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Volumn 1, Issue 12, 2002, Pages 1147-1151

Overcoming immune tolerance to cancer by heat shock protein vaccines

Author keywords

[No Author keywords available]

Indexed keywords

CANCER VACCINE; HEAT SHOCK PROTEIN;

EID: 0037670279     PISSN: 15357163     EISSN: 15388514     Source Type: Journal    
DOI: None     Document Type: Short Survey
Times cited : (44)

References (73)
  • 1
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist, S. The heat-shock response. Annu. Rev. Biochem., 55: 1151-1191, 1986. (Pubitemid 16070798)
    • (1986) Annual Review of Biochemistry , vol.VOL. 55 , pp. 1151-1191
    • Lindquist, S.1
  • 2
    • 0033057848 scopus 로고    scopus 로고
    • Heat-shock proteins, molecular chaperones, and the stress response: Evolutionary and ecological physiology
    • DOI 10.1146/annurev.physiol.61.1.243
    • Feder, M. E., and Hofmann, G. E. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu. Rev. Physiol., 61: 243-282, 1999. (Pubitemid 29143171)
    • (1999) Annual Review of Physiology , vol.61 , pp. 243-282
    • Feder, M.E.1    Hofmann, G.E.2
  • 3
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection
    • Morimoto, R. I., and Santoro, M. G. Stress-inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection. Nat. Biotechnol., 16: 833-838, 1998. (Pubitemid 28405852)
    • (1998) Nature Biotechnology , vol.16 , Issue.9 , pp. 833-838
    • Morimoto, R.I.1    Gabriella, S.M.2
  • 4
    • 0031252213 scopus 로고    scopus 로고
    • Priming of T cells by heat shock protein-peptide complexes as the basis of tumor vaccines
    • DOI 10.1006/smim.1997.0087
    • Li, Z. Priming of T cells by heat shock protein-peptide complexes as the basis of tumor vaccines. Semin. Immunol., 9: 315-322, 1997. (Pubitemid 28077729)
    • (1997) Seminars in Immunology , vol.9 , Issue.5 , pp. 315-322
    • Li, Z.1
  • 5
    • 0035238398 scopus 로고    scopus 로고
    • The roles of heat shock proteins in tumor immunity
    • Li, Z. The roles of heat shock proteins in tumor immunity. Cancer Chemother. Biol. Response Modif., 19: 371-383, 2001.
    • (2001) Cancer Chemother. Biol. Response Modif. , vol.19 , pp. 371-383
    • Li, Z.1
  • 6
    • 0032101221 scopus 로고    scopus 로고
    • Heat shock proteins come of age: Primitive functions acquire new roles in an adaptive world
    • DOI 10.1016/S1074-7613(00)80570-1
    • Srivastava, P. K., Menoret, A., Basu, S., Binder, R. J., and McQuade, K. L. Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world. Immunity, 8: 657-665, 1998. (Pubitemid 28294512)
    • (1998) Immunity , vol.8 , Issue.6 , pp. 657-665
    • Srivastava, P.K.1    Menoret, A.2    Basu, S.3    Binder, R.J.4    McQuade, K.L.5
  • 7
    • 0021339151 scopus 로고
    • The serologically unique cell surface antigen of Zajdela Ascitic Hepatoma is also its tumor-associated transplantation antigen
    • DOI 10.1002/ijc.2910330321
    • Srivastava, P. K., and Das, M. R. The serologically unique cell surface antigen of Zajdela ascitic hepatoma is also its tumor-associated transplantation antigen. Int. J. Cancer, 33: 417-422, 1984. (Pubitemid 14159040)
    • (1984) International Journal of Cancer , vol.33 , Issue.3 , pp. 417-422
    • Srivastava, P.K.1    Das, M.R.2
  • 9
    • 0027260585 scopus 로고
    • Heat shock protein 70-associated peptides elicit specific cancer immunity
    • Udono, H., and Srivastava, P. K. Heat shock protein 70-associated peptides elicit specific cancer immunity. J. Exp. Med., 178: 1391-1396, 1993. (Pubitemid 23277370)
    • (1993) Journal of Experimental Medicine , vol.178 , Issue.4 , pp. 1391-1396
    • Udono, H.1    Srivastava, P.K.2
  • 11
    • 0028301079 scopus 로고
    • Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90, and hsp70
    • Udono, H., and Srivastava, P. K. Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90, and hsp70. J. Immunol., 152: 5398-5403, 1994. (Pubitemid 24152988)
    • (1994) Journal of Immunology , vol.152 , Issue.11 , pp. 5398-5403
    • Udono, H.1    Srivastava, P.K.2
  • 12
    • 0033103513 scopus 로고    scopus 로고
    • Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity
    • DOI 10.1084/jem.189.5.797
    • Basu, S., and Srivastava, P. K. Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity. J. Exp. Med., 189: 797-802, 1999. (Pubitemid 29189684)
    • (1999) Journal of Experimental Medicine , vol.189 , Issue.5 , pp. 797-802
    • Basu, S.1    Srivastava, P.K.2
  • 13
    • 0033152788 scopus 로고    scopus 로고
    • Calreticulin displays in vivo peptide-binding activity and can elicit CTL responses against bound peptides
    • Nair, S., Wearsch, P. A., Mitchell, D. A., Wassenberg, J. J., Gilboa, E., and Nicchitta, C. V. Calreticulin displays in vivo peptide-binding activity and can elicit CTL responses against bound peptides. J. Immunol., 162: 6426-6432, 1999. (Pubitemid 29309363)
    • (1999) Journal of Immunology , vol.162 , Issue.11 , pp. 6426-6432
    • Nair, S.1    Wearsch, P.A.2    Mitchell, D.A.3    Wassenberg, J.J.4    Gilboa, E.5    Nicchitta, C.V.6
  • 14
    • 0035167866 scopus 로고    scopus 로고
    • Characterization of heat shock protein 110 and glucose-regulated protein 170 as cancer vaccines and the effect of fever-range hyperthermia on vaccine activity
    • Wang, X. Y., Kazim, L., Repasky, E. A., and Subjeck, J. R. Characterization of heat shock protein 110 and glucose-regulated protein 170 as cancer vaccines and the effect of fever-range hyperthermia on vaccine activity. J. Immunol., 166: 490-497, 2001. (Pubitemid 32038468)
    • (2001) Journal of Immunology , vol.166 , Issue.1 , pp. 490-497
    • Wang, X.-Y.1    Kazim, L.2    Repasky, E.A.3    Subjeck, J.R.4
  • 17
    • 0032473485 scopus 로고    scopus 로고
    • Immunization with a lymphocytic choriomeningitis virus peptide mixed with heat shock protein 70 results in protective antiviral immunity and specific cytotoxic T lymphocytes
    • DOI 10.1084/jem.187.5.685
    • Ciupitu, A. M., Petersson, M., O'Donnell, C. L., Williams, K., Jindal, S., Kiessling, R., and Welsh, R. M. Immunization with a lymphocytic choriomeningitis virus peptide mixed with heat shock protein 70 results in protective antiviral immunity and specific cytotoxic T lymphocytes. J. Exp. Med., 187: 685-691, 1998. (Pubitemid 28115184)
    • (1998) Journal of Experimental Medicine , vol.187 , Issue.5 , pp. 685-691
    • Ciupitu, A.-M.T.1    Petersson, M.2    O'Donnell, C.L.3    Williams, K.4    Jindal, S.5    Kiessling, R.6    Welsh, R.M.7
  • 18
    • 0036133062 scopus 로고    scopus 로고
    • Immunization with chaperone-peptide complex induces low-avidity cytotoxic T lymphocytes providing transient protection against herpes simplex virus infection
    • DOI 10.1128/JVI.76.1.136-141.2002
    • Kumaraguru, U., Gierynska, M., Norman, S., Bruce, B. D., and Rouse, B. T. Immunization with chaperone-peptide complex induces low-avidity cytotoxic T lymphocytes providing transient protection against herpes simplex virus infection. J. Virol., 76: 136-141, 2002. (Pubitemid 33138999)
    • (2002) Journal of Virology , vol.76 , Issue.1 , pp. 136-141
    • Kumaraguru, U.1    Gierynska, M.2    Norman, S.3    Bruce, B.D.4    Rouse, B.T.5
  • 19
    • 0035007320 scopus 로고    scopus 로고
    • gp96-peptide vaccination of mice against intracellular bacteria
    • DOI 10.1128/IAI.69.6.4164-4167.2001
    • Zugel, U., Sponaas, A. M., Neckermann, J., Schoel, B., and Kaufmann, S. H. gp96-peptide vaccination of mice against intracellular bacteria. Infect. Immunol., 69: 4164-4167, 2001. (Pubitemid 32493345)
    • (2001) Infection and Immunity , vol.69 , Issue.6 , pp. 4164-4167
    • Zugel, U.1    Sponaas, A.-M.2    Neckermann, J.3    Schoel, B.4    Kaufmann, S.H.E.5
  • 21
    • 0035855872 scopus 로고    scopus 로고
    • Rae1 and H60 ligands of the NKG2D receptor stimulate tumour immunity
    • DOI 10.1038/35093109
    • Diefenbach, A., Jensen, E. R., Jamieson, A. M., and Raulet, D. H. Rae1 and H60 ligands of the NKG2D receptor stimulate tumour immunity. Nature (Lond.), 413: 165-171, 2001. (Pubitemid 32867877)
    • (2001) Nature , vol.413 , Issue.6852 , pp. 165-171
    • Diefenbach, A.1    Jensen, E.R.2    Jamieson, A.M.3    Raulet, D.H.4
  • 22
    • 0036143496 scopus 로고    scopus 로고
    • Induction of tumor-specific T cell memory by NK cell-mediated tumor rejection
    • DOI 10.1038/ni746
    • Kelly, J. M., Darcy, P. K., Markby, J. L., Godfrey, D. I., Takeda, K., Yagita, H., and Smyth, M. J. Induction of tumor-specific T cell memory by NK cell-mediated tumor rejection. Nat. Immunol., 3: 83-90, 2002. (Pubitemid 34065622)
    • (2002) Nature Immunology , vol.3 , Issue.1 , pp. 83-90
    • Kelly, J.M.1    Darcy, P.K.2    Markby, J.L.3    Godfrey, D.I.4    Takeda, K.5    Yagita, H.6    Smyth, M.J.7
  • 23
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • DOI 10.1038/32588
    • Banchereau, J., and Steinman, R. M. Dendritic cells and the control of immunity. Nature (Lond.), 392: 245-252, 1998. (Pubitemid 28155090)
    • (1998) Nature , vol.392 , Issue.6673 , pp. 245-252
    • Banchereau, J.1    Steinman, R.M.2
  • 24
    • 0028201732 scopus 로고
    • Tolerance, danger, and the extended family
    • Matzinger, P. Tolerance, danger, and the extended family. Annu. Rev. Immunol., 12: 991-1045, 1994. (Pubitemid 24140436)
    • (1994) Annual Review of Immunology , vol.12 , pp. 991-1045
    • Matzinger, P.1
  • 25
    • 0036512171 scopus 로고    scopus 로고
    • Roles of heat-shock proteins in innate and adaptive immunity
    • Srivastava, P. K. Roles of heat-shock proteins in innate and adaptive immunity. Nat. Rev. Immunol., 2: 185-194, 2002.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 185-194
    • Srivastava, P.K.1
  • 26
    • 0036512501 scopus 로고    scopus 로고
    • An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in immune response
    • Li, Z., Dai, J., Zheng, H., Liu, B., and Caudill, M. An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in immune response. Front. Biosci., 7: 731-751, 2002.
    • (2002) Front. Biosci. , vol.7 , pp. 731-751
    • Li, Z.1    Dai, J.2    Zheng, H.3    Liu, B.4    Caudill, M.5
  • 27
    • 0034252620 scopus 로고    scopus 로고
    • CD91: A receptor for heat shock protein gp96
    • Binder, R. J., Han, D. K., and Srivastava, P. K. CD91: a receptor for heat shock protein gp96. Nat. Immunol., 1: 151-155, 2000.
    • (2000) Nat. Immunol. , vol.1 , pp. 151-155
    • Binder, R.J.1    Han, D.K.2    Srivastava, P.K.3
  • 28
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • DOI 10.1016/S1074-7613(01)00111-X
    • Basu, S., Binder, R. J., Ramalingam, T., and Srivastava, P. K. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity, 14: 303-313, 2001. (Pubitemid 32289294)
    • (2001) Immunity , vol.14 , Issue.3 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 29
    • 0035893009 scopus 로고    scopus 로고
    • Cell surface targeting of heat shock protein gp96 induces dendritic cell maturation and antitumor immunity
    • Zheng, H., Dai, J., Stoilova, D., and Li, Z. Cell surface targeting of heat shock protein gp96 induces dendritic cell maturation and antitumor immunity. J. Immunol., 167: 6731-6735, 2001. (Pubitemid 33144162)
    • (2001) Journal of Immunology , vol.167 , Issue.12 , pp. 6731-6735
    • Zheng, H.1    Dai, J.2    Stoilova, D.3    Li, Z.4
  • 30
    • 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., and 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
  • 31
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick, J., Dul, J. L., and Argon, Y. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature (Lond.), 370: 373-375, 1994.
    • (1994) Nature (Lond.) , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 32
    • 0034795208 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
    • DOI 10.1038/ncb1001-891
    • Randow, F., and Seed, B. Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. Nat. Cell Biol., 3: 891-896, 2001. (Pubitemid 32952253)
    • (2001) Nature Cell Biology , vol.3 , Issue.10 , pp. 891-896
    • Randow, F.1    Seed, B.2
  • 33
    • 0034252699 scopus 로고    scopus 로고
    • gp96 - The immune system's Swiss army knife
    • Schild, H., and Rammensee, H. G. gp96-the immune system's Swiss army knife. Nat. Immunol., 1: 100-101, 2000.
    • (2000) Nat. Immunol. , vol.1 , pp. 100-101
    • Schild, H.1    Rammensee, H.G.2
  • 34
    • 0035348164 scopus 로고    scopus 로고
    • HSPPC-96: A personalised cancer vaccine
    • Caudill, M. M., and Li, Z. HSPPC-96: a personalised cancer vaccine. Exp. Opin. Biol. Ther., 1: 539-547, 2001. (Pubitemid 33768668)
    • (2001) Expert Opinion on Biological Therapy , vol.1 , Issue.3 , pp. 539-547
    • Caudill, M.M.1
  • 35
    • 0034328883 scopus 로고    scopus 로고
    • Immunotherapy of human cancer: Lessons from mice
    • Srivastava, P. K. Immunotherapy of human cancer: lessons from mice. Nat. Immunol., 1: 363-366, 2000.
    • (2000) Nat. Immunol. , vol.1 , pp. 363-366
    • Srivastava, P.K.1
  • 36
    • 0030272588 scopus 로고    scopus 로고
    • Do human cancers express shared protective antigens? or The necessity of remembrance of things past
    • DOI 10.1006/smim.1996.0038
    • Srivastava, P. K. Do human cancers express shared protective antigens? Or the necessity of remembrance of things past? Semin. Immunol., 8: 295-302, 1996. (Pubitemid 26413870)
    • (1996) Seminars in Immunology , vol.8 , Issue.5 , pp. 295-302
    • Srivastava, P.K.1
  • 39
    • 0023663430 scopus 로고
    • T cell tolerance by clonal elimination in the thymus
    • Kappler, J. W., Roehm, N., and Marrack, P. T cell tolerance by clonal elimination in the thymus. Cell, 49: 273-280, 1987.
    • (1987) Cell , vol.49 , pp. 273-280
    • Kappler, J.W.1    Roehm, N.2    Marrack, P.3
  • 40
    • 0025339512 scopus 로고
    • Self-nonself discrimination by T cells
    • Wash. DC
    • von Boehmer, H., and Kisielow, P. Self-nonself discrimination by T cells. Science (Wash. DC), 248: 1369-1373, 1990.
    • (1990) Science , vol.248 , pp. 1369-1373
    • Von Boehmer, H.1    Kisielow, P.2
  • 41
    • 0035059416 scopus 로고    scopus 로고
    • Cross-presentation, dendritic cells, tolerance and immunity
    • DOI 10.1146/annurev.immunol.19.1.47
    • Heath, W. R., and Carbone, F. R. Cross-presentation, dendritic cells, tolerance and immunity. Annu. Rev. Immunol., 19: 47-64, 2001. (Pubitemid 32368029)
    • (2001) Annual Review of Immunology , vol.19 , pp. 47-64
    • Heath, W.R.1    Carbone, F.R.2
  • 42
    • 0014941813 scopus 로고
    • A theory of self-nonself discrimination
    • Wash. DC
    • Bretscher, P., and Cohn, M. A theory of self-nonself discrimination. Science (Wash. DC), 169: 1042-1049, 1970.
    • (1970) Science , vol.169 , pp. 1042-1049
    • Bretscher, P.1    Cohn, M.2
  • 43
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway, C. A., Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb. Symp. Quant. Biol., 54: 1-13, 1989.
    • (1989) Cold Spring Harb. Symp. Quant. Biol. , vol.54 , pp. 1-13
    • Janeway Jr., C.A.1
  • 44
    • 0035056017 scopus 로고    scopus 로고
    • CTLA-4-mediated inhibition in regulation of T cell responses: Mechanisms and manipulation in tumor immunotherapy
    • DOI 10.1146/annurev.immunol.19.1.565
    • Chambers, C. A., Kuhns, M. S., Egen, J. G., and Allison, J. P. CTLA-4-mediated inhibition in regulation of T cell responses: mechanisms and manipulation in tumor immunotherapy. Annu. Rev. Immunol., 19: 565-594, 2001. (Pubitemid 32368046)
    • (2001) Annual Review of Immunology , vol.19 , pp. 565-594
    • Chambers, C.A.1    Kuhns, M.S.2    Egen, J.G.3    Allison, J.P.4
  • 45
    • 0027078670 scopus 로고
    • Costimulation of antitumor immunity by the B7 counterreceptor for the T lymphocyte molecules CD28 and CTLA-4
    • DOI 10.1016/S0092-8674(05)80059-5
    • Chen, L., Ashe, S., Brady, W. A., Hellstrom, I., Hellstrom, K. E., Ledbetter, J. A., McGowan, P., and Linsley, P. S. Costimulation of antitumor immunity by the B7 counterreceptor for the T lymphocyte molecules CD28 and CTLA-4. Cell, 71: 1093-1102, 1992. (Pubitemid 23016545)
    • (1992) Cell , vol.71 , Issue.7 , pp. 1093-1102
    • Chen, L.1    Ashe, S.2    Brady, W.A.3    Hellstrom, I.4    Hellstrom, K.E.5    Ledbetter, J.A.6    McGowan, P.7    Linsley, P.S.8
  • 46
    • 0028908324 scopus 로고
    • Paracrine cytokine adjuvants in cancer immunotherapy
    • Pardoll, D. M. Paracrine cytokine adjuvants in cancer immunotherapy. Annu. Rev. Immunol., 13: 399-415, 1995.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 399-415
    • Pardoll, D.M.1
  • 47
    • 0035266293 scopus 로고    scopus 로고
    • T cell-dependent antitumor immunity mediated by secondary lymphoid tissue chemokine: Augmentation of dendritic cell-based immunotherapy
    • Kirk, C. J., Hartigan-O'Connor, D., Nickoloff, B. J., Chamberlain, J. S., Giedlin, M., Aukerman, L., and Mule, J. J. T cell-dependent antitumor immunity mediated by secondary lymphoid tissue chemokine: augmentation of dendritic cell-based immunotherapy. Cancer Res., 61: 2062-2070, 2001. (Pubitemid 32692028)
    • (2001) Cancer Research , vol.61 , Issue.5 , pp. 2062-2070
    • Kirk, C.J.1    Hartigan-O'Connor, D.2    Nickoloff, B.J.3    Chamberlain, J.S.4    Giedlin, M.5    Aukerman, L.6    Mule, J.J.7
  • 48
    • 0027848783 scopus 로고
    • Antitumor protection from the murine T-cell leukemia/lymphoma EL4 by the continuous subcutaneous coadministration of recombinant macrophage-colony stimulating factor and interleukin-2
    • Vallera, D. A., Taylor, P. A., Aukerman, S. L., and Blazar, B. R. Antitumor protection from the murine T-cell leukemia/lymphoma EL4 by the continuous subcutaneous coadministration of recombinant macrophage-colony stimulating factor and interleukin-2. Cancer Res., 53: 4273-4280, 1993. (Pubitemid 24146778)
    • (1993) Cancer Research , vol.53 , Issue.18 , pp. 4273-4280
    • Vallera, D.A.1    Taylor, P.A.2    Aukerman, S.L.3    Blazar, B.R.4
  • 50
    • 0034551671 scopus 로고    scopus 로고
    • Dendritic cells as immunologic adjuvants for the treatment of cancer
    • Baggers, J., Ratzinger, G., and Young, J. W. Dendritic cells as immunologic adjuvants for the treatment of cancer. J. Clin. Oncol., 18: 3879-3882, 2000.
    • (2000) J. Clin. Oncol. , vol.18 , pp. 3879-3882
    • Baggers, J.1    Ratzinger, G.2    Young, J.W.3
  • 51
    • 0035989690 scopus 로고    scopus 로고
    • Dendritic cell maturation in active immunotherapy strategies
    • DOI 10.1517/14712598.2.1.35
    • Morse, M. A., Mosca, P. J., Clay, T. M., and Lyerly, H. K. Dendritic cell maturation in active immunotherapy strategies. Exp. Opin. Biol. Ther., 2: 35-43, 2002. (Pubitemid 34462459)
    • (2002) Expert Opinion on Biological Therapy , vol.2 , Issue.1 , pp. 35-43
    • Morse, M.A.1    Mosca, P.J.2    Clay, T.M.3    Lyerly, H.K.4
  • 52
    • 0030820099 scopus 로고    scopus 로고
    • Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations
    • DOI 10.1126/science.278.5335.117
    • Tamura, Y., Peng, P., Liu, K., Daou, M., and Srivastava, P. K. Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations. Science (Wash. DC), 278: 117-120, 1997. (Pubitemid 27446289)
    • (1997) Science , vol.278 , Issue.5335 , pp. 117-120
    • Tamura, Y.1    Peng, P.2    Liu, K.3    Daou, M.4    Srivastava, P.K.5
  • 54
    • 0037086266 scopus 로고    scopus 로고
    • Development of a recombinant HSP110-HER-2/neu vaccine using the chaperoning properties of HSP110
    • Manjili, M. H., Henderson, R., Wang, X. Y., Chen, X., Li, Y., Repasky, E., Kazim, L., and Subjeck, J. R. Development of a recombinant HSP110-HER-2/neu vaccine using the chaperoning properties of HSP110. Cancer Res., 62: 1737-1742, 2002. (Pubitemid 34408496)
    • (2002) Cancer Research , vol.62 , Issue.6 , pp. 1737-1742
    • Manjili, M.H.1    Henderson, R.2    Wang, X.-Y.3    Chen, X.4    Li, Y.5    Repasky, E.6    Kazim, L.7    Subjeck, J.R.8
  • 55
    • 0033571087 scopus 로고    scopus 로고
    • Cutting edge: Tumor secreted heat shock-fusion protein elicits CD8 cells for rejection
    • Yamazaki, K., Nguyen, T., and Podack, E. R. Cutting edge: tumor secreted heat shock-fusion protein elicits CD8 cells for rejection. J. Immunol., 163: 5178-5182, 1999.
    • (1999) J. Immunol. , vol.163 , pp. 5178-5182
    • Yamazaki, K.1    Nguyen, T.2    Podack, E.R.3
  • 56
    • 0031836938 scopus 로고    scopus 로고
    • Tumor immunogenicity is determined by the mechanism of cell death via induction of heat shock protein expression
    • DOI 10.1038/nm0598-581
    • Melcher, A., Todryk, S., Hardwick, N., Ford, M., Jacobson, M., and Vile, R. G. Tumor immunogenicity is determined by the mechanism of cell death via induction of heat shock protein expression. Nat. Med., 4: 581-587, 1998. (Pubitemid 28237357)
    • (1998) Nature Medicine , vol.4 , Issue.5 , pp. 581-587
    • Melcher, A.1    Todryk, S.2    Hardwick, N.3    Ford, M.4    Jacobson, M.5    Vile, R.G.6
  • 57
    • 0033179274 scopus 로고    scopus 로고
    • Heat shock protein 70 induced during tumor cell killing induces Th1 cytokines and targets immature dendritic cell precursors to enhance antigen uptake
    • Todryk, S., Melcher, A. A., Hardwick, N., Linardakis, E., Bateman, A., Colombo, M. P., Stoppacciaro, A., and Vile, R. G. Heat shock protein 70 induced during tumor cell killing induces Th1 cytokines and targets immature dendritic cell precursors to enhance antigen uptake. J. Immunol., 163: 1398-1408, 1999. (Pubitemid 29352760)
    • (1999) Journal of Immunology , vol.163 , Issue.3 , pp. 1398-1408
    • Todryk, S.1    Melcher, A.A.2    Hardwick, N.3    Linardakis, E.4    Bateman, A.5    Colombo, M.P.6    Stoppacciaro, A.7    Vile, R.G.8
  • 58
    • 0032695108 scopus 로고    scopus 로고
    • Natural adjuvants: Endogenous activators of dendritic cells
    • DOI 10.1038/15200
    • Gallucci, S., Lolkema, M., and Matzinger, P. Natural adjuvants: endogenous activators of dendritic cells. Nat. Med., 5: 1249-1255, 1999. (Pubitemid 29535601)
    • (1999) Nature Medicine , vol.5 , Issue.11 , pp. 1249-1255
    • Gallucci, S.1    Lolkema, M.2    Matzinger, P.3
  • 59
    • 0034614897 scopus 로고    scopus 로고
    • Consequences of cell death: Exposure to necrotic tumor cells, but not primary tissue cells or apoptotic cells, induces the maturation of immunostimulatory dendritic cells
    • Sauter, B., Albert, M. L., Francisco, L., Larsson, M., Somersan, S., and Bhardwaj, N. Consequences of cell death: exposure to necrotic tumor cells, but not primary tissue cells or apoptotic cells, induces the maturation of immunostimulatory dendritic cells. J. Exp. Med., 191: 423-434, 2000.
    • (2000) J. Exp. Med. , vol.191 , pp. 423-434
    • Sauter, B.1    Albert, M.L.2    Francisco, L.3    Larsson, M.4    Somersan, S.5    Bhardwaj, N.6
  • 60
    • 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., Binder, R. J., Suto, R., Anderson, K. M., and Srivastava, P. K. 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.
    • (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
  • 61
    • 0035500779 scopus 로고    scopus 로고
    • Primary tumor tissue lysates are enriched in heat shock proteins and induce the maturation of human dendritic cells
    • Somersan, S., Larsson, M., Fonteneau, J. F., Basu, S., Srivastava, P., and Bhardwaj, N. Primary tumor tissue lysates are enriched in heat shock proteins and induce the maturation of human dendritic cells. J. Immunol., 167: 4844-4852, 2001. (Pubitemid 33009712)
    • (2001) Journal of Immunology , vol.167 , Issue.9 , pp. 4844-4852
    • Somersan, S.1    Larsson, M.2    Fonteneau, J.F.3    Basu, S.4    Srivastava, P.5    Bhardwaj, N.6
  • 62
    • 0035890823 scopus 로고    scopus 로고
    • Comparative analysis of necrotic and apoptotic tumor cells as a source of antigen(s) in dendritic cell-based immunization
    • Kotera, Y., Shimizu, K., and Mule, J. J. Comparative analysis of necrotic and apoptotic tumor cells as a source of antigen(s) in dendritic cell-based immunization. Cancer Res., 61: 8105-8109, 2001. (Pubitemid 33091598)
    • (2001) Cancer Research , vol.61 , Issue.22 , pp. 8105-8109
    • Kotera, Y.1    Shimizu, K.2    Mule, J.J.3
  • 63
    • 0031055601 scopus 로고    scopus 로고
    • Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular chaperones
    • Wiest, D. L., Bhandoola, A., Punt, J., Kreibich, G., McKean, D., and Singer, A. Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular chaperones. Proc. Natl. Acad. Sci. USA, 94: 1884-1889, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1884-1889
    • Wiest, D.L.1    Bhandoola, A.2    Punt, J.3    Kreibich, G.4    McKean, D.5    Singer, A.6
  • 64
    • 0034014134 scopus 로고    scopus 로고
    • Reduced amount of the glucose-regulated protein GRP94 in skeletal myoblasts results in loss of fusion competence
    • Gorza, L., and Vitadello, M. Reduced amount of the glucose-regulated protein GRP94 in skeletal myoblasts results in loss of fusion competence. FASEB J., 14: 461-475, 2000. (Pubitemid 30143165)
    • (2000) FASEB Journal , vol.14 , Issue.3 , pp. 461-475
    • Gorza, L.1    Vitadello, M.2
  • 65
    • 0029838338 scopus 로고    scopus 로고
    • Tumor-specific cell surface expression of the -KDEL containing, endoplasmic reticular heat shock protein gp96
    • DOI 10.1002/(SICI)1097-0215(19960822)69:4<340:
    • Altmeyer, A., Maki, R. G., Feldweg, A. M., Heike, M., Protopopov, V. P., Masur, S. K., and Srivastava, P. K. Tumor-specific cell surface expression of the-KDEL containing, endoplasmic reticular heat shock protein gp96. Int. J. Cancer, 69: 340-349, 1996. (Pubitemid 26298302)
    • (1996) International Journal of Cancer , vol.69 , Issue.4 , pp. 340-349
    • Altmeyer, A.1    Maki, R.G.2    Feldweg, A.M.3    Heike, M.4    Protopopov, V.P.5    Masur, S.K.6    Srivastava, P.K.7
  • 66
    • 0345035504 scopus 로고    scopus 로고
    • Cell surface expression of the endoplasmic reticular heat shock protein gp96 is phylogenetically conserved
    • Robert, J., Menoret, A., and Cohen, N. Cell surface expression of the endoplasmic reticular heat shock protein gp96 is phylogenetically conserved. J. Immunol., 163: 4133-4139, 1999. (Pubitemid 29474475)
    • (1999) Journal of Immunology , vol.163 , Issue.8 , pp. 4133-4139
    • Robert, J.1    Menoret, A.2    Cohen, N.3
  • 67
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • DOI 10.1016/0092-8674(89)90019-6
    • Booth, C., and Koch, G. L. Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell, 59: 729-737, 1989. (Pubitemid 19282880)
    • (1989) Cell , vol.59 , Issue.4 , pp. 729-737
    • Booth, C.1    Koch, G.L.E.2
  • 68
    • 0035873090 scopus 로고    scopus 로고
    • Calreticulin, a potential cell surface receptor involved in cell penetration of anti-DNA antibodies
    • Seddiki, N., Nato, F., Lafaye, P., Amoura, Z., Piette, J. C., and Mazie, J. C. Calreticulin, a potential cell surface receptor involved in cell penetration of anti-DNA antibodies. J. Immunol., 166: 6423-6429, 2001. (Pubitemid 32440777)
    • (2001) Journal of Immunology , vol.166 , Issue.10 , pp. 6423-6429
    • Seddiki, N.1    Nato, F.2    Lafaye, P.3    Amoura, Z.4    Piette, J.C.5    Mazie, J.C.6
  • 69
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and cd91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden, C. A., deCathelineau, A., Hoffmann, P. R., Bratton, D., Ghebrehiwet, B., Fadok, V. A., and Henson, P. M. C1q and mannose binding lectin engagement of cell surface calreticulin and cd91 initiates macropinocytosis and uptake of apoptotic cells. J. Exp. Med., 194: 781-796, 2001.
    • (2001) J. Exp. Med. , vol.194 , pp. 781-796
    • Ogden, C.A.1    DeCathelineau, A.2    Hoffmann, P.R.3    Bratton, D.4    Ghebrehiwet, B.5    Fadok, V.A.6    Henson, P.M.7
  • 70
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD 14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • DOI 10.1038/74697
    • Asea, A., Kraeft, S. K., Kurt-Jones, E. A., Stevenson, M. A., Chen, L. B., Finberg, R. W., Koo, G. C., and Calderwood, S. K. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat. Med., 6: 435-442, 2000. (Pubitemid 30208161)
    • (2000) Nature Medicine , vol.6 , Issue.4 , 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
  • 71
    • 0033555665 scopus 로고    scopus 로고
    • Intranuclear targeted delivery of functional NF-κB by 70 kDa heat shock protein
    • DOI 10.1093/emboj/18.2.411
    • Fujihara, S. M., and Nadler, S. G. Intranuclear targeted delivery of functional NF-κB by 70 kDa heat shock protein. EMBO J., 18: 411-419, 1999. (Pubitemid 29041949)
    • (1999) EMBO Journal , vol.18 , Issue.2 , pp. 411-419
    • Fujihara, S.M.1    Nadler, S.G.2
  • 73
    • 0031647680 scopus 로고    scopus 로고
    • The regulation of heat shock proteins and their role in systemic lupus erythematosus
    • Stephanou, A., Latchman, D. S., and Isenberg, D. A. The regulation of heat shock proteins and their role in systemic lupus erythematosus. Semin. Arthritis Rheum., 28: 155-162, 1998. (Pubitemid 28563927)
    • (1998) Seminars in Arthritis and Rheumatism , vol.28 , Issue.3 , pp. 155-162
    • Stephanou, A.1    Latchman, D.S.2    Isenberg, D.A.3


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