S. Lindquist and E. A. Craig, “The heat-shock proteins,” Annual Review of Genetics, vol. 22, pp. 631–677, 1988.
[2]
P. Srivastava, “Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses,” Annual Review of Immunology, vol. 20, pp. 395–425, 2002.
[3]
R. Rajaiah and K. D. Moudgil, “Heat-shock proteins can promote as well as regulate autoimmunity,” Autoimmunity Reviews, vol. 8, no. 5, pp. 388–393, 2009.
[4]
H. H. Kampinga, J. Hageman, M. J. Vos et al., “Guidelines for the nomenclature of the human heat shock proteins,” Cell Stress and Chaperones, vol. 14, no. 1, pp. 105–111, 2009.
[5]
Y. Shoenfeld, D. Harats, and J. George, “Heat shock protein 60/65, β2-glycoprotein I and oxidized LDL as players in murine atherosclerosis,” Journal of Autoimmunity, vol. 15, no. 2, pp. 199–202, 2000.
[6]
B. De Paepe and J. L. De Bleecker, “The nonnecrotic invaded muscle fibers of polymyositis and sporadic inclusion body myositis: on the interplay of chemokines and stress proteins,” Neuroscience Letters, vol. 535, pp. 18–23, 2013.
[7]
F. Geraci, G. Turturici, and G. Sconzo, “Hsp70 and its molecular role in nervous system diseases,” Biochemistry Research International, vol. 2011, Article ID 618127, 18 pages, 2011.
[8]
D. Harats, N. Yacov, B. Gilburd, Y. Shoenfeld, and J. George, “Oral tolerance with heat shock protein 65 attenuates Mycobacterium tuberculosis-induced and high-fat-diet-driven atherosclerotic lesions,” Journal of the American College of Cardiology, vol. 40, no. 7, pp. 1333–1338, 2002.
[9]
M. J. van Herwijnen, L. Wieten, R. van der Zee, et al., “Regulatory T cells that recognize a ubiquitous stress-inducible self-antigen are long-lived suppressors of autoimmune arthritis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 35, pp. 14134–14139, 2012.
[10]
A. Motta, C. Schmitz, L. Rodrigues et al., “Mycobacterium tuberculosis heat-shock protein 70 impairs maturation of dendritic cells from bone marrow precursors, induces interleukin-10 production and inhibits T-cell proliferation in vitro,” Immunology, vol. 121, no. 4, pp. 462–472, 2007.
[11]
A. M. Shields, S. J. Thompson, G. S. Panayi, and V. M. Corrigall, “Pro-resolution immunological networks: binding immunoglobulin protein and other resolution-associated molecular patterns,” Rheumatology, vol. 51, no. 5, pp. 780–788, 2012.
[12]
I. R. Cohen, “The cognitive paradigm and the immunological homunculus,” Immunology Today, vol. 13, no. 12, pp. 490–494, 1992.
[13]
S. M. Anderton, R. van der Zee, B. Prakken, A. Noordzij, and W. van Eden, “Activation of T cells recognizing self 60-kD heat shock protein can protect against experimental arthritis,” Journal of Experimental Medicine, vol. 181, no. 3, pp. 943–952, 1995.
[14]
K. D. Moudgil, T. T. Chang, H. Eradat et al., “Diversification of T cell responses to carboxy-terminal determinants within the 65-kD heat-shock protein is involved in regulation of autoimmune arthritis,” Journal of Experimental Medicine, vol. 185, no. 7, pp. 1307–1316, 1997.
[15]
S. K. Calderwood and D. R. Ciocca, “Heat shock proteins: stress proteins with Janus-like properties in cancer,” International Journal of Hyperthermia, vol. 24, no. 1, pp. 31–39, 2008.
[16]
R. J. Binder and P. K. Srivastava, “Peptides chaperoned by heat-shock proteins are a necessary and sufficient source of antigen in the cross-priming of CD8+ T cells,” Nature Immunology, vol. 6, no. 6, pp. 593–599, 2005.
[17]
V. Coelho, F. Broere, R. J. Binder, Y. Shoenfeld, and K. D. Moudgil, “Heat-shock proteins: inflammatory versus regulatory attributes,” Cell Stress and Chaperones, vol. 13, no. 2, pp. 119–125, 2008.
[18]
L. K. Slack, M. Muthana, K. Hopkinson et al., “Administration of the stress protein gp96 prolongs rat cardiac allograft survival, modifies rejection-associated inflammatory events, and induces a state of peripheral T-cell hyporesponsiveness,” Cell Stress and Chaperones, vol. 12, no. 1, pp. 71–82, 2007.
[19]
V. A. L. Huurman, P. E. van der Meide, G. Duinkerken et al., “Immunological efficacy of heat shock protein 60 peptide DiaPep277 therapy in clinical type I diabetes,” Clinical and Experimental Immunology, vol. 152, no. 3, pp. 488–497, 2008.
[20]
E. C. Koffeman, M. Genovese, D. Amox et al., “Epitope-specific immunotherapy of rheumatoid arthritis: clinical responsiveness occurs with immune deviation and relies on the expression of a cluster of molecules associated with T cell tolerance in a double-blind, placebo-controlled, pilot phase II trial,” Arthritis and Rheumatism, vol. 60, no. 11, pp. 3207–3216, 2009.
