메뉴 건너뛰기




Volumn 3, Issue MAR, 2012, Pages

ER stress proteins in autoimmune and inflammatory diseases

Author keywords

Autoimmunity; ER stress; ERAD; Inflammation; Molecular chaperone

Indexed keywords


EID: 84872892910     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2012.00048     Document Type: Review
Times cited : (54)

References (123)
  • 1
    • 0016709754 scopus 로고
    • Antibodies to cellular antigens in Sjogren's syndrome
    • Alspaugh, M. A., and Tan, E. M. (1975). Antibodies to cellular antigens in Sjogren's syndrome. J. Clin. Invest. 55, 1067-1073.
    • (1975) J. Clin. Invest. , vol.55 , pp. 1067-1073
    • Alspaugh, M.A.1    Tan, E.M.2
  • 2
    • 0029838338 scopus 로고    scopus 로고
    • Tumorspecific cell surface expression of the-KDEL containing, endoplasmic reticular heat shock protein gp96
    • Altmeyer, A., Maki, R. G., Feldweg, A. M., Heike, M., Protopopov, V. P., Masur, S. K., and Srivastava, P. K. (1996). Tumorspecific cell surface expression of the-KDEL containing, endoplasmic reticular heat shock protein gp96. Int. J. Cancer 69, 340-349.
    • (1996) Int. J. Cancer , vol.69 , pp. 340-349
    • Altmeyer, A.1    Maki, R.G.2    Feldweg, A.M.3    Heike, M.4    Protopopov, V.P.5    Masur, S.K.6    Srivastava, P.K.7
  • 6
    • 0031902051 scopus 로고    scopus 로고
    • The p68 autoantigen characteristic of rheumatoid arthritis is reactive with carbohydrate epitope specific autoantibodies
    • Blass, S., Meier, C., Vohr, H. W., Schwochau, M., Specker, C., and Burmester, G. R. (1998). The p68 autoantigen characteristic of rheumatoid arthritis is reactive with carbohydrate epitope specific autoantibodies. Ann. Rheum. Dis. 57, 220-225.
    • (1998) Ann. Rheum. Dis. , vol.57 , pp. 220-225
    • Blass, S.1    Meier, C.2    Vohr, H.W.3    Schwochau, M.4    Specker, C.5    Burmester, G.R.6
  • 7
    • 0028944484 scopus 로고
    • Novel 68 kDa autoantigen detected by rheumatoid arthritis specific antibodies
    • Blass, S., Specker, C., Lakomek, H. J., Schneider, E. M., and Schwochau, M. (1995). Novel 68 kDa autoantigen detected by rheumatoid arthritis specific antibodies. Ann. Rheum. Dis. 54, 355-360.
    • (1995) Ann. Rheum. Dis. , vol.54 , pp. 355-360
    • Blass, S.1    Specker, C.2    Lakomek, H.J.3    Schneider, E.M.4    Schwochau, M.5
  • 9
    • 0041777783 scopus 로고    scopus 로고
    • BiP,a putative autoantigen in rheumatoid arthritis, stimulates IL-10-producing CD8-positive T cells from normal individuals
    • (Oxford)
    • Bodman-Smith, M. D., Corrigall, V. M., Kemeny, D. M., and Panayi, G. S. (2003). BiP,a putative autoantigen in rheumatoid arthritis, stimulates IL-10-producing CD8-positive T cells from normal individuals. Rheumatology (Oxford) 42, 637-644.
    • (2003) Rheumatology , vol.42 , pp. 637-644
    • Bodman-Smith, M.D.1    Corrigall, V.M.2    Kemeny, D.M.3    Panayi, G.S.4
  • 10
    • 0028232957 scopus 로고
    • Systemic lupus erythematosus is associated with increased autoantibody 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. (1994). Systemic lupus erythematosus is associated with increased autoantibody titers against calreticulin and grp94, but calreticulin is not the Ro/SS-A antigen. Eur. J. Clin. Invest. 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
  • 11
    • 0031128320 scopus 로고    scopus 로고
    • ER-associated and proteasomemediated protein degradation: how two topologically restricted events came together
    • Brodsky, J. L., and McCracken, A. A. (1997). ER-associated and proteasomemediated protein degradation: how two topologically restricted events came together. Trends Cell Biol. 7, 151-156.
    • (1997) Trends Cell Biol , vol.7 , pp. 151-156
    • Brodsky, J.L.1    McCracken, A.A.2
  • 12
    • 33644910399 scopus 로고    scopus 로고
    • Treatment of murine collageninduced arthritis by the stress protein BiP via interleukin-4-producing regulatory T cells: a novel function for an ancient protein
    • Brownlie, R. J., Myers, L. K., Wooley, P. H., Corrigall, V. M., Bodman-Smith, M. D., Panayi, G. S., and Thompson, S. J. (2006). Treatment of murine collageninduced arthritis by the stress protein BiP via interleukin-4-producing regulatory T cells: a novel function for an ancient protein. Arthritis Rheum. 54, 854-863.
    • (2006) Arthritis Rheum , vol.54 , pp. 854-863
    • Brownlie, R.J.1    Myers, L.K.2    Wooley, P.H.3    Corrigall, V.M.4    Bodman-Smith, M.D.5    Panayi, G.S.6    Thompson, S.J.7
  • 13
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B., Weissman, J., and Horwich, A. (2006). Molecular chaperones and protein quality control. Cell 125, 443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 14
    • 0028288510 scopus 로고
    • Autoantigens targeted in systemic lupus erythematosus are clustered in two populations of surface structures on apoptotic keratinocytes
    • Casciola-Rosen, L. A., Anhalt, G., and Rosen, A. (1994). Autoantigens targeted in systemic lupus erythematosus are clustered in two populations of surface structures on apoptotic keratinocytes. J. Exp. Med. 179, 1317-1330.
    • (1994) J. Exp. Med. , vol.179 , pp. 1317-1330
    • Casciola-Rosen, L.A.1    Anhalt, G.2    Rosen, A.3
  • 15
    • 0029889209 scopus 로고    scopus 로고
    • Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen
    • Cheng, S. T., Nguyen, T. Q., Yang, Y. S., Capra, J. D., and Sontheimer, R. D. (1996). Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen. J. Immunol. 156, 4484-4491.
    • (1996) J. Immunol. , vol.156 , pp. 4484-4491
    • Cheng, S.T.1    Nguyen, T.Q.2    Yang, Y.S.3    Capra, J.D.4    Sontheimer, R.D.5
  • 16
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson, J. C., Shaler, T. A., Tyler, R. E., and Kopito, R. R. (2008). OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat. Cell Biol. 10, 272-282.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 17
    • 0014444829 scopus 로고
    • Characterization of a soluble cytoplasmic antigen reactive with sera from patients with systemic lupus erythmatosus
    • Clark, G., Reichlin, M., and Tomasi, T. B. Jr. (1969). Characterization of a soluble cytoplasmic antigen reactive with sera from patients with systemic lupus erythmatosus. J. Immunol. 102, 117-122.
    • (1969) J. Immunol. , vol.102 , pp. 117-122
    • Clark, G.1    Reichlin, M.2    Tomasi Jr., T.B.3
  • 18
    • 73249153202 scopus 로고    scopus 로고
    • From HLA-B27 to spondyloarthritis: a journey through the ER
    • Colbert, R. A., Delay, M. L., Klenk, E. I., and Layh-Schmitt, G. (2010). From HLA-B27 to spondyloarthritis: a journey through the ER. Immunol. Rev. 233, 181-202.
    • (2010) Immunol. Rev. , vol.233 , pp. 181-202
    • Colbert, R.A.1    Delay, M.L.2    Klenk, E.I.3    Layh-Schmitt, G.4
  • 19
    • 0024430243 scopus 로고
    • Sequence homology of a canine brain calciumbinding protein with calregulin and the human Ro/SS-A antigen
    • Collins, J. H., Xi, Z. J.,Alderson-Lang, B. H., Treves, S., and Volpe, P. (1989). Sequence homology of a canine brain calciumbinding protein with calregulin and the human Ro/SS-A antigen. Biochem. Biophys. Res. Commun. 164, 575-579.
    • (1989) Biochem. Biophys. Res. Commun. , vol.164 , pp. 575-579
    • Collins, J.H.1    Xi, Z.J.2    Alderson-Lang, B.H.3    Treves, S.4    Volpe, P.5
  • 20
    • 1842683012 scopus 로고    scopus 로고
    • Inhibition of antigenpresenting cell function and stimulation of human peripheral blood mononuclear cells to express an antiinflammatory cytokine profile by the stress protein BiP: relevance to the treatment of inflammatory arthritis
    • Corrigall, V. M., Bodman-Smith, M. D., Brunst, M., Cornell, H., and Panayi, G. S. (2004). Inhibition of antigenpresenting cell function and stimulation of human peripheral blood mononuclear cells to express an antiinflammatory cytokine profile by the stress protein BiP: relevance to the treatment of inflammatory arthritis. Arthritis Rheum. 50, 1164-1171.
    • (2004) Arthritis Rheum , vol.50 , pp. 1164-1171
    • Corrigall, V.M.1    Bodman-Smith, M.D.2    Brunst, M.3    Cornell, H.4    Panayi, G.S.5
  • 23
    • 0036626120 scopus 로고    scopus 로고
    • The 78 kDa glucoseregulated protein (GRP78/BIP) is expressed on the cell membrane, is released into cell culture medium and is also present in human peripheral circulation
    • Delpino, A., and Castelli, M. (2002). The 78 kDa glucoseregulated protein (GRP78/BIP) is expressed on the cell membrane, is released into cell culture medium and is also present in human peripheral circulation. Biosci. Rep. 22, 407-420.
    • (2002) Biosci. Rep. , vol.22 , pp. 407-420
    • Delpino, A.1    Castelli, M.2
  • 24
    • 0037087262 scopus 로고    scopus 로고
    • Alphaactinin is a crossreactive renal target for pathogenic anti-DNA antibodies
    • Deocharan, B., Qing, X., Lichauco, J., and Putterman, C. (2002). Alphaactinin is a crossreactive renal target for pathogenic anti-DNA antibodies. J. Immunol. 168, 3072-3078.
    • (2002) J. Immunol. , vol.168 , pp. 3072-3078
    • Deocharan, B.1    Qing, X.2    Lichauco, J.3    Putterman, C.4
  • 25
    • 22544467505 scopus 로고    scopus 로고
    • More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle
    • Deprez, P., Gautschi, M., and Helenius, A. (2005). More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle. Mol. Cell 19, 183-195.
    • (2005) Mol. Cell , vol.19 , pp. 183-195
    • Deprez, P.1    Gautschi, M.2    Helenius, A.3
  • 26
    • 77952589171 scopus 로고    scopus 로고
    • GRP94 in ER quality control and stress responses
    • Eletto, D., Dersh, D., and Argon, Y. (2010). GRP94 in ER quality control and stress responses. Semin. Cell Dev. Biol. 21, 479-485.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 479-485
    • Eletto, D.1    Dersh, D.2    Argon, Y.3
  • 27
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: substrate interactions and functional properties
    • Ellgaard, L., and Ruddock, L. W. (2005). The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep. 6, 28-32.
    • (2005) EMBO Rep , vol.6 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 28
    • 9644275225 scopus 로고    scopus 로고
    • Autoantibodies to a collagenspecific molecular chaperone, heatshock protein 47, in systemic sclerosis
    • Fujimoto, M., Hamaguchi, Y., Yazawa, N., Komura, K., Takehara, K., and Sato, S. (2004). Autoantibodies to a collagenspecific molecular chaperone, heatshock protein 47, in systemic sclerosis. Clin. Exp. Immunol. 138, 534-539.
    • (2004) Clin. Exp. Immunol. , vol.138 , pp. 534-539
    • Fujimoto, M.1    Hamaguchi, Y.2    Yazawa, N.3    Komura, K.4    Takehara, K.5    Sato, S.6
  • 30
    • 80053952650 scopus 로고    scopus 로고
    • Chaperoneassisted protein folding: the path to discovery from a personal perspective
    • Hartl, F. U. (2011). Chaperoneassisted protein folding: the path to discovery from a personal perspective. Nat. Med. 17, 1206-1210.
    • (2011) Nat. Med. , vol.17 , pp. 1206-1210
    • Hartl, F.U.1
  • 31
    • 0032576992 scopus 로고    scopus 로고
    • Isolation and characterization of a rheumatoid arthritisspecific antigen (RA-A47) from a human chondrocytic cell line (HCS-2/8)
    • Hattori, T., Fujisawa, T., Sasaki, K., Yutani, Y., Nakanishi, T., Takahashi, K., and Takigawa, M. (1998). Isolation and characterization of a rheumatoid arthritisspecific antigen (RA-A47) from a human chondrocytic cell line (HCS-2/8). Biochem. Biophys. Res. Commun. 245, 679-683.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 679-683
    • Hattori, T.1    Fujisawa, T.2    Sasaki, K.3    Yutani, Y.4    Nakanishi, T.5    Takahashi, K.6    Takigawa, M.7
  • 32
    • 0141595092 scopus 로고    scopus 로고
    • Downregulation of a rheumatoid arthritisrelated antigen (RA-A47) by raa47 antisense oligonucleotides induces inflammatory factors in chondrocytes
    • Hattori, T., Kawaki, H., Kubota, S., Yutani, Y., De Crombrugghe, B., Von Der Mark, K., and Takigawa, M. (2003). Downregulation of a rheumatoid arthritisrelated antigen (RA-A47) by raa47 antisense oligonucleotides induces inflammatory factors in chondrocytes. J. Cell. Physiol. 197, 94-102.
    • (2003) J. Cell. Physiol. , vol.197 , pp. 94-102
    • Hattori, T.1    Kawaki, H.2    Kubota, S.3    Yutani, Y.4    De Crombrugghe, B.5    Von Der Mark, K.6    Takigawa, M.7
  • 33
    • 0035149654 scopus 로고    scopus 로고
    • Change in cellular localization of a rheumatoid arthritisrelated antigen (RA-A47) with downregulation upon stimulation by inflammatory cytokines in chondrocytes
    • Hattori, T., Kubota, S., Yutani, Y., Fuji-Sawa, T., Nakanishi, T., Takahashi, K., and Takigawa, M. (2001). Change in cellular localization of a rheumatoid arthritisrelated antigen (RA-A47) with downregulation upon stimulation by inflammatory cytokines in chondrocytes. J. Cell. Physiol. 186, 268-281.
    • (2001) J. Cell. Physiol. , vol.186 , pp. 268-281
    • Hattori, T.1    Kubota, S.2    Yutani, Y.3    Fuji-Sawa, T.4    Nakanishi, T.5    Takahashi, K.6    Takigawa, M.7
  • 34
    • 0033773162 scopus 로고    scopus 로고
    • Rheumatoid arthritisrelated antigen 47kDa (RA-A47) is a product of colligin-2 and acts as a human HSP47
    • Hattori,T.,Takahash,K.,Yutani,Y.,Fuji-Sawa,T.,Nakanishi,T.,and Takigawa, M. (2000). Rheumatoid arthritisrelated antigen 47kDa (RA-A47) is a product of colligin-2 and acts as a human HSP47. J. Bone Miner. Metab. 18, 328-334.
    • (2000) J. Bone Miner. Metab. , vol.18 , pp. 328-334
    • Hattori, T.1    Takahash, K.2    Yutani, Y.3    Fuji-Sawa, T.4    Nakanishi, T.5    Takigawa, M.6
  • 35
    • 10044236471 scopus 로고    scopus 로고
    • Downregulation of rheumatoid arthritisrelated antigen RA-A47 (HSP47/colligin-2) in chondrocytic cell lines induces apoptosis and cellsurface expression of RA-A47 in association with CD9
    • Hattori, T., Von Der Mark, K., Kawaki, H., Yutani, Y., Kubota, S., Nakanishi, T., Eberspaecher, H., De Crombrugghe, B., and Taki-Gawa, M. (2005). Downregulation of rheumatoid arthritisrelated antigen RA-A47 (HSP47/colligin-2) in chondrocytic cell lines induces apoptosis and cellsurface expression of RA-A47 in association with CD9. J. Cell. Physiol. 202, 191-204.
    • (2005) J. Cell. Physiol. , vol.202 , pp. 191-204
    • Hattori, T.1    Von Der Mark, K.2    Kawaki, H.3    Yutani, Y.4    Kubota, S.5    Nakanishi, T.6    Eberspaecher, H.7    De Crombrugghe, B.8    Taki-Gawa, M.9
  • 37
    • 0033135750 scopus 로고    scopus 로고
    • Cell surface colligin/Hsp47 associates with tetraspanin protein CD9 in epidermoid carcinoma cell lines
    • Hebert, C., Norris, K., Della Coletta, R., Reynolds, M., Ordonez, J., and Sauk, J. J. (1999). Cell surface colligin/Hsp47 associates with tetraspanin protein CD9 in epidermoid carcinoma cell lines. J. Cell. Biochem. 73, 248-258.
    • (1999) J. Cell. Biochem. , vol.73 , pp. 248-258
    • Hebert, C.1    Norris, K.2    Della Coletta, R.3    Reynolds, M.4    Ordonez, J.5    Sauk, J.J.6
  • 38
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert, D. N., Foellmer, B., and Helenius, A. (1995). Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81, 425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 40
    • 77951927662 scopus 로고    scopus 로고
    • The endoplasmic reticulum stressinducible protein, Herp, is a potential triggering antigen for anti-DNA response
    • Hirabayashi, Y., Oka, Y., Ikeda, T., Fujii, H., Ishii, T., Sasaki, T., and Harigae, H. (2010). The endoplasmic reticulum stressinducible protein, Herp, is a potential triggering antigen for anti-DNA response. J. Immunol. 184, 3276-3283.
    • (2010) J. Immunol. , vol.184 , pp. 3276-3283
    • Hirabayashi, Y.1    Oka, Y.2    Ikeda, T.3    Fujii, H.4    Ishii, T.5    Sasaki, T.6    Harigae, H.7
  • 41
    • 0033544930 scopus 로고    scopus 로고
    • Separate cisacting DNA elements control cell typeand tissuespecific expression of collagen binding molecular chaperone HSP47
    • Hirata, H., Yamamura, I., Yasuda, K., Kobayashi, A., Tada, N., Suzuki, M., Hirayoshi, K., Hosokawa, N., and Nagata, K. (1999). Separate cisacting DNA elements control cell typeand tissuespecific expression of collagen binding molecular chaperone HSP47. J. Biol. Chem. 274, 35703-35710.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35703-35710
    • Hirata, H.1    Yamamura, I.2    Yasuda, K.3    Kobayashi, A.4    Tada, N.5    Suzuki, M.6    Hirayoshi, K.7    Hosokawa, N.8    Nagata, K.9
  • 42
    • 75649114551 scopus 로고    scopus 로고
    • Mechanism and components of endoplasmic reticulumassociated degradation
    • Hoseki, J., Ushioda, R., and Nagata, K. (2010). Mechanism and components of endoplasmic reticulumassociated degradation. J. Biochem. 147, 19-25.
    • (2010) J. Biochem. , vol.147 , pp. 19-25
    • Hoseki, J.1    Ushioda, R.2    Nagata, K.3
  • 44
    • 34447320202 scopus 로고    scopus 로고
    • Fifty years of antids DNA antibodies: are we approaching journey's end?
    • Isenberg, D. A., Manson, J. J., Ehren-Stein, M. R., and Rahman, A. (2007). Fifty years of antids DNA antibodies: are we approaching journey's end? Rheumatology (Oxford) 46, 1052-1056.
    • (2007) Rheumatology (Oxford) , vol.46 , pp. 1052-1056
    • Isenberg, D.A.1    Manson, J.J.2    Ehren-Stein, M.R.3    Rahman, A.4
  • 45
    • 79959326422 scopus 로고    scopus 로고
    • Hsp47 as a collagenspecific molecular chaperone
    • Ishida, Y., and Nagata, K. (2011). Hsp47 as a collagenspecific molecular chaperone. Meth. Enzymol. 499, 167-182.
    • (2011) Meth. Enzymol. , vol.499 , pp. 167-182
    • Ishida, Y.1    Nagata, K.2
  • 46
    • 78951491490 scopus 로고    scopus 로고
    • The polypeptide binding conformation of calreticulin facilitates its cellsurface expression under conditions of endoplasmic reticulum stress
    • Jeffery, E., Peters, L. R., and Raghavan, M. (2011). The polypeptide binding conformation of calreticulin facilitates its cellsurface expression under conditions of endoplasmic reticulum stress. J. Biol. Chem. 286, 2402-2415.
    • (2011) J. Biol. Chem. , vol.286 , pp. 2402-2415
    • Jeffery, E.1    Peters, L.R.2    Raghavan, M.3
  • 47
    • 0031920272 scopus 로고    scopus 로고
    • Gastric administration of recombinant 65 kDa heat shock protein delays the severity of type II collagen induced arthritis in mice
    • Jorgensen, C., Gedon, E., Jaquet, C., and Sany, J. (1998). Gastric administration of recombinant 65 kDa heat shock protein delays the severity of type II collagen induced arthritis in mice. J. Rheumatol. 25, 763-767.
    • (1998) J. Rheumatol. , vol.25 , pp. 763-767
    • Jorgensen, C.1    Gedon, E.2    Jaquet, C.3    Sany, J.4
  • 48
    • 57249101996 scopus 로고    scopus 로고
    • High serum concentrations of autoantibodies to HSP47 in nonspecific interstitial pneumonia compared with idiopathic pulmonary fibrosis
    • doi:10.1186/1471-2466-8-23
    • Kakugawa, T., Yokota, S., Mukae, H., Kubota, H., Sakamoto, N., Mizu-Noe, S., Matsuoka, Y., Kadota, J., Fujii, N., Nagata, K., and Kohno, S. (2008). High serum concentrations of autoantibodies to HSP47 in nonspecific interstitial pneumonia compared with idiopathic pulmonary fibrosis. BMC Pulm. Med. 8, 23. doi:10.1186/1471-2466-8-23
    • (2008) BMC Pulm. Med. , vol.8 , pp. 23
    • Kakugawa, T.1    Yokota, S.2    Mukae, H.3    Kubota, H.4    Sakamoto, N.5    Mizu-Noe, S.6    Matsuoka, Y.7    Kadota, J.8    Fujii, N.9    Nagata, K.10    Kohno, S.11
  • 49
    • 22144447152 scopus 로고    scopus 로고
    • Gene expression in response to endoplasmic reticulum stress in Arabidopsis thaliana
    • Kamauchi, S., Nakatani, H., Nakano, C., and Urade, R. (2005). Gene expression in response to endoplasmic reticulum stress in Arabidopsis thaliana. FEBS J. 272, 3461-3476.
    • (2005) FEBS J , vol.272 , pp. 3461-3476
    • Kamauchi, S.1    Nakatani, H.2    Nakano, C.3    Urade, R.4
  • 51
    • 79953152999 scopus 로고    scopus 로고
    • Herp regulates Hrd1-mediated ubiquitylation in a ubiquitinlike domaindependent manner
    • Kny, M., Standera, S., Hartmann-Petersen, R., Kloetzel, P. M., and Seeger, M. (2011). Herp regulates Hrd1-mediated ubiquitylation in a ubiquitinlike domaindependent manner. J. Biol. Chem. 286, 5151-5156.
    • (2011) J. Biol. Chem. , vol.286 , pp. 5151-5156
    • Kny, M.1    Standera, S.2    Hartmann-Petersen, R.3    Kloetzel, P.M.4    Seeger, M.5
  • 52
    • 0034693217 scopus 로고    scopus 로고
    • Herp, a new ubiquitinlike membrane protein induced by endoplasmic reticulum stress
    • Kokame, K., Agarwala, K. L., Kato, H., and Miyata, T. (2000). Herp, a new ubiquitinlike membrane protein induced by endoplasmic reticulum stress. J. Biol. Chem. 275, 32846-32853.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32846-32853
    • Kokame, K.1    Agarwala, K.L.2    Kato, H.3    Miyata, T.4
  • 53
    • 0035937721 scopus 로고    scopus 로고
    • Identification of ERSE-II, a new cisacting element responsible for the ATF6-dependent mammalian unfolded protein response
    • Kokame, K., Kato, H., and Miyata, T. (2001). Identification of ERSE-II, a new cisacting element responsible for the ATF6-dependent mammalian unfolded protein response. J. Biol. Chem. 276, 9199-9205.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9199-9205
    • Kokame, K.1    Kato, H.2    Miyata, T.3
  • 54
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley, B. N., and Ploegh, H. L. (2004). A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429, 834-840.
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 55
    • 26244431960 scopus 로고    scopus 로고
    • Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane
    • Lilley, B. N., and Ploegh, H. L. (2005). Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane. Proc. Natl. Acad. Sci. U.S.A. 102, 14296-14301.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 14296-14301
    • Lilley, B.N.1    Ploegh, H.L.2
  • 56
    • 0346734122 scopus 로고    scopus 로고
    • Cell surface expression of an endoplasmic reticulum resident heat shock protein gp96 triggers MyD88-dependent systemic autoimmune diseases
    • Liu, B., Dai, J., Zheng, H., Stoilova, D., Sun, S., and Li, Z. (2003). Cell surface expression of an endoplasmic reticulum resident heat shock protein gp96 triggers MyD88-dependent systemic autoimmune diseases. Proc. Natl. Acad. Sci. U.S.A. 100, 15824-15829.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 15824-15829
    • Liu, B.1    Dai, J.2    Zheng, H.3    Stoilova, D.4    Sun, S.5    Li, Z.6
  • 57
    • 0027135438 scopus 로고
    • A calreticulinlike protein copurifies with a "60 kD" component of Ro/SSA, but is not recognized by antibodies in Sjogren's syndrome sera
    • Lu, J., Willis, A. C., and Sim, R. B. (1993). A calreticulinlike protein copurifies with a "60 kD" component of Ro/SSA, but is not recognized by antibodies in Sjogren's syndrome sera. Clin. Exp. Immunol. 94, 429-434.
    • (1993) Clin. Exp. Immunol. , vol.94 , pp. 429-434
    • Lu, J.1    Willis, A.C.2    Sim, R.B.3
  • 58
    • 0021333696 scopus 로고
    • Responsiveness of autoimmune and normal mice to nucleic acid antigens
    • Madaio, M. P., Hodder, S., Schwartz, R. S., and Stollar, B. D. (1984). Responsiveness of autoimmune and normal mice to nucleic acid antigens. J. Immunol. 132, 872-876.
    • (1984) J. Immunol. , vol.132 , pp. 872-876
    • Madaio, M.P.1    Hodder, S.2    Schwartz, R.S.3    Stollar, B.D.4
  • 60
    • 12344322951 scopus 로고    scopus 로고
    • Accumulation of type IV collagen in dilated ER leads to apoptosis in Hsp47-knockout mouse embryos via induction of CHOP
    • Marutani, T., Yamamoto, A., Nagai, N., Kubota, H., and Nagata, K. (2004). Accumulation of type IV collagen in dilated ER leads to apoptosis in Hsp47-knockout mouse embryos via induction of CHOP. J. Cell. Sci. 117, 5913-5922.
    • (2004) J. Cell. Sci. , vol.117 , pp. 5913-5922
    • Marutani, T.1    Yamamoto, A.2    Nagai, N.3    Kubota, H.4    Nagata, K.5
  • 61
    • 0028113925 scopus 로고
    • Coexpression of the collagenbinding stress protein HSP47 gene and the alpha 1(I) and alpha 1(III) collagen genes in carbon tetrachlorideinduced rat liver fibrosis
    • Masuda, H., Fukumoto, M., Hirayoshi, K., and Nagata, K. (1994). Coexpression of the collagenbinding stress protein HSP47 gene and the alpha 1(I) and alpha 1(III) collagen genes in carbon tetrachlorideinduced rat liver fibrosis. J. Clin. Invest. 94, 2481-2488.
    • (1994) J. Clin. Invest. , vol.94 , pp. 2481-2488
    • Masuda, H.1    Fukumoto, M.2    Hirayoshi, K.3    Nagata, K.4
  • 62
    • 0032406170 scopus 로고    scopus 로고
    • Expression and localization of collagenbinding stress protein Hsp47 in mouse embryo development: comparison with types I and II collagen
    • Masuda, H., Hosokawa, N., and Nagata, K. (1998). Expression and localization of collagenbinding stress protein Hsp47 in mouse embryo development: comparison with types I and II collagen. Cell Stress Chaperones 3, 256-264.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 256-264
    • Masuda, H.1    Hosokawa, N.2    Nagata, K.3
  • 63
    • 4644234938 scopus 로고    scopus 로고
    • Insufficient folding of type IV collagen and formation of abnormal basement membranelike structure in embryoid bodies derived from Hsp47-null embryonic stem cells
    • Matsuoka, Y., Kubota, H., Adachi, E., Nagai, N., Marutani, T., Hosokawa, N., and Nagata, K. (2004). Insufficient folding of type IV collagen and formation of abnormal basement membranelike structure in embryoid bodies derived from Hsp47-null embryonic stem cells. Mol. Biol. Cell 15, 4467-4475.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4467-4475
    • Matsuoka, Y.1    Kubota, H.2    Adachi, E.3    Nagai, N.4    Marutani, T.5    Hosokawa, N.6    Nagata, K.7
  • 64
    • 0025345647 scopus 로고
    • A human Ro/SS-A autoantigen is the homologue of calreticulin and is highly homologous with onchocercal RAL-1 antigen and an aplysia "memory molecule
    • McCauliffe, D. P., Zappi, E., Lieu, T. S., Michalak, M., Sontheimer, R. D., and Capra, J. D. (1990). A human Ro/SS-A autoantigen is the homologue of calreticulin and is highly homologous with onchocercal RAL-1 antigen and an aplysia "memory molecule." J. Clin. Invest. 86, 332-335.
    • (1990) J. Clin. Invest. , vol.86 , pp. 332-335
    • McCauliffe, D.P.1    Zappi, E.2    Lieu, T.S.3    Michalak, M.4    Sontheimer, R.D.5    Capra, J.D.6
  • 65
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP
    • McCracken, A. A., and Brodsky, J. L. (1996). Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J. Cell Biol. 132, 291-298.
    • (1996) J. Cell Biol. , vol.132 , pp. 291-298
    • McCracken, A.A.1    Brodsky, J.L.2
  • 67
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • Molinari, M., Calanca, V., Galli, C., Lucca, P., and Paganetti, P. (2003). Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299, 1397-1400.
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calanca, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 68
    • 0034716887 scopus 로고    scopus 로고
    • Tripartite management of unfolded proteins in the endoplasmic reticulum
    • Mori, K. (2000). Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell 101, 451-454
    • (2000) Cell , vol.101 , pp. 451-454
    • Mori, K.1
  • 69
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto, R. I. (1998). Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12, 3788-3796.
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 71
    • 50449107542 scopus 로고    scopus 로고
    • SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
    • Mueller, B., Klemm, E. J., Spooner, E., Claessen, J. H., and Ploegh, H. L. (2008). SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins. Proc. Natl. Acad. Sci. U.S.A. 105, 12325-12330
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 12325-12330
    • Mueller, B.1    Klemm, E.J.2    Spooner, E.3    Claessen, J.H.4    Ploegh, H.L.5
  • 72
    • 33750359201 scopus 로고    scopus 로고
    • SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER
    • Mueller, B., Lilley, B. N., and Ploegh, H. L. (2006). SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER. J. Cell Biol. 175, 261-270.
    • (2006) J. Cell Biol. , vol.175 , pp. 261-270
    • Mueller, B.1    Lilley, B.N.2    Ploegh, H.L.3
  • 73
    • 33645959208 scopus 로고    scopus 로고
    • Heat shock proteins in immunity
    • Multhoff, G. (2006). Heat shock proteins in immunity. Handb. Exp. Pharmacol. 172, 279-304.
    • (2006) Handb. Exp. Pharmacol. , vol.172 , pp. 279-304
    • Multhoff, G.1
  • 74
    • 0034683570 scopus 로고    scopus 로고
    • Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis
    • Nagai, N., Hosokawa, M., Itohara, S., Adachi, E., Matsushita, T., Hosokawa, N., and Nagata, K. (2000). Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. J. Cell Biol. 150, 1499-1506.
    • (2000) J. Cell Biol. , vol.150 , pp. 1499-1506
    • Nagai, N.1    Hosokawa, M.2    Itohara, S.3    Adachi, E.4    Matsushita, T.5    Hosokawa, N.6    Nagata, K.7
  • 75
    • 0742304951 scopus 로고    scopus 로고
    • HSP47 as a collagenspecific molecular chaperone: function and expression in normal mouse development
    • Nagata, K. (2003). HSP47 as a collagenspecific molecular chaperone: function and expression in normal mouse development. Semin. Cell Dev. Biol. 14, 275-282.
    • (2003) Semin. Cell Dev. Biol. , vol.14 , pp. 275-282
    • Nagata, K.1
  • 78
    • 34447558236 scopus 로고    scopus 로고
    • ER chaperones in mammalian development and human diseases
    • Ni, M., and Lee, A. S. (2007). ER chaperones in mammalian development and human diseases. FEBS Lett. 581, 3641-3651.
    • (2007) FEBS Lett , vol.581 , pp. 3641-3651
    • Ni, M.1    Lee, A.S.2
  • 79
    • 79953113775 scopus 로고    scopus 로고
    • Circulating heat shock protein 70 in health, aging and disease
    • doi:10.1186/1471-2172-12-24
    • Njemini, R., Bautmans, I., Onyema, O. O., Van Puyvelde, K., Demanet, C., and Mets, T. (2011). Circulating heat shock protein 70 in health, aging and disease. BMC Immunol. 12, 24. doi:10.1186/1471-2172-12-24
    • (2011) BMC Immunol , vol.12 , pp. 24
    • Njemini, R.1    Bautmans, I.2    Onyema, O.O.3    Van Puyvelde, K.4    Demanet, C.5    Mets, T.6
  • 80
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda, Y., Hosokawa, N., Wada, I., and Nagata, K. (2003). EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299, 1394-1397.
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 81
    • 31944450850 scopus 로고    scopus 로고
    • Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation
    • Oda, Y., Okada, T., Yoshida, H., Kauf-Man, R. J., Nagata, K., and Mori, K. (2006). Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation. J. Cell Biol. 172, 383-393.
    • (2006) J. Cell Biol. , vol.172 , pp. 383-393
    • Oda, Y.1    Okada, T.2    Yoshida, H.3    Kauf-Man, R.J.4    Nagata, K.5    Mori, K.6
  • 82
    • 0034680917 scopus 로고    scopus 로고
    • Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum
    • Okazaki, Y., Ohno, H., Takase, K., Ochiai, T., and Saito, T. (2000). Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum. J. Biol. Chem. 275, 35751-35758.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35751-35758
    • Okazaki, Y.1    Ohno, H.2    Takase, K.3    Ochiai, T.4    Saito, T.5
  • 83
    • 36249022750 scopus 로고    scopus 로고
    • Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp
    • Okuda-Shimizu, Y., and Hendershot, L. M. (2007). Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp. Mol. Cell 28, 544-554.
    • (2007) Mol. Cell , vol.28 , pp. 544-554
    • Okuda-Shimizu, Y.1    Hendershot, L.M.2
  • 84
    • 0029885782 scopus 로고    scopus 로고
    • Complete congenital heart block is associated with increased autoantibody titers against calreticulin
    • Orth, T., Dorner, T., Meyer Zum Buschenfelde, K. H., and Mayet, W. J. (1996). Complete congenital heart block is associated with increased autoantibody titers against calreticulin. Eur. J. Clin. Invest. 26, 205-215
    • (1996) Eur. J. Clin. Invest. , vol.26 , pp. 205-215
    • Orth, T.1    Dorner, T.2    Meyer Zum Buschenfelde, K.H.3    Mayet, W.J.4
  • 85
    • 0042071558 scopus 로고    scopus 로고
    • Identification and purification from the plasma of Type 1 diabetic subjects of a proteolytically active Grp94Evidence that Grp94 is entirely responsible for plasma proteolytic activity
    • Pagetta, A., Folda, A., Brunati, A. M., and Finotti, P. (2003). Identification and purification from the plasma of Type 1 diabetic subjects of a proteolytically active Grp94Evidence that Grp94 is entirely responsible for plasma proteolytic activity. Diabetologia 46, 996-1006.
    • (2003) Diabetologia , vol.46 , pp. 996-1006
    • Pagetta, A.1    Folda, A.2    Brunati, A.M.3    Finotti, P.4
  • 86
    • 31144432093 scopus 로고    scopus 로고
    • BiP regulates autoimmune inflammation and tissue damage
    • Panayi, G. S., and Corrigall, V. M. (2006). BiP regulates autoimmune inflammation and tissue damage. Autoimmun. Rev. 5, 140-142.
    • (2006) Autoimmun. Rev. , vol.5 , pp. 140-142
    • Panayi, G.S.1    Corrigall, V.M.2
  • 87
    • 0025284721 scopus 로고
    • Endogenous circulating DNA in systemic lupus erythematosus Occurrence as multimeric complexes bound to histone
    • Rumore, P. M., and Steinman, C. R. (1990). Endogenous circulating DNA in systemic lupus erythematosus. Occurrence as multimeric complexes bound to histone. J. Clin. Invest. 86, 69-74.
    • (1990) J. Clin. Invest. , vol.86 , pp. 69-74
    • Rumore, P.M.1    Steinman, C.R.2
  • 89
    • 67349165090 scopus 로고    scopus 로고
    • Latest update on the Ro/SS-A autoantibody system
    • Schulte-Pelkum, J., Fritzler, M., and Mahler, M. (2009). Latest update on the Ro/SS-A autoantibody system. Autoimmun. Rev. 8, 632-637.
    • (2009) Autoimmun. Rev. , vol.8 , pp. 632-637
    • Schulte-Pelkum, J.1    Fritzler, M.2    Mahler, M.3
  • 90
    • 81455161068 scopus 로고    scopus 로고
    • Detection of autoantibody to citrullinated BiP in rheumatoid arthritis patients and proinflammatory roles of citrullinated BiP in collageninduced arthritis
    • Shoda, H., Fujio, K., Shibuya, M., Oka-Mura, T., Sumitomo, S., Okamoto, A., Sawada, T., and Yamamoto, K. (2011). Detection of autoantibody to citrullinated BiP in rheumatoid arthritis patients and proinflammatory roles of citrullinated BiP in collageninduced arthritis. Arthritis Res. Ther. 13, R191.
    • (2011) Arthritis Res. Ther. , vol.13
    • Shoda, H.1    Fujio, K.2    Shibuya, M.3    Oka-Mura, T.4    Sumitomo, S.5    Okamoto, A.6    Sawada, T.7    Yamamoto, K.8
  • 91
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: targeting proteins for degradation in the endoplasmic reticulum
    • Smith, M. H., Ploegh, H. L., and Weiss-Man, J. S. (2011). Road to ruin: targeting proteins for degradation in the endoplasmic reticulum. Science 334, 1086-1090.
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weiss-Man, J.S.3
  • 93
    • 34948865716 scopus 로고    scopus 로고
    • Citrullination by peptidylarginine deiminase in rheumatoid arthritis
    • Suzuki, A., Yamada, R., and Yamamoto, K. (2007). Citrullination by peptidylarginine deiminase in rheumatoid arthritis. Ann. N. Y. Acad. Sci. 1108, 323-339.
    • (2007) Ann. N. Y. Acad. Sci. , vol.1108 , pp. 323-339
    • Suzuki, A.1    Yamada, R.2    Yamamoto, K.3
  • 95
    • 50249116184 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress response in immunity and autoimmunity
    • Todd, D. J., Lee, A. H., and Glimcher, L. H. (2008). The endoplasmic reticulum stress response in immunity and autoimmunity. Nat. Rev. Immunol. 8, 663-674.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 663-674
    • Todd, D.J.1    Lee, A.H.2    Glimcher, L.H.3
  • 96
    • 0036270698 scopus 로고    scopus 로고
    • Retrotranslocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B., Ye, Y., and Rapoport, T. A. (2002). Retrotranslocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol. 3, 246-255.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 97
    • 0029961386 scopus 로고    scopus 로고
    • 150-kD oxygenregulated protein is expressed in human atherosclerotic plaques and allows mononuclear phagocytes to withstand cellular stress on exposure to hypoxia and modified low density lipoprotein
    • Tsukamoto, Y., Kuwabara, K., Hirota, S., Ikeda, J., Stern, D., Yanagi, H., Matsumoto, M., Ogawa, S., and Kita-Mura, Y. (1996). 150-kD oxygenregulated protein is expressed in human atherosclerotic plaques and allows mononuclear phagocytes to withstand cellular stress on exposure to hypoxia and modified low density lipoprotein. J. Clin. Invest. 98, 1930-1941.
    • (1996) J. Clin. Invest. , vol.98 , pp. 1930-1941
    • Tsukamoto, Y.1    Kuwabara, K.2    Hirota, S.3    Ikeda, J.4    Stern, D.5    Yanagi, H.6    Matsumoto, M.7    Ogawa, S.8    Kita-Mura, Y.9
  • 98
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: mechanisms and consequences
    • Tu, B. P., and Weissman, J. S. (2004). Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell Biol. 164, 341-346.
    • (2004) J. Cell Biol. , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 99
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
    • Ushioda, R., Hoseki, J.,Araki, K., Jansen, G., Thomas, D. Y., and Nagata, K. (2008). ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321, 569-572.
    • (2008) Science , vol.321 , pp. 569-572
    • Ushioda, R.1    Hoseki, J.2    Araki, K.3    Jansen, G.4    Thomas, D.Y.5    Nagata, K.6
  • 100
    • 79251497991 scopus 로고    scopus 로고
    • The endoplasmic reticulumassociated degradation and disulfide reductase ERdj5
    • Ushioda, R., and Nagata, K. (2011). The endoplasmic reticulumassociated degradation and disulfide reductase ERdj5. Meth. Enzymol. 490, 235-258.
    • (2011) Meth. Enzymol. , vol.490 , pp. 235-258
    • Ushioda, R.1    Nagata, K.2
  • 102
    • 35548988445 scopus 로고    scopus 로고
    • Stress, heat shock proteins, and autoimmunity: how immune responses to heat shock proteins are to be used for the control of chronic inflammatory diseases
    • Van Eden, W., Wick, G., Albani, S., and Cohen, I. (2007). Stress, heat shock proteins, and autoimmunity: how immune responses to heat shock proteins are to be used for the control of chronic inflammatory diseases. Ann. N. Y. Acad. Sci. 1113, 217-237.
    • (2007) Ann. N. Y. Acad. Sci. , vol.1113 , pp. 217-237
    • Van Eden, W.1    Wick, G.2    Albani, S.3    Cohen, I.4
  • 105
    • 0242720407 scopus 로고    scopus 로고
    • PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease
    • Vossenaar, E. R., Zendman, A. J., Van Venrooij, W. J., and Pruijn, G. J. (2003). PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. Bioessays 25, 1106-1118.
    • (2003) Bioessays , vol.25 , pp. 1106-1118
    • Vossenaar, E.R.1    Zendman, A.J.2    Van Venrooij, W.J.3    Pruijn, G.J.4
  • 106
    • 23844434236 scopus 로고    scopus 로고
    • Breaking of tolerance to native DNA in nonautoimmune mice by immunization with natural protein/DNA complexes
    • Voynova, E. N., Tchorbanov, A. I., Todorov, T. A., and Vassilev, T. L. (2005). Breaking of tolerance to native DNA in nonautoimmune mice by immunization with natural protein/DNA complexes. Lupus 14, 543-550.
    • (2005) Lupus , vol.14 , pp. 543-550
    • Voynova, E.N.1    Tchorbanov, A.I.2    Todorov, T.A.3    Vassilev, T.L.4
  • 107
    • 0030815129 scopus 로고    scopus 로고
    • Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin
    • Wada, I., Kai, M., Imai, S., Sakane, F., and Kanoh, H. (1997). Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin. EMBO J. 16, 5420-5432.
    • (1997) EMBO J , vol.16 , pp. 5420-5432
    • Wada, I.1    Kai, M.2    Imai, S.3    Sakane, F.4    Kanoh, H.5
  • 109
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter, P., and Ron, D. (2011). The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 110
    • 34948853214 scopus 로고    scopus 로고
    • GRP94 is essential for mesoderm induction and muscle development because it regulates insulinlikegrowthfactorsecretion
    • Wanderling, S., Simen, B. B., Ostro-Vsky, O., Ahmed, N. T., Vogen, S. M., Gidalevitz, T., and Argon, Y. (2007). GRP94 is essential for mesoderm induction and muscle development because it regulates insulinlikegrowthfactorsecretion.Mol. Biol. Cell 18, 3764-3775.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3764-3775
    • Wanderling, S.1    Simen, B.B.2    Ostro-Vsky, O.3    Ahmed, N.T.4    Vogen, S.M.5    Gidalevitz, T.6    Argon, Y.7
  • 113
    • 0034163391 scopus 로고    scopus 로고
    • A conserved mycobacterial heat shock protein (hsp) 70 sequence prevents adjuvant arthritis upon nasal administration and induces IL-10-producing T cells that crossreact with the mammalian selfhsp70 homologue
    • Wendling, U., Paul, L., Van Der Zee, R., Prakken, B., Singh, M., and Van Eden, W. (2000). A conserved mycobacterial heat shock protein (hsp) 70 sequence prevents adjuvant arthritis upon nasal administration and induces IL-10-producing T cells that crossreact with the mammalian selfhsp70 homologue. J. Immunol. 164, 2711-2717.
    • (2000) J. Immunol. , vol.164 , pp. 2711-2717
    • Wendling, U.1    Paul, L.2    Van Der Zee, R.3    Prakken, B.4    Singh, M.5    Van Eden, W.6
  • 114
    • 33645080188 scopus 로고    scopus 로고
    • Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum
    • Williams, D. B. (2006). Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J. Cell. Sci. 119, 615-623.
    • (2006) J. Cell. Sci. , vol.119 , pp. 615-623
    • Williams, D.B.1
  • 116
    • 0032489281 scopus 로고    scopus 로고
    • Transcriptional activation of the mouse HSP47 gene in mouse osteoblast MC3T3-E1 cells by TGF-beta 1
    • Yamamura, I., Hirata, H., Hosokawa, N., and Nagata, K. (1998). Transcriptional activation of the mouse HSP47 gene in mouse osteoblast MC3T3-E1 cells by TGF-beta 1. Biochem. Biophys. Res. Commun. 244, 68-74.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 68-74
    • Yamamura, I.1    Hirata, H.2    Hosokawa, N.3    Nagata, K.4
  • 117
    • 0346037326 scopus 로고    scopus 로고
    • The Kruppellike factor Zf9 and proteins in the Sp1 family regulate the expression of HSP47, a collagenspecific molecular chaperone
    • Yasuda, K., Hirayoshi, K., Hirata, H., Kubota, H., Hosokawa, N., and Nagata, K. (2002). The Kruppellike factor Zf9 and proteins in the Sp1 family regulate the expression of HSP47, a collagenspecific molecular chaperone. J. Biol. Chem. 277, 44613-44622.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44613-44622
    • Yasuda, K.1    Hirayoshi, K.2    Hirata, H.3    Kubota, H.4    Hosokawa, N.5    Nagata, K.6
  • 118
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H. H., and Rapoport, T. A. (2001). The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414, 652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 119
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye, Y., Meyer, H. H., and Rapoport, T. A. (2003). Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162, 71-84.
    • (2003) J. Cell Biol. , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 120
    • 77951710442 scopus 로고    scopus 로고
    • Immunomodulatory activity of extracellular heat shock proteins and their autoantibodies
    • Yokota, S., and Fujii, N. (2010). Immunomodulatory activity of extracellular heat shock proteins and their autoantibodies. Microbiol. Immunol. 54, 299-307.
    • (2010) Microbiol. Immunol. , vol.54 , pp. 299-307
    • Yokota, S.1    Fujii, N.2
  • 122
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • Yoshida, H. (2007). ER stress and diseases. FEBS J. 274, 630-658.
    • (2007) FEBS J , vol.274 , pp. 630-658
    • Yoshida, H.1
  • 123
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cisacting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucoseregulated proteins Involvement of basic leucine zipper transcription factors
    • Yoshida, H., Haze, K., Yanagi, H., Yura, T., and Mori, K. (1998). Identification of the cisacting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucoseregulated proteins. Involvement of basic leucine zipper transcription factors. J. Biol. Chem. 273, 33741-33749.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.