메뉴 건너뛰기




Volumn 25, Issue 8, 2009, Pages 617-625

Heat shock proteins in antigen traffickingImplications on antigen presentation to T cells

Author keywords

Antigen processing; ERAD; HSP; Proteasome; Ubiquitin

Indexed keywords

HEAT SHOCK PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEASOME; UBIQUITIN;

EID: 73649126594     PISSN: 02656736     EISSN: 14645157     Source Type: Journal    
DOI: 10.3109/02656730902902183     Document Type: Review
Times cited : (18)

References (64)
  • 1
    • 0024383535 scopus 로고
    • Antigen recognition by class I-restricted T lymphocytes
    • Townsend A, Bodmer H. Antigen recognition by class I-restricted T lymphocytes. Annu Rev Immunol 1989;7:601-624.
    • (1989) Annu Rev Immunol , vol.7 , pp. 601-624
    • Townsend, A.1    Bodmer, H.2
  • 2
    • 0027399243 scopus 로고
    • Peptides naturally presented by MHC class i molecules
    • Rammensee HG, Falk K, Rotzschke O. Peptides naturally presented by MHC class I molecules. Annu Rev Immunol 1993;11:213-244.
    • (1993) Annu Rev Immunol , vol.11 , pp. 213-244
    • Rammensee, H.G.1    Falk, K.2    Rotzschke, O.3
  • 3
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • Rock KL, Goldberg AL. Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu Rev Immunol 1999;17:739-779.
    • (1999) Annu Rev Immunol , vol.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 4
  • 5
    • 0030239693 scopus 로고    scopus 로고
    • Defective ribosomal products (DRiPs): A major source of antigenic peptides for MHC class i molecules?
    • Yewdell JW, Anton LC, Bennink JR. Defective ribosomal products (DRiPs): A major source of antigenic peptides for MHC class I molecules? J Immunol 1996;157:1823-1826.
    • (1996) J Immunol , vol.157 , pp. 1823-1826
    • Yewdell, J.W.1    Anton, L.C.2    Bennink, J.R.3
  • 6
    • 33745301876 scopus 로고    scopus 로고
    • Tight linkage between translation and MHC class i peptide ligand generation implies specialized antigen processing for defective ribosomal products
    • Qian SB, Reits E, Neefjes J, Deslich JM, Bennink JR, Yewdell JW. Tight linkage between translation and MHC class I peptide ligand generation implies specialized antigen processing for defective ribosomal products. J Immunol 2006;177:227-233.
    • (2006) J Immunol , vol.177 , pp. 227-233
    • Qian, S.B.1    Reits, E.2    Neefjes, J.3    Deslich, J.M.4    Bennink, J.R.5    Yewdell, J.W.6
  • 7
  • 8
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata S, Minami Y, Minami M, Chiba T, Tanaka K. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep 2001;2:1133-1138.
    • (2001) EMBO Rep , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 9
    • 0037401714 scopus 로고    scopus 로고
    • CHIP: A quality-control E3 ligase collaborating with molecular chaperones
    • Murata S, Chiba T, Tanaka K. CHIP: A quality-control E3 ligase collaborating with molecular chaperones. Int J Biochem Cell Biol 2003;35:572-578.
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 572-578
    • Murata, S.1    Chiba, T.2    Tanaka, K.3
  • 10
    • 33646575879 scopus 로고    scopus 로고
    • Hsp90α chaperones large C-terminally extended proteolytic intermediates in the MHC class i antigen processing pathway
    • Kunisawa J, Shastri N. Hsp90α chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway. Immunity 2006;24:523-534.
    • (2006) Immunity , vol.24 , pp. 523-534
    • Kunisawa, J.1    Shastri, N.2
  • 11
    • 0141750441 scopus 로고    scopus 로고
    • The group II chaperonin TRiC protects proteolytic intermediates from degradation in the MHC class i antigen processing pathway
    • Kunisawa J, Shastri N. The group II chaperonin TRiC protects proteolytic intermediates from degradation in the MHC class I antigen processing pathway. Mol Cell 2003;12:565-576.
    • (2003) Mol Cell , vol.12 , pp. 565-576
    • Kunisawa, J.1    Shastri, N.2
  • 12
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, Patterson C. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol 1999;19:4535-4545.
    • (1999) Mol Cell Biol , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 13
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • McDonough H, Patterson C. CHIP: A link between the chaperone and proteasome systems. Cell Stress Chaperones 2003;8:303-308.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 14
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 2001; 3:100-105.
    • (2001) Nat Cell Biol , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 15
    • 0141596941 scopus 로고    scopus 로고
    • Overview: Translating Hsp90 biology into Hsp90 drugs
    • Workman P. Overview: Translating Hsp90 biology into Hsp90 drugs. Curr Cancer Drug Targets 2003;3:297-300.
    • (2003) Curr Cancer Drug Targets , vol.3 , pp. 297-300
    • Workman, P.1
  • 16
    • 36549047011 scopus 로고    scopus 로고
    • Heat shock protein 90 regulates the stability of c-Jun in HEK293 cells
    • Lu C, Chen D, Zhang Z, Fang F, Wu Y, Luo L, Yin Z. Heat Shock Protein 90 regulates the stability of c-Jun in HEK293 Cells. Mol Cells 2007;24:210-214. (Pubitemid 350177180)
    • (2007) Molecules and Cells , vol.24 , Issue.2 , pp. 210-214
    • Lu, C.1    Chen, D.2    Zhang, Z.3    Fang, F.4    Wu, Y.5    Luo, L.6    Yin, Z.7
  • 17
    • 34249717858 scopus 로고    scopus 로고
    • Regulation of deathassociated protein kinase. Stabilization by HSP90 heterocomplexes
    • Zhang L, Nephew KP, Gallagher PJ. Regulation of deathassociated protein kinase. Stabilization by HSP90 heterocomplexes. J Biol Chem 2007;282:11795- 11804.
    • (2007) J Biol Chem , vol.282 , pp. 11795-11804
    • Zhang, L.1    Nephew, K.P.2    Gallagher, P.J.3
  • 18
    • 33846982944 scopus 로고    scopus 로고
    • The platelet-derived growth factor receptor α is destabilized by geldanamycins in cancer cells
    • Matei D, Satpathy M, Cao L, Lai YC, Nakshatri H, Donner DB. The platelet-derived growth factor receptor α is destabilized by geldanamycins in cancer cells. J Biol Chem 2007;282:445-453.
    • (2007) J Biol Chem , vol.282 , pp. 445-453
    • Matei, D.1    Satpathy, M.2    Cao, L.3    Lai, Y.C.4    Nakshatri, H.5    Donner, D.B.6
  • 19
    • 0037099735 scopus 로고    scopus 로고
    • Two distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class i antigen processing
    • Yamano T, Murata S, Shimbara N, Tanaka N, Chiba T, Tanaka K, Yui K, Udono H. Two distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class I antigen processing. J Exp Med 2002;196:185-196.
    • (2002) J Exp Med , vol.196 , pp. 185-196
    • Yamano, T.1    Murata, S.2    Shimbara, N.3    Tanaka, N.4    Chiba, T.5    Tanaka, K.6    Yui, K.7    Udono, H.8
  • 20
    • 40349088739 scopus 로고    scopus 로고
    • Heat-shock protein 90 associates with N-terminal extended peptides and is required for direct and indirect antigen presentation
    • Callahan MK, Garg MM, Srivastava PK. Heat-shock protein 90 associates with N-terminal extended peptides and is required for direct and indirect antigen presentation. Proc Natl Acad Sci USA 2008;105:1662-1667.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1662-1667
    • Callahan, M.K.1    Garg, M.M.2    Srivastava, P.K.3
  • 21
    • 0032401771 scopus 로고    scopus 로고
    • Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
    • Loo MA, Jensen TJ, Cui L, Hou Y, Chang XB, Riordan JR. Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J 1998;17:6879-6887.
    • (1998) EMBO J , vol.17 , pp. 6879-6887
    • Loo, M.A.1    Jensen, T.J.2    Cui, L.3    Hou, Y.4    Chang, X.B.5    Riordan, J.R.6
  • 22
    • 0034532302 scopus 로고    scopus 로고
    • Post-translational disruption of the delta F508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes delta F508 CFTR in the rabbit reticulocyte lysate
    • Fuller W, Cuthbert AW. Post-translational disruption of the delta F508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes delta F508 CFTR in the rabbit reticulocyte lysate. J Biol Chem 2000;275:37462-37468.
    • (2000) J Biol Chem , vol.275 , pp. 37462-37468
    • Fuller, W.1    Cuthbert, A.W.2
  • 23
    • 57649118512 scopus 로고    scopus 로고
    • Hsp90-mediated assembly of the 26 S proteasome is involved in major histocompatibility complex class i antigen processing
    • Yamano T, Mizukami S, Murata S, Chiba T, Tanaka K, Udono H. Hsp90-mediated assembly of the 26 S proteasome is involved in major histocompatibility complex class I antigen processing. J Biol Chem 2008; 283:28060-28065.
    • (2008) J Biol Chem , vol.283 , pp. 28060-28065
    • Yamano, T.1    Mizukami, S.2    Murata, S.3    Chiba, T.4    Tanaka, K.5    Udono, H.6
  • 24
    • 0042313977 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome
    • Imai J, Maruya M, Yashiroda H, Yahara I, Tanaka K. The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J 2003; 22:3557-3567.
    • (2003) EMBO J , vol.22 , pp. 3557-3567
    • Imai, J.1    Maruya, M.2    Yashiroda, H.3    Yahara, I.4    Tanaka, K.5
  • 27
    • 34247627809 scopus 로고    scopus 로고
    • Distinct pathways of antigen uptake and intracellular routing in CD4 and CD8T cell activation
    • Burgdorf S, Kautz A, Bohnert V, Knolle PA, Kurts C. Distinct pathways of antigen uptake and intracellular routing in CD4 and CD8T cell activation. Science 2007;316:612-616.
    • (2007) Science , vol.316 , pp. 612-616
    • Burgdorf, S.1    Kautz, A.2    Bohnert, V.3    Knolle, P.A.4    Kurts, C.5
  • 28
    • 33645916426 scopus 로고    scopus 로고
    • A role for the Hsp90 molecular chaperone family in antigen presentation to T lymphocytes via major histocompatibility complex class II molecules
    • Rajagopal D, Bal V, Mayor S, George A, Rath S. A role for the Hsp90 molecular chaperone family in antigen presentation to T lymphocytes via major histocompatibility complex class II molecules. Eur J Immunol 2006;36:828-841.
    • (2006) Eur J Immunol , vol.36 , pp. 828-841
    • Rajagopal, D.1    Bal, V.2    Mayor, S.3    George, A.4    Rath, S.5
  • 29
    • 33749512465 scopus 로고    scopus 로고
    • Exiting the outside world for cross-presentation
    • Rock KL. Exiting the outside world for cross-presentation. Immunity 2006;25:523-525.
    • (2006) Immunity , vol.25 , pp. 523-525
    • Rock, K.L.1
  • 30
    • 51349141264 scopus 로고    scopus 로고
    • Dendritic cells in vivo: A key target for a new vaccine science
    • Steinman RM. Dendritic cells in vivo: A key target for a new vaccine science. Immunity 2008;29:319-324.
    • (2008) Immunity , vol.29 , pp. 319-324
    • Steinman, R.M.1
  • 31
    • 0029882212 scopus 로고    scopus 로고
    • In vivo cross-priming of MHC class I-restricted antigens requires the TAP transporter
    • Huang AY, Bruce AT, Pardoll DM, Levitsky HI. In vivo cross-priming of MHC class I-restricted antigens requires the TAP transporter. Immunity 1996;4:349-355.
    • (1996) Immunity , vol.4 , pp. 349-355
    • Huang, A.Y.1    Bruce, A.T.2    Pardoll, D.M.3    Levitsky, H.I.4
  • 32
    • 33645098031 scopus 로고    scopus 로고
    • Cross-priming
    • 2006
    • Bevan MJ. 2006. Cross-priming. Nat Immunol 2006; 7:363-365.
    • (2006) Nat Immunol , vol.7 , pp. 363-365
    • Bevan, M.J.1
  • 33
    • 33749522738 scopus 로고    scopus 로고
    • A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells
    • Ackerman AL, Giodini A, Cresswell P. A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells. Immunity 2006;25:607-617.
    • (2006) Immunity , vol.25 , pp. 607-617
    • Ackerman, A.L.1    Giodini, A.2    Cresswell, P.3
  • 35
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai B, Ye Y, Rapoport TA. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat Rev Mol Cell Biol 2002;3:246-255.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 37
    • 0141707939 scopus 로고    scopus 로고
    • ER-phagosome fusion defines an MHC class i cross-presentation compartment in dendritic cells
    • Guermonprez P, Saveanu L, Kleijmeer M, Davoust J, Van Endert P, Amigorena S. ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells. Nature 2003;425:397-402.
    • (2003) Nature , vol.425 , pp. 397-402
    • Guermonprez, P.1    Saveanu, L.2    Kleijmeer, M.3    Davoust, J.4    Van Endert, P.5    Amigorena, S.6
  • 40
    • 43449108856 scopus 로고    scopus 로고
    • The cell biology of cross-presentation and the role of dendritic cell subsets
    • Lin ML, Zhan Y, Villadangos JA, Lew AM. The cell biology of cross-presentation and the role of dendritic cell subsets. Immunol Cell Biol 2008;86:353-362.
    • (2008) Immunol Cell Biol , vol.86 , pp. 353-362
    • Lin, M.L.1    Zhan, Y.2    Villadangos, J.A.3    Lew, A.M.4
  • 41
    • 34250745700 scopus 로고    scopus 로고
    • The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulumassociated degradation)
    • Brodsky JL. The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulumassociated degradation). Biochem J 2007;404:353-363.
    • (2007) Biochem J , vol.404 , pp. 353-363
    • Brodsky, J.L.1
  • 42
    • 21044431965 scopus 로고    scopus 로고
    • Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)
    • Nishikawa S, Brodsky JL, Nakatsukasa K. Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). J Biochem 2005;137:551-555.
    • (2005) J Biochem , vol.137 , pp. 551-555
    • Nishikawa, S.1    Brodsky, J.L.2    Nakatsukasa, K.3
  • 44
    • 4444355303 scopus 로고    scopus 로고
    • Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein
    • Huyer G, Piluek WF, Fansler Z, Kreft SG, Hochstrasser M, Brodsky JL, Michaelis S. Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J Biol Chem 2004; 279:38369-38378.
    • (2004) J Biol Chem , vol.279 , pp. 38369-38378
    • Huyer, G.1    Piluek, W.F.2    Fansler, Z.3    Kreft, S.G.4    Hochstrasser, M.5    Brodsky, J.L.6    Michaelis, S.7
  • 45
    • 2442451126 scopus 로고    scopus 로고
    • Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control
    • Vashist S, Ng DT. Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. J Cell Biol 2004;165:41-52.
    • (2004) J Cell Biol , vol.165 , pp. 41-52
    • Vashist, S.1    Ng, D.T.2
  • 46
    • 37649025515 scopus 로고    scopus 로고
    • Dissecting the ER-associated degradation of a misfolded polytopic membrane protein
    • Nakatsukasa K, Huyer G, Michaelis S, Brodsky JL. Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell 2008;132:101-112.
    • (2008) Cell , vol.132 , pp. 101-112
    • Nakatsukasa, K.1    Huyer, G.2    Michaelis, S.3    Brodsky, J.L.4
  • 47
    • 12444339508 scopus 로고    scopus 로고
    • Exogenous antigens are processed through the endoplasmic reticulum-associated degradation (ERAD) in cross-presentation by dendritic cells
    • Imai J, Hasegawa H, Maruya M, Koyasu S, Yahara I. Exogenous antigens are processed through the endoplasmic reticulum-associated degradation (ERAD) in cross-presentation by dendritic cells. Int Immunol 2005;17:45-53.
    • (2005) Int Immunol , vol.17 , pp. 45-53
    • Imai, J.1    Hasegawa, H.2    Maruya, M.3    Koyasu, S.4    Yahara, I.5
  • 48
    • 0027260585 scopus 로고
    • Heat shock protein 70-associated peptides elicit specific cancer immunity
    • Udono H, Srivastava PK. Heat shock protein 70-associated peptides elicit specific cancer immunity. J Exp Med 1993;178:1391-1396.
    • (1993) J Exp Med , vol.178 , pp. 1391-1396
    • Udono, H.1    Srivastava, P.K.2
  • 49
    • 0030820099 scopus 로고    scopus 로고
    • Immunotherapy of tumors with autologous tumorderived heat shock protein preparations
    • Tamura Y, Peng P, Liu K, Daou M, Srivastava PK. Immunotherapy of tumors with autologous tumorderived heat shock protein preparations. Science 1997;278:117-120.
    • (1997) Science , vol.278 , pp. 117-120
    • Tamura, Y.1    Peng, P.2    Liu, K.3    Daou, M.4    Srivastava, P.K.5
  • 50
    • 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, Udono H, Yamano T, Ohta H, Uenaka A, Ono T, Hizuta A, Tanaka N, Srivastava PK, Nakayama E. Isolation of MHC class I-restricted tumor antigen peptide and its precursors associated with heat shock proteins hsp70, hsp90, and gp96. J Immunol 1999; 162:1303-1309.
    • (1999) J Immunol , vol.162 , pp. 1303-1309
    • Ishii, T.1    Udono, H.2    Yamano, T.3    Ohta, H.4    Uenaka, A.5    Ono, T.6    Hizuta, A.7    Tanaka, N.8    Srivastava, P.K.9    Nakayama, E.10
  • 51
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • Suto R, Srivastava PK. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 1995;269:1585-1588.
    • (1995) Science , vol.269 , pp. 1585-1588
    • Suto, R.1    Srivastava, P.K.2
  • 52
    • 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 2002;20:395-425.
    • (2002) Annu Rev Immunol , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 53
    • 0034252620 scopus 로고    scopus 로고
    • CD91: A receptor for heat shock protein gp96
    • Binder RJ, Han DK, Srivastava PK. CD91: A receptor for heat shock protein gp96. Nat Immunol 2000;1:151-155.
    • (2000) Nat Immunol , vol.1 , pp. 151-155
    • Binder, R.J.1    Han, D.K.2    Srivastava, P.K.3
  • 54
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu S, Binder RJ, Ramalingam T, Srivastava PK. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 2001;14:303-313.
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 56
    • 8444247044 scopus 로고    scopus 로고
    • Cutting edge: Cross-presentation of cellassociated antigens to MHC class i molecule is regulated by a major transcription factor for heat shock proteins
    • Zheng H, Li Z. Cutting edge: Cross-presentation of cellassociated antigens to MHC class I molecule is regulated by a major transcription factor for heat shock proteins. J Immunol 2004;173:5929-5933.
    • (2004) J Immunol , vol.173 , pp. 5929-5933
    • Zheng, H.1    Li, Z.2
  • 58
    • 1542357672 scopus 로고    scopus 로고
    • Cellular protein is the source of crosspriming antigen in vivo
    • Shen L, Rock KL. Cellular protein is the source of crosspriming antigen in vivo. Proc Natl Acad Sci USA 2004; 101:3035-3040.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3035-3040
    • Shen, L.1    Rock, K.L.2
  • 60
    • 34547882750 scopus 로고    scopus 로고
    • Hsp110 and Grp170, members of the Hsp70 superfamily, bind to scavenger receptor-A and scavenger receptor expressed by endothelial cells-I
    • Facciponte JG, Wang XY, Subjeck JR. Hsp110 and Grp170, members of the Hsp70 superfamily, bind to scavenger receptor-A and scavenger receptor expressed by endothelial cells-I. Eur J Immunol 2007;37:2268-2279.
    • (2007) Eur J Immunol , vol.37 , pp. 2268-2279
    • Facciponte, J.G.1    Wang, X.Y.2    Subjeck, J.R.3
  • 61
    • 0034782206 scopus 로고    scopus 로고
    • Generation of cytotoxic T lymphocytes by MHC class i ligands fused to heat shock cognate protein 70
    • Udono H, Yamano T, Kawabata Y, Ueda M, Yui K. Generation of cytotoxic T lymphocytes by MHC class I ligands fused to heat shock cognate protein 70. Int Immunol 2001;13:1233-1242.
    • (2001) Int Immunol , vol.13 , pp. 1233-1242
    • Udono, H.1    Yamano, T.2    Kawabata, Y.3    Ueda, M.4    Yui, K.5
  • 63
    • 1542514777 scopus 로고    scopus 로고
    • Myeloid differentiation factor 88 is required for cross-priming in vivo
    • Palliser D, Ploegh H, Boes M. Myeloid differentiation factor 88 is required for cross-priming in vivo. J Immunol 2004;172:3415-3421.
    • (2004) J Immunol , vol.172 , pp. 3415-3421
    • Palliser, D.1    Ploegh, H.2    Boes, M.3
  • 64
    • 42449157557 scopus 로고    scopus 로고
    • Spatial and mechanistic separation of cross-presentation and endogenous antigen presentation
    • Burgdorf S, Scholz C, Kautz A, Tampe R, Kurts C. Spatial and mechanistic separation of cross-presentation and endogenous antigen presentation. Nat Immunol 2008; 9:558-566.
    • (2008) Nat Immunol , vol.9 , pp. 558-566
    • Burgdorf, S.1    Scholz, C.2    Kautz, A.3    Tampe, R.4    Kurts, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.