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Volumn 42, Issue 9, 2012, Pages 2419-2430

Modulation of cellular immunity by antibodies against calreticulin

Author keywords

Anti CRT antibodies; Calreticulin; Immunoregulation

Indexed keywords

CALRETICULIN; CALRETICULIN ANTIBODY; GAMMA INTERFERON; IMMUNOMODULATING AGENT; INTERLEUKIN 4; KEYHOLE LIMPET HEMOCYANIN; PROTEIN ANTIBODY; PROTEIN KINASE B; RECOMBINANT PROTEIN; SOLUBLE RECOMBINANT CALRETICULIN; UNCLASSIFIED DRUG;

EID: 84865775308     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201142320     Document Type: Article
Times cited : (5)

References (53)
  • 1
    • 0030897340 scopus 로고    scopus 로고
    • Calreticulin
    • Krause, K. H. and Michalak M., Calreticulin. Cell 1997. 88: 439-443.
    • (1997) Cell , vol.88 , pp. 439-443
    • Krause, K.H.1    Michalak, M.2
  • 2
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver golgi
    • Spiro, R. G., Zhu, Q., Bhoyroo, V. and Soling, H. D., Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver golgi. J. Biol. Chem. 1996. 271: 11588-11594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Soling, H.D.4
  • 3
    • 26944462066 scopus 로고    scopus 로고
    • Delineation of the lectin site of the molecular chaperone calreticulin
    • Thomson, S. P. and Williams, D. B., Delineation of the lectin site of the molecular chaperone calreticulin. Cell Stress Chaperones 2005. 10: 242-251.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 242-251
    • Thomson, S.P.1    Williams, D.B.2
  • 4
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • Vassilakos, A., Michalak, M., Lehrman, M. A. and Williams, D. B., Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 1998. 37: 3480-3490.
    • (1998) Biochemistry , vol.37 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Williams, D.B.4
  • 5
    • 59849120392 scopus 로고    scopus 로고
    • Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
    • Michalak, M., Groenendyk, J., Szabo, E., Gold, L. I. and Opas, M., Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem. J. 2009. 417: 651-666.
    • (2009) Biochem. J. , vol.417 , pp. 651-666
    • Michalak, M.1    Groenendyk, J.2    Szabo, E.3    Gold, L.I.4    Opas, M.5
  • 6
    • 0035279679 scopus 로고    scopus 로고
    • The ins and outs of calreticulin: from the ER lumen to the extracellular space
    • Johnson, S., Michalak, M., Opas, M. and Eggleton, P., The ins and outs of calreticulin: from the ER lumen to the extracellular space. Trend Cell. Biol. 2001. 11: 122-129.
    • (2001) Trend Cell. Biol. , vol.11 , pp. 122-129
    • Johnson, S.1    Michalak, M.2    Opas, M.3    Eggleton, P.4
  • 7
    • 78049508966 scopus 로고    scopus 로고
    • Functional analysis of recombinant calreticulin fragment 39-272: implications for immunobiological activities of calreticulin in health and disease
    • Hong, C., Qiu, X., Li, Y., Huang, Q., Zhong, Z., Zhang, Y., Liu, X. et al., Functional analysis of recombinant calreticulin fragment 39-272: implications for immunobiological activities of calreticulin in health and disease. J. Immunol. 2010. 185: 4561-4569.
    • (2010) J. Immunol. , vol.185 , pp. 4561-4569
    • Hong, C.1    Qiu, X.2    Li, Y.3    Huang, Q.4    Zhong, Z.5    Zhang, Y.6    Liu, X.7
  • 8
    • 77957682653 scopus 로고    scopus 로고
    • Extracellular calreticulin is present in the joints of patients with rheumatoid arthritis and inhibits FasL (CD95L)-mediated apoptosis of T cells
    • Tarr, J. M., Winyard, P. G., Ryan, B., Harries, L. W., Haigh, R., Viner, N. and Eggleton, P., Extracellular calreticulin is present in the joints of patients with rheumatoid arthritis and inhibits FasL (CD95L)-mediated apoptosis of T cells. Arthritis Rheum. 2010. 62: 2919-2929.
    • (2010) Arthritis Rheum. , vol.62 , pp. 2919-2929
    • Tarr, J.M.1    Winyard, P.G.2    Ryan, B.3    Harries, L.W.4    Haigh, R.5    Viner, N.6    Eggleton, P.7
  • 9
    • 0034680794 scopus 로고    scopus 로고
    • Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin
    • Goicoechea, S., Orr, A. W., Pallero, M. A., Eggleton, P. and Murphy-Ullrich, J. E., Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin. J. Biol. Chem. 2000. 275: 36358-36368.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36358-36368
    • Goicoechea, S.1    Orr, A.W.2    Pallero, M.A.3    Eggleton, P.4    Murphy-Ullrich, J.E.5
  • 10
    • 0029054487 scopus 로고
    • Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading
    • White, T. K., Zhu, Q. and Tanzer, M. L., Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading. J. Biol. Chem. 1995. 270: 15926-15929.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15926-15929
    • White, T.K.1    Zhu, Q.2    Tanzer, M.L.3
  • 11
    • 0037308834 scopus 로고    scopus 로고
    • C1q-calreticulin induced oxidative neurotoxicity: relevance for the neuropathogenesis of Alzheimer's disease
    • Luo, X., Weber, G. A., Zheng, J., Gendelman, H. E. and Ikezu, T., C1q-calreticulin induced oxidative neurotoxicity: relevance for the neuropathogenesis of Alzheimer's disease. J. Neuroimmunol. 2003. 135: 62-71.
    • (2003) J. Neuroimmunol. , vol.135 , pp. 62-71
    • Luo, X.1    Weber, G.A.2    Zheng, J.3    Gendelman, H.E.4    Ikezu, T.5
  • 12
    • 26844468253 scopus 로고    scopus 로고
    • Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte
    • Gardai, S. J., McPhillips, K. A., Frasch, S. C., Janssen, W. J., Starefeldt, A., Murphy-Ullrich, J. E., Bratton, D. L. et al., Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte. Cell 2005. 123: 321-334.
    • (2005) Cell , vol.123 , pp. 321-334
    • Gardai, S.J.1    McPhillips, K.A.2    Frasch, S.C.3    Janssen, W.J.4    Starefeldt, A.5    Murphy-Ullrich, J.E.6    Bratton, D.L.7
  • 13
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden, C. A., deCathelineau, A., Hoffmann, P. R., Bratton, D., Ghebrehiwet, B., Fadok, V. A. and Henson, P. M., C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J. Exp. Med. 2001. 194: 781-795.
    • (2001) J. Exp. Med. , vol.194 , pp. 781-795
    • Ogden, C.A.1    deCathelineau, A.2    Hoffmann, P.R.3    Bratton, D.4    Ghebrehiwet, B.5    Fadok, V.A.6    Henson, P.M.7
  • 14
    • 0036785571 scopus 로고    scopus 로고
    • Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: calreticulin and CD91 as a common collectin receptor complex
    • Vandivier, R. W., Ogden, C. A., Fadok, V. A., Hoffmann, P. R., Brown, K. K., Botto, M., Walport, M. J. et al., Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: calreticulin and CD91 as a common collectin receptor complex. J. Immunol. 2002. 169: 3978-3986.
    • (2002) J. Immunol. , vol.169 , pp. 3978-3986
    • Vandivier, R.W.1    Ogden, C.A.2    Fadok, V.A.3    Hoffmann, P.R.4    Brown, K.K.5    Botto, M.6    Walport, M.J.7
  • 15
    • 0034993230 scopus 로고    scopus 로고
    • Activation of human monocyte cell line U937 via cell surface calreticulin
    • Cho, J. H., Homma, K. J., Kanegasaki, S. and Natori, S., Activation of human monocyte cell line U937 via cell surface calreticulin. Cell Stress Chaperones 2001. 6: 148-152.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 148-152
    • Cho, J.H.1    Homma, K.J.2    Kanegasaki, S.3    Natori, S.4
  • 16
    • 0038756766 scopus 로고    scopus 로고
    • Calreticulin is at the surface of circulating neutrophils and uses CD59 as an adaptor molecule
    • Ghiran, I., Klickstein, L. B. and Nicholson-Weller, A., Calreticulin is at the surface of circulating neutrophils and uses CD59 as an adaptor molecule. J. Biol. Chem. 2003. 278: 21024-21031.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21024-21031
    • Ghiran, I.1    Klickstein, L.B.2    Nicholson-Weller, A.3
  • 17
    • 0020080177 scopus 로고
    • Stimulation of a human polymorphonuclear leukocyte oxidative response by the C1q subunit of the first complement component
    • Tenner, A. J. and Cooper, N. R., Stimulation of a human polymorphonuclear leukocyte oxidative response by the C1q subunit of the first complement component. J. Immunol. 1982. 128: 2547-2552.
    • (1982) J. Immunol. , vol.128 , pp. 2547-2552
    • Tenner, A.J.1    Cooper, N.R.2
  • 18
    • 0033572799 scopus 로고    scopus 로고
    • Activation of human neutrophils by a synthetic anti-microbial peptide, KLKLLLLLKLK-NH2, via cell surface calreticulin
    • Cho, J. H., Homma, K., Kanegasaki, S. and Natori, S., Activation of human neutrophils by a synthetic anti-microbial peptide, KLKLLLLLKLK-NH2, via cell surface calreticulin. Eur. J. Biochem. 1999. 266: 878-885.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 878-885
    • Cho, J.H.1    Homma, K.2    Kanegasaki, S.3    Natori, S.4
  • 19
    • 1842634071 scopus 로고    scopus 로고
    • Binding between azurocidin and calreticulin: its involvement in the activation of peripheral monocytes
    • Okuyama, Y., Cho, J. H., Nakajima, Y., Homma, K., Sekimizu, K. and Natori, S., Binding between azurocidin and calreticulin: its involvement in the activation of peripheral monocytes. J. Biochem. 2004. 135: 171-177.
    • (2004) J. Biochem. , vol.135 , pp. 171-177
    • Okuyama, Y.1    Cho, J.H.2    Nakajima, Y.3    Homma, K.4    Sekimizu, K.5    Natori, S.6
  • 20
    • 0037238363 scopus 로고    scopus 로고
    • Maturation-dependent expression of C1q binding proteins on the cell surface of human monocyte-derived dendritic cells
    • Vegh, Z., Goyarts, E. C., Rozengarten, K., Mazumder, A. and Ghebrehiwet, B., Maturation-dependent expression of C1q binding proteins on the cell surface of human monocyte-derived dendritic cells. Int. Immunopharmacol. 2003. 3: 39-51.
    • (2003) Int. Immunopharmacol. , vol.3 , pp. 39-51
    • Vegh, Z.1    Goyarts, E.C.2    Rozengarten, K.3    Mazumder, A.4    Ghebrehiwet, B.5
  • 21
    • 0242331619 scopus 로고    scopus 로고
    • Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens
    • Ackerman, A. L., Kyritsis, C., Tampe, R. and Cresswell, P., Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens. Proc. Natl. Acad. Sci. USA 2003. 100: 12889-12894.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12889-12894
    • Ackerman, A.L.1    Kyritsis, C.2    Tampe, R.3    Cresswell, P.4
  • 22
    • 33748489532 scopus 로고    scopus 로고
    • Dendritic cell surface calreticulin is a receptor for NY-ESO-1: direct interactions between tumor-associated antigen and the innate immune system
    • Zeng, G., Aldridge, M. E., Tian, X., Seiler, D., Zhang, X., Jin, Y., Rao, J. et al., Dendritic cell surface calreticulin is a receptor for NY-ESO-1: direct interactions between tumor-associated antigen and the innate immune system. J. Immunol. 2006. 177: 3582-3589.
    • (2006) J. Immunol. , vol.177 , pp. 3582-3589
    • Zeng, G.1    Aldridge, M.E.2    Tian, X.3    Seiler, D.4    Zhang, X.5    Jin, Y.6    Rao, J.7
  • 23
    • 38449100924 scopus 로고    scopus 로고
    • The rheumatoid arthritis shared epitope triggers innate immune signaling via cell surface calreticulin
    • Ling, S., Pi, X. and Holoshitz, J., The rheumatoid arthritis shared epitope triggers innate immune signaling via cell surface calreticulin. J. Immunol. 2007. 179: 6359-6367.
    • (2007) J. Immunol. , vol.179 , pp. 6359-6367
    • Ling, S.1    Pi, X.2    Holoshitz, J.3
  • 24
    • 33846882318 scopus 로고    scopus 로고
    • Calreticulin exposure increases cancer immunogenicity
    • Clarke, C. and Smyth, M. J., Calreticulin exposure increases cancer immunogenicity. Nat. Biotechnol. 2007. 25: 192-193.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 192-193
    • Clarke, C.1    Smyth, M.J.2
  • 27
    • 0026782109 scopus 로고
    • Calreticulin in T-lymphocytes. Identification of calreticulin in T-lymphocytes and demonstration that activation of T cells correlates with increased levels of calreticulin mRNA and protein
    • Burns, K., Helgason, C. D., Bleackley, R. C. and Michalak, M., Calreticulin in T-lymphocytes. Identification of calreticulin in T-lymphocytes and demonstration that activation of T cells correlates with increased levels of calreticulin mRNA and protein. J. Biol. Chem. 1992. 267: 19039-19042.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19039-19042
    • Burns, K.1    Helgason, C.D.2    Bleackley, R.C.3    Michalak, M.4
  • 28
    • 0033546416 scopus 로고    scopus 로고
    • Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules
    • Arosa, F. A., de Jesus, O., Porto, G., Carmo, A. M. and de Sousa, M., Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules. J. Biol. Chem. 1999. 274: 16917-16922.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16917-16922
    • Arosa, F.A.1    de Jesus, O.2    Porto, G.3    Carmo, A.M.4    de Sousa, M.5
  • 29
    • 33751190060 scopus 로고    scopus 로고
    • Endogenous thrombospondin-1 is a cell-surface ligand for regulation of integrin-dependent T-lymphocyte adhesion
    • Li, S. S., Liu, Z., Uzunel, M. and Sundqvist, K. G., Endogenous thrombospondin-1 is a cell-surface ligand for regulation of integrin-dependent T-lymphocyte adhesion. Blood 2006. 108: 3112-3120.
    • (2006) Blood , vol.108 , pp. 3112-3120
    • Li, S.S.1    Liu, Z.2    Uzunel, M.3    Sundqvist, K.G.4
  • 30
    • 33846504735 scopus 로고    scopus 로고
    • Receptor communication within the lymphocyte plasma membrane: a role for the thrombospondin family of matricellular proteins
    • Forslow, A., Liu, Z. and Sundqvist, K. G., Receptor communication within the lymphocyte plasma membrane: a role for the thrombospondin family of matricellular proteins. Cell. Mol. Life Sci. 2007. 64: 66-76.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 66-76
    • Forslow, A.1    Liu, Z.2    Sundqvist, K.G.3
  • 31
    • 11844291403 scopus 로고    scopus 로고
    • Autocrine regulation of T-cell motility by calreticulin-thrombospondin-1 interaction
    • Li, S. S., Forslow, A. and Sundqvist, K. G., Autocrine regulation of T-cell motility by calreticulin-thrombospondin-1 interaction. J. Immunol. 2005. 174: 654-661.
    • (2005) J. Immunol. , vol.174 , pp. 654-661
    • Li, S.S.1    Forslow, A.2    Sundqvist, K.G.3
  • 32
    • 70349326304 scopus 로고    scopus 로고
    • A CD26-controlled cell surface cascade for regulation of T-cell motility and chemokine signals
    • Liu, Z., Christensson, M., Forslow, A., De Meester, I. and Sundqvist, K. G., A CD26-controlled cell surface cascade for regulation of T-cell motility and chemokine signals. J. Immunol. 2009. 183: 3616-3624.
    • (2009) J. Immunol. , vol.183 , pp. 3616-3624
    • Liu, Z.1    Christensson, M.2    Forslow, A.3    De Meester, I.4    Sundqvist, K.G.5
  • 33
    • 0026583842 scopus 로고
    • Targeted disruption of mu chain membrane exon causes loss of heavy-chain allelic exclusion
    • Kitamura, D. and Rajewsky, K., Targeted disruption of mu chain membrane exon causes loss of heavy-chain allelic exclusion. Nature 1992. 356: 154-156.
    • (1992) Nature , vol.356 , pp. 154-156
    • Kitamura, D.1    Rajewsky, K.2
  • 34
    • 0034193990 scopus 로고    scopus 로고
    • DO11.10 and OT-II T cells recognize a C-terminal ovalbumin 323-339 epitope
    • Robertson, J. M., Jensen, P. E. and Evavold, B. D., DO11.10 and OT-II T cells recognize a C-terminal ovalbumin 323-339 epitope. J. Immunol. 2000. 164: 4706-4712.
    • (2000) J. Immunol. , vol.164 , pp. 4706-4712
    • Robertson, J.M.1    Jensen, P.E.2    Evavold, B.D.3
  • 35
    • 62149150660 scopus 로고    scopus 로고
    • Deficiency of thrombospondin-1 reduces Th17 differentiation and attenuates experimental autoimmune encephalomyelitis
    • Yang, K., Vega, J. L., Hadzipasic, M., Schatzmann Peron, J. P., Zhu, B., Carrier, Y., Masli, S. et al., Deficiency of thrombospondin-1 reduces Th17 differentiation and attenuates experimental autoimmune encephalomyelitis. J. Autoimmun. 2009. 32: 94-103.
    • (2009) J. Autoimmun. , vol.32 , pp. 94-103
    • Yang, K.1    Vega, J.L.2    Hadzipasic, M.3    Schatzmann Peron, J.P.4    Zhu, B.5    Carrier, Y.6    Masli, S.7
  • 37
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster, L. J., De Hoog, C. L. and Mann, M., Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc. Natl. Acad. Sci. USA 2003. 100: 5813-5818.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 38
    • 0242624487 scopus 로고    scopus 로고
    • Systematic identification of regulatory proteins critical for T-cell activation
    • Chu, P., Pardo, J., Zhao, H., Li, C. C., Pali, E., Shen, M. M., Qu, K. et al., Systematic identification of regulatory proteins critical for T-cell activation. J. Biol. 2003. 2: 21.
    • (2003) J. Biol. , vol.2 , pp. 21
    • Chu, P.1    Pardo, J.2    Zhao, H.3    Li, C.C.4    Pali, E.5    Shen, M.M.6    Qu, K.7
  • 39
    • 0037306407 scopus 로고    scopus 로고
    • The roles of membrane microdomains (rafts) in T-cell activation
    • Horejsi, V., The roles of membrane microdomains (rafts) in T-cell activation. Immunol. Rev. 2003. 191: 148-164.
    • (2003) Immunol. Rev. , vol.191 , pp. 148-164
    • Horejsi, V.1
  • 40
    • 33646137152 scopus 로고    scopus 로고
    • Immunological synapse and microclusters: the site for recognition and activation of T cells
    • Saito, T. and Yokosuka, T., Immunological synapse and microclusters: the site for recognition and activation of T cells. Curr. Opin. Immunol. 2006. 18: 305-313.
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 305-313
    • Saito, T.1    Yokosuka, T.2
  • 41
    • 14844352487 scopus 로고    scopus 로고
    • Impaired cytolytic activity in calreticulin-deficient CTLs
    • Sipione, S., Ewen, C., Shostak, I., Michalak, M. and Bleackley, R. C., Impaired cytolytic activity in calreticulin-deficient CTLs. J. Immunol. 2005. 174: 3212-3219.
    • (2005) J. Immunol. , vol.174 , pp. 3212-3219
    • Sipione, S.1    Ewen, C.2    Shostak, I.3    Michalak, M.4    Bleackley, R.C.5
  • 44
    • 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
  • 45
    • 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. V., Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells. EMBO J. 2003. 22: 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.V.7
  • 46
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu, S., Binder, R. J., Ramalingam, T. and Srivastava, P. K., CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 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
  • 48
    • 54949141219 scopus 로고    scopus 로고
    • Regulatory B cells inhibit EAE initiation in mice while other B cells promote disease progression
    • Matsushita, T., Yanaba, K., Bouaziz, J. D., Fujimoto, M. and Tedder, T. F., Regulatory B cells inhibit EAE initiation in mice while other B cells promote disease progression. J. Clin. Invest. 2008. 118: 3420-3430.
    • (2008) J. Clin. Invest. , vol.118 , pp. 3420-3430
    • Matsushita, T.1    Yanaba, K.2    Bouaziz, J.D.3    Fujimoto, M.4    Tedder, T.F.5
  • 49
    • 84855712718 scopus 로고    scopus 로고
    • CD91-dependent programming of T-helper cell responses following heat shock protein immunization
    • Pawaria, S. and Binder, R. J., CD91-dependent programming of T-helper cell responses following heat shock protein immunization. Nat. Commun. 2011. 2: 521.
    • (2011) Nat. Commun. , vol.2 , pp. 521
    • Pawaria, S.1    Binder, R.J.2
  • 50
    • 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-kappa B pathway
    • Basu, S., Binder, R. J., Suto, R., Anderson, K. M. and Srivastava, P. K., Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway. Int. Immunol. 2000. 12: 1539-1546.
    • (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
  • 53
    • 0028232957 scopus 로고
    • Systemic lupus erythematosus is associated with increased auto-antibody titers against calreticulin and grp94, but calreticulin is not the Ro/SS-A antigen
    • Boehm, J., Orth, T., Van Nguyen, P. and Soling, H. D., Systemic lupus erythematosus is associated with increased auto-antibody titers against calreticulin and grp94, but calreticulin is not the Ro/SS-A antigen. Eur. J. Clin. Invest. 1994. 24: 248-257.
    • (1994) Eur. J. Clin. Invest. , vol.24 , pp. 248-257
    • Boehm, J.1    Orth, T.2    Van Nguyen, P.3    Soling, H.D.4


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