메뉴 건너뛰기




Volumn 46, Issue 7, 2009, Pages 1326-1339

Surface expression of a C-terminal α-helix region in heat shock protein 72 on murine LL/2 lung carcinoma can be recognized by innate immune sentinels

Author keywords

B16 melanoma; Cell surface expression; Heat shock protein; Innate immunity; LL 2 lung carcinoma

Indexed keywords

CD11B ANTIGEN; GLYCOPROTEIN P 15095; HEAT SHOCK PROTEIN 72; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN;

EID: 62549155289     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2008.11.020     Document Type: Article
Times cited : (5)

References (63)
  • 2
    • 0034113617 scopus 로고    scopus 로고
    • Hsp70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea A., Kraeft S.-K., Kurt-Jones E., Stevenson M.A., Chen L.B., Finberg R.W., Koo G.C., and Calderwood S.K. Hsp70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine. Nat. Med. 6 (2000) 435-442
    • (2000) Nat. Med. , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.-K.2    Kurt-Jones, E.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6    Koo, G.C.7    Calderwood, S.K.8
  • 3
    • 0037177825 scopus 로고    scopus 로고
    • Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4
    • Asea A., Rehli M., Kabingu E., Boch J.A., Bare O., Auron P.E., Stevenson M.A., and Calderwood S.K. Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4. J. Biol. Chem. 277 (2002) 15028-15034
    • (2002) J. Biol. Chem. , vol.277 , pp. 15028-15034
    • Asea, A.1    Rehli, M.2    Kabingu, E.3    Boch, J.A.4    Bare, O.5    Auron, P.E.6    Stevenson, M.A.7    Calderwood, S.K.8
  • 4
    • 0037144808 scopus 로고    scopus 로고
    • CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes
    • Becker T., Hartl F.-U., and Wieland F. CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. J. Cell Biol. 158 (2002) 1277-1285
    • (2002) J. Cell Biol. , vol.158 , pp. 1277-1285
    • Becker, T.1    Hartl, F.-U.2    Wieland, F.3
  • 5
    • 0345305789 scopus 로고    scopus 로고
    • Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells
    • Berwin B., Hart J.P., Rice S., Gass C., Pizzo S.V., Post S.R., and Nicchitta C. Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells. EMBO J. 22 (2003) 6127-6136
    • (2003) EMBO J. , vol.22 , pp. 6127-6136
    • Berwin, B.1    Hart, J.P.2    Rice, S.3    Gass, C.4    Pizzo, S.V.5    Post, S.R.6    Nicchitta, C.7
  • 6
    • 10944228434 scopus 로고    scopus 로고
    • SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin
    • Berwin B., Delneste Y., Lovingood R.V., Post S.R., and Pizzo S.V. SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin. J. Biol. Chem. 279 (2004) 51250-51257
    • (2004) J. Biol. Chem. , vol.279 , pp. 51250-51257
    • Berwin, B.1    Delneste, Y.2    Lovingood, R.V.3    Post, S.R.4    Pizzo, S.V.5
  • 7
    • 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 (2000) 151-155
    • (2000) Nat. Immunol. , vol.1 , pp. 151-155
    • Binder, R.J.1    Han, D.K.2    Srivastava, P.K.3
  • 8
    • 4744371115 scopus 로고    scopus 로고
    • The heat-shock protein receptors: some answers and more questions
    • Binder R.J., Vatner R., and Srivastava P. The heat-shock protein receptors: some answers and more questions. Tissue Antigens 64 (2004) 442-451
    • (2004) Tissue Antigens , vol.64 , pp. 442-451
    • Binder, R.J.1    Vatner, R.2    Srivastava, P.3
  • 10
    • 0030454056 scopus 로고    scopus 로고
    • Heat-shock protein72 cell-surface expression on human lung carcinoma cells is associated with an increased sensitivity to lysis mediated by adherent natural killer cells
    • Botzler C., Issels R., and Multhoff G. Heat-shock protein72 cell-surface expression on human lung carcinoma cells is associated with an increased sensitivity to lysis mediated by adherent natural killer cells. Cancer Immunol. Immunother. 43 (1996) 226-230
    • (1996) Cancer Immunol. Immunother. , vol.43 , pp. 226-230
    • Botzler, C.1    Issels, R.2    Multhoff, G.3
  • 11
    • 0031945664 scopus 로고    scopus 로고
    • Definition of extracellular localized epitopes of Hsp70 involved in an NK immune response
    • Botzler C., Li G., Issels R., and Multhoff G. Definition of extracellular localized epitopes of Hsp70 involved in an NK immune response. Cell Stress Chaperones 3 (1998) 6-11
    • (1998) Cell Stress Chaperones , vol.3 , pp. 6-11
    • Botzler, C.1    Li, G.2    Issels, R.3    Multhoff, G.4
  • 12
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., and Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell 92 (1998) 351-366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 13
    • 0034608370 scopus 로고    scopus 로고
    • Receptor-mediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways
    • Castellino F., Boucher P.E., Eichelberg K., Mayhew M., Rothman J.E., Houghton A.N., and Germain R.N. Receptor-mediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways. J. Exp. Med. 191 (2000) 1957-1964
    • (2000) J. Exp. Med. , vol.191 , pp. 1957-1964
    • Castellino, F.1    Boucher, P.E.2    Eichelberg, K.3    Mayhew, M.4    Rothman, J.E.5    Houghton, A.N.6    Germain, R.N.7
  • 14
    • 0033559496 scopus 로고    scopus 로고
    • Human 60-kDa heat-shock protein: a danger signal to the innate immune system
    • Chen W., Syldath U., Bellmann K., Burkart V., and Kolb H. Human 60-kDa heat-shock protein: a danger signal to the innate immune system. J. Immunol. 162 (1999) 3212-3219
    • (1999) J. Immunol. , vol.162 , pp. 3212-3219
    • Chen, W.1    Syldath, U.2    Bellmann, K.3    Burkart, V.4    Kolb, H.5
  • 15
    • 0027397058 scopus 로고
    • The roles of heat shock proteins and immediate early genes in central nervous system normal function and pathology
    • Chopp M. The roles of heat shock proteins and immediate early genes in central nervous system normal function and pathology. Curr. Opin. Neurol. Neurosurg. 6 (1993) 6-10
    • (1993) Curr. Opin. Neurol. Neurosurg. , vol.6 , pp. 6-10
    • Chopp, M.1
  • 17
    • 0027955522 scopus 로고
    • Heat-shock proteins expressed on the surface of human T cell leukemia virus type I-infected cell lines induce autantibodies in rabbits
    • Chouchane L., Bowers F.S., Sawasdaikosol S., Simpson R.M., and Kindt T.J. Heat-shock proteins expressed on the surface of human T cell leukemia virus type I-infected cell lines induce autantibodies in rabbits. J. Infect. Dis. 169 (1994) 253-259
    • (1994) J. Infect. Dis. , vol.169 , pp. 253-259
    • Chouchane, L.1    Bowers, F.S.2    Sawasdaikosol, S.3    Simpson, R.M.4    Kindt, T.J.5
  • 18
    • 0028322083 scopus 로고
    • Multiple natural killer cell-activationg signals are inhibited by major histocompatibility complex class I expression in target cells
    • Correa I., Corral L., and Raulet D.H. Multiple natural killer cell-activationg signals are inhibited by major histocompatibility complex class I expression in target cells. Eur. J. Immunol. 24 (1994) 1323-1331
    • (1994) Eur. J. Immunol. , vol.24 , pp. 1323-1331
    • Correa, I.1    Corral, L.2    Raulet, D.H.3
  • 21
    • 0026690529 scopus 로고
    • Surface expressed heat-shock proteins by stressed or human immunodeficiency virus (HIV)-infected lymphoid cells represent the target for antibody-dependent cellular cytotoxicity
    • Di-Cesare S., Poccia F., mastino A., and Colozzo V. Surface expressed heat-shock proteins by stressed or human immunodeficiency virus (HIV)-infected lymphoid cells represent the target for antibody-dependent cellular cytotoxicity. Immunology 76 (1992) 341-343
    • (1992) Immunology , vol.76 , pp. 341-343
    • Di-Cesare, S.1    Poccia, F.2    mastino, A.3    Colozzo, V.4
  • 24
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • Ferrarini M., Heltai S., Raffaella M.Z., and Rugarli C. Unusual expression and localization of heat-shock proteins in human tumor cells. Int. J. Cancer 51 (1992) 613-619
    • (1992) Int. J. Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Raffaella, M.Z.3    Rugarli, C.4
  • 25
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething M.-J., and Sambrook J. Protein folding in the cell. Nature 355 (1992) 33-45
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 26
    • 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., and Multhoff G. Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94. Biol. Chem. 384 (2003) 267-279
    • (2003) Biol. Chem. , vol.384 , pp. 267-279
    • Gross, C.1    Hansch, D.2    Gastpar, R.3    Multhoff, G.4
  • 27
    • 0029992278 scopus 로고    scopus 로고
    • Morecular cheperones in cellular protein folding
    • Hartl F.U. Morecular cheperones in cellular protein folding. Nature 381 (1996) 571-580
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 28
    • 0035525290 scopus 로고    scopus 로고
    • Cross-presentation in viral immunity and self-tolerance
    • Heath W.R., and Carbone F.R. Cross-presentation in viral immunity and self-tolerance. Nat. Rev. Immunol. 1 (2001) 126-134
    • (2001) Nat. Rev. Immunol. , vol.1 , pp. 126-134
    • Heath, W.R.1    Carbone, F.R.2
  • 29
    • 0026535812 scopus 로고
    • Cell surface localization of a 72 kilodalton heat shock protein in retroocular fibroblasts from patients with Graves' ophthalmopathy
    • Heufelder A.E., Wenzel B.E., and Bahn R.S. Cell surface localization of a 72 kilodalton heat shock protein in retroocular fibroblasts from patients with Graves' ophthalmopathy. J. Clin. Endocrinol. Metab. 74 (1992) 732-736
    • (1992) J. Clin. Endocrinol. Metab. , vol.74 , pp. 732-736
    • Heufelder, A.E.1    Wenzel, B.E.2    Bahn, R.S.3
  • 32
    • 0022616253 scopus 로고
    • Selective rejection of H-2-deficient lymphoma variants suggests alternative immune defence strategy
    • Kärre K., Ljunggren H.G., Piontek G., and Kiessling R. Selective rejection of H-2-deficient lymphoma variants suggests alternative immune defence strategy. Nature 319 (1986) 675-678
    • (1986) Nature , vol.319 , pp. 675-678
    • Kärre, K.1    Ljunggren, H.G.2    Piontek, G.3    Kiessling, R.4
  • 33
    • 0027196670 scopus 로고
    • Human peripheral gamma delta T cells recognize hsp60 molecules on Daudi Burkitt's lymphoma cells
    • Kaur I., Voss S.D., Gupta R.S., Schell K., Fisch P., and Sondel P.M. Human peripheral gamma delta T cells recognize hsp60 molecules on Daudi Burkitt's lymphoma cells. J. Immunol. 150 (1993) 2046-2055
    • (1993) J. Immunol. , vol.150 , pp. 2046-2055
    • Kaur, I.1    Voss, S.D.2    Gupta, R.S.3    Schell, K.4    Fisch, P.5    Sondel, P.M.6
  • 34
    • 0033557202 scopus 로고    scopus 로고
    • Chlamydial and human heat shock protein 60 s activate human vascular endothelium, smooth muscle cells, and macrophages
    • Kol A., Bourcier T., Lichtman A.H., and Libby P. Chlamydial and human heat shock protein 60 s activate human vascular endothelium, smooth muscle cells, and macrophages. J. Clin. Invest. 103 (1999) 571-577
    • (1999) J. Clin. Invest. , vol.103 , pp. 571-577
    • Kol, A.1    Bourcier, T.2    Lichtman, A.H.3    Libby, P.4
  • 36
    • 0024674842 scopus 로고
    • The mycobacterial GroEL stress protein: a common target of T-cell recognition in infection and autoimmunity
    • Lamb J.R., Bal V., Rothbard J.B., Mehlert A., Mendez-Samperino P., and Young D.B. The mycobacterial GroEL stress protein: a common target of T-cell recognition in infection and autoimmunity. J. Autoimmun. 2 Suppl. (1989) 93-100s
    • (1989) J. Autoimmun. , vol.2 , Issue.SUPPL
    • Lamb, J.R.1    Bal, V.2    Rothbard, J.B.3    Mehlert, A.4    Mendez-Samperino, P.5    Young, D.B.6
  • 37
    • 0028201732 scopus 로고
    • Tolerance, danger, and the extended family
    • Matzinger P. Tolerance, danger, and the extended family. Annu. Rev. Immunol. 12 (1994) 991-1045
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 991-1045
    • Matzinger, P.1
  • 38
    • 0032191916 scopus 로고    scopus 로고
    • An innate sense of danger
    • Matzinger P. An innate sense of danger. Semin. Immunol. 10 (1998) 399-415
    • (1998) Semin. Immunol. , vol.10 , pp. 399-415
    • Matzinger, P.1
  • 39
    • 0028912572 scopus 로고
    • Heat shock protein reactivity of lymphocytes isolated from heterotopic rat cardiac allografts
    • Moliterno R., Valdivia L., Pan F., and Duquesnoy R.J. Heat shock protein reactivity of lymphocytes isolated from heterotopic rat cardiac allografts. Transplantation 59 (1995) 598-604
    • (1995) Transplantation , vol.59 , pp. 598-604
    • Moliterno, R.1    Valdivia, L.2    Pan, F.3    Duquesnoy, R.J.4
  • 40
    • 0028953056 scopus 로고
    • A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells
    • Multhoff G., Botzler C., Wiesnet M., Müller E., Meier T., Wilmanns W., and Issels R.D. A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells. Int. J. Cancer 61 (1995) 272-279
    • (1995) Int. J. Cancer , vol.61 , pp. 272-279
    • Multhoff, G.1    Botzler, C.2    Wiesnet, M.3    Müller, E.4    Meier, T.5    Wilmanns, W.6    Issels, R.D.7
  • 42
    • 6344241182 scopus 로고    scopus 로고
    • Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity
    • Ohno M., Kitabatake N., and Tani F. Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity. FEBS Lett. 576 (2004) 381-386
    • (2004) FEBS Lett. , vol.576 , pp. 381-386
    • Ohno, M.1    Kitabatake, N.2    Tani, F.3
  • 43
    • 0026793232 scopus 로고
    • Recognition and killing of tumour cells expressing heat shock protein 65 kDa with immunotoxins containing saporin
    • Poccia F., Piselli P., Di-Cesare S., Bach S., Colizzi V., mattei M., Bolognesi A., and Stirpe F. Recognition and killing of tumour cells expressing heat shock protein 65 kDa with immunotoxins containing saporin. Br. J. Cancer 66 (1992) 427-432
    • (1992) Br. J. Cancer , vol.66 , pp. 427-432
    • Poccia, F.1    Piselli, P.2    Di-Cesare, S.3    Bach, S.4    Colizzi, V.5    mattei, M.6    Bolognesi, A.7    Stirpe, F.8
  • 44
    • 0025894722 scopus 로고
    • Heat shock proteins in host-parasite interactions
    • Polla B.S. Heat shock proteins in host-parasite interactions. Immunol. Today 76 (1991) A38-41
    • (1991) Immunol. Today , vol.76
    • Polla, B.S.1
  • 45
    • 0025811860 scopus 로고
    • A hypothetical model for the peptide binding domain of hsp70 based on the peptide binding domain of HLA
    • Rippmann F., Taylor W.R., Rothbard J.B., and Green N.M. A hypothetical model for the peptide binding domain of hsp70 based on the peptide binding domain of HLA. EMBO J. 10 (1991) 1053-1059
    • (1991) EMBO J. , vol.10 , pp. 1053-1059
    • Rippmann, F.1    Taylor, W.R.2    Rothbard, J.B.3    Green, N.M.4
  • 46
    • 0041026092 scopus 로고    scopus 로고
    • Interaction of Hsp70 chaperones with substrates
    • Rüdiger S., Buchberger A., and Bukau B. Interaction of Hsp70 chaperones with substrates. Nat. Struct. Biol. 4 (1997) 342-349
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 342-349
    • Rüdiger, S.1    Buchberger, A.2    Bukau, B.3
  • 47
    • 0024461782 scopus 로고
    • Identification of multiple HTF-island associated genes in the human major histocompatibility complex class III region
    • Sargent C.A., Dunham I., and Campbell R.D. Identification of multiple HTF-island associated genes in the human major histocompatibility complex class III region. EMBO J. 8 (1989) 2305-2312
    • (1989) EMBO J. , vol.8 , pp. 2305-2312
    • Sargent, C.A.1    Dunham, I.2    Campbell, R.D.3
  • 50
    • 0024392729 scopus 로고
    • Human major histocompatibility complex contains a minimum of 19 genes between the complement cluster and HLA-B
    • Spies T., Bresnahan M., and Strominger J.L. Human major histocompatibility complex contains a minimum of 19 genes between the complement cluster and HLA-B. Proc. Natl. Acad. Sci. USA 86 (1989) 8955-8958
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8955-8958
    • Spies, T.1    Bresnahan, M.2    Strominger, J.L.3
  • 51
    • 0032101221 scopus 로고    scopus 로고
    • Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world
    • 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 (1998) 657-665
    • (1998) Immunity , vol.8 , pp. 657-665
    • Srivastava, P.K.1    Menoret, A.2    Basu, S.3    Binder, R.J.4    McQuade, K.L.5
  • 52
    • 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 (2002) 185-194
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 185-194
    • Srivastava, P.K.1
  • 53
    • 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 (2002) 395-425
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 54
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • Suto R., and Srivastava P.K. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 269 (1995) 1585-1588
    • (1995) Science , vol.269 , pp. 1585-1588
    • Suto, R.1    Srivastava, P.K.2
  • 55
    • 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., Stoppaciaro 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 (1999) 1398-1408
    • (1999) J. Immunol. , vol.163 , pp. 1398-1408
    • Todryk, S.1    Melcher, A.A.2    Hardwick, N.3    Linardakis, E.4    Bateman, A.5    Colombo, M.P.6    Stoppaciaro, A.7    Vile, R.G.8
  • 56
    • 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 (1993) 1391-1396
    • (1993) J. Exp. Med. , vol.178 , pp. 1391-1396
    • Udono, H.1    Srivastava, P.K.2
  • 57
    • 0025854087 scopus 로고
    • Surface expression by mononuclear phagocytes of an epitope shared with mycobacterial heat shock protein 60
    • Wand-Württenberger A., Schoel B., Ivanyi J., and Kaufmann S.H. Surface expression by mononuclear phagocytes of an epitope shared with mycobacterial heat shock protein 60. Eur. J. Immunol. 21 (1991) 1089-1092
    • (1991) Eur. J. Immunol. , vol.21 , pp. 1089-1092
    • Wand-Württenberger, A.1    Schoel, B.2    Ivanyi, J.3    Kaufmann, S.H.4
  • 59
    • 0032856673 scopus 로고    scopus 로고
    • Receptor mediated and fluid phase pathways for internalization of the ER Hsp90 chaperone GRP94 in murine macrophages
    • Wassenberg J.J., Dezfulian C., and Nicchitta C.V. Receptor mediated and fluid phase pathways for internalization of the ER Hsp90 chaperone GRP94 in murine macrophages. J. Cell Sci. 112 (1999) 2167-2175
    • (1999) J. Cell Sci. , vol.112 , pp. 2167-2175
    • Wassenberg, J.J.1    Dezfulian, C.2    Nicchitta, C.V.3
  • 60
    • 0028138250 scopus 로고
    • T cells reactive to an inducible heat shock protein induce disease in toxin-induced interstitial nephritis
    • Weiss R.A., Madaio M.P., Tomaszewski J.E., and Kelly C.J. T cells reactive to an inducible heat shock protein induce disease in toxin-induced interstitial nephritis. J. Exp. Med. 180 (1994) 2239-2250
    • (1994) J. Exp. Med. , vol.180 , pp. 2239-2250
    • Weiss, R.A.1    Madaio, M.P.2    Tomaszewski, J.E.3    Kelly, C.J.4
  • 61
    • 0024827184 scopus 로고
    • Stress proteins, arthritis, and autimmunity
    • Winfield J.B. Stress proteins, arthritis, and autimmunity. Arthritis Rheum. 32 (1989) 1497-1504
    • (1989) Arthritis Rheum. , vol.32 , pp. 1497-1504
    • Winfield, J.B.1
  • 62
    • 0033062377 scopus 로고    scopus 로고
    • + T cell responses to infectious agents, tumors, transplants, and vaccines
    • + T cell responses to infectious agents, tumors, transplants, and vaccines. Adv. Immunol. 73 (1999) 1-77
    • (1999) Adv. Immunol. , vol.73 , pp. 1-77
    • Yewdell, J.W.1    Norbury, C.C.2    Bennink, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.