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Volumn 17, Issue 2, 2006, Pages 886-894

Hsp27 enhances recovery of splicing as well as rephosphorylation of SRp38 after heat shock

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; CALYCULIN A; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROTEIN SRP38; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 31944446927     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-07-0596     Document Type: Article
Times cited : (39)

References (65)
  • 1
    • 0037180825 scopus 로고    scopus 로고
    • The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila
    • Andrulis, E. D., Werner, J., Nazarian, A., Erdjument-Bromage, H., Tempst, P., and Lis, J. T. (2002). The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila. Nature 420, 837-841.
    • (2002) Nature , vol.420 , pp. 837-841
    • Andrulis, E.D.1    Werner, J.2    Nazarian, A.3    Erdjument-Bromage, H.4    Tempst, P.5    Lis, J.T.6
  • 2
    • 0027513233 scopus 로고
    • Alpha B-crystallin expression in mouse NIH 3T3 fibroblasts: Glucocorticoid responsiveness and involvement in thermal protection
    • Aoyama, A., Frohli, E., Schafer, R., and Klemenz, R. (1993). Alpha B-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protection. Mol. Cell. Biol. 13, 1824-1835.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1824-1835
    • Aoyama, A.1    Frohli, E.2    Schafer, R.3    Klemenz, R.4
  • 4
    • 0023697402 scopus 로고
    • Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein
    • Arrigo, A. P., Suhan, J. P., and Welch, W. J. (1988). Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein. Mol. Cell. Biol. 8, 5059-5071.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5059-5071
    • Arrigo, A.P.1    Suhan, J.P.2    Welch, W.J.3
  • 5
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • Basso, A. D., Solit, D. B., Chiosis, G., Giri, B., Tsichlis, P., and Rosen, N. (2002). Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J. Biol. Chem. 277, 39858-39866.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 6
    • 0024114933 scopus 로고
    • Heat shock but not other stress inducers leads to the disruption of a sub-set of snRNPs and inhibition of in vitro splicing in HeLa cells
    • Bond, U. (1988). Heat shock but not other stress inducers leads to the disruption of a sub-set of snRNPs and inhibition of in vitro splicing in HeLa cells. EMBO J. 7, 3509-3518.
    • (1988) EMBO J. , vol.7 , pp. 3509-3518
    • Bond, U.1
  • 7
    • 0034212138 scopus 로고    scopus 로고
    • Dynamic changes in small nuclear ribonucleoproteins of heat-stressed and thermotolerant HeLa cells
    • Bond, U., and James, T. C. (2000). Dynamic changes in small nuclear ribonucleoproteins of heat-stressed and thermotolerant HeLa cells. Int. J. Biochem. Cell Biol. 32, 643-656.
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 643-656
    • Bond, U.1    James, T.C.2
  • 8
    • 0032786256 scopus 로고    scopus 로고
    • Reassembly and protection of small nuclear ribonucleoprotein particles by heat shock proteins in yeast cells
    • Bracken, A. P., and Bond, U. (1999). Reassembly and protection of small nuclear ribonucleoprotein particles by heat shock proteins in yeast cells. RNA. 5, 1586-1596.
    • (1999) RNA , vol.5 , pp. 1586-1596
    • Bracken, A.P.1    Bond, U.2
  • 10
    • 0029076694 scopus 로고
    • Lipofection reagents prepared by a simple ethanol injection technique
    • Campbell, M. J. (1995). Lipofection reagents prepared by a simple ethanol injection technique. Biotechniques 18, 1027-1032.
    • (1995) Biotechniques , vol.18 , pp. 1027-1032
    • Campbell, M.J.1
  • 11
    • 0030802907 scopus 로고    scopus 로고
    • Heat shock protein 27 stimulates recovery of RNA and protein synthesis following a heat shock
    • Carper, S. W., Rocheleau, T. A., Cimino, D., and Storm, F. K. (1997). Heat shock protein 27 stimulates recovery of RNA and protein synthesis following a heat shock. J. Cell. Biochem. 66, 153-164.
    • (1997) J. Cell. Biochem. , vol.66 , pp. 153-164
    • Carper, S.W.1    Rocheleau, T.A.2    Cimino, D.3    Storm, F.K.4
  • 12
    • 21244466032 scopus 로고    scopus 로고
    • A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104
    • Cashikar, A. G., Duennwald, M., and Lindquist, S. L. (2005). A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J. Biol. Chem. 280, 23869-23875.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23869-23875
    • Cashikar, A.G.1    Duennwald, M.2    Lindquist, S.L.3
  • 14
    • 0026704970 scopus 로고
    • Splicing thermotolerance maintains pre-mRNA transcripts in the splicing pathway during severe heat shock
    • Corell, R. A., and Gross, R. H. (1992). Splicing thermotolerance maintains pre-mRNA transcripts in the splicing pathway during severe heat shock. Exp. Cell Res. 202, 233-242.
    • (1992) Exp. Cell Res. , vol.202 , pp. 233-242
    • Corell, R.A.1    Gross, R.H.2
  • 15
    • 0025892598 scopus 로고
    • Detection and characterization of a factor which rescues spliceosome assembly from a heat-inactivated HeLa cell nuclear extract
    • Delannoy, P., and Caruthers, M. H. (1991). Detection and characterization of a factor which rescues spliceosome assembly from a heat-inactivated HeLa cell nuclear extract. Mol. Cell. Biol. 11, 3425-3431.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3425-3431
    • Delannoy, P.1    Caruthers, M.H.2
  • 17
    • 1842610010 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Integrating mRNA production and turnover with export through the nuclear pore
    • Dimaano, C., and Ullman, K. S. (2004). Nucleocytoplasmic transport: integrating mRNA production and turnover with export through the nuclear pore. Mol. Cell. Biol. 24, 3069-3076.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3069-3076
    • Dimaano, C.1    Ullman, K.S.2
  • 18
    • 0348010381 scopus 로고    scopus 로고
    • Translational thermotolerance provided by small heat shock proteins is limited to cap-dependent initiation and inhibited by 2-aminopurine
    • Doerwald, L., Onnekink, C., van Genesen, S. T., de Jong, W. W., and Lubsen, N. H. (2003). Translational thermotolerance provided by small heat shock proteins is limited to cap-dependent initiation and inhibited by 2-aminopurine. J. Biol. Chem. 278, 49743-49750.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49743-49750
    • Doerwald, L.1    Onnekink, C.2    Van Genesen, S.T.3    De Jong, W.W.4    Lubsen, N.H.5
  • 19
    • 0344541106 scopus 로고    scopus 로고
    • Heat-shock-specific phosphorylation and transcriptional activity of RNA polymerase II
    • Egyhazi, E., Ossoinak, A., Lee, J. M., Greenleaf, A. L., Makela, T. P., and Pigon, A. (1998). Heat-shock-specific phosphorylation and transcriptional activity of RNA polymerase II. Exp. Cell Res. 242, 211-221.
    • (1998) Exp. Cell Res. , vol.242 , pp. 211-221
    • Egyhazi, E.1    Ossoinak, A.2    Lee, J.M.3    Greenleaf, A.L.4    Makela, T.P.5    Pigon, A.6
  • 20
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger, M., Graber, S., Gaestel, M., and Buchner, J. (1997). Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16, 221-229.
    • (1997) EMBO J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 21
    • 22444435897 scopus 로고    scopus 로고
    • Process or perish: Quality control in mRNA biogenesis
    • Fasken, M. B., and Corbett, A. H. (2005). Process or perish: quality control in mRNA biogenesis. Nat. Struct. Mol. Biol. 12, 482-488.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 482-488
    • Fasken, M.B.1    Corbett, A.H.2
  • 22
    • 0036090023 scopus 로고    scopus 로고
    • Invited review: Interplay between molecular chaperones and signaling pathways in survival of heat shock
    • Gabai, V. L., and Sherman, M. Y. (2002). Invited review: interplay between molecular chaperones and signaling pathways in survival of heat shock. J. Appl. Physiol. 92, 1743-1748.
    • (2002) J. Appl. Physiol. , vol.92 , pp. 1743-1748
    • Gabai, V.L.1    Sherman, M.Y.2
  • 23
    • 0036372749 scopus 로고    scopus 로고
    • sHsp-phosphorylation: Enzymes, signaling pathways and functional implications
    • Gaestel, M. (2002). sHsp-phosphorylation: enzymes, signaling pathways and functional implications. Prog. Mol. Subcell. Biol. 28, 151-169.
    • (2002) Prog. Mol. Subcell. Biol. , vol.28 , pp. 151-169
    • Gaestel, M.1
  • 25
    • 0037205441 scopus 로고    scopus 로고
    • Phosphorylation-dependent cellular localization and thermoprotective role of heat shock protein 25 in hippocampal progenitor cells
    • Geum, D., Son, G. H., and Kim, K. (2002). Phosphorylation-dependent cellular localization and thermoprotective role of heat shock protein 25 in hippocampal progenitor cells. J. Biol. Chem. 277, 19913-19921.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19913-19921
    • Geum, D.1    Son, G.H.2    Kim, K.3
  • 27
    • 0034659241 scopus 로고    scopus 로고
    • RNA polymerase II and the integration of nuclear events
    • Hirose, Y., and Manley, J. L. (2000). RNA polymerase II and the integration of nuclear events. Genes Dev. 14, 1415-1429.
    • (2000) Genes Dev. , vol.14 , pp. 1415-1429
    • Hirose, Y.1    Manley, J.L.2
  • 28
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • Hsu, A. L., Murphy, C. T., and Kenyon, C. (2003). Regulation of aging and age-related disease by DAF-16 and heat-shock factor. Science 300, 1142-1145.
    • (2003) Science , vol.300 , pp. 1142-1145
    • Hsu, A.L.1    Murphy, C.T.2    Kenyon, C.3
  • 29
    • 14644445227 scopus 로고    scopus 로고
    • SRprises along a messenger's journey
    • Huang, Y., and Steitz, J. A. (2005). SRprises along a messenger's journey. Mol. Cell 17, 613-615.
    • (2005) Mol. Cell , vol.17 , pp. 613-615
    • Huang, Y.1    Steitz, J.A.2
  • 30
    • 0037716756 scopus 로고    scopus 로고
    • Early formation of mRNP: License for export or quality control?
    • Jensen, T. H., Dower, K., Libri, D., and Rosbash, M. (2003). Early formation of mRNP: license for export or quality control? Mol. Cell 11, 1129-1138.
    • (2003) Mol. Cell , vol.11 , pp. 1129-1138
    • Jensen, T.H.1    Dower, K.2    Libri, D.3    Rosbash, M.4
  • 31
    • 0033553878 scopus 로고    scopus 로고
    • Intron-independent association of splicing factors with active genes
    • Jolly, C., Vourc'h, C., Robert-Nicoud, M., Morimoto, R. I. (1999). Intron-independent association of splicing factors with active genes. J. Cell Biol. 145, 1133-1143.
    • (1999) J. Cell Biol. , vol.145 , pp. 1133-1143
    • Jolly, C.1    Vourc'h, C.2    Robert-Nicoud, M.3    Morimoto, R.I.4
  • 33
    • 0036359596 scopus 로고    scopus 로고
    • Expression and phosphorylation of mammalian small heat shock proteins
    • Kato, K., Ito, H., and Inaguma, Y. (2002). Expression and phosphorylation of mammalian small heat shock proteins. Prog. Mol. Subcell. Biol. 28, 129-150.
    • (2002) Prog. Mol. Subcell. Biol. , vol.28 , pp. 129-150
    • Kato, K.1    Ito, H.2    Inaguma, Y.3
  • 34
    • 0030785701 scopus 로고    scopus 로고
    • Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27
    • Konishi, H., Matsuzaki, H., Tanaka, M., Takemura, Y., Kuroda, S., Ono, Y., and Kikkawa, U. (1997). Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27. FEBS Lett. 410, 493-498.
    • (1997) FEBS Lett. , vol.410 , pp. 493-498
    • Konishi, H.1    Matsuzaki, H.2    Tanaka, M.3    Takemura, Y.4    Kuroda, S.5    Ono, Y.6    Kikkawa, U.7
  • 35
    • 0036359488 scopus 로고    scopus 로고
    • Hsp27 in the nervous system: Expression in pathophysiology and in the aging brain
    • Krueger-Naug, A. M., Plumier, J. C., Hopkins, D. A., and Currie, R. W. (2002). Hsp27 in the nervous system: expression in pathophysiology and in the aging brain. Prog. Mol. Subcell. Biol. 28, 235-251.
    • (2002) Prog. Mol. Subcell. Biol. , vol.28 , pp. 235-251
    • Krueger-Naug, A.M.1    Plumier, J.C.2    Hopkins, D.A.3    Currie, R.W.4
  • 36
    • 0027417852 scopus 로고
    • Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization
    • Lavoie, J. N., Gingras-Breton, G., Tanguay, R. M., and Landry, J. (1993). Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization. J. Biol. Chem. 268, 3420-3429.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3420-3429
    • Lavoie, J.N.1    Gingras-Breton, G.2    Tanguay, R.M.3    Landry, J.4
  • 37
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee, G. J., Roseman, A. M., Saibil, H. R., and Vierling, E. (1997). A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16, 659-671.
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 38
    • 17744393658 scopus 로고    scopus 로고
    • Inhibition of neurogenesis by SRp38, a neuroD-regulated RNA-binding protein
    • Liu, K. J., and Harland, R. M. (2005). Inhibition of neurogenesis by SRp38, a neuroD-regulated RNA-binding protein. Development 132, 1511-1523.
    • (2005) Development , vol.132 , pp. 1511-1523
    • Liu, K.J.1    Harland, R.M.2
  • 39
    • 0030603146 scopus 로고    scopus 로고
    • Distinct effects of heat shock and ATP depletion on distribution and isoform patterns of human Hsp27 in endothelial cells
    • Loktionova, S. A., Ilyinskaya, O. P., Gabai, V. L., and Kabakov, A. E. (1996). Distinct effects of heat shock and ATP depletion on distribution and isoform patterns of human Hsp27 in endothelial cells. FEBS Lett. 392, 100-104.
    • (1996) FEBS Lett. , vol.392 , pp. 100-104
    • Loktionova, S.A.1    Ilyinskaya, O.P.2    Gabai, V.L.3    Kabakov, A.E.4
  • 40
    • 0034704201 scopus 로고    scopus 로고
    • Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon
    • Lykke-Andersen, J., Shu, M. D., and Steitz, J. A. (2000). Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon. Cell 103, 1121-1131.
    • (2000) Cell , vol.103 , pp. 1121-1131
    • Lykke-Andersen, J.1    Shu, M.D.2    Steitz, J.A.3
  • 41
    • 18344364099 scopus 로고    scopus 로고
    • Understanding alternative splicing: Towards a cellular code
    • Matlin, A. J., Clark, F., and Smith, C. W. (2005). Understanding alternative splicing: towards a cellular code. Nat. Rev. Mol. Cell. Biol. 6, 386-398.
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 386-398
    • Matlin, A.J.1    Clark, F.2    Smith, C.W.3
  • 42
    • 0028043718 scopus 로고
    • Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism
    • Mermoud, J. E., Cohen, P. T., and Lamond, A. I. (1994). Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism. EMBO J. 13, 5679-5688.
    • (1994) EMBO J. , vol.13 , pp. 5679-5688
    • Mermoud, J.E.1    Cohen, P.T.2    Lamond, A.I.3
  • 43
    • 5444253157 scopus 로고    scopus 로고
    • A key role for stress-induced satellite III transcripts in the relocalization of splicing factors into nuclear stress granules
    • Metz, A., Soret, J., Vourc'h, C., Tazi, J., Jolly, C. (2004). A key role for stress-induced satellite III transcripts in the relocalization of splicing factors into nuclear stress granules. J. Cell Sci. 117, 4551-4558.
    • (2004) J. Cell Sci. , vol.117 , pp. 4551-4558
    • Metz, A.1    Soret, J.2    Vourc'h, C.3    Tazi, J.4    Jolly, C.5
  • 44
    • 0742323000 scopus 로고    scopus 로고
    • Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones
    • Morley, J. F., and Morimoto, R. I. (2004). Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. Mol. Biol. Cell 15, 657-664.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 657-664
    • Morley, J.F.1    Morimoto, R.I.2
  • 46
    • 0141815505 scopus 로고    scopus 로고
    • Investigating RNA polymerase II carboxyl-terminal domain (CTD) phosphorylation
    • Palancade, B., and Bensaude, O. (2003). Investigating RNA polymerase II carboxyl-terminal domain (CTD) phosphorylation. Eur. J. Biochem. 270, 3859-3870.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3859-3870
    • Palancade, B.1    Bensaude, O.2
  • 48
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R. D., and Misteli, T. (2000). High mobility of proteins in the mammalian cell nucleus. Nature 404, 604-609.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 49
    • 0036366525 scopus 로고    scopus 로고
    • Cytoskeletal competence requires protein chaperones
    • Quinlan, R. (2002). Cytoskeletal competence requires protein chaperones. Prog. Mol. Subcell. Biol. 28, 219-233.
    • (2002) Prog. Mol. Subcell. Biol. , vol.28 , pp. 219-233
    • Quinlan, R.1
  • 50
    • 0035793574 scopus 로고    scopus 로고
    • p38 kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils
    • Rane, M. J., Coxon, P. Y., Powell, D. W., Webster, R., Klein, J. B., Pierce, W., Ping, P., McLeish, K. R. (2001). p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils. J. Biol. Chem. 276, 3517-3523.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3517-3523
    • Rane, M.J.1    Coxon, P.Y.2    Powell, D.W.3    Webster, R.4    Klein, J.B.5    Pierce, W.6    Ping, P.7    McLeish, K.R.8
  • 52
    • 1842632326 scopus 로고    scopus 로고
    • A novel role for shuttling SR proteins in mRNA translation
    • Sanford, J. R., Gray, N. K., Beckmann, K., and Caceres, J. F. (2004). A novel role for shuttling SR proteins in mRNA translation. Genes Dev. 18, 755-768.
    • (2004) Genes Dev. , vol.18 , pp. 755-768
    • Sanford, J.R.1    Gray, N.K.2    Beckmann, K.3    Caceres, J.F.4
  • 53
    • 1142310938 scopus 로고    scopus 로고
    • Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock
    • Shin, C., Feng, Y., and Manley, J. L. (2004). Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock. Nature 427, 553-558.
    • (2004) Nature , vol.427 , pp. 553-558
    • Shin, C.1    Feng, Y.2    Manley, J.L.3
  • 54
    • 24344483048 scopus 로고    scopus 로고
    • Multiple properties of the splicing repressor SRp38 distinguish it from typical SR proteins
    • Shin, C., Kleiman, F. E., and Manley, J. L. (2005). Multiple properties of the splicing repressor SRp38 distinguish it from typical SR proteins. Mol. Cell. Biol. 25, 8334-8343.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8334-8343
    • Shin, C.1    Kleiman, F.E.2    Manley, J.L.3
  • 55
    • 0036848091 scopus 로고    scopus 로고
    • The SR protein SRp38 represses splicing in M phase cells
    • Shin, C., and Manley, J. L. (2002). The SR protein SRp38 represses splicing in M phase cells. Cell 111, 407-417.
    • (2002) Cell , vol.111 , pp. 407-417
    • Shin, C.1    Manley, J.L.2
  • 56
    • 4444272979 scopus 로고    scopus 로고
    • Cell signalling and the control of pre-mRNA splicing
    • Shin, C., and Manley, J. L. (2004). Cell signalling and the control of pre-mRNA splicing. Nat. Rev. Mol. Cell. Biol. 5, 727-738.
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 727-738
    • Shin, C.1    Manley, J.L.2
  • 57
    • 0026587114 scopus 로고
    • A splicing factor that is inactivated during in vivo heat shock is functionally equivalent to the [U4/U6.U5] triple snRNP-specific proteins
    • Utans, U., Behrens, S. E., Luhrmann, R., Kole, R., and Kramer, A. (1992). A splicing factor that is inactivated during in vivo heat shock is functionally equivalent to the [U4/U6.U5] triple snRNP-specific proteins. Genes Dev. 6, 631-641.
    • (1992) Genes Dev. , vol.6 , pp. 631-641
    • Utans, U.1    Behrens, S.E.2    Luhrmann, R.3    Kole, R.4    Kramer, A.5
  • 58
    • 0043205911 scopus 로고    scopus 로고
    • Nuclear speckle localisation of the small heat shock protein alpha B-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation
    • van den IJssel, P., Wheelock, R., Prescott, A., Russell, P., Quinlan, R. A. (2003). Nuclear speckle localisation of the small heat shock protein alpha B-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation. Exp. Cell Res. 287, 249-261.
    • (2003) Exp. Cell Res. , vol.287 , pp. 249-261
    • Van Den Ijssel, P.1    Wheelock, R.2    Prescott, A.3    Russell, P.4    Quinlan, R.A.5
  • 60
    • 0043132253 scopus 로고    scopus 로고
    • Nuclear staining for the small heat shock protein alphaB-crystallin colocalizes with splicing factor SC35
    • van Rijk, A. E., Stege, G. J., Bennink, E. J., May, A., and Bloemendal, H. (2003). Nuclear staining for the small heat shock protein alphaB-crystallin colocalizes with splicing factor SC35. Eur. J. Cell Biol. 82, 361-368.
    • (2003) Eur. J. Cell Biol. , vol.82 , pp. 361-368
    • Van Rijk, A.E.1    Stege, G.J.2    Bennink, E.J.3    May, A.4    Bloemendal, H.5
  • 61
    • 0033863553 scopus 로고    scopus 로고
    • Alpha-crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner
    • Wang, K., and Spector, A. (2000). alpha-crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner. Eur. J. Biochem. 267, 4705-4712.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4705-4712
    • Wang, K.1    Spector, A.2
  • 62
    • 0022531458 scopus 로고
    • RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesis
    • Yost, H. J., and Lindquist, S. (1986). RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesis. Cell 45, 185-193.
    • (1986) Cell , vol.45 , pp. 185-193
    • Yost, H.J.1    Lindquist, S.2
  • 63
    • 0024268031 scopus 로고
    • Translation of unspliced transcripts after heat shock
    • Yost, H. J., and Lindquist, S. (1988). Translation of unspliced transcripts after heat shock. Science 242, 1544-1548.
    • (1988) Science , vol.242 , pp. 1544-1548
    • Yost, H.J.1    Lindquist, S.2
  • 64
    • 0026011111 scopus 로고
    • Heat shock proteins affect RNA processing during the heat shock response of Saccharomyces cerevisiae
    • Yost, H. J., and Lindquist, S. (1991). Heat shock proteins affect RNA processing during the heat shock response of Saccharomyces cerevisiae. Mol. Cell. Biol. 11, 1062-1068.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1062-1068
    • Yost, H.J.1    Lindquist, S.2


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