메뉴 건너뛰기




Volumn 10, Issue 7, 1998, Pages 943-950

T cells discriminate between differentially phosphorylated forms of αB-crystallin, a major central nervous system myelin antigen

Author keywords

B crystallin; Epitope analysis; Heal shock protein; I A(s) binding motif; Phosphorylation; Post translational modification; TCR

Indexed keywords

ALPHA CRYSTALLIN; MYELIN;

EID: 0031842239     PISSN: 09538178     EISSN: None     Source Type: Journal    
DOI: 10.1093/intimm/10.7.943     Document Type: Article
Times cited : (63)

References (31)
  • 1
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
    • Stern, L. J., Brown, J, H., Jardetzky, T. S., Gorga, J. C., Urban, R. G., Strominger, J. L. and Wiley, D. C. 1994. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 368:215.
    • (1994) Nature , vol.368 , pp. 215
    • Stern, L.J.1    Brown, J.H.2    Jardetzky, T.S.3    Gorga, J.C.4    Urban, R.G.5    Strominger, J.L.6    Wiley, D.C.7
  • 3
    • 0024428038 scopus 로고
    • Tumor necrosis factor-α induces the phosphorylation of 28kDa stress proteins in endothelial cells: Possible role in protection against cytotoxicity?
    • Robaye, B., Hepburn, A., Lecocq, R., Fiers, W., Boeynaems, J.-M. and Dumont, J. E. 1989. Tumor necrosis factor-α induces the phosphorylation of 28kDa stress proteins in endothelial cells: possible role in protection against cytotoxicity? Biochem. Biophys. Res. Commun. 163:301.
    • (1989) Biochem. Biophys. Res. Commun. , vol.163 , pp. 301
    • Robaye, B.1    Hepburn, A.2    Lecocq, R.3    Fiers, W.4    Boeynaems, J.-M.5    Dumont, J.E.6
  • 5
    • 0025933221 scopus 로고
    • Phosphorylation of α-crystallin B in Alexander's disease brain
    • Mann, E., McDermott, M. J., Goldman, J., Chiesa, R. and Spector, A. 1991. Phosphorylation of α-crystallin B in Alexander's disease brain. FEBS Lett. 294:133.
    • (1991) FEBS Lett. , vol.294 , pp. 133
    • Mann, E.1    McDermott, M.J.2    Goldman, J.3    Chiesa, R.4    Spector, A.5
  • 6
    • 0027724243 scopus 로고
    • Overexpression and abnormal modification of the stress proteins αB-crystallin and HSP27 in Alexander disease
    • Head, M. W., Corbin, E. and Goldman, J. E. 1993. Overexpression and abnormal modification of the stress proteins αB-crystallin and HSP27 in Alexander disease. Am. J. Pathol. 143:1743.
    • (1993) Am. J. Pathol. , vol.143 , pp. 1743
    • Head, M.W.1    Corbin, E.2    Goldman, J.E.3
  • 7
    • 0029018625 scopus 로고
    • 2 but phosphorylation has no effect on chaperone activity
    • 2 but phosphorylation has no effect on chaperone activity. Exp. Eye Res. 61:115.
    • (1995) Exp. Eye Res. , vol.61 , pp. 115
    • Wang, K.1    Ma, W.2    Spector, A.3
  • 10
    • 0030613774 scopus 로고    scopus 로고
    • Phosphorylation of αB-crystallin in response to various types of stress
    • Ito, H., Okamoto, K., Nakayama, H., Isobe, T. and Kato, K. 1997. Phosphorylation of αB-crystallin in response to various types of stress. J. Biol. Chem. 272:29934.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29934
    • Ito, H.1    Okamoto, K.2    Nakayama, H.3    Isobe, T.4    Kato, K.5
  • 11
    • 0023888625 scopus 로고
    • Definition and comparison of the phosphorylation sites of the a and B chains of bovine alpha-crystallin
    • Chiesa, R., Gawinowicz-Kolks, M. A., Kleirnan, N. J. and Spector, A. 1988. Definition and comparison of the phosphorylation sites of the A and B chains of bovine alpha-crystallin. Exp. Eye Res. 46:199.
    • (1988) Exp. Eye Res. , vol.46 , pp. 199
    • Chiesa, R.1    Gawinowicz-Kolks, M.A.2    Kleirnan, N.J.3    Spector, A.4
  • 13
    • 0027074090 scopus 로고
    • Identification of the posttranslational modifications of bovine lens αB-crystallins by mass spectrometry
    • Smith, J. B., Sun, Y., Smith, D. L. and Green, B. 1992. Identification of the posttranslational modifications of bovine lens αB-crystallins by mass spectrometry. Protein Sci. 1:601.
    • (1992) Protein Sci. , vol.1 , pp. 601
    • Smith, J.B.1    Sun, Y.2    Smith, D.L.3    Green, B.4
  • 14
    • 0027256807 scopus 로고
    • Identification of a major encephalitogenic epitope of proteolipid protein (residues 56-70) for the induction of experimental allergic encephalomyelitis in Biozzi AB/H and nonobese diabetic mice
    • Amor, S., Baker, D., Groome, N. and Turk, J. L. 1993. Identification of a major encephalitogenic epitope of proteolipid protein (residues 56-70) for the induction of experimental allergic encephalomyelitis in Biozzi AB/H and nonobese diabetic mice. J. Immunol. 150:5666.
    • (1993) J. Immunol. , vol.150 , pp. 5666
    • Amor, S.1    Baker, D.2    Groome, N.3    Turk, J.L.4
  • 16
    • 0001433241 scopus 로고
    • Knowledge based modelling of homologous proteins. Part I: Three-dimensional frameworks derived from the simultaneous superposition of multiple structures
    • Sutcliffe, M. J., Haneef, I., Carney, D. and Blundell, T. L. 1987. Knowledge based modelling of homologous proteins. Part I: three-dimensional frameworks derived from the simultaneous superposition of multiple structures. Protein Eng. 1:377.
    • (1987) Protein Eng. , vol.1 , pp. 377
    • Sutcliffe, M.J.1    Haneef, I.2    Carney, D.3    Blundell, T.L.4
  • 17
    • 0000179199 scopus 로고
    • Knowledge based modelling of homologous proteins, Part II: Rules for the conformations of substituted side chains
    • Sutcliffe, M. J., Hayes, F. R. and Blundell, T. L. 1987. Knowledge based modelling of homologous proteins, Part II: Rules for the conformations of substituted side chains. Protein Eng. 1:385.
    • (1987) Protein Eng. , vol.1 , pp. 385
    • Sutcliffe, M.J.1    Hayes, F.R.2    Blundell, T.L.3
  • 18
    • 0022974996 scopus 로고
    • T cell epitope of the autoantigen myelin basic protein that induces encephalomyelitis
    • Zamvil, S. S., Mitchell, D. J., Moore, A. C., Kitamura, K., Steinman, L. and Rothbard, J. B. 1986, T cell epitope of the autoantigen myelin basic protein that induces encephalomyelitis. Nature 324:258.
    • (1986) Nature , vol.324 , pp. 258
    • Zamvil, S.S.1    Mitchell, D.J.2    Moore, A.C.3    Kitamura, K.4    Steinman, L.5    Rothbard, J.B.6
  • 21
    • 0022445121 scopus 로고
    • Sequence analysis and structure-function correlations of murine q, k, u, s, and f haplotype I-A beta cDNA clones
    • Estess, P., Begovich, A. B., Koo, M., Jones, P. P. and McDevitt, H. O. 1986 Sequence analysis and structure-function correlations of murine q, k, u, s, and f haplotype I-A beta cDNA clones. Proc. Natl Acad. Sci. USA 83:3594.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 3594
    • Estess, P.1    Begovich, A.B.2    Koo, M.3    Jones, P.P.4    McDevitt, H.O.5
  • 24
    • 0029788330 scopus 로고    scopus 로고
    • Antigen processing and presentation of a naturally glycosylated protein elicits major histocompatibility complex class II-restricted, carbohydrate-specific T cells
    • Michaelsson, E., Broddefalk, J., Engstrom, A., Kihlberg, J. and Holmdahl, R. 1996. Antigen processing and presentation of a naturally glycosylated protein elicits major histocompatibility complex class II-restricted, carbohydrate-specific T cells. Eur. J. Immunol. 26:1906.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1906
    • Michaelsson, E.1    Broddefalk, J.2    Engstrom, A.3    Kihlberg, J.4    Holmdahl, R.5
  • 25
    • 0030891492 scopus 로고    scopus 로고
    • Proteins phosphorylated during stress-induced apoptosis are common targets for autoantibody production in patients with systemic lupus erythematosus
    • Utz, P. J., Hottelet, M., Schur, P. H. and Anderson, P. 1997. Proteins phosphorylated during stress-induced apoptosis are common targets for autoantibody production in patients with systemic lupus erythematosus. J. Exp. Med. 185:843.
    • (1997) J. Exp. Med. , vol.185 , pp. 843
    • Utz, P.J.1    Hottelet, M.2    Schur, P.H.3    Anderson, P.4
  • 26
    • 0025210036 scopus 로고
    • Induction of HSP27 phosphorylation and thermoresistance in Chinese hamster cells by arsenite, cycloheximide, A23187, and EGTA
    • Crete, P. and Landry, J. 1990. Induction of HSP27 phosphorylation and thermoresistance in Chinese hamster cells by arsenite, cycloheximide, A23187, and EGTA. Radiat. Res. 121:320.
    • (1990) Radiat. Res. , vol.121 , pp. 320
    • Crete, P.1    Landry, J.2
  • 27
    • 0026570931 scopus 로고
    • Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II
    • Landry J., Lambert, H., Zhou, M., Lavoie, J. N., Hickey, E., Weber, L. A. and Anderson, C. W. 1992. Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II. J. Biol. Chem. 267:794.
    • (1992) J. Biol. Chem. , vol.267 , pp. 794
    • Landry, J.1    Lambert, H.2    Zhou, M.3    Lavoie, J.N.4    Hickey, E.5    Weber, L.A.6    Anderson, C.W.7
  • 28
    • 0028015872 scopus 로고
    • Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27
    • Freshney, N. W., Rawlinson, L., Guesdon, F., Jones, E., Cowley, S., Hsuan, J. and Saklatvala, J. 1994. Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27. Cell 78:1039.
    • (1994) Cell , vol.78 , pp. 1039
    • Freshney, N.W.1    Rawlinson, L.2    Guesdon, F.3    Jones, E.4    Cowley, S.5    Hsuan, J.6    Saklatvala, J.7
  • 29
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse, J., Cohen, P., Trigon, S., Morange, M., Alonso-Llamazares, A., Zamanillo, D., Hunt, T. and Nebreda, A. R. 1994. A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell 78:1027.
    • (1994) Cell , vol.78 , pp. 1027
    • Rouse, J.1    Cohen, P.2    Trigon, S.3    Morange, M.4    Alonso-Llamazares, A.5    Zamanillo, D.6    Hunt, T.7    Nebreda, A.R.8
  • 30
    • 0023741341 scopus 로고
    • Enhanced constitutive expression of the 27-kDa heat shock proteins in heat-resistant variants from Chinese hamster cells
    • Chretien, P. and Landry, J. 1988. Enhanced constitutive expression of the 27-kDa heat shock proteins in heat-resistant variants from Chinese hamster cells. J. Cell. Physiol. 137:157.
    • (1988) J. Cell. Physiol. , vol.137 , pp. 157
    • Chretien, P.1    Landry, J.2
  • 31
    • 0027957356 scopus 로고
    • Stress- and mitogen-induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance
    • Knauf, U., Jakob, U., Engel, K., Buchner, J. and Gaestel, M. 1994. Stress- and mitogen-induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance. EMBO J. 13:54.
    • (1994) EMBO J. , vol.13 , pp. 54
    • Knauf, U.1    Jakob, U.2    Engel, K.3    Buchner, J.4    Gaestel, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.