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Volumn 60, Issue 2, 1996, Pages 153-158

Heat shock protein-peptide complexes for use in vaccines

Author keywords

Antigen presentation; gp96; HSP70; HSP90; T cells; Tumor immunology

Indexed keywords

CANCER VACCINE; CHAPERONE; GLYCOPROTEIN 96; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PEPTIDE; UNCLASSIFIED DRUG;

EID: 0029741634     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1002/jlb.60.2.153     Document Type: Review
Times cited : (37)

References (75)
  • 1
    • 0022534393 scopus 로고
    • Tumor rejection antigens of chemically induced sarcomas of inbred mice
    • Srivastava, P.K., DeLeo, A., Old, L.J. (1986) Tumor rejection antigens of chemically induced sarcomas of inbred mice. Proc. Natl. Acad. Sci. USA 83, 3407-3411.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3407-3411
    • Srivastava, P.K.1    DeLeo, A.2    Old, L.J.3
  • 3
    • 0023478338 scopus 로고
    • Cloning and nucleotide sequence of the murine hsp84 cDNA and chromosome assignment of related sequences
    • Moore, S.K., Kozak, C., Robinson, E.A., Ullrich, S.J., Appella, E. (1987) Cloning and nucleotide sequence of the murine hsp84 cDNA and chromosome assignment of related sequences. Gene 56, 29-40.
    • (1987) Gene , vol.56 , pp. 29-40
    • Moore, S.K.1    Kozak, C.2    Robinson, E.A.3    Ullrich, S.J.4    Appella, E.5
  • 4
    • 0025354155 scopus 로고
    • Human homologue of murine tumor rejection antigen gp96: 5′-regulatory and coding regions and relationship to stress-induced proteins
    • Maki, R.G., Old, L.J., Srivastava, P.K. (1990) Human homologue of murine tumor rejection antigen gp96: 5′-regulatory and coding regions and relationship to stress-induced proteins. Proc. Natl. Acad. Sci. USA 87, 5658-5662.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5658-5662
    • Maki, R.G.1    Old, L.J.2    Srivastava, P.K.3
  • 5
    • 0027260585 scopus 로고
    • Heat shock protein 70-associated peptides elicit specific cancer immunity
    • Udono, H., Srivastava, P.K. (1993) Heat shock protein 70-associated peptides elicit specific cancer immunity. J. Exp. Med. 178, 1391-1396.
    • (1993) J. Exp. Med. , vol.178 , pp. 1391-1396
    • Udono, H.1    Srivastava, P.K.2
  • 7
    • 0028301079 scopus 로고
    • Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90, and hsp70
    • Udono, H., Srivastava, P.K. (1994) Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90, and hsp70. J. Immunol. 152, 5398-5403.
    • (1994) J. Immunol. , vol.152 , pp. 5398-5403
    • Udono, H.1    Srivastava, P.K.2
  • 8
    • 0023228980 scopus 로고
    • 5′-structural analysis of genes encoding polymorphic antigens of chemically induced tumors
    • Srivastava, P.K., Chen, Y.-T., Old, L.J. (1987) 5′-structural analysis of genes encoding polymorphic antigens of chemically induced tumors. Proc. Natl. Acad. Sci. USA 84, 3807-3811.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3807-3811
    • Srivastava, P.K.1    Chen, Y.-T.2    Old, L.J.3
  • 9
    • 0025325602 scopus 로고
    • Characterization of the mouse 84-kD heat shack protein gene family
    • Moore, S.K., Rijli, F., Appella, E. (1990) Characterization of the mouse 84-kD heat shack protein gene family. DNA Cell Biol. 9, 387-400.
    • (1990) DNA Cell Biol. , vol.9 , pp. 387-400
    • Moore, S.K.1    Rijli, F.2    Appella, E.3
  • 11
    • 0025932078 scopus 로고
    • Tumor-specific immunogenicity of stress-induced proteins: Convergence of two evolutionary pathways of antigen presentation?
    • Srivastava, P.K., Heike, M. (1991) Tumor-specific immunogenicity of stress-induced proteins: convergence of two evolutionary pathways of antigen presentation? Semin. Immunol. 3, 57-64.
    • (1991) Semin. Immunol. , vol.3 , pp. 57-64
    • Srivastava, P.K.1    Heike, M.2
  • 12
  • 13
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick, J.P., Hartl, F.-U. (1993) Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.-U.2
  • 14
    • 0028061311 scopus 로고
    • Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell
    • Craig, E.A., Weissman, J.S., Horwich, A.L. (1994) Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell. Cell 78, 365-372.
    • (1994) Cell , vol.78 , pp. 365-372
    • Craig, E.A.1    Weissman, J.S.2    Horwich, A.L.3
  • 15
    • 0023664518 scopus 로고
    • ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (CRP94)
    • Mazzarella, R.A., Green, M. (1987) ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (CRP94). J. Biol. Chem. 262, 8875-8883.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8875-8883
    • Mazzarella, R.A.1    Green, M.2
  • 16
    • 0023133224 scopus 로고
    • Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells
    • Lee, A. (1987) Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells. Trends Biol. Sci. 12, 20-23.
    • (1987) Trends Biol. Sci. , vol.12 , pp. 20-23
    • Lee, A.1
  • 17
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmatic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi, Y., Segal, M., Normington, K., Gething, M.-J., Sambrook, J. (1988) The presence of malfolded proteins in the endoplasmatic reticulum signals the induction of glucose-regulated proteins. Nature 332, 462-464.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.-J.4    Sambrook, J.5
  • 18
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth, C., Koch, L. (1989) Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 59, 729-737.
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, L.2
  • 19
    • 0027208741 scopus 로고
    • Tumor rejection antigen gp96/grp94 is an ATPase: Implications for protein folding and antigen presentation
    • Li, Z., Srivastava, P.K. (1993) Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation. EMBO J. 12, 3143-3151.
    • (1993) EMBO J. , vol.12 , pp. 3143-3151
    • Li, Z.1    Srivastava, P.K.2
  • 20
    • 0025784485 scopus 로고
    • A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum
    • Navarro, D., Qadri, I., Pereira, L. (1991) A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum. Virology 184, 253-264.
    • (1991) Virology , vol.184 , pp. 253-264
    • Navarro, D.1    Qadri, I.2    Pereira, L.3
  • 21
    • 0026742999 scopus 로고
    • HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells
    • Schaiff, W.T., Hruska, K.A., Jr., McCourt, D.W., Green, M., Schwartz, B.D. (1992) HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. J. Exp. Med. 176, 657-666.
    • (1992) J. Exp. Med. , vol.176 , pp. 657-666
    • Schaiff, W.T.1    Hruska Jr., K.A.2    McCourt, D.W.3    Green, M.4    Schwartz, B.D.5
  • 22
    • 0028965533 scopus 로고
    • Molecular chaperones in antigen presentation
    • Williams, D.B., Watts, T.H. (1995) Molecular chaperones in antigen presentation. Curr. Opin. Immunol. 7, 77-84.
    • (1995) Curr. Opin. Immunol. , vol.7 , pp. 77-84
    • Williams, D.B.1    Watts, T.H.2
  • 23
    • 0026808864 scopus 로고
    • The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains
    • Melnick, J., Aviel, S., Argon, Y. (1992) The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains. J. Biol. Chem. 267, 21303-21306.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21303-21306
    • Melnick, J.1    Aviel, S.2    Argon, Y.3
  • 24
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick, J., Dul, J.L., Argon, Y. (1994) Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 370, 373-375.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 25
    • 0028923597 scopus 로고
    • Molecular chaperones and the biosynthesis of antigen receptors
    • Melnick, J., Argon, Y. (1995) Molecular chaperones and the biosynthesis of antigen receptors. Immunol Today 16, 243-250.
    • (1995) Immunol Today , vol.16 , pp. 243-250
    • Melnick, J.1    Argon, Y.2
  • 26
    • 0028114348 scopus 로고
    • Heat shock protein-peptide complexes in cancer immunotherapy
    • Srivastava, P.K., Udono, H. (1994) Heat shock protein-peptide complexes in cancer immunotherapy. Curr. Opin. Immunol. 6, 728-732.
    • (1994) Curr. Opin. Immunol. , vol.6 , pp. 728-732
    • Srivastava, P.K.1    Udono, H.2
  • 27
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • Suto, R., Srivastava, P.K. (1995) A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 269, 1585-1588.
    • (1995) Science , vol.269 , pp. 1585-1588
    • Suto, R.1    Srivastava, P.K.2
  • 28
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and CTL priming
    • Srivastava, P.K., Udono, H., Blachere, N.E., Li, Z. (1994) Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics 39, 93-98.
    • (1994) Immunogenetics , vol.39 , pp. 93-98
    • Srivastava, P.K.1    Udono, H.2    Blachere, N.E.3    Li, Z.4
  • 29
    • 0029127770 scopus 로고
    • Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96
    • Arnold, D., Faath, S., Rammensee, H.-G., Schild, H. (1995) Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96. J. Exp. Med. 182, 885-889.
    • (1995) J. Exp. Med. , vol.182 , pp. 885-889
    • Arnold, D.1    Faath, S.2    Rammensee, H.-G.3    Schild, H.4
  • 30
    • 0017126775 scopus 로고
    • Cross-priming for a secondary cytotoxic response Io minor H antigens with H-2 congenic cells which do not cross-react in the cytotoxicity assay
    • Bevan, M.J. (1976) Cross-priming for a secondary cytotoxic response Io minor H antigens with H-2 congenic cells which do not cross-react in the cytotoxicity assay. J. Exp. Med. 143, 1283-1288.
    • (1976) J. Exp. Med. , vol.143 , pp. 1283-1288
    • Bevan, M.J.1
  • 31
    • 0018834104 scopus 로고
    • H-2 antigen requirements in the in vitro induction of SV40-specific cytotoxic T lymphocytes
    • Gooding, L.R., Edwards, C.B. (1980) H-2 antigen requirements in the in vitro induction of SV40-specific cytotoxic T lymphocytes. J. Immunol. 124, 1258-1262.
    • (1980) J. Immunol. , vol.124 , pp. 1258-1262
    • Gooding, L.R.1    Edwards, C.B.2
  • 34
    • 0023192503 scopus 로고
    • Identification of a peptide binding protein that plays a role in antigen presentation
    • Lakey, E.K., Margoliash, E., Pierce, S.K. (1987) Identification of a peptide binding protein that plays a role in antigen presentation. Proc. Natl. Acad. Sci. USA 84, 1659-1663.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1659-1663
    • Lakey, E.K.1    Margoliash, E.2    Pierce, S.K.3
  • 35
    • 0024392717 scopus 로고
    • A peptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock family
    • Vanbuskirk, A., Crump, B.L., Margoliash, E., Pierce, S.K. (1989) A peptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock family. J. Exp. Med. 170, 1799-1809.
    • (1989) J. Exp. Med. , vol.170 , pp. 1799-1809
    • Vanbuskirk, A.1    Crump, B.L.2    Margoliash, E.3    Pierce, S.K.4
  • 36
    • 0025981503 scopus 로고
    • Cellular and subcellular distribution of PBP72/74, a peptide-binding protein that plays a role in antigen processing
    • VanBuskirk, A.M., DeNagel, D.C., Guagliardi, L.E., Brodsky, F.M., Pierce, S.K. (1991) Cellular and subcellular distribution of PBP72/74, a peptide-binding protein that plays a role in antigen processing. J. Immunol. 146, 500-506.
    • (1991) J. Immunol. , vol.146 , pp. 500-506
    • VanBuskirk, A.M.1    DeNagel, D.C.2    Guagliardi, L.E.3    Brodsky, F.M.4    Pierce, S.K.5
  • 37
    • 0027263325 scopus 로고
    • Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family
    • Domanico, S.Z., DeNagel, D.C., Dahlseid, J.N., Green, J.M., Pierre, S.K. (1993) Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family. Mol. Cell. Biol. 13, 3598-3610.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3598-3610
    • Domanico, S.Z.1    DeNagel, D.C.2    Dahlseid, J.N.3    Green, J.M.4    Pierre, S.K.5
  • 38
    • 0026665249 scopus 로고
    • Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP78) and GRP94
    • Clairmont, C.A., De Maio, A.D., Hirschberg, C.B. (1992) Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP78) and GRP94. J. Biol. Chem. 267, 3983-3990.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3983-3990
    • Clairmont, C.A.1    De Maio, A.D.2    Hirschberg, C.B.3
  • 40
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., Nimmesgern, E., Ohtsuka, K., Hartl, U. (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370, 111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, U.4
  • 41
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang, P.J., Ostermann, J., Shilling, J., Neupert, W., Craig, E.A., Pfanner, N. (1990) Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 348, 137-143.
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 42
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann, R.P., Mizzen, L.E., Welch, W.J. (1990) Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science 248, 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.E.2    Welch, W.J.3
  • 43
    • 0026623463 scopus 로고
    • Examining the function and regulation of hsp 70 in cells subjected to metabolic stress
    • Beckmann, R.P., Lovett, M., Welch, W.J. (1992) Examining the function and regulation of hsp 70 in cells subjected to metabolic stress. J. Cell Biol. 117, 1137-1150.
    • (1992) J. Cell Biol. , vol.117 , pp. 1137-1150
    • Beckmann, R.P.1    Lovett, M.2    Welch, W.J.3
  • 44
    • 0027455464 scopus 로고
    • Posttranslational folding of vesicular stomatitis virus G protein in the ER: Involvement of noncovalent and covalent complexes
    • de Silva, A., Braakman, I., Helenius, A. (1993) Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes. J. Cell Biol. 120, 647-655.
    • (1993) J. Cell Biol. , vol.120 , pp. 647-655
    • De Silva, A.1    Braakman, I.2    Helenius, A.3
  • 45
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond, C., Helenius, A. (1994) Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J. Cell Biol. 126, 41-52.
    • (1994) J. Cell Biol. , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 46
    • 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., Green, N.M. (1991) A hypothetical model for the peptide binding domain of hsp70 based on the peptide binding domain of HLA. EMBO J. 10, 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
  • 47
    • 0026595140 scopus 로고
    • Different conformations for the same polypeptide bound to chaperones DnaK and CroEL
    • Landry, S.J., Jordan, R., McMacken, R., Gierasch, L.M. (1992) Different conformations for the same polypeptide bound to chaperones DnaK and CroEL. Nature 355, 455-457.
    • (1992) Nature , vol.355 , pp. 455-457
    • Landry, S.J.1    Jordan, R.2    McMacken, R.3    Gierasch, L.M.4
  • 48
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn, C.C., Pohl, J., Flocco, M.T., Rothman, J.E. (1991) Peptide-binding specificity of the molecular chaperone BiP. Nature 353, 726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, C.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 49
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • Blond Elguindi, S., Cwirla, S.E., Dower, W.J., Lipshutz, R.J., Sprang, S.R., Sambrook, J.F., Gething, M.J. (1993) Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75, 717-728.
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond Elguindi, S.1    Cwirla, S.E.2    Dower, W.J.3    Lipshutz, R.J.4    Sprang, S.R.5    Sambrook, J.F.6    Gething, M.J.7
  • 50
    • 0025085667 scopus 로고
    • Different tumor-derived p53 mutants exhibit distinct biological activities
    • Halevy, O., Michalovitz, D., Oren, M. (1990) Different tumor-derived p53 mutants exhibit distinct biological activities. Science 250, 113-116.
    • (1990) Science , vol.250 , pp. 113-116
    • Halevy, O.1    Michalovitz, D.2    Oren, M.3
  • 51
    • 0025618980 scopus 로고
    • Mutant p53 DNA clones from human colon carcinomas cooperate with ras in transforming primary rat cells: A comparison of the "hot spot" mutant phenotypes
    • Hinds, P.W., Finlay, C.A., Quartin, R.S., Baker, S.J., Fearon, E.R., Vogelstein, B., Levine, A.J. (1990) Mutant p53 DNA clones from human colon carcinomas cooperate with ras in transforming primary rat cells: a comparison of the "hot spot" mutant phenotypes. Cell Growth Diff. 1, 571-580.
    • (1990) Cell Growth Diff. , vol.1 , pp. 571-580
    • Hinds, P.W.1    Finlay, C.A.2    Quartin, R.S.3    Baker, S.J.4    Fearon, E.R.5    Vogelstein, B.6    Levine, A.J.7
  • 52
    • 0025266522 scopus 로고
    • The v-rel oncogene product is complexed with cellular proteins including its proto-oncogene product and heat shock protein 70
    • Lim, M.Y., Davis, N., Zhang, J.Y., Bose, H.R., Jr. (1990) The v-rel oncogene product is complexed with cellular proteins including its proto-oncogene product and heat shock protein 70. Virology 175, 149-160.
    • (1990) Virology , vol.175 , pp. 149-160
    • Lim, M.Y.1    Davis, N.2    Zhang, J.Y.3    Bose Jr., H.R.4
  • 53
    • 0026803306 scopus 로고
    • Vaccinia virus infection induces a stress response that leads to association of Hsp70 with viral proteins
    • Jindal, S., Young, R.A. (1992) Vaccinia virus infection induces a stress response that leads to association of Hsp70 with viral proteins. J. Virol. 66, 5357-5362.
    • (1992) J. Virol. , vol.66 , pp. 5357-5362
    • Jindal, S.1    Young, R.A.2
  • 54
    • 0026567911 scopus 로고
    • A case for chaperones in antigen processing
    • DeNagel, D.C., Pierce, S.K. (1992) A case for chaperones in antigen processing. Immunol. Today 13, 86-89.
    • (1992) Immunol. Today , vol.13 , pp. 86-89
    • DeNagel, D.C.1    Pierce, S.K.2
  • 55
    • 0028358733 scopus 로고
    • Peptide transporter independent, stress protein-mediated endosomal processing of endogenous protein antigens for major histocompatibility complex class 1 presentation
    • Schirmbeck, R., Reimann, J. (1994) Peptide transporter independent, stress protein-mediated endosomal processing of endogenous protein antigens for major histocompatibility complex class 1 presentation. Eur. J. Immunol. 24, 1478-1486.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 1478-1486
    • Schirmbeck, R.1    Reimann, J.2
  • 57
    • 0027385461 scopus 로고
    • 70 kDa heat shock cognate protein is a transformation-associated antigen and a possible target for the host's anti-tumor immunity
    • Tamura, Y., Tsuboi, N., Sato, N., Kikuchi, K. (1993) 70 kDa heat shock cognate protein is a transformation-associated antigen and a possible target for the host's anti-tumor immunity. J. Immunol. 151, 5516-5524.
    • (1993) J. Immunol. , vol.151 , pp. 5516-5524
    • Tamura, Y.1    Tsuboi, N.2    Sato, N.3    Kikuchi, K.4
  • 58
    • 0026525090 scopus 로고
    • Mycobacterial heat-shock proteins as carrier molecules. II: The use of the 70-kDa mycobacterial heat-shock protein as carrier for conjugated vaccines can circumvent the need for adjuvants and Bacillus Calmette Guerin priming
    • Barrios, C., Lussow, A.R., Van Embden, J., Van der Zee, R., Rappuoli, R., Costantino, P., Louis, J.A., Lambert, P.H., Del Giudice, G. (1992) Mycobacterial heat-shock proteins as carrier molecules. II: The use of the 70-kDa mycobacterial heat-shock protein as carrier for conjugated vaccines can circumvent the need for adjuvants and Bacillus Calmette Guerin priming. Eur. J. Immunol. 22, 1365-1372.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1365-1372
    • Barrios, C.1    Lussow, A.R.2    Van Embden, J.3    Van Der Zee, R.4    Rappuoli, R.5    Costantino, P.6    Louis, J.A.7    Lambert, P.H.8    Del Giudice, G.9
  • 59
    • 0026529909 scopus 로고
    • Immune response to p53 is dependent upon p53/HSP70 complexes in breast cancers
    • Davidoff, A.M., Iglehart, J.D., Marks, J.R. (1992) Immune response to p53 is dependent upon p53/HSP70 complexes in breast cancers. Proc. Natl. Acad. Sci. USA 89, 3439-3442.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3439-3442
    • Davidoff, A.M.1    Iglehart, J.D.2    Marks, J.R.3
  • 60
    • 0029079390 scopus 로고
    • Co-segregation of tumor immunogenicity with expression of inducible but not constitutive hsp70 in rat colon carcinomas
    • Menoret, A., Patry, Y., Burg, C., Le Pendu, J. (1995) Co-segregation of tumor immunogenicity with expression of inducible but not constitutive hsp70 in rat colon carcinomas. J. Immunol. 155, 740-747.
    • (1995) J. Immunol. , vol.155 , pp. 740-747
    • Menoret, A.1    Patry, Y.2    Burg, C.3    Le Pendu, J.4
  • 61
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: Interactions with a steroid receptor and a protein kinase
    • Nathan, D.F., Lindquist, S. (1995) Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell Biol. 15, 3917-3925.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 62
    • 0026778032 scopus 로고
    • Hsp90 chaperones protein folding in vitro
    • Wiech, H., Buchner, J., Zimmermann, R., Jakob, U. (1992) Hsp90 chaperones protein folding in vitro. Nature 358, 169-170.
    • (1992) Nature , vol.358 , pp. 169-170
    • Wiech, H.1    Buchner, J.2    Zimmermann, R.3    Jakob, U.4
  • 63
    • 0027475243 scopus 로고
    • Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases
    • Nadeau, K., Das, A., Walsh, C.T. (1993) Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases. J. Biol. Chem. 268, 1479-1487.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1479-1487
    • Nadeau, K.1    Das, A.2    Walsh, C.T.3
  • 64
    • 0029015872 scopus 로고
    • ATP induces dissociation of the 90 kDa heat shock protein (hsp90) from F-actin: Interference with the binding of heavy meromyosin
    • Kellermayer, M.S., Csermely, P. (1995) ATP induces dissociation of the 90 kDa heat shock protein (hsp90) from F-actin: interference with the binding of heavy meromyosin. Biochem. Biophys. Res. Commun. 211, 166-174.
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 166-174
    • Kellermayer, M.S.1    Csermely, P.2
  • 65
    • 0029162385 scopus 로고
    • Antigen presentation to cytotoxic T lymphocytes in vivo
    • Bevan, M.J. (1995) Antigen presentation to cytotoxic T lymphocytes in vivo. J. Exp. Med. 182, 639-641.
    • (1995) J. Exp. Med. , vol.182 , pp. 639-641
    • Bevan, M.J.1
  • 66
    • 0028298224 scopus 로고
    • Cancer antigens: Immune recognition of self and altered self
    • Houghton, A. (1994) Cancer antigens: immune recognition of self and altered self. J. Exp. Med. 180, 1-4.
    • (1994) J. Exp. Med. , vol.180 , pp. 1-4
    • Houghton, A.1
  • 67
    • 0028298850 scopus 로고
    • Tumour antigens. A new look for the 1990s
    • Pardoll, D.M. (1994) Tumour antigens. A new look for the 1990s. Nature 369, 357-358.
    • (1994) Nature , vol.369 , pp. 357-358
    • Pardoll, D.M.1
  • 68
    • 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., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., Goldberg, A.L. (1994) 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) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 70
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • Ferrarini, M., Heltai, S., Zocchi, M.R., Rugarli, C. (1992) Unusual expression and localization of heat-shock proteins in human tumor cells. Int. J. Cancer 51, 613-619.
    • (1992) Int. J. Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.R.3    Rugarli, C.4
  • 73
    • 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., Muller, R., Meier, T., Wilmanns, W., Issels, R.D. (1995) 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, 272-279.
    • (1995) Int. J. Cancer , vol.61 , pp. 272-279
    • Multhoff, G.1    Botzler, C.2    Wiesnet, M.3    Muller, R.4    Meier, T.5    Wilmanns, W.6    Issels, R.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.