1
  • 4
    • 0034996852 scopus 로고    scopus 로고
    • The role of heat shock proteins and their receptors in the activation of the immune system
    • Singh-Jasuja H, Hilf N, Arnold-Schild D, Schild H. The role of heat shock proteins and their receptors in the activation of the immune system. Biol. Chem. 382, 629-636 (2001).
    • (2001) Biol. Chem , vol.382 , pp. 629-636
    • Singh-Jasuja, H.1    Hilf, N.2    Arnold-Schild, D.3    Schild, H.4
  • 5
    • 34548259088 scopus 로고    scopus 로고
    • Hsp70 chaperone as a survival factor in cell pathology
    • Guzhova I, Margulis B. Hsp70 chaperone as a survival factor in cell pathology. Int. Rev. Cytol. 254, 101-149 (2006).
    • (2006) Int. Rev. Cytol , vol.254 , pp. 101-149
    • Guzhova, I.1    Margulis, B.2
  • 6
    • 85012430068 scopus 로고    scopus 로고
    • Heat shock proteins in health and disease: Therapeutic targets or therapeutic agents?
    • Pockley AG. Heat shock proteins in health and disease: therapeutic targets or therapeutic agents? Expert Rev. Mol. Med. 3, 1-21 (2001).
    • (2001) Expert Rev. Mol. Med , vol.3 , pp. 1-21
    • Pockley, A.G.1
  • 7
    • 0038268180 scopus 로고    scopus 로고
    • HSF1 interacts with Ral binding protein 1 (RalBP1) in a stress-responsive multi-protein complex with HSP90 in vivo
    • Hu Y, Mivechi NF. HSF1 interacts with Ral binding protein 1 (RalBP1) in a stress-responsive multi-protein complex with HSP90 in vivo. J. Biol. Chem. 278(19), 17299-17306 (2003).
    • (2003) J. Biol. Chem , vol.278 , Issue.19 , pp. 17299-17306
    • Hu, Y.1    Mivechi, N.F.2
  • 8
    • 0033890818 scopus 로고    scopus 로고
    • Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of Hsp90-binding agents
    • Bagatell R, Paine-Murrieta GD, Taylor CW et al. Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of Hsp90-binding agents. Clin. Cancer Res. 6, 3312-3318 (2000).
    • (2000) Clin. Cancer Res , vol.6 , pp. 3312-3318
    • Bagatell, R.1    Paine-Murrieta, G.D.2    Taylor, C.W.3
  • 9
    • 0031866191 scopus 로고    scopus 로고
    • HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes
    • Ali A, Bharadwaj S, O'Carroll R, Ovsenek N. HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes. Mol. Cell. Biol. 18(9), 4949-4960 (1998).
    • (1998) Mol. Cell. Biol , vol.18 , Issue.9 , pp. 4949-4960
    • Ali, A.1    Bharadwaj, S.2    O'Carroll, R.3    Ovsenek, N.4
  • 10
    • 0033499798 scopus 로고    scopus 로고
    • Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 in vivo
    • Bharadwaj S, Ali A, Ovsenek N. Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 in vivo. Mol. Cell. Biol. 19(10), 8033-8041 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , Issue.10 , pp. 8033-8041
    • Bharadwaj, S.1    Ali, A.2    Ovsenek, N.3
  • 11
    • 17144417382 scopus 로고    scopus 로고
    • Heat-shock proteins induce T cell regulation of chronic inflammation
    • Eden W, Zee R, Prakken B. Heat-shock proteins induce T cell regulation of chronic inflammation. Nat. Rev. Immunol. 5, 318-330 (2005).
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 318-330
    • Eden, W.1    Zee, R.2    Prakken, B.3
  • 13
    • 85190519642 scopus 로고    scopus 로고
    • Robert J. Evolution of heat shock protein and immunity. Dev. Comp. Immunol. 27, 449-464 (2003). • Broadly explains the conserved roles of HSPs, especially Gp96, in eliciting immune responses within different organisms, including Xenopus, mice and humans.
    • Robert J. Evolution of heat shock protein and immunity. Dev. Comp. Immunol. 27, 449-464 (2003). • Broadly explains the conserved roles of HSPs, especially Gp96, in eliciting immune responses within different organisms, including Xenopus, mice and humans.
  • 14
    • 53849112237 scopus 로고    scopus 로고
    • Ciupitu AM. Hsp70 in immunotherapy: a potential vector in cancer and viral vaccines. Stockholm (Thesis), 2000.
    • Ciupitu AM. Hsp70 in immunotherapy: a potential vector in cancer and viral vaccines. Stockholm (Thesis), 2000.
  • 15
    • 0033625965 scopus 로고    scopus 로고
    • The Hsp110 and Grp170 stress proteins: Newly recognized relatives of the Hsp70s
    • Easton DP, Kaneko Y, Subjeck JR. The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s. Cell Stress Chaperones 5(4), 276-290 (2000).
    • (2000) Cell Stress Chaperones , vol.5 , Issue.4 , pp. 276-290
    • Easton, D.P.1    Kaneko, Y.2    Subjeck, J.R.3
  • 16
    • 1242269219 scopus 로고    scopus 로고
    • Mechanisms for regulation of Hsp70 function by Hsp40
    • Fan CY, Lee S, Cyr DM. Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress Chaperones 8(4), 309-316 (2003).
    • (2003) Cell Stress Chaperones , vol.8 , Issue.4 , pp. 309-316
    • Fan, C.Y.1    Lee, S.2    Cyr, D.M.3
  • 17
    • 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 (2), 173-182 (2005).
    • (2005) Mol. Cells , vol.20 , Issue.2 , pp. 173-182
    • Yang, Y.1    Li, Z.2
  • 18
    • 0036606130 scopus 로고    scopus 로고
    • Three-step purification of gp96 from human liver tumor tissues suitable for isolation of gp96-bound peptides
    • Meng SD, Song J, Rao Z, Tien P, Gao GF. Three-step purification of gp96 from human liver tumor tissues suitable for isolation of gp96-bound peptides. J. Immunol. Methods 264, 29-35 (2002).
    • (2002) J. Immunol. Methods , vol.264 , pp. 29-35
    • Meng, S.D.1    Song, J.2    Rao, Z.3    Tien, P.4    Gao, G.F.5
  • 19
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function and clinical applications: a comprehensive review
    • Csermely P, Schnaider T, Soti C, Prohaszka Z, Nardai G. The 90-kDa molecular chaperone family: structure, function and clinical applications: a comprehensive review. Pharmacol. Ther. 79(2), 129-168 (1998).
    • (1998) Pharmacol. Ther , vol.79 , Issue.2 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaszka, Z.4    Nardai, G.5
  • 20
    • 0037011072 scopus 로고    scopus 로고
    • GRP94 (gp96) and GRP94 N-terminal geldanamycin binding domain elicit tissue non-restricted tumor suppression
    • Baker-LePain JC, Sarzotti M, Fields TA, Li CY, Nicchitta CV. GRP94 (gp96) and GRP94 N-terminal geldanamycin binding domain elicit tissue non-restricted tumor suppression. J. Exp. Med. 196, 1447-1459 (2002).
    • (2002) J. Exp. Med , vol.196 , pp. 1447-1459
    • Baker-LePain, J.C.1    Sarzotti, M.2    Fields, T.A.3    Li, C.Y.4    Nicchitta, C.V.5
  • 21
    • 10844266556 scopus 로고    scopus 로고
    • Generation of murine CTL by a hepatitis B virus-specific peptide and evaluation of the adjuvant effect of heat shock protein glycoprotein 96 and its terminal fragments
    • Demonstrates the potency of the N-terminal Gp96 fragment as a possible adjuvant to augment cytotoxic T-lymphocyte response against HBV infection and hepatocellular carcinoma, ••
    • Li H, Zhou M, Han J et al. Generation of murine CTL by a hepatitis B virus-specific peptide and evaluation of the adjuvant effect of heat shock protein glycoprotein 96 and its terminal fragments. J. Immunol. 174, 195-204 (2005). •• Demonstrates the potency of the N-terminal Gp96 fragment as a possible adjuvant to augment cytotoxic T-lymphocyte response against HBV infection and hepatocellular carcinoma.
    • (2005) J. Immunol , vol.174 , pp. 195-204
    • Li, H.1    Zhou, M.2    Han, J.3
  • 22
    • 0034007999 scopus 로고    scopus 로고
    • Identification of the peptide-binding site in the heat shock chaperone/tumor rejection antigen gp96 (Grp94)
    • Linderoth NA, Popowicz A, Sastry S. Identification of the peptide-binding site in the heat shock chaperone/tumor rejection antigen gp96 (Grp94). J. Biol. Chem. 275(8), 5472-5477 (2000).
    • (2000) J. Biol. Chem , vol.275 , Issue.8 , pp. 5472-5477
    • Linderoth, N.A.1    Popowicz, A.2    Sastry, S.3
  • 24
    • 0027208741 scopus 로고
    • Tumor rejection antigen gp96/grp94 is an ATPase: Implications for protein folding and antigen presentation
    • Li Z, Srivastava PK. Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation. EMBO J. 12(8), 3143-3151 (1993).
    • (1993) EMBO J , vol.12 , Issue.8 , pp. 3143-3151
    • Li, Z.1    Srivastava, P.K.2
  • 25
    • 0035823550 scopus 로고    scopus 로고
    • An endoplasmic reticulum protein implicated in chaperoning peptides to major histocompatibility of class I is an aminopeptidase
    • Menoret A, Li Z, Niswonger ML, Altmeyer A, Srivastava PK. An endoplasmic reticulum protein implicated in chaperoning peptides to major histocompatibility of class I is an aminopeptidase. J. Biol. Chem. 276(36), 33313-33318 (2001).
    • (2001) J. Biol. Chem , vol.276 , Issue.36 , pp. 33313-33318
    • Menoret, A.1    Li, Z.2    Niswonger, M.L.3    Altmeyer, A.4    Srivastava, P.K.5
  • 26
    • 19944425916 scopus 로고    scopus 로고
    • Heat shock proteins and their use as anticancer vaccines
    • Parmiani G, Testori A, Maio M et al. Heat shock proteins and their use as anticancer vaccines. Clin. Cancer Res. 10, 8142-8146 (2004).
    • (2004) Clin. Cancer Res , vol.10 , pp. 8142-8146
    • Parmiani, G.1    Testori, A.2    Maio, M.3
  • 27
    • 0036467388 scopus 로고    scopus 로고
    • Roles of heat-shock proteins in antigen presentation and cross-presentation
    • Li Z, Menoret A, Srivastava P. Roles of heat-shock proteins in antigen presentation and cross-presentation. Curr. Opin. Immunol. 14, 45-51 (2002).
    • (2002) Curr. Opin. Immunol , vol.14 , pp. 45-51
    • Li, Z.1    Menoret, A.2    Srivastava, P.3
  • 28
    • 1142299729 scopus 로고    scopus 로고
    • Purification of heat shock protein 70-associated tumor peptides and its anti-tumor immunity on hepatoma in mice
    • Chen DX, Su YR, Shao GZ, Qian ZC. Purification of heat shock protein 70-associated tumor peptides and its anti-tumor immunity on hepatoma in mice. World J. Gastroenterol. 10(3), 361-365 (2004).
    • (2004) World J. Gastroenterol , vol.10 , Issue.3 , pp. 361-365
    • Chen, D.X.1    Su, Y.R.2    Shao, G.Z.3    Qian, Z.C.4
  • 29
    • 12744269479 scopus 로고    scopus 로고
    • The messenger and the message: Gp96 (GRP94)-peptide interactions in cellular immunity
    • Nicchitta CV, Carrick DM, Baker-LePain JC. The messenger and the message: gp96 (GRP94)-peptide interactions in cellular immunity. Cell Stress Chaperones 9(4), 325-331(2004).
    • (2004) Cell Stress Chaperones , vol.9 , Issue.4 , pp. 325-331
    • Nicchitta, C.V.1    Carrick, D.M.2    Baker-LePain, J.C.3
  • 30
    • 0030775140 scopus 로고    scopus 로고
    • Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity
    • Blachere NE, Li Z, Chandawarkar RY et al. Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity. J. Exp. Med. 186(8), 1315-1322 (1997).
    • (1997) J. Exp. Med , vol.186 , Issue.8 , pp. 1315-1322
    • Blachere, N.E.1    Li, Z.2    Chandawarkar, R.Y.3
  • 31
    • 0034608387 scopus 로고    scopus 로고
    • Cross-presentation of Gp96-associated antigens on MHC class I molecules requires receptor-mediated endocytosis
    • Singh-Jasuja H, Toes REM, Spee P et al. Cross-presentation of Gp96-associated antigens on MHC class I molecules requires receptor-mediated endocytosis. J. Exp. Med. 191, 1965-1974 (2000).
    • (2000) J. Exp. Med , vol.191 , pp. 1965-1974
    • Singh-Jasuja, H.1    Toes, R.E.M.2    Spee, P.3
  • 32
    • 0344443767 scopus 로고    scopus 로고
    • Bacterial stimulation upregulates the surface expression of the stress protein gp96 on B cells in the frog Xenopus
    • Morales H, Muharemagic A, Gantress J, Cohen N, Robert J. Bacterial stimulation upregulates the surface expression of the stress protein gp96 on B cells in the frog Xenopus. Cell Stress Chaperones 8(3), 265-271 (2003).
    • (2003) Cell Stress Chaperones , vol.8 , Issue.3 , pp. 265-271
    • Morales, H.1    Muharemagic, A.2    Gantress, J.3    Cohen, N.4    Robert, J.5
  • 34
    • 22244467721 scopus 로고    scopus 로고
    • Differences in glycosylation patterns of heat shock protein, gp96: Implications for prostate cancer prevention
    • Suriano R, Ghosh SK, Ashok BT et al. Differences in glycosylation patterns of heat shock protein, gp96: implications for prostate cancer prevention. Cancer Res. 65, 6466-6475 (2005).
    • (2005) Cancer Res , vol.65 , pp. 6466-6475
    • Suriano, R.1    Ghosh, S.K.2    Ashok, B.T.3
  • 35
    • 0033520019 scopus 로고    scopus 로고
    • Activation of cytotoxic T cells in vitro by recombinant gp96 fusion proteins irrespective of the fused antigenic peptide sequence
    • More S, Breloer M, Fleischer B, Bonin A. Activation of cytotoxic T cells in vitro by recombinant gp96 fusion proteins irrespective of the fused antigenic peptide sequence. Immunol. Lett. 69(2), 275-282 (1999).
    • (1999) Immunol. Lett , vol.69 , Issue.2 , pp. 275-282
    • More, S.1    Breloer, M.2    Fleischer, B.3    Bonin, A.4
  • 37
    • 1942501656 scopus 로고    scopus 로고
    • Essential role of CD91 in re-presentation of gp96-chaperoned peptides
    • Binder RJ, Srivastava PK. Essential role of CD91 in re-presentation of gp96-chaperoned peptides. Proc. Natl Acad. Sci. USA 101(16), 6128-6133 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.16 , pp. 6128-6133
    • Binder, R.J.1    Srivastava, P.K.2
  • 38
    • 0038603179 scopus 로고    scopus 로고
    • The heat-shock protein receptor CD91 is up-regulated in monocytes of HIV-1-infected "true" long-term nonprogressors
    • Stebbing J, Gazzard B, Kim L et al. The heat-shock protein receptor CD91 is up-regulated in monocytes of HIV-1-infected "true" long-term nonprogressors. Blood 101(10), 4000-4004 (2003).
    • (2003) Blood , vol.101 , Issue.10 , pp. 4000-4004
    • Stebbing, J.1    Gazzard, B.2    Kim, L.3
  • 39
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70 and calreticulin
    • Basu S, Binder RJ, Ramalingam T, Srivastava PK. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70 and calreticulin. Immunity 14, 303-313 (2001).
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 40
    • 0035871711 scopus 로고    scopus 로고
    • 2-macroglobulin, an independent ligand for the heat shock protein receptor CD91
    • 2-macroglobulin, an independent ligand for the heat shock protein receptor CD91. J. Immunol. 166, 4968-4972 (2001).
    • (2001) J. Immunol , vol.166 , pp. 4968-4972
    • Binder, R.J.1    Karimeddini, D.2    Srivastava, P.K.3
  • 41
    • 0033839045 scopus 로고    scopus 로고
    • The heat shock protein Gp96 induces maturation of dendritic cells and down-regulation of its receptor
    • Singh-Jasuja H, Scherer HU, Hilf N et al. The heat shock protein Gp96 induces maturation of dendritic cells and down-regulation of its receptor. Eur. J. Immunol. 30, 2211-2215 (2000).
    • (2000) Eur. J. Immunol , vol.30 , pp. 2211-2215
    • Singh-Jasuja, H.1    Scherer, H.U.2    Hilf, N.3
  • 42
    • 0034526159 scopus 로고    scopus 로고
    • The heat shock protein Gp96- a receptor-targeted cross-priming carrier and activator of dendritic cells
    • Singh-Jasuja H, Hilf N, Scherer HU et al. The heat shock protein Gp96- a receptor-targeted cross-priming carrier and activator of dendritic cells. Cell Stress Chaperones 5, 462-470 (2001).
    • (2001) Cell Stress Chaperones , vol.5 , pp. 462-470
    • Singh-Jasuja, H.1    Hilf, N.2    Scherer, H.U.3
  • 43
    • 4744371115 scopus 로고    scopus 로고
    • The heat-shock protein receptors: Some answers and more questions
    • Binder RJ, Vatner R, Srivastava P. The heat-shock protein receptors: some answers and more questions. Tissue Antigens 64, 442-451 (2004).
    • (2004) Tissue Antigens , vol.64 , pp. 442-451
    • Binder, R.J.1    Vatner, R.2    Srivastava, P.3
  • 44
    • 24044532894 scopus 로고    scopus 로고
    • Testing the role of gp96 as peptide chaperone in antigen processing
    • Demine R, Walden P. Testing the role of gp96 as peptide chaperone in antigen processing. J. Biol. Chem. 280(18), 17573-17578 (2005).
    • (2005) J. Biol. Chem , vol.280 , Issue.18 , pp. 17573-17578
    • Demine, R.1    Walden, P.2
  • 45
    • 1542468771 scopus 로고    scopus 로고
    • Chaperokine-induced signal transduction pathways
    • Asea A. Chaperokine-induced signal transduction pathways. Exerc. Immunol. Rev. 9, 25-33 (2003).
    • (2003) Exerc. Immunol. Rev , vol.9 , pp. 25-33
    • Asea, A.1
  • 46
    • 33646336921 scopus 로고    scopus 로고
    • Stress proteins and initiation of immune response: Chaperokine activity of Hsp72
    • Asea A. Stress proteins and initiation of immune response: chaperokine activity of Hsp72. Exerc. Immunol. Rev. 11, 34-45 (2005).
    • (2005) Exerc. Immunol. Rev , vol.11 , pp. 34-45
    • Asea, A.1
  • 47
    • 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, Hilf N, Rechtsteiner G 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(32), 22545-22553 (2006).
    • (2006) J. Biol. Chem , vol.281 , Issue.32 , pp. 22545-22553
    • Warger, T.1    Hilf, N.2    Rechtsteiner, G.3
  • 48
    • 33646675316 scopus 로고    scopus 로고
    • Heat shock proteins as vaccine adjuvants in infections and cancer
    • Segal BH, Wang XY, Dennis CG et al. Heat shock proteins as vaccine adjuvants in infections and cancer. Drug Discov.Today 11(11/12), 534-540 (2006).
    • (2006) Drug Discov.Today , vol.11 , Issue.11-12 , pp. 534-540
    • Segal, B.H.1    Wang, X.Y.2    Dennis, C.G.3
  • 51
    • 35748934798 scopus 로고    scopus 로고
    • Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling
    • Bendz H, Ruhland SC, Pandya MJ et al. Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling. J. Biol. Chem. 282, 31688-31702 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 31688-31702
    • Bendz, H.1    Ruhland, S.C.2    Pandya, M.J.3
  • 52
    • 33947491607 scopus 로고    scopus 로고
    • Flagellin contamination of recombinant heat shock protein 70 is responsible for its activity on T cells
    • Ye Z, Gan YH. Flagellin contamination of recombinant heat shock protein 70 is responsible for its activity on T cells. J. Biol. Chem. 282(7), 4479-4484 (2007).
    • (2007) J. Biol. Chem , vol.282 , Issue.7 , pp. 4479-4484
    • Ye, Z.1    Gan, Y.H.2
  • 53
    • 1842854683 scopus 로고    scopus 로고
    • Immune modulation with high-dose heat shock protein Gp96: Therapy of murine autoimmune diabetes and encephalomyelitis
    • Chandawarkar RY, Wagh MS, Kovalchin JT, Srivastava P. Immune modulation with high-dose heat shock protein Gp96: therapy of murine autoimmune diabetes and encephalomyelitis. Int. Immunol. 16(4), 615-624 (2004).
    • (2004) Int. Immunol , vol.16 , Issue.4 , pp. 615-624
    • Chandawarkar, R.Y.1    Wagh, M.S.2    Kovalchin, J.T.3    Srivastava, P.4
  • 54
    • 33646369952 scopus 로고    scopus 로고
    • Immunostimulatory functions of membrane-bound and exported heat shock protein 70
    • Radons J, Multhoff G. Immunostimulatory functions of membrane-bound and exported heat shock protein 70. Exerc. Immunol. Rev. 11, 17-33 (2005).
    • (2005) Exerc. Immunol. Rev , vol.11 , pp. 17-33
    • Radons, J.1    Multhoff, G.2
  • 55
    • 33645959208 scopus 로고    scopus 로고
    • Heat shock proteins in immunity
    • Multhoff G. Heat shock proteins in immunity. Handb. Exp. Pharmacol. 172, 279-304 (2006).
    • (2006) Handb. Exp. Pharmacol , vol.172 , pp. 279-304
    • Multhoff, G.1
  • 56
    • 0037298742 scopus 로고    scopus 로고
    • Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94
    • Gross C, Hansch D, Gastpar R, Multhoff G. Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94. Biol. Chem. 384, 267-279 (2003).
    • (2003) Biol. Chem , vol.384 , pp. 267-279
    • Gross, C.1    Hansch, D.2    Gastpar, R.3    Multhoff, G.4
  • 57
    • 0142103373 scopus 로고    scopus 로고
    • Gross C, Koelch W, DeMaio A, Arispe N, Multhoff G. Cell surface-bound heat shock protein 70 (Hsp70) mediates perforin-independent apoptosis by specific binding and uptake of granzyme B. J. Biol. Chem. 278, 41173-41181 (2003).
    • Gross C, Koelch W, DeMaio A, Arispe N, Multhoff G. Cell surface-bound heat shock protein 70 (Hsp70) mediates perforin-independent apoptosis by specific binding and uptake of granzyme B. J. Biol. Chem. 278, 41173-41181 (2003).
  • 58
    • 0037087398 scopus 로고    scopus 로고
    • Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs
    • Panjwani NN, Popova L, Srivastava PK. Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs. J. Immunol. 168, 2997-3003 (2002).
    • (2002) J. Immunol , vol.168 , pp. 2997-3003
    • Panjwani, N.N.1    Popova, L.2    Srivastava, P.K.3
  • 59
    • 0141625683 scopus 로고    scopus 로고
    • Augmentation of DNA vaccine potency through secretory heat shock protein-mediated antigen targeting
    • Hauser H, Chen SY. Augmentation of DNA vaccine potency through secretory heat shock protein-mediated antigen targeting. Methods 31, 225-231 (2003).
    • (2003) Methods , vol.31 , pp. 225-231
    • Hauser, H.1    Chen, S.Y.2
  • 60
    • 0035077790 scopus 로고    scopus 로고
    • Enhancement of suicidal DNA vaccine potency by linking Mycobacterium tuberculosis heat shock protein 70 to an antigen
    • Hsu KF, Hung CF, Cheng WF et al. Enhancement of suicidal DNA vaccine potency by linking Mycobacterium tuberculosis heat shock protein 70 to an antigen. Gene Ther. 8, 376-383 (2001).
    • (2001) Gene Ther , vol.8 , pp. 376-383
    • Hsu, K.F.1    Hung, C.F.2    Cheng, W.F.3
  • 61
    • 0034652784 scopus 로고    scopus 로고
    • Enhancement of DNA vaccine potency by linkage of antigen gene to an HSP70 gene
    • Chen CH, Wang TL, Hung CF. Enhancement of DNA vaccine potency by linkage of antigen gene to an HSP70 gene. Cancer Res. 15, 1035-1042 (2000).
    • (2000) Cancer Res , vol.15 , pp. 1035-1042
    • Chen, C.H.1    Wang, T.L.2    Hung, C.F.3
  • 62
    • 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 NR, Wu HB, Wu TC, Boux LJ, Siegel MI, Mizzen LA. 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).
    • (2000) Clin. Exp. Immunol , vol.121 , pp. 216-225
    • Chu, N.R.1    Wu, H.B.2    Wu, T.C.3    Boux, L.J.4    Siegel, M.I.5    Mizzen, L.A.6
  • 63
    • 36348983898 scopus 로고    scopus 로고
    • DNA vaccine encoding heat shock protein 60 co-linked to HPV-16E6 and E7 tumor antigens generates more potent immunotherapeutic effects than respective E6 or E7 tumor antigens
    • Huang CY, Chen CA, Lee CN. DNA vaccine encoding heat shock protein 60 co-linked to HPV-16E6 and E7 tumor antigens generates more potent immunotherapeutic effects than respective E6 or E7 tumor antigens. Gynecol. Oncol. 107(3), 404-412 (2007).
    • (2007) Gynecol. Oncol , vol.107 , Issue.3 , pp. 404-412
    • Huang, C.Y.1    Chen, C.A.2    Lee, C.N.3
  • 64
    • 1842865717 scopus 로고    scopus 로고
    • Rapp UK, Kaufmann SHE. DNA vaccination with gp96-peptide fusion proteins induces protection against an intracellular bacterial pathogen. Int. Immunol.16 (4), 597-605 (2004). •• Reports that DNA vaccination with Gp96 linked to immunodominant peptide of Listeria monocytogenes produces strong epitope-specific IFN-γ and cytotoxic T-cell responses.
    • Rapp UK, Kaufmann SHE. DNA vaccination with gp96-peptide fusion proteins induces protection against an intracellular bacterial pathogen. Int. Immunol.16 (4), 597-605 (2004). •• Reports that DNA vaccination with Gp96 linked to immunodominant peptide of Listeria monocytogenes produces strong epitope-specific IFN-γ and cytotoxic T-cell responses.
  • 65
    • 2942571812 scopus 로고    scopus 로고
    • DNA vaccines expressing antigens with a stress protein-capturing domain display enhanced immunogenicity
    • Reimann J, Schirmbeck R. DNA vaccines expressing antigens with a stress protein-capturing domain display enhanced immunogenicity. Immunol. Rev. 199, 54-67 (2004).
    • (2004) Immunol. Rev , vol.199 , pp. 54-67
    • Reimann, J.1    Schirmbeck, R.2
  • 66
    • 37549066302 scopus 로고    scopus 로고
    • Generation and characterization of a preventive and therapeutic HPV DNA vaccine
    • Kim D, Gambhira R, Karanam B et al. Generation and characterization of a preventive and therapeutic HPV DNA vaccine. Vaccine 26(3), 351-360 (2008).
    • (2008) Vaccine , vol.26 , Issue.3 , pp. 351-360
    • Kim, D.1    Gambhira, R.2    Karanam, B.3
  • 67
    • 0033566165 scopus 로고    scopus 로고
    • Therapy of tuberculosis in mice by DNA vaccination
    • Lowrie DB, Tascon RE, Bonato VL et al. Therapy of tuberculosis in mice by DNA vaccination. Nature 400, 269-271 (1999).
    • (1999) Nature , vol.400 , pp. 269-271
    • Lowrie, D.B.1    Tascon, R.E.2    Bonato, V.L.3
  • 68
    • 11144246547 scopus 로고    scopus 로고
    • Enhancement of DNA vaccine potency by linkage a Plasmodium falciparum malaria antigen gene fused with a fragment of HSP70 gene
    • Qazi KR, Wikman M, Vasconcelos NM, Berzins K, Stahl S, Fernandez C. Enhancement of DNA vaccine potency by linkage a Plasmodium falciparum malaria antigen gene fused with a fragment of HSP70 gene. Vaccine 23(9), 1114-1125 (2005).
    • (2005) Vaccine , vol.23 , Issue.9 , pp. 1114-1125
    • Qazi, K.R.1    Wikman, M.2    Vasconcelos, N.M.3    Berzins, K.4    Stahl, S.5    Fernandez, C.6
  • 69
    • 44749083900 scopus 로고    scopus 로고
    • Enhanced immunogenicity of HPV16E7 accompanied by Gp96 as an adjuvant in two vaccination strategies
    • Indicates the potential value of DNA vaccination using codelivery of E7 and Gp96. It reveals that the combined DNA vaccine induces an E7-specific IFN-γ response, ••
    • Bolhassani A, Zahedifard F, Taghikhani M, Rafati S. Enhanced immunogenicity of HPV16E7 accompanied by Gp96 as an adjuvant in two vaccination strategies. Vaccine 26, 3362-3370 (2008). •• Indicates the potential value of DNA vaccination using codelivery of E7 and Gp96. It reveals that the combined DNA vaccine induces an E7-specific IFN-γ response.
    • (2008) Vaccine , vol.26 , pp. 3362-3370
    • Bolhassani, A.1    Zahedifard, F.2    Taghikhani, M.3    Rafati, S.4
  • 70
    • 34247352104 scopus 로고    scopus 로고
    • Rafati S, Gholami E, Hassani N et al. Leishmania major heat shock protein 70 (HSP70) is not protective in murine models of cutaneous leishmaniasis and stimulates strong humoral responses in cutaneous and visceral leishmaniasis patients. Vaccine 25, 4159-4169 (2007). •• Shows the roles of Leishmania major HSP70 and its fragments in stimulation of immune responses in human and animal models. Describes the potential value of anti-Leishmania antibodies to monitor the levels of host immune responses to Leishmania infection, but with a limited value of HSP70-based vaccine for the control of cutaneous leishmaniasis in mouse models.
    • Rafati S, Gholami E, Hassani N et al. Leishmania major heat shock protein 70 (HSP70) is not protective in murine models of cutaneous leishmaniasis and stimulates strong humoral responses in cutaneous and visceral leishmaniasis patients. Vaccine 25, 4159-4169 (2007). •• Shows the roles of Leishmania major HSP70 and its fragments in stimulation of immune responses in human and animal models. Describes the potential value of anti-Leishmania antibodies to monitor the levels of host immune responses to Leishmania infection, but with a limited value of HSP70-based vaccine for the control of cutaneous leishmaniasis in mouse models.
  • 71
    • 0033759568 scopus 로고    scopus 로고
    • Larreta R, Soto M, Alonso C, Requena JM. Leishmania infantum: gene cloning of the GRP94 homologue, its expression as recombinant protein and analysis of antigenicity. Exp. Parasitol. 96(2), 108-118 (2000). •• Demonstrates the immunogenic and antigenic properties of the Leishmania infantum GRP94 in infected dogs' sera. Shows that this protein could be used for diagnostic purposes. Also, this protein is a potential candidate for studies of protective immunogenicity.
    • Larreta R, Soto M, Alonso C, Requena JM. Leishmania infantum: gene cloning of the GRP94 homologue, its expression as recombinant protein and analysis of antigenicity. Exp. Parasitol. 96(2), 108-118 (2000). •• Demonstrates the immunogenic and antigenic properties of the Leishmania infantum GRP94 in infected dogs' sera. Shows that this protein could be used for diagnostic purposes. Also, this protein is a potential candidate for studies of protective immunogenicity.
  • 72
    • 33745271556 scopus 로고    scopus 로고
    • The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells
    • Biswas C, Sriram U, Ciric B, Ostrovsky O, Gallucci S, Argon Y. The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells. Int. Immunol. 18(7), 1147-1157 (2006).
    • (2006) Int. Immunol , vol.18 , Issue.7 , pp. 1147-1157
    • Biswas, C.1    Sriram, U.2    Ciric, B.3    Ostrovsky, O.4    Gallucci, S.5    Argon, Y.6
  • 73
    • 44749093899 scopus 로고    scopus 로고
    • Host-derived adjuvants
    • Kaufmann SHE Ed, Weinheim, Germany
    • Hilf N, Radsak M, Schild H. Host-derived adjuvants. In: Novel vaccination strategies. Kaufmann SHE (Ed.). Weinheim, Germany, 129-145 (2004).
    • (2004) Novel vaccination strategies , pp. 129-145
    • Hilf, N.1    Radsak, M.2    Schild, H.3
  • 74
    • 34250331531 scopus 로고    scopus 로고
    • The perfect mix: Recent progress in adjuvant research
    • Guy B. The perfect mix: recent progress in adjuvant research. Nat. Rev. Microbiol. 5, 505-517 (2007).
    • (2007) Nat. Rev. Microbiol , vol.5 , pp. 505-517
    • Guy, B.1
  • 75
    • 10744224734 scopus 로고    scopus 로고
    • CpG oligodeoxynucleotide and montanide ISA51 adjuvant combination enhanced the protective efficacy of a subunit malaria vaccine
    • Kumar S, Jones TR, Oakley MS et al. CpG oligodeoxynucleotide and montanide ISA51 adjuvant combination enhanced the protective efficacy of a subunit malaria vaccine. Infect. Immun. 72(2), 949-957 (2004).
    • (2004) Infect. Immun , vol.72 , Issue.2 , pp. 949-957
    • Kumar, S.1    Jones, T.R.2    Oakley, M.S.3
  • 76
    • 0141514408 scopus 로고    scopus 로고
    • DNA vaccine strategies: Candidates for immune modulation and immunization regimens
    • Doria-Rose NA, Haigwood NL. DNA vaccine strategies: candidates for immune modulation and immunization regimens. Methods 31, 207-216 (2003).
    • (2003) Methods , vol.31 , pp. 207-216
    • Doria-Rose, N.A.1    Haigwood, N.L.2
  • 77
    • 2942748077 scopus 로고    scopus 로고
    • Secretory heat-shock protein as a dendritic cell-targeting molecule: A new strategy to enhance the potency of genetic vaccines
    • Hauser H, Shen L, Gu QL, Krueger S, Chen SY. Secretory heat-shock protein as a dendritic cell-targeting molecule: a new strategy to enhance the potency of genetic vaccines. Gene Ther. 11(11), 924-932 (2004).
    • (2004) Gene Ther , vol.11 , Issue.11 , pp. 924-932
    • Hauser, H.1    Shen, L.2    Gu, Q.L.3    Krueger, S.4    Chen, S.Y.5
  • 78
    • 0033382112 scopus 로고    scopus 로고
    • Immunostimulatory properties of the Leishmania infantum heat shock proteins HSP70 and HSP83
    • Rico AI, Sergio OA, Alonso C, Requena JM. Immunostimulatory properties of the Leishmania infantum heat shock proteins HSP70 and HSP83. Mol. Immunol. 36, 1131-1139 (1999).
    • (1999) Mol. Immunol , vol.36 , pp. 1131-1139
    • Rico, A.I.1    Sergio, O.A.2    Alonso, C.3    Requena, J.M.4
  • 79
    • 0031964659 scopus 로고    scopus 로고
    • Characterization of the immunostimulatory property of L. infantum HSP70 by fusion to the E. coli MBP in normal and nu/nu BALB/c mice
    • Rico AI, Del Real G, Soto M et al. Characterization of the immunostimulatory property of L. infantum HSP70 by fusion to the E. coli MBP in normal and nu/nu BALB/c mice. Infect. Immun. 66(1), 347-352 (1998).
    • (1998) Infect. Immun , vol.66 , Issue.1 , pp. 347-352
    • Rico, A.I.1    Del Real, G.2    Soto, M.3
  • 80
    • 0028980575 scopus 로고
    • Immune responses of leishmaniasis patients to heat shock proteins of Leishmania species and humans
    • Skeiky YAW, Benson DR, Guderian JA et al. Immune responses of leishmaniasis patients to heat shock proteins of Leishmania species and humans. Infection 63, 4105-14 (1995).
    • (1995) Infection , vol.63 , pp. 4105-4114
    • Skeiky, Y.A.W.1    Benson, D.R.2    Guderian, J.A.3
  • 81
    • 0030224682 scopus 로고    scopus 로고
    • Identification of the C-terminal region of 70 kDa heat shock protein from Leishmania (Viannia) braziliensis as a target for the human immune response
    • Amorim AG, Cardoso de Almeida ML. Identification of the C-terminal region of 70 kDa heat shock protein from Leishmania (Viannia) braziliensis as a target for the human immune response. Cell Stress Chaperones 1(3), 177-187 (1996).
    • (1996) Cell Stress Chaperones , vol.1 , Issue.3 , pp. 177-187
    • Amorim, A.G.1    Cardoso de Almeida, M.L.2
  • 82
    • 0026769293 scopus 로고
    • Mapping of visceral leishmaniasis-specific immunodominant B-cell epitope of Leishmania donovani HSP70
    • Wallace GR, Ball AE, MacFarlane J, Safi SH, Miles MA, Kelly JM. Mapping of visceral leishmaniasis-specific immunodominant B-cell epitope of Leishmania donovani HSP70. Infect Immun. 60, 2688-2693 (1992).
    • (1992) Infect Immun , vol.60 , pp. 2688-2693
    • Wallace, G.R.1    Ball, A.E.2    MacFarlane, J.3    Safi, S.H.4    Miles, M.A.5    Kelly, J.M.6
  • 83
    • 0033128314 scopus 로고    scopus 로고
    • T cell response of asymptomatic Leishmania chagasi infected subjects to recombinant Leishmania antigens
    • Costa SR, D'Oliveira A Jr, Bacellar O, Carvalho EM. T cell response of asymptomatic Leishmania chagasi infected subjects to recombinant Leishmania antigens. Mem. Inst. Oswaldo Cruz. 94(3), 367-370 (1999).
    • (1999) Mem. Inst. Oswaldo Cruz , vol.94 , Issue.3 , pp. 367-370
    • Costa, S.R.1    D'Oliveira Jr, A.2    Bacellar, O.3    Carvalho, E.M.4
  • 84
    • 34247340099 scopus 로고    scopus 로고
    • Identification of sero-specific epitope of recombinant heat shock protein (HSP70) of Leishmania donovani
    • Arora SK, Kaur D, Sehgal S, Datta U. Identification of sero-specific epitope of recombinant heat shock protein (HSP70) of Leishmania donovani. J. Parasitic Dis. 24(1), 21-26 (2000).
    • (2000) J. Parasitic Dis , vol.24 , Issue.1 , pp. 21-26
    • Arora, S.K.1    Kaur, D.2    Sehgal, S.3    Datta, U.4
  • 85
    • 0032190655 scopus 로고    scopus 로고
    • Analysis of the antigenic properties of the L. infantum HSP70: Design of synthetic peptides for specific serodiagnosis of human leishmaniasis
    • Quijada L, Requena JM, Soto M, Alonso C. Analysis of the antigenic properties of the L. infantum HSP70: design of synthetic peptides for specific serodiagnosis of human leishmaniasis. Immunol. Lett. 63, 169-174 (1998).
    • (1998) Immunol. Lett , vol.63 , pp. 169-174
    • Quijada, L.1    Requena, J.M.2    Soto, M.3    Alonso, C.4
  • 86
    • 1342331442 scopus 로고    scopus 로고
    • Human papillomavirus vaccine as a new way of preventing cervical cancer: A dream or the future?
    • Mandic A, Vujkov T. Human papillomavirus vaccine as a new way of preventing cervical cancer: a dream or the future? Ann. Oncol. 15, 197-200 (2004).
    • (2004) Ann. Oncol , vol.15 , pp. 197-200
    • Mandic, A.1    Vujkov, T.2
  • 87
    • 5144225454 scopus 로고    scopus 로고
    • Therapeutic cancer vaccines: Using unique antigens
    • Lewis JJ. Therapeutic cancer vaccines: using unique antigens. Proc. Natl Acad. Sci. USA 101 (2), 14653-14656 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.2 , pp. 14653-14656
    • Lewis, J.J.1
  • 88
    • 30344457591 scopus 로고    scopus 로고
    • Prophylactic, therapeutic and anti-metastatic effects of an HPV16mE6δ/mE7/TBhsp70δ fusion protein vaccine in an animal model
    • Qian X, Lu Y, Liu Q, Chen K, Zhao Q, Song J. Prophylactic, therapeutic and anti-metastatic effects of an HPV16mE6δ/mE7/TBhsp70δ fusion protein vaccine in an animal model. Immunol Lett. 102(2), 191-201 (2006).
    • (2006) Immunol Lett , vol.102 , Issue.2 , pp. 191-201
    • Qian, X.1    Lu, Y.2    Liu, Q.3    Chen, K.4    Zhao, Q.5    Song, J.6
  • 89
    • 18944376330 scopus 로고    scopus 로고
    • Characterization of DNA vaccines encoding the domains of calreticulin for their ability to elicit tumor-specific immunity and antiangiogenesis
    • Cheng WF, Hung CF, Chen CA et al. Characterization of DNA vaccines encoding the domains of calreticulin for their ability to elicit tumor-specific immunity and antiangiogenesis. Vaccine 23(29), 3864-3874 (2005).
    • (2005) Vaccine , vol.23 , Issue.29 , pp. 3864-3874
    • Cheng, W.F.1    Hung, C.F.2    Chen, C.A.3
  • 90
    • 39249084560 scopus 로고    scopus 로고
    • Liu B, Ye D, Song X et al. A novel therapeutic fusion protein vaccine by two different families of heat shock proteins linked with HPV16 E7 generates potent anti-tumor immunity and anti-angiogenesis. Vaccine 26, 1387-1396 (2008). •• Shows that the structural domains of HSPs are important for generating effective anti-tumor immunity. The authors point out the therapeutic potential of the recombinant NT-CRT/E7/CT-HSP70 fusion protein for enhancing the potency of the HPV16 E7 therapeutic vaccine.
    • Liu B, Ye D, Song X et al. A novel therapeutic fusion protein vaccine by two different families of heat shock proteins linked with HPV16 E7 generates potent anti-tumor immunity and anti-angiogenesis. Vaccine 26, 1387-1396 (2008). •• Shows that the structural domains of HSPs are important for generating effective anti-tumor immunity. The authors point out the therapeutic potential of the recombinant NT-CRT/E7/CT-HSP70 fusion protein for enhancing the potency of the HPV16 E7 therapeutic vaccine.
  • 91
    • 0037009446 scopus 로고    scopus 로고
    • Leishmania LPG3 encodes a GRP94 homolog required for phosphoglycan synthesis implicated in parasite virulence but not viability
    • Descoteaux A, Avila HA, Zhang K, Turco SJ, Beverley SM. Leishmania LPG3 encodes a GRP94 homolog required for phosphoglycan synthesis implicated in parasite virulence but not viability. EMBO J. 21(17), 4458-4469 (2002).
    • (2002) EMBO J , vol.21 , Issue.17 , pp. 4458-4469
    • Descoteaux, A.1    Avila, H.A.2    Zhang, K.3    Turco, S.J.4    Beverley, S.M.5
  • 92
    • 0037843480 scopus 로고    scopus 로고
    • Targeted immunotherapy using reconstituted chaperone complexes of heat shock protein 110 and melanoma-associated antigen gp100
    • Wang XY, Chen X, Manjili MH, Repasky E, Henderson R, Subjeck JR. Targeted immunotherapy using reconstituted chaperone complexes of heat shock protein 110 and melanoma-associated antigen gp100. Cancer Res. 63, 2553-2560 (2003).
    • (2003) Cancer Res , vol.63 , pp. 2553-2560
    • Wang, X.Y.1    Chen, X.2    Manjili, M.H.3    Repasky, E.4    Henderson, R.5    Subjeck, J.R.6
  • 93
    • 32344436447 scopus 로고    scopus 로고
    • Chaperone-related immune dysfunction: An emergent property of distorted chaperone networks
    • Nardai G, Vegh E, Prohaszka Z, Csermely P. Chaperone-related immune dysfunction: an emergent property of distorted chaperone networks. Trends Immunol. 27(2), 75-79 (2006).
    • (2006) Trends Immunol , vol.27 , Issue.2 , pp. 75-79
    • Nardai, G.1    Vegh, E.2    Prohaszka, Z.3    Csermely, P.4
  • 94
    • 0038737428 scopus 로고    scopus 로고
    • Role of heat shock proteins in protection from and pathogenesis of infectious diseases
    • Zugel U, Kaufmann SHE. Role of heat shock proteins in protection from and pathogenesis of infectious diseases. Clin. Microbiol. Rev. 12(1), 19-39 (1999).
    • (1999) Clin. Microbiol. Rev , vol.12 , Issue.1 , pp. 19-39
    • Zugel, U.1    Kaufmann, S.H.E.2
  • 95
    • 0026444210 scopus 로고
    • Are heat shock proteins involved in autoimmunity?
    • Gaston JSH. Are heat shock proteins involved in autoimmunity? Int. J. Clin. Lab. Res. 22(1-4), 90-94 (1992).
    • (1992) Int. J. Clin. Lab. Res , vol.22 , Issue.1-4 , pp. 90-94
    • Gaston, J.S.H.1


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