메뉴 건너뛰기




Volumn 3, Issue 5, 2003, Pages 427-432

Re-evaluating the role of heat-shock protein-peptide interactions in tumour immunity

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN GP 96; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PEPTIDE; SARCOMA GLYCOPROTEIN GP96 REJECTION ANTIGENS; TUMOR ANTIGEN;

EID: 0038387444     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri1089     Document Type: Review
Times cited : (102)

References (55)
  • 1
    • 84965157146 scopus 로고
    • Antigenic properties of methylcholanthrene-induced tumors in mice of the same strain of origin
    • Foley, E. J. Antigenic properties of methylcholanthrene-induced tumors in mice of the same strain of origin. Cancer Res. 13, 835-837 (1953).
    • (1953) Cancer Res. , vol.13 , pp. 835-837
    • Foley, E.J.1
  • 2
    • 70449193189 scopus 로고
    • Immunity to methylcholanthrene-induced sarcomas
    • Prehn, R. T. & Main, J. M. Immunity to methylcholanthrene-induced sarcomas. J. Natl Cancer Inst. 18, 769-778 (1957).
    • (1957) J. Natl. Cancer Inst. , vol.18 , pp. 769-778
    • Prehn, R.T.1    Main, J.M.2
  • 3
    • 78651120598 scopus 로고
    • Demonstration of resistance against methylcholanthrene-induced sarcomas in the primary autochthonous host
    • Klein, G., Sjögren, H. O., Klein, E. & Hellström, K. E. Demonstration of resistance against methylcholanthrene-induced sarcomas in the primary autochthonous host. Cancer Res. 20, 1561-1572 (1960).
    • (1960) Cancer Res. , vol.20 , pp. 1561-1572
    • Klein, G.1    Sjögren, H.O.2    Klein, E.3    Hellström, K.E.4
  • 4
    • 0022534393 scopus 로고
    • Tumor rejection antigens of chemically induced tumors of inbred mice
    • Srivastava, P. K., DeLeo, A. B. & Old, L. J. Tumor rejection antigens of chemically induced tumors of inbred mice. Proc. Natl Acad. Sci. USA 83, 3407-3411 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3407-3411
    • Srivastava, P.K.1    DeLeo, A.B.2    Old, L.J.3
  • 5
    • 0023228980 scopus 로고
    • 5′-structural analysis of genes encoding polymorphic antigens of chemically induced tumors
    • Srivastava, P. K., Chen, Y. T. & Old, L. J. 5′-structural analysis of genes encoding polymorphic antigens of chemically induced tumors. Proc. Natl Acad Sci. USA 84, 3807-3811 (1987).
    • (1987) Proc. Natl. Acad Sci. USA , vol.84 , pp. 3807-3811
    • Srivastava, P.K.1    Chen, Y.T.2    Old, L.J.3
  • 6
    • 0024393778 scopus 로고
    • Peptide binding and release by proteins implicated as catalysts of protein assembly
    • Flynn, G. C., Chappell, T. G. & Rothman, J. E. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245, 385-390 (1989).
    • (1989) Science , vol.245 , pp. 385-390
    • Flynn, G.C.1    Chappell, T.G.2    Rothman, J.E.3
  • 7
    • 0026069595 scopus 로고
    • Stress-induced proteins in immune response to cancer
    • Srivastava, P. K. & Maki, R. G. Stress-induced proteins in immune response to cancer. Curr. Top. Microbiol. Immunol. 167, 109-123 (1991).
    • (1991) Curr. Top. Microbiol. Immunol. , vol.167 , pp. 109-123
    • Srivastava, P.K.1    Maki, R.G.2
  • 8
    • 0025932078 scopus 로고
    • Tumor-specific immunogenicity of stress-induced proteins: Convergence of two evolutionary pathways of antigen presentation?
    • Srivastava, P. K. & Heike, M. Tumor-specific immunogenicity of stress-induced proteins: convergence of two evolutionary pathways of antigen presentation? Semin. Immunol. 3, 57-64 (1991).
    • (1991) Semin. Immunol. , vol.3 , pp. 57-64
    • Srivastava, P.K.1    Heike, M.2
  • 9
    • 0036776742 scopus 로고    scopus 로고
    • Beyond the proteasome: Trimming, degradation and generation of MHC class I ligands by auxiliary proteases
    • Saveanu, L., Fruci, D. & van Endert, P. Beyond the proteasome: trimming, degradation and generation of MHC class I ligands by auxiliary proteases. Mol. Immunol. 39, 203-215 (2002).
    • (2002) Mol. Immunol. , vol.39 , pp. 203-215
    • Saveanu, L.1    Fruci, D.2    Van Endert, P.3
  • 10
    • 0031906738 scopus 로고    scopus 로고
    • Isolation of processed, H-2Kb-binding ovalbumin-derived peptides associated with the stress proteins HSP70 and gp96
    • Breloer, M., Marti, T., Fleischer, B. & von Bonin, A. Isolation of processed, H-2Kb-binding ovalbumin-derived peptides associated with the stress proteins HSP70 and gp96. Eur. J. Immunol. 28, 1016-1021 (1998).
    • (1998) Eur. J. Immunol. , vol.28 , pp. 1016-1021
    • Breloer, M.1    Marti, T.2    Fleischer, B.3    Von Bonin, A.4
  • 11
    • 0029892849 scopus 로고    scopus 로고
    • Isolation of an immunodominant viral peptide that is endogenously bound to the stress protein gp96/GRP94
    • Nieland, T. J. et al. Isolation of an immunodominant viral peptide that is endogenously bound to the stress protein gp96/GRP94. Proc. Natl Acad. Sci. USA 93, 6135-619 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6135-6619
    • Nieland, T.J.1
  • 12
    • 0033083413 scopus 로고    scopus 로고
    • Isolation of MHC class I-restricted tumor antigen peptide and its precursors associated with heat shock proteins hsp70, hsp90, and gp96
    • Ishii, T. et al. Isolation of MHC class I-restricted tumor antigen peptide and its precursors associated with heat shock proteins hsp70, hsp90, and gp96. J. Immunol. 162, 1303-1309 (1999).
    • (1999) J. Immunol. , vol.162 , pp. 1303-1309
    • Ishii, T.1
  • 13
    • 0017850921 scopus 로고
    • Unique and common tumor-specific transplantation antigens of chemically induced mouse sarcomas
    • Hellstrom, K. E., Hellstrom, I. & Brown, J. P. Unique and common tumor-specific transplantation antigens of chemically induced mouse sarcomas. Int. J. Cancer 21, 317-322 (1978).
    • (1978) Int. J. Cancer , vol.21 , pp. 317-322
    • Hellstrom, K.E.1    Hellstrom, I.2    Brown, J.P.3
  • 14
    • 0017695544 scopus 로고
    • Common transplantation antigens on methylcholanthrene-induced murine sarcomas detected by three assays of tumor rejection
    • Leffell, M. S. & Coggin, J. H. Jr. Common transplantation antigens on methylcholanthrene-induced murine sarcomas detected by three assays of tumor rejection. Cancer Res. 87, 4112-4119 (1977).
    • (1977) Cancer Res. , vol.87 , pp. 4112-4119
    • Leffell, M.S.1    Coggin J.H., Jr.2
  • 15
    • 0017617716 scopus 로고
    • Common tumor rejection antigens in methylcholanthrene-induced squamous cell carcinomas of mice detected by tumor protection and a radioisotopic footpad assay
    • Economou, G. C., Takeichi, N. & Boone, C. W. Common tumor rejection antigens in methylcholanthrene-induced squamous cell carcinomas of mice detected by tumor protection and a radioisotopic footpad assay. Cancer Res. 37, 37-41 (1977).
    • (1977) Cancer Res. , vol.37 , pp. 37-41
    • Economou, G.C.1    Takeichi, N.2    Boone, C.W.3
  • 17
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K. L. et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78, 761-771 (1994).
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1
  • 18
    • 0033198680 scopus 로고    scopus 로고
    • Tripeptidyl peptidases: Enzymes that count
    • Tomkinson, B. Tripeptidyl peptidases: enzymes that count. Trends Biochem. Sci. 24, 355-359 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 355-359
    • Tomkinson, B.1
  • 19
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-γ can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
    • Beninga, J., Rock, K. L. & Goldberg, A. L. Interferon-γ can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem. 273, 18734-18742 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 18734-18742
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.L.3
  • 20
    • 0036884090 scopus 로고    scopus 로고
    • The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues
    • York, I. A. et al. The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nature Immunol. 3, 1177-1184 (2002).
    • (2002) Nature Immunol. , vol.3 , pp. 1177-1184
    • York, I.A.1
  • 21
    • 0034913229 scopus 로고    scopus 로고
    • ER aminopeptidases generate a unique pool of peptides for MHC class I molecules
    • Serwold, T., Gaw, S. & Shastri, N. ER aminopeptidases generate a unique pool of peptides for MHC class I molecules. Nature Immunol. 2, 644-651 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 644-651
    • Serwold, T.1    Gaw, S.2    Shastri, N.3
  • 22
    • 0034351417 scopus 로고    scopus 로고
    • The immunological properties of endoplasmic reticulum chaperones: A conflict of interest?
    • Nicchitta, C. V. & Reed, R. C. The immunological properties of endoplasmic reticulum chaperones: a conflict of interest? Essays Biochem. 36, 15-25 (2000).
    • (2000) Essays Biochem. , vol.36 , pp. 15-25
    • Nicchitta, C.V.1    Reed, R.C.2
  • 23
    • 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. et al. 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).
    • (1997) J. Exp. Med. , vol.186 , pp. 1315-1322
    • Blachere, N.E.1
  • 24
    • 0037290769 scopus 로고    scopus 로고
    • ISO a critical evaluation of the role of peptides in heat shock/ chaperone protein-mediated tumor rejection
    • Baker-LePain, J. C., Reed, R. C. & Nicchitta, C. V. ISO: a critical evaluation of the role of peptides in heat shock/chaperone protein-mediated tumor rejection. Curr. Opin. Immunol. 15, 89-94 (2003).
    • (2003) Curr. Opin. Immunol. , vol.15 , pp. 89-94
    • Baker-LePain, J.C.1    Reed, R.C.2    Nicchitta, C.V.3
  • 25
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young, J. C., Moarefl, I. & Hartl, F. U. Hsp90: a specialized but essential protein-folding tool. J. Cell Biol. 154, 267-273 (2001).
    • (2001) J. Cell Biol. , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefl, I.2    Hartl, F.U.3
  • 26
    • 0031895351 scopus 로고    scopus 로고
    • The hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
    • Pratt, W. B. The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc. Soc. Exp. Biol. Med. 217, 420-434 (1998).
    • (1998) Proc. Soc. Exp. Biol. Med. , vol.217 , pp. 420-434
    • Pratt, W.B.1
  • 27
    • 0031848850 scopus 로고    scopus 로고
    • Recent advances in the study of hsp90 structure and mechanism of action
    • Toft, D. O. Recent advances in the study of hsp90 structure and mechanism of action. Trends Endocrinol. Metab. 9, 238-243 (1998).
    • (1998) Trends Endocrinol. Metab. , vol.9 , pp. 238-243
    • Toft, D.O.1
  • 28
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn, G. C., Pohl, J., Flocco, M. T. & Rothman, J. E. Peptide-binding specificity of the molecular chaperone BiP. Nature 353, 726-730 (1991).
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 29
    • 0028850872 scopus 로고
    • Effect of nucleotide on the binding of peptides to 70-kDa heat shock protein
    • Greene, L. E., Zinner, R., Naficy, S. & Eisenberg, E. Effect of nucleotide on the binding of peptides to 70-kDa heat shock protein. J. Biol. Chem. 270, 2967-2973 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2967-2973
    • Greene, L.E.1    Zinner, R.2    Naficy, S.3    Eisenberg, E.4
  • 30
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specifity of BiP
    • Blond-Elguindi, S. et al. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specifity of BiP. Cell 75, 717-728 (1993).
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond-Elguindi, S.1
  • 31
    • 0030805217 scopus 로고    scopus 로고
    • TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin
    • Spee, P. & Neefjes, J. TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin. Eur. J. Immunol. 27, 2441-2449 (1997).
    • (1997) Eur. J. Immunol. , vol.27 , pp. 2441-2449
    • Spee, P.1    Neefjes, J.2
  • 32
    • 0024295428 scopus 로고
    • Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER
    • Geetha-Habib, M., Noiva, R., Kaplan, H. A. & Lennarz, W. J. Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER. Cell 54, 1053-1060 (1988).
    • (1988) Cell , vol.54 , pp. 1053-1060
    • Geetha-Habib, M.1    Noiva, R.2    Kaplan, H.A.3    Lennarz, W.J.4
  • 33
    • 0026066361 scopus 로고
    • Peptide binding by protein disulfide isomerase, a resident protein of the endoplasmic reticulum lumen
    • Noiva, R., Kimura, H., Roos, J. & Lennarz, W. J. Peptide binding by protein disulfide isomerase, a resident protein of the endoplasmic reticulum lumen. J. Biol. Chem. 266, 19645-19649 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 19645-19649
    • Noiva, R.1    Kimura, H.2    Roos, J.3    Lennarz, W.J.4
  • 34
    • 0033566953 scopus 로고    scopus 로고
    • Intracellular rate-limiting steps in MHC class I antigen processing
    • Montoya, M. & Del Val, M. Intracellular rate-limiting steps in MHC class I antigen processing. J. Immunol. 163, 1914-1922 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 1914-1922
    • Montoya, M.1    Del Val, M.2
  • 35
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert, U. et al. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404, 770-774 (2000).
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1
  • 36
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk, K., Rotzschke, O., Stevanovic, S., Jung, G. & Rammensee, H. G. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 351, 290-296 (1991).
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rotzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.G.5
  • 37
    • 0033179885 scopus 로고    scopus 로고
    • Discrete proteolytic intermediates in the MHC class I antigen processing pathway and MHC I-dependent peptide trimming in the ER
    • Paz, P., Brouwenstijn, N., Perry, R. & Shastri, N. Discrete proteolytic intermediates in the MHC class I antigen processing pathway and MHC I-dependent peptide trimming in the ER. Immunity 11, 241-251 (1999).
    • (1999) Immunity , vol.11 , pp. 241-251
    • Paz, P.1    Brouwenstijn, N.2    Perry, R.3    Shastri, N.4
  • 38
    • 0037242017 scopus 로고    scopus 로고
    • Peptides in living cells: Diffusion, protection and degradation in nuclear and cytoplasmic compartments before antigen presentation by MHC class I
    • Reits, E. et al. Peptides in living cells: diffusion, protection and degradation in nuclear and cytoplasmic compartments before antigen presentation by MHC class I. Immunity 18, 97-108 (2003).
    • (2003) Immunity , vol.18 , pp. 97-108
    • Reits, E.1
  • 39
    • 0037342270 scopus 로고    scopus 로고
    • Quantitating protein synthesis, degradation and endogenous antigen processing
    • Princiotta, M. F. et al. Quantitating protein synthesis, degradation and endogenous antigen processing. Immunity 18, 343-354 (2003).
    • (2003) Immunity , vol.18 , pp. 343-354
    • Princiotta, M.F.1
  • 40
    • 0037067702 scopus 로고    scopus 로고
    • GRP94-associated enzymatic activities Resolution by chromatographic fractionation
    • Reed, R. C., Zheng, T. & Nicchitta, C. V. GRP94-associated enzymatic activities Resolution by chromatographic fractionation. J. Biol. Chem. 277, 25082-25089 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 25082-25089
    • Reed, R.C.1    Zheng, T.2    Nicchitta, C.V.3
  • 41
    • 0037011072 scopus 로고    scopus 로고
    • GRP94 (gp96) and GRP94 N-terminal geldanamycin binding domain elicit tissue nonrestricted tumor suppression
    • Baker-LePain, J. C., Sarzotti, M., Fields, T. A., Li, C. Y. & Nicchitta, C. V. GRP94 (gp96) and GRP94 N-terminal geldanamycin binding domain elicit tissue nonrestricted 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
  • 42
    • 0036214288 scopus 로고    scopus 로고
    • Interaction of heat shock proteins with peptides and antigen presenting cells: Chaperoning of the innate and adaptive immune responses
    • Srivastava, P. Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. Annu. Rev. Immunol. 20, 395-425 (2002).
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 44
    • 0033839045 scopus 로고    scopus 로고
    • The heat shock protein gp96 induces maturation of dendritic cells and down-regulation of its receptor
    • Singh-Jasuja, H. 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
  • 46
    • 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. & 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
  • 47
    • 0037102374 scopus 로고    scopus 로고
    • The role of IFN-γ in rejection of established tumors by IL-12: Source of production and target
    • Segal, J. G., Lee, N. C., Tsung, Y. L., Norton, J. A. & Tsung, K. The role of IFN-γ in rejection of established tumors by IL-12: source of production and target. Cancer Res. 62, 4696-4703 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 4696-4703
    • Segal, J.G.1    Lee, N.C.2    Tsung, Y.L.3    Norton, J.A.4    Tsung, K.5
  • 48
    • 0036847667 scopus 로고    scopus 로고
    • Therapeutic and specific antitumor immunity induced by co-administration of immature dendritic cells and adenoviral vector expressing biologically active IL-18
    • Tanaka, F., Hashimoto, W., Robbins, P. D., Lotze, M. T. & Tahara, H. Therapeutic and specific antitumor immunity induced by co-administration of immature dendritic cells and adenoviral vector expressing biologically active IL-18. Gene Ther. 9, 1480-1486 (2002).
    • (2002) Gene Ther. , vol.9 , pp. 1480-1486
    • Tanaka, F.1    Hashimoto, W.2    Robbins, P.D.3    Lotze, M.T.4    Tahara, H.5
  • 49
    • 0036645278 scopus 로고    scopus 로고
    • A critical role for natural killer T cells in immunosurveillance of methylcholanthrene-induced sarcomas
    • Crowe, N. Y., Smyth, M. J. & Godfrey, D. I. A critical role for natural killer T cells in immunosurveillance of methylcholanthrene-induced sarcomas. J. Exp. Med. 196, 119-127 (2002).
    • (2002) J. Exp. Med. , vol.196 , pp. 119-127
    • Crowe, N.Y.1    Smyth, M.J.2    Godfrey, D.I.3
  • 50
    • 0035451072 scopus 로고    scopus 로고
    • Immune rejection of a large sarcoma following cyclophosphamide and IL-12 treatment requires both NK and NK T cells and is associated with the induction of a novel NK T cell population
    • Karnbach, C., Daws, M. R., Niemi, E. C. & Nakamura, M. C. Immune rejection of a large sarcoma following cyclophosphamide and IL-12 treatment requires both NK and NK T cells and is associated with the induction of a novel NK T cell population. J. Immunol. 167, 2569-2576 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 2569-2576
    • Karnbach, C.1    Daws, M.R.2    Niemi, E.C.3    Nakamura, M.C.4
  • 51
    • 0035071525 scopus 로고    scopus 로고
    • NK cells and NK T cells collaborate in host protection from methylcholanthrene-induced fibrosarcoma
    • Smyth, M. J., Crowe, N. Y. & Godfrey, D. I. NK cells and NK T cells collaborate in host protection from methylcholanthrene-induced fibrosarcoma. Int. Immunol. 13, 459-463 (2001).
    • (2001) Int. Immunol. , vol.13 , pp. 459-463
    • Smyth, M.J.1    Crowe, N.Y.2    Godfrey, D.I.3
  • 52
    • 0036785091 scopus 로고    scopus 로고
    • Heat shock fusion protein gp96-Ig mediates strong CD8 CTL expansion in vivo
    • Strbo, N., Yamazaki, K., Lee, K., Rukavina, D. & Podack, E. R. Heat shock fusion protein gp96-Ig mediates strong CD8 CTL expansion in vivo. Am. J. Reprod. Immunol. 48, 220-225 (2002).
    • (2002) Am. J. Reprod. Immunol. , vol.48 , pp. 220-225
    • Strbo, N.1    Yamazaki, K.2    Lee, K.3    Rukavina, D.4    Podack, E.R.5
  • 53
    • 0036569356 scopus 로고    scopus 로고
    • Cutting edge: CD91-independent cross-presentation of GRP94(gp96)-associated peptides
    • Berwin, B., Hart, J. P., Pizzo, S. V. & Nicchitta, C. V. Cutting edge: CD91-independent cross-presentation of GRP94(gp96)-associated peptides. J. Immunol. 168, 4282-4286 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 4282-4286
    • Berwin, B.1    Hart, J.P.2    Pizzo, S.V.3    Nicchitta, C.V.4
  • 54
    • 0033057848 scopus 로고    scopus 로고
    • Heat-shock proteins, molecular chaperones, and the stress response: Evolutionary and ecological physiology
    • Feder, M. E. & Hofmann, G. E. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu. Rev. Physiol. 61, 243-282 (1999).
    • (1999) Annu. Rev. Physiol. , vol.61 , pp. 243-282
    • Feder, M.E.1    Hofmann, G.E.2
  • 55
    • 0036556684 scopus 로고    scopus 로고
    • The mammalian endoplasmic reticulum as a sensor for cellular stress
    • Ma, Y. & Hendershot, L. M. The mammalian endoplasmic reticulum as a sensor for cellular stress. Cell Stress Chaperones 7, 222-229 (2002).
    • (2002) Cell Stress Chaperones , vol.7 , pp. 222-229
    • Ma, Y.1    Hendershot, L.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.