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Volumn 207, Issue 1, 1996, Pages 75-88

Spatial and temporal activity of the αB-crystallin/small heat shock protein gene promoter in transgenic mice

Author keywords

Crystallin; Development; Heat Shock; Promoter; Transgenic Mouse

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; CRYSTALLIN; HEAT SHOCK PROTEIN;

EID: 0029781314     PISSN: 10588388     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0177(199609)207:1<75::AID-AJA8>3.0.CO;2-T     Document Type: Article
Times cited : (52)

References (80)
  • 1
    • 0026341897 scopus 로고
    • αB-crystallin in skeletal muscle: Purification and localization
    • Atomi, Y., Yamada, S., Strohman, R., and Nonomura, Y. (1991) αB-crystallin in skeletal muscle: Purification and localization. J. Biochem. 110:812-822.
    • (1991) J. Biochem. , vol.110 , pp. 812-822
    • Atomi, Y.1    Yamada, S.2    Strohman, R.3    Nonomura, Y.4
  • 2
    • 0025130408 scopus 로고
    • Coexpression of α-sarcomeric actin, α-smooth muscle actin and desmin during myogenesis in rat and mouse embryos. I. Skeletal muscle
    • Babai, F., Musevi-Aghdam, J., Schurch, W., Royal, A., and Gabbiani, G. (1990) Coexpression of α-sarcomeric actin, α-smooth muscle actin and desmin during myogenesis in rat and mouse embryos. I. Skeletal muscle. Differentiation 144:132-142.
    • (1990) Differentiation , vol.144 , pp. 132-142
    • Babai, F.1    Musevi-Aghdam, J.2    Schurch, W.3    Royal, A.4    Gabbiani, G.5
  • 3
    • 0026694490 scopus 로고
    • αB-crystallin in cardiac tissue: Association with actin and desmin filaments
    • Bennardini, F., Wrzosek, A., and Chiesi, M. (1992) αB-crystallin in cardiac tissue: Association with actin and desmin filaments. Circ. Res. 71:288-294.
    • (1992) Circ. Res. , vol.71 , pp. 288-294
    • Bennardini, F.1    Wrzosek, A.2    Chiesi, M.3
  • 4
    • 0024578954 scopus 로고
    • αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues
    • Bhat, S.P., and Nagineni, C.N. (1989) αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues. Biochem. Biophys. Res. Commun. 158:319-325.
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 319-325
    • Bhat, S.P.1    Nagineni, C.N.2
  • 7
    • 0026534294 scopus 로고
    • Making muscles in mammals
    • Buckingham, M. (1992) Making muscles in mammals. Trends Genet. 8:144-149.
    • (1992) Trends Genet. , vol.8 , pp. 144-149
    • Buckingham, M.1
  • 8
    • 0028831015 scopus 로고
    • In vitro studies on the assembly properties of the lens proteins CP49, CP115: Coassembly with α-crystallin but not with vimentin
    • Carter, J.M., Hutcheson, A.M., and Quinlan, R.A. (1995) In vitro studies on the assembly properties of the lens proteins CP49, CP115: Coassembly with α-crystallin but not with vimentin. Exp. Eye Res. 60:181-192.
    • (1995) Exp. Eye Res. , vol.60 , pp. 181-192
    • Carter, J.M.1    Hutcheson, A.M.2    Quinlan, R.A.3
  • 9
    • 0025176675 scopus 로고
    • A simple screening method for transgenic mice using the polymerase chain reaction
    • Chen, S., and Evans, G.A. (1990) A simple screening method for transgenic mice using the polymerase chain reaction. BioTechniques 8:32-33.
    • (1990) BioTechniques , vol.8 , pp. 32-33
    • Chen, S.1    Evans, G.A.2
  • 10
    • 0023644471 scopus 로고
    • The phosphorylation of the primary gene products of alpha-crystallin
    • Chiesa, R., Gawinowicz-Kolks, M.A., and Spector, A. (1987) The phosphorylation of the primary gene products of alpha-crystallin. J. Biol. Chem. 262:1438-1441.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1438-1441
    • Chiesa, R.1    Gawinowicz-Kolks, M.A.2    Spector, A.3
  • 11
    • 0026534772 scopus 로고
    • Hypertonic stress induces αB-crystallin expression
    • Dasgupta, S., Hohman, T.C., and Carper, D. (1992) Hypertonic stress induces αB-crystallin expression. Exp. Eye Res. 54:461-470.
    • (1992) Exp. Eye Res. , vol.54 , pp. 461-470
    • Dasgupta, S.1    Hohman, T.C.2    Carper, D.3
  • 13
    • 0027472047 scopus 로고
    • Evolution of the α-crystallin/small heat-shock protein family
    • de Jong, W.W., Leunissen, J.A.M., and Voorter, C.E.M. (1993) Evolution of the α-crystallin/small heat-shock protein family. Mol. Biol. Evol. 10:103-126.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 103-126
    • De Jong, W.W.1    Leunissen, J.A.M.2    Voorter, C.E.M.3
  • 14
    • 0021749672 scopus 로고
    • The relationship between stress fiber-like structures and nascent myofibrils in cultured cardiac myocytes
    • Dlugosz, A.A., Antin, P.B., Nachmias, V.T., and Holtzer, H. (1984) The relationship between stress fiber-like structures and nascent myofibrils in cultured cardiac myocytes. J. Cell Biol. 99:2268-2278.
    • (1984) J. Cell Biol. , vol.99 , pp. 2268-2278
    • Dlugosz, A.A.1    Antin, P.B.2    Nachmias, V.T.3    Holtzer, H.4
  • 15
    • 0024580908 scopus 로고
    • Expression of the murine αB-crystallin gene is not restricted to the lens
    • Dubin, R.A., Wawrousek, E.F., and Piatigorsky, J. (1989) Expression of the murine αB-crystallin gene is not restricted to the lens. Mol. Cell. Biol. 9:1083-1091.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1083-1091
    • Dubin, R.A.1    Wawrousek, E.F.2    Piatigorsky, J.3
  • 16
    • 0025785768 scopus 로고
    • Expression of the murine αB-crystallin gene in lens and skeletal muscle: Identification of a muscle-preferred enhancer
    • Dubin, R.A., Gopal-Srivastava, R., Wawrousek, E.F., and Piatigorsky, J. (1991) Expression of the murine αB-crystallin gene in lens and skeletal muscle: Identification of a muscle-preferred enhancer. Mol. Cell. Biol. 11:4340-4349.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4340-4349
    • Dubin, R.A.1    Gopal-Srivastava, R.2    Wawrousek, E.F.3    Piatigorsky, J.4
  • 17
    • 0026443780 scopus 로고
    • The gene for the helix-loop-helix protein, Id, is specifically expressed in neural precursors
    • Duncan, M.K., DiCicco-Bloom, E.M., Xiang, X., Benezra, R., and Chada, K. (1992) The gene for the helix-loop-helix protein, Id, is specifically expressed in neural precursors. Dev. Biol. 154:1-10.
    • (1992) Dev. Biol. , vol.154 , pp. 1-10
    • Duncan, M.K.1    DiCicco-Bloom, E.M.2    Xiang, X.3    Benezra, R.4    Chada, K.5
  • 18
    • 0028987659 scopus 로고
    • Chicken βB1-crystallin: Gene sequence and evidence for functional conservation of promoter activity between chicken and mouse
    • Duncan, M.K., Roth, H.J., Thompson, M., Kantorow, M., and Piatigorsky, J. (1995) Chicken βB1-crystallin: Gene sequence and evidence for functional conservation of promoter activity between chicken and mouse. Biochim. Biophys. Acta 1261:68-76.
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 68-76
    • Duncan, M.K.1    Roth, H.J.2    Thompson, M.3    Kantorow, M.4    Piatigorsky, J.5
  • 20
    • 0028586015 scopus 로고
    • Structure and alternate tissue-preferred transcription initiation of the mouse αB-crystallin/small heat shock protein gene
    • Frederikse, P.H., Dubin, R.A., Haynes II, J.I., and Piatigorsky, J. (1994) Structure and alternate tissue-preferred transcription initiation of the mouse αB-crystallin/small heat shock protein gene. Nucleic Acids Res. 22:5686-5694.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5686-5694
    • Frederikse, P.H.1    Dubin, R.A.2    Haynes II, J.I.3    Piatigorsky, J.4
  • 21
    • 0027193606 scopus 로고
    • Development and tissue-specific distribution of mouse small heat shock protein hsp25
    • Gernold, M., Knauf, U., Gaestel, M., Stahl, J., and Kloetzel, P.-M. (1993) Development and tissue-specific distribution of mouse small heat shock protein hsp25. Dev. Gen. 14:103-111.
    • (1993) Dev. Gen. , vol.14 , pp. 103-111
    • Gernold, M.1    Knauf, U.2    Gaestel, M.3    Stahl, J.4    Kloetzel, P.-M.5
  • 22
    • 0026076159 scopus 로고
    • Rosenthal fibers contain ubiquitinated alpha B-crystallin
    • Goldman, J.E., and Corbin, E. (1991) Rosenthal fibers contain ubiquitinated alpha B-crystallin. Am. J. Pathol. 139:933-938.
    • (1991) Am. J. Pathol. , vol.139 , pp. 933-938
    • Goldman, J.E.1    Corbin, E.2
  • 23
    • 0027330980 scopus 로고
    • The murine αB-crystallin/small heat shock protein enhancer: Identification of αBE-1, αBE-2, αBE-3, and MRF control elements
    • Gopal-Srivastava, R., and Piatigorsky, J. (1993) The murine αB-crystallin/small heat shock protein enhancer: Identification of αBE-1, αBE-2, αBE-3, and MRF control elements. Mol. Cell. Biol. 13:7144-7152.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7144-7152
    • Gopal-Srivastava, R.1    Piatigorsky, J.2
  • 24
    • 0028217892 scopus 로고
    • Identification of a lens-specific regulatory region (LSR) of the murine αB-crystallin gene
    • Gopal-Srivastava, R., and Piatigorsky, J. (1994) Identification of a lens-specific regulatory region (LSR) of the murine αB-crystallin gene. Nucleic Acids. Res. 22:1281-1286.
    • (1994) Nucleic Acids. Res. , vol.22 , pp. 1281-1286
    • Gopal-Srivastava, R.1    Piatigorsky, J.2
  • 25
    • 0028972717 scopus 로고
    • Regulation of the murine αB-crystallin/small heat shock protein gene in cardiac muscle
    • Gopal-Srivastava, R., Haynes II, J.I., and Piatigorsky, J. (1995) Regulation of the murine αB-crystallin/small heat shock protein gene in cardiac muscle. Mol. Cell. Biol. 15:7081-7090.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7081-7090
    • Gopal-Srivastava, R.1    Haynes II, J.I.2    Piatigorsky, J.3
  • 26
    • 0023141516 scopus 로고
    • In situ detection of β-galactosidase in lenses of transgenic mice with a gamma-crystallin/lacZ gene
    • Goring, D.R., Rossant, J., Clapoff, S., Breitman, M.L., and Tsui, L.-C. (1987) In situ detection of β-galactosidase in lenses of transgenic mice with a gamma-crystallin/lacZ gene. Science 235:456-458.
    • (1987) Science , vol.235 , pp. 456-458
    • Goring, D.R.1    Rossant, J.2    Clapoff, S.3    Breitman, M.L.4    Tsui, L.-C.5
  • 27
    • 0027269795 scopus 로고
    • Developmental regulation and cell type-specific expression of the murine γF-crystallin gene is mediated through a lens-specific element containing the γF-1 binding site
    • Goring, D.R., Bryce, D.M., Tsui, L.-C., Breitman, M.L., and Liu, Q. (1993) Developmental regulation and cell type-specific expression of the murine γF-crystallin gene is mediated through a lens-specific element containing the γF-1 binding site. Dev. Dyn. 196:143-152.
    • (1993) Dev. Dyn. , vol.196 , pp. 143-152
    • Goring, D.R.1    Bryce, D.M.2    Tsui, L.-C.3    Breitman, M.L.4    Liu, Q.5
  • 29
    • 0026285616 scopus 로고
    • In situ hybridization: An improved wholemount method for Xenopus embryos
    • Harland, R.M. (1991) In situ hybridization: An improved wholemount method for Xenopus embryos. Methods Cell Biol. 36:685-695.
    • (1991) Methods Cell Biol. , vol.36 , pp. 685-695
    • Harland, R.M.1
  • 30
    • 0028968296 scopus 로고
    • Differential use of the regulatory elements of the αB-crystallin enhancer in cultured murine lung (MLg), lens (αTN4-1) and muscle (C2C12) cells
    • Haynes II, J.I., Gopal-Srivastava, R., Frederikse, P.H., and Piatigorsky, J. (1995) Differential use of the regulatory elements of the αB-crystallin enhancer in cultured murine lung (MLg), lens (αTN4-1) and muscle (C2C12) cells. Gene 155:151-158.
    • (1995) Gene , vol.155 , pp. 151-158
    • Haynes II, J.I.1    Gopal-Srivastava, R.2    Frederikse, P.H.3    Piatigorsky, J.4
  • 31
    • 0027968222 scopus 로고
    • Coordinate and independent regulation of αB-crystallin and HSP27 expression in response to physiological stress
    • Head, M.W., Corbin, E., and Goldman, J.E. (1994) Coordinate and independent regulation of αB-crystallin and HSP27 expression in response to physiological stress. J. Cell. Physiol. 159:41-50.
    • (1994) J. Cell. Physiol. , vol.159 , pp. 41-50
    • Head, M.W.1    Corbin, E.2    Goldman, J.E.3
  • 32
    • 0025073811 scopus 로고
    • Early tissue interactions leading to embryonic lens formation in Xenopus laevis
    • Henry, J.J., and Grainger, R.M. (1990) Early tissue interactions leading to embryonic lens formation in Xenopus laevis. Dev. Biol. 141: 149-163.
    • (1990) Dev. Biol. , vol.141 , pp. 149-163
    • Henry, J.J.1    Grainger, R.M.2
  • 33
    • 0023967439 scopus 로고
    • Rapid, reversible staining of Northern blots prior to hybridization
    • Herrin, D.L., and Schmidt, G.W. (1988) Rapid, reversible staining of Northern blots prior to hybridization. BioTechniques 6:196-200.
    • (1988) BioTechniques , vol.6 , pp. 196-200
    • Herrin, D.L.1    Schmidt, G.W.2
  • 35
    • 0026356772 scopus 로고
    • Heat shock proteins in human and mouse embryonic cells after exposure to heat shock or teratogenic agents
    • Honda, K., Hatayama, T., Takahashi, K., and Yukioka, M. (1992) Heat shock proteins in human and mouse embryonic cells after exposure to heat shock or teratogenic agents. Teratogen. Carcinogen. Mutagen. 11:235-244.
    • (1992) Teratogen. Carcinogen. Mutagen. , vol.11 , pp. 235-244
    • Honda, K.1    Hatayama, T.2    Takahashi, K.3    Yukioka, M.4
  • 36
    • 0026483279 scopus 로고
    • α-crystallin can function as a molecular chaperone
    • Horwitz, J. (1992) α-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. U.S.A. 89:10449-10453.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 37
    • 0026575146 scopus 로고
    • Translocation and induction of αB-crystallin by heat shock in rat glioma (GA-1) cells
    • Inaguma, Y., Shinohara, H., Goto, S., and Kato, S. (1992) Translocation and induction of αB-crystallin by heat shock in rat glioma (GA-1) cells. Biochem. Biophys. Res. Commun. 182:844-850.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 844-850
    • Inaguma, Y.1    Shinohara, H.2    Goto, S.3    Kato, S.4
  • 38
    • 0029004307 scopus 로고
    • Induction of the synthesis of hsp27 and αB crystallin in tissues of heat-stressed rats and its suppression by ethanol or an α1-adrenergic antagonist
    • Inaguma, Y., Hasegawa, K., Goto, S., Ito H., and Kato, K. (1995) Induction of the synthesis of hsp27 and αB crystallin in tissues of heat-stressed rats and its suppression by ethanol or an α1-adrenergic antagonist. J. Biochem. 117:1238-1243.
    • (1995) J. Biochem. , vol.117 , pp. 1238-1243
    • Inaguma, Y.1    Hasegawa, K.2    Goto, S.3    Ito, H.4    Kato, K.5
  • 39
    • 0025652002 scopus 로고
    • Multiple mRNAs of rat brain α-crystallin B chain result from alternative transcriptional initiation
    • Iwaki, A., Iwaki, T., Goldman, J.E., and Liem, R.K.H. (1990) Multiple mRNAs of rat brain α-crystallin B chain result from alternative transcriptional initiation. J. Biol. Chem. 265:22197-22203.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22197-22203
    • Iwaki, A.1    Iwaki, T.2    Goldman, J.E.3    Liem, R.K.H.4
  • 40
    • 0025101570 scopus 로고
    • Cellular distribution of αB-crystallin in non-lenticular tissues
    • Iwaki, T., Kume-Iwaki, A., and Goldman, J.E. (1990) Cellular distribution of αB-crystallin in non-lenticular tissues. J. Histochem. Cytochem. 38:31-39.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 31-39
    • Iwaki, T.1    Kume-Iwaki, A.2    Goldman, J.E.3
  • 41
    • 0025766466 scopus 로고
    • Expression of αB-crystallin in the developing rat kidney
    • Iwaki, T., Iwaki, A., Liem, R.K.H., and Goldman, J.E. (1991) Expression of αB-crystallin in the developing rat kidney. Kidney Int. 40: 52-56.
    • (1991) Kidney Int. , vol.40 , pp. 52-56
    • Iwaki, T.1    Iwaki, A.2    Liem, R.K.H.3    Goldman, J.E.4
  • 42
    • 0027742866 scopus 로고
    • αB-crystallin and 27-kd heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers
    • Iwaki, T., Iwaki, A., Tateishi, J., Sakaki, Y., and Goldman, J.E. (1993) αB-crystallin and 27-kd heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers. Am. J. Pathol. 143:487-495.
    • (1993) Am. J. Pathol. , vol.143 , pp. 487-495
    • Iwaki, T.1    Iwaki, A.2    Tateishi, J.3    Sakaki, Y.4    Goldman, J.E.5
  • 43
    • 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. U.S.A. 91:3112-3116.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 3112-3116
    • Kantorow, M.1    Piatigorsky, J.2
  • 44
    • 0029083170 scopus 로고
    • Conversion from oligomers to tetramers enhances autophosphorylation by lens αA-crystallin: Specificity between αA- and αB-crystallin subunits
    • 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: Specificity between αA- and αB-crystallin subunits. J. Biol. Chem. 270:17215-17220.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17215-17220
    • Kantorow, M.1    Horwitz, J.2    Van Boekel, M.A.M.3    De Jong, W.W.4    Piatigorsky, J.5
  • 45
    • 0026040828 scopus 로고
    • Immunoreactive αA-crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method
    • Kato, K., Shinohara, H., Kurobe, N., Goto, S., Inaguma, Y., and Ohshima, K. (1991) Immunoreactive αA-crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method. Biochim. Biophys. Acta 1080:173-180.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 173-180
    • Kato, K.1    Shinohara, H.2    Kurobe, N.3    Goto, S.4    Inaguma, Y.5    Ohshima, K.6
  • 46
    • 0026774629 scopus 로고
    • Copurification of small heat shock protein with αB crystallin from human skeletal muscle
    • Kato, K., Shinohara, H., Goto, S., Inaguma, Y., Morishita, R., and Asano, T. (1992) Copurification of small heat shock protein with αB crystallin from human skeletal muscle. J. Biol. Chem. 267:7718-7725.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7718-7725
    • Kato, K.1    Shinohara, H.2    Goto, S.3    Inaguma, Y.4    Morishita, R.5    Asano, T.6
  • 47
    • 0027495153 scopus 로고
    • Coinduction of two low-molecular-weight stress proteins, αB crystallin and HSP28, by heat or arsenite stress in human glioma cells
    • Kato, K., Goto, S., Hasegawa, K., and Inaguma, Y. (1993) Coinduction of two low-molecular-weight stress proteins, αB crystallin and HSP28, by heat or arsenite stress in human glioma cells. J. Biochem. 114:640-647.
    • (1993) J. Biochem. , vol.114 , pp. 640-647
    • Kato, K.1    Goto, S.2    Hasegawa, K.3    Inaguma, Y.4
  • 50
    • 0027441406 scopus 로고
    • Expression of the murine small heat shock proteins hsp 25 and αB crystallin in the absence of stress
    • Klemenz, R., Andres, A.-C., Frohli, E., Schafer, R., and Aoyama, A. (1993) Expression of the murine small heat shock proteins hsp 25 and αB crystallin in the absence of stress. J. Cell Biol. 120:639-645.
    • (1993) J. Cell Biol. , vol.120 , pp. 639-645
    • Klemenz, R.1    Andres, A.-C.2    Frohli, E.3    Schafer, R.4    Aoyama, A.5
  • 51
    • 23444441161 scopus 로고
    • Pax-6 is first expressed in a region of ectoderm anterior to the early neural plate: Implications for stepwise determination of the lens
    • Li, H.-S., Yang, J.-M., Jacobson, R.D., Pasko, D., and Sundin, O. (1994) Pax-6 is first expressed in a region of ectoderm anterior to the early neural plate: Implications for stepwise determination of the lens. Dev. Biol. 162:181-194.
    • (1994) Dev. Biol. , vol.162 , pp. 181-194
    • Li, H.-S.1    Yang, J.-M.2    Jacobson, R.D.3    Pasko, D.4    Sundin, O.5
  • 52
    • 0029077013 scopus 로고
    • Serum response element associated transcription factors in mouse embryos: Serum response factor, YY1, and PEA3 factor
    • Liu, S.H., Peng, B.H., Ma, J.T., Liu, Y.C., and Ng, S.Y. (1995) Serum response element associated transcription factors in mouse embryos: Serum response factor, YY1, and PEA3 factor. Dev. Genet. 16:229-240.
    • (1995) Dev. Genet. , vol.16 , pp. 229-240
    • Liu, S.H.1    Peng, B.H.2    Ma, J.T.3    Liu, Y.C.4    Ng, S.Y.5
  • 53
  • 55
    • 0026541969 scopus 로고
    • αB-crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease
    • Lowe, J., McDermott, H., Pike, I., Spendlove, I., Landon, M., and Mayer, R.J. (1992b) αB-crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease. J. Pathol. 166:61-68.
    • (1992) J. Pathol. , vol.166 , pp. 61-68
    • Lowe, J.1    McDermott, H.2    Pike, I.3    Spendlove, I.4    Landon, M.5    Mayer, R.J.6
  • 56
    • 0001756836 scopus 로고
    • Use of E. coli lacZ (β-galactosidase) as a reporter gene
    • Murray, E.J. and Walker, J.M. (eds). Clifton, NJ: Humana Press, Inc.
    • MacGregor, G.R., Nolan, G.P., Fiering, S., Roederer, M., and Herzenberg, L.A. (1989) Use of E. coli lacZ (β-galactosidase) as a reporter gene. In: "Methods in Molecular Biology," Vol. 7, Murray, E.J. and Walker, J.M. (eds). Clifton, NJ: Humana Press, Inc.
    • (1989) Methods in Molecular Biology , vol.7
    • MacGregor, G.R.1    Nolan, G.P.2    Fiering, S.3    Roederer, M.4    Herzenberg, L.A.5
  • 57
    • 0028152490 scopus 로고
    • The basic helix-loop-helix protein upstream stimulating factor regulates the cardiac ventricular myosin light-chain 2 gene via independent cis regulatory elements
    • Navankasattusas, S., Sawadogo, M., van Bilsen, M., Dang, C.V., and Chien, K.R. (1994) The basic helix-loop-helix protein upstream stimulating factor regulates the cardiac ventricular myosin light-chain 2 gene via independent cis regulatory elements. Mol. Cell. Biol. 14:7331-7339.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7331-7339
    • Navankasattusas, S.1    Sawadogo, M.2    Van Bilsen, M.3    Dang, C.V.4    Chien, K.R.5
  • 58
    • 0028176579 scopus 로고
    • Chaperone activity of α-crystallins modulates intermediate filament assembly
    • Nicholl, I.D., and Quinlan, R.A. (1994) Chaperone activity of α-crystallins modulates intermediate filament assembly. EMBO J. 13: 945-953.
    • (1994) EMBO J. , vol.13 , pp. 945-953
    • Nicholl, I.D.1    Quinlan, R.A.2
  • 60
    • 0025805798 scopus 로고
    • Early expression of the myogenic regulatory gene, myf-5, in precursor cells of skeletal muscle in the mouse embryo
    • Ott, M.-O., Bober, E., Lyons, G., Arnold, H., and Buckingham, M. (1991) Early expression of the myogenic regulatory gene, myf-5, in precursor cells of skeletal muscle in the mouse embryo. Development 111:1097-1107.
    • (1991) Development , vol.111 , pp. 1097-1107
    • Ott, M.-O.1    Bober, E.2    Lyons, G.3    Arnold, H.4    Buckingham, M.5
  • 61
    • 0022351502 scopus 로고
    • Lens-specific expression and developmental regulation of the bacterial chloramphenicol acetyltransferase gene driven by the murine αA-crystallin promoter in transgenic mice. Proc
    • Overbeek, P.A., Chepelinsky, A.B., Khillan, J.S., Piatigorsky, J., and Westphal, H. (1985) Lens-specific expression and developmental regulation of the bacterial chloramphenicol acetyltransferase gene driven by the murine αA-crystallin promoter in transgenic mice. Proc. Natl. Acad. Sci. U.S.A. 82:7815-7819.
    • (1985) Natl. Acad. Sci. U.S.A. , vol.82 , pp. 7815-7819
    • Overbeek, P.A.1    Chepelinsky, A.B.2    Khillan, J.S.3    Piatigorsky, J.4    Westphal, H.5
  • 62
    • 0026754720 scopus 로고
    • Lens crystallins: Innovation associated with changes in gene regulation
    • Piatigorsky, J. (1992) Lens crystallins: Innovation associated with changes in gene regulation. J. Biol. Chem. 267:4277-4280.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4277-4280
    • Piatigorsky, J.1
  • 63
    • 0024520027 scopus 로고
    • Enzyme/crystallins: Gene sharing as an evolutionary strategy
    • Piatigorsky, J., and Wistow, G.J. (1989) Enzyme/crystallins: Gene sharing as an evolutionary strategy. Cell 57:197-199.
    • (1989) Cell , vol.57 , pp. 197-199
    • Piatigorsky, J.1    Wistow, G.J.2
  • 64
    • 0022988979 scopus 로고
    • Use of a recombinant retrovirus to study post-implantation cell lineage in mouse embryos
    • Sanes, J.R., Rubinstein, J.L., and Nicolas, J.F. (1986) Use of a recombinant retrovirus to study post-implantation cell lineage in mouse embryos. EMBO J. 5:3133-3142.
    • (1986) EMBO J. , vol.5 , pp. 3133-3142
    • Sanes, J.R.1    Rubinstein, J.L.2    Nicolas, J.F.3
  • 65
    • 0028254544 scopus 로고
    • Expression of the α-crystallin/small heat shock protein/molecular chaperone genes in the lens and other tissues
    • Sax, C.M., and Piatigorsky, J. (1994) Expression of the α-crystallin/small heat shock protein/molecular chaperone genes in the lens and other tissues. Adv. Enzymol. 69:155-201.
    • (1994) Adv. Enzymol. , vol.69 , pp. 155-201
    • Sax, C.M.1    Piatigorsky, J.2
  • 66
    • 0025797233 scopus 로고
    • Ubiquitin-protein conjugates and αB crystallin are selectively present in cells undergoing major cytomorphological reorganisation in early chicken embryos
    • Scotting, P., McDermott, H., and Mayer, R.J. (1991) Ubiquitin-protein conjugates and αB crystallin are selectively present in cells undergoing major cytomorphological reorganisation in early chicken embryos. FEBS Lett. 285:71-79.
    • (1991) FEBS Lett. , vol.285 , pp. 71-79
    • Scotting, P.1    McDermott, H.2    Mayer, R.J.3
  • 68
    • 0026470980 scopus 로고
    • αA-crystallin is expressed in non-ocular tissues
    • Srinivasan, A.N., Nagineni, C.N., and Bhat, S.P. (1992) αA-crystallin is expressed in non-ocular tissues. J. Biol. Chem. 267:23337-23341.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23337-23341
    • Srinivasan, A.N.1    Nagineni, C.N.2    Bhat, S.P.3
  • 69
    • 0024226522 scopus 로고
    • Escherichia coli heat shock gene mutants are defective in proteolysis
    • Straus, D.B., Walter, W.A., and Gross, C.A. (1988) Escherichia coli heat shock gene mutants are defective in proteolysis. Genes Dev. 2:1851-1858.
    • (1988) Genes Dev. , vol.2 , pp. 1851-1858
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 70
    • 0025869777 scopus 로고
    • Rosenthal fibers share epitopes with αB-crystallin, glial fibrillary acidic protein, and ubiquitin, but not with vimentin. Immunoelectron microscopy with colloidal gold
    • Tomokane, N., Iwaki, T., Tateishi, J., Iwaki, A., and Goldman, J.E. (1991) Rosenthal fibers share epitopes with αB-crystallin, glial fibrillary acidic protein, and ubiquitin, but not with vimentin. Immunoelectron microscopy with colloidal gold. Am. J. Pathol. 138: 933-938.
    • (1991) Am. J. Pathol. , vol.138 , pp. 933-938
    • Tomokane, N.1    Iwaki, T.2    Tateishi, J.3    Iwaki, A.4    Goldman, J.E.5
  • 72
    • 0026808677 scopus 로고
    • Relocalization of αB-crystallin by heat shock in ovarian carcinoma cells
    • Voorter, C.E.M., Wintjes, L., Bloemendal, H., and de Jong, W.W. (1992) Relocalization of αB-crystallin by heat shock in ovarian carcinoma cells. FEBS Lett. 309:111-114.
    • (1992) FEBS Lett. , vol.309 , pp. 111-114
    • Voorter, C.E.M.1    Wintjes, L.2    Bloemendal, H.3    De Jong, W.W.4
  • 73
    • 0026340588 scopus 로고
    • Pax-6, a murine paired box gene, is expressed in the developing CNS
    • Walther, C., and Gruss, P. (1991) Pax-6, a murine paired box gene, is expressed in the developing CNS. Development 113:1435-1449.
    • (1991) Development , vol.113 , pp. 1435-1449
    • Walther, C.1    Gruss, P.2
  • 75
    • 0022379715 scopus 로고
    • Morphological study of the mammalian stress response: Characterization of changes in cytoplasmic organelles, cytoskeleton, and nucleoli, and appearance of intranuclear actin filaments in rat fibroblasts after heat shock treatment
    • Welsh, W.J., and Suhan, J.P. (1985) Morphological study of the mammalian stress response: Characterization of changes in cytoplasmic organelles, cytoskeleton, and nucleoli, and appearance of intranuclear actin filaments in rat fibroblasts after heat shock treatment. J. Cell Biol. 101:1198-1211.
    • (1985) J. Cell Biol. , vol.101 , pp. 1198-1211
    • Welsh, W.J.1    Suhan, J.P.2
  • 76
    • 0025878249 scopus 로고
    • Crystallin mRNA concentrations and distribution in lens of normal and galactosemic rats: Implications in development of sugar cataracts
    • Wen, Y., Shi, S., Unakar, N.J., and Bekhor, I. (1991) Crystallin mRNA concentrations and distribution in lens of normal and galactosemic rats: Implications in development of sugar cataracts. Invest. Ophthalmol. Vis. Sci. 32:1638-1647.
    • (1991) Invest. Ophthalmol. Vis. Sci. , vol.32 , pp. 1638-1647
    • Wen, Y.1    Shi, S.2    Unakar, N.J.3    Bekhor, I.4
  • 77
    • 0027225772 scopus 로고
    • Lens crystallins: Gene recruitment and evolutionary dynamism
    • Wistow, G. (1993) Lens crystallins: Gene recruitment and evolutionary dynamism. Trends Biochem. Sci. 18:301-306.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 301-306
    • Wistow, G.1
  • 78
    • 0023917935 scopus 로고
    • Lens crystallins: Evolution and expression of proteins for a highly specialized tissue
    • Wistow, G., and Piatigorsky, J. (1988) Lens crystallins: Evolution and expression of proteins for a highly specialized tissue. Ann. Rev. Biochem. 57:479-504.
    • (1988) Ann. Rev. Biochem. , vol.57 , pp. 479-504
    • Wistow, G.1    Piatigorsky, J.2
  • 79
    • 0026632361 scopus 로고
    • Heat shock protein 27 and αB-crystallin can form a complex, which dissociates by heat shock
    • Zantema, A., Verlaan-De Vries, M., Maasdam, D., Bol, S., and ver der Eb, A. (1992) Heat shock protein 27 and αB-crystallin can form a complex, which dissociates by heat shock. J. Biol. Chem. 267: 12936-12941.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12936-12941
    • Zantema, A.1    Verlaan-De Vries, M.2    Maasdam, D.3    Bol, S.4    Ver Der Eb, A.5
  • 80
    • 0020567328 scopus 로고
    • The appearance of α-crystallin in relation to cell cycle phase in the embryonic mouse lens
    • Zwaan, J. (1983) The appearance of α-crystallin in relation to cell cycle phase in the embryonic mouse lens. Dev. Biol. 96:173-181.
    • (1983) Dev. Biol. , vol.96 , pp. 173-181
    • Zwaan, J.1


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