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Volumn 378, Issue 10, 1997, Pages 1183-1186

Autokinase activity of α-crystallin inhibits its specific interaction with the DOTIS element in the murine γD/E/F-Crystallin promoter in vitro

Author keywords

crystallin; DNA protein interaction; Phosphorylation

Indexed keywords

ALPHA CRYSTALLIN;

EID: 0030684773     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (17)
  • 2
    • 0024584286 scopus 로고
    • Differential synthesis and phosphorylation of the α-crystallin a and B chains during bovine lens fiber cell differentiation
    • Chiesa, R., McDermott, M.J., and Spector, A. (1989). Differential synthesis and phosphorylation of the α-crystallin A and B chains during bovine lens fiber cell differentiation. Curr. Eye Res. 8, 151-158.
    • (1989) Curr. Eye Res. , vol.8 , pp. 151-158
    • Chiesa, R.1    McDermott, M.J.2    Spector, A.3
  • 3
    • 0023888625 scopus 로고
    • Definition and comparison of the phosphorylation sites of the a and B chains of bovine α-crystallin
    • Chiesa, R., Gawinowicz-Kolks, M.A., Kleiman, N.J., and Spector, A. (1988). Definition and comparison of the phosphorylation sites of the A and B chains of bovine α-crystallin. Exp. Eye Res. 46, 199-208.
    • (1988) Exp. Eye Res. , vol.46 , pp. 199-208
    • Chiesa, R.1    Gawinowicz-Kolks, M.A.2    Kleiman, N.J.3    Spector, A.4
  • 4
    • 0026777207 scopus 로고
    • Temporal regulation of six crystallin transcripts during mouse lens development
    • Goring, D.R., Breitman, M.L., and Tsui, L.-C. (1992). Temporal regulation of six crystallin transcripts during mouse lens development. Exp. Eye Res. 54, 785-795.
    • (1992) Exp. Eye Res. , vol.54 , pp. 785-795
    • Goring, D.R.1    Breitman, M.L.2    Tsui, L.-C.3
  • 6
  • 7
    • 0028023344 scopus 로고
    • Structure and modifications of the junior chaperone α-crystallin. From lens transparency to molecular pathology
    • Groenen, P.J.T.A., Merck, K.B., de Jong, W.W., and Bloemendal, H. (1994). Structure and modifications of the junior chaperone α-crystallin. From lens transparency to molecular pathology. Eur. J. Biochem. 225, 1-19.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 1-19
    • Groenen, P.J.T.A.1    Merck, K.B.2    De Jong, W.W.3    Bloemendal, H.4
  • 9
    • 0022235381 scopus 로고
    • Complete structure of the hamster αA crystallin gene. Reflection of an evolutionary history by means of exon shuffling
    • van den Heuvel, R., Hendriks, W., Quax, W., and Bloemendal, H. (1985). Complete structure of the hamster αA crystallin gene. Reflection of an evolutionary history by means of exon shuffling. J. Mol. Biol. 185, 273-284.
    • (1985) J. Mol. Biol. , vol.185 , pp. 273-284
    • Van Den Heuvel, R.1    Hendriks, W.2    Quax, W.3    Bloemendal, H.4
  • 11
    • 0028180509 scopus 로고
    • α-Crystallin/small heat-shock protein has autokinase activity
    • Kantorow, M., and Piatigorsky, J. (1994). α-Crystallin/small heat-shock protein has autokinase activity. Proc. Natl. Acad. Sci. USA 91, 3112-3116.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3112-3116
    • Kantorow, M.1    Piatigorsky, J.2
  • 12
    • 0029083170 scopus 로고
    • Conversion from oligomers to tetramers enhances autophosphorylation by lens αA-crystallin
    • Kantorow, M., Horwitz, J., van Boekel, M.A.M., de Jong, W.W., and Piatigorsky, J. (1995). Conversion from oligomers to tetramers enhances autophosphorylation by lens αA-crystallin. J. Biol. Chem. 270, 17215-17200.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17215-117200
    • Kantorow, M.1    Horwitz, J.2    Van Boekel, M.A.M.3    De Jong, W.W.4    Piatigorsky, J.5
  • 13
    • 0002527685 scopus 로고
    • Untersuchungen der Proteinsubstanzen in den lichtbrechenden Medien des Auges
    • Mörner, C.T. (1893). Untersuchungen der Proteinsubstanzen in den lichtbrechenden Medien des Auges. Z. Physiol. Chem. 18, 61-106.
    • (1893) Z. Physiol. Chem. , vol.18 , pp. 61-106
    • Mörner, C.T.1
  • 14
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • Pearson, R.B., and Kemp, B.E. (1991). Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. Meth. Enzymol. 200, 62-81.
    • (1991) Meth. Enzymol. , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 15
    • 0028168805 scopus 로고
    • α-Crystallins are involved in specific interactions with the murine γD/E/F-crystallin encoding gene
    • Pietrowski, D., Durante, M.J., Liebstein, A., Schmitt-John, T., Werner, T., and Graw, J. (1994). α-Crystallins are involved in specific interactions with the murine γD/E/F-crystallin encoding gene. Gene 144, 171-178.
    • (1994) Gene , vol.144 , pp. 171-178
    • Pietrowski, D.1    Durante, M.J.2    Liebstein, A.3    Schmitt-John, T.4    Werner, T.5    Graw, J.6
  • 16
    • 0022366830 scopus 로고
    • CAMP-dependent phosphorylation of bovine lens α-crystallin
    • Spector, A., Chiesa, R., Sredy, J., and Garner, W. (1985). cAMP-dependent phosphorylation of bovine lens α-crystallin. Proc. Natl. Acad. Sci. USA 82, 4712-4716.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4712-4716
    • Spector, A.1    Chiesa, R.2    Sredy, J.3    Garner, W.4
  • 17
    • 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, 115-124.
    • (1995) Exp. Eye Res. , vol.61 , pp. 115-124
    • Wang, K.1    Ma, W.2    Spector, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.