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Volumn 36, Issue 2, 2003, Pages 88-96

Effect of histone deacetylase inhibitors on heat shock protein gene expression during Xenopus development

Author keywords

Acetylation; Chromatin; In situ; Messenger RNA

Indexed keywords

HEAT SHOCK PROTEIN; HISTONE DEACETYLASE INHIBITOR; MESSENGER RNA;

EID: 0038692918     PISSN: 1526954X     EISSN: None     Source Type: Journal    
DOI: 10.1002/gene.10202     Document Type: Article
Times cited : (27)

References (68)
  • 1
    • 0034254857 scopus 로고    scopus 로고
    • NuRD and SIN3: Histone deacetylase complexes in development
    • Ahringer J. 2000. NuRD and SIN3: histone deacetylase complexes in development. Trends Genet 16:351-356.
    • (2000) Trends Genet , vol.16 , pp. 351-356
    • Ahringer, J.1
  • 2
    • 0027225560 scopus 로고
    • Expression of endogenous and microinjected hsp30 genes in early Xenopus laevis embryos
    • Ali A, Krone P, Heikkila JJ. 1993. Expression of endogenous and microinjected hsp30 genes in early Xenopus laevis embryos. Dev Genet 14:42-50.
    • (1993) Dev Genet , vol.14 , pp. 42-50
    • Ali, A.1    Krone, P.2    Heikkila, J.J.3
  • 3
    • 0029990717 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA encoding a Xenopus 70-kDa heat shock cognate protein, hsc70.I
    • Ali A, Salter-Cid L, Flajnik MF, Heikkila JJ. 1996. Isolation and characterization of a cDNA encoding a Xenopus 70-kDa heat shock cognate protein, hsc70.I. Comp Biochem Physiol 113B:681-687.
    • (1996) Comp Biochem Physiol , vol.113 B , pp. 681-687
    • Ali, A.1    Salter-Cid, L.2    Flajnik, M.F.3    Heikkila, J.J.4
  • 4
    • 0031445745 scopus 로고    scopus 로고
    • Preferential activation of HSF-binding activity and hsp70 gene expression in Xenopus heart after mild hyperthermia
    • Ali A, Fernando P, Smith WL, Ovsenek N, Lepock JR, Heikkila JJ. 1997. Preferential activation of HSF-binding activity and hsp70 gene expression in Xenopus heart after mild hyperthermia. Cell Stress Chaperones 2:229-237.
    • (1997) Cell Stress Chaperones , vol.2 , pp. 229-237
    • Ali, A.1    Fernando, P.2    Smith, W.L.3    Ovsenek, N.4    Lepock, J.R.5    Heikkila, J.J.6
  • 6
    • 0027971019 scopus 로고
    • Histone acetylation influences both gene expression and development of Xenopus laevis
    • Almouzni G, Khochbin S, Dimitrov S, Wolffe AP. 1994. Histone acetylation influences both gene expression and development of Xenopus laevis. Dev Biol 165:654-669.
    • (1994) Dev Biol , vol.165 , pp. 654-669
    • Almouzni, G.1    Khochbin, S.2    Dimitrov, S.3    Wolffe, A.P.4
  • 7
    • 0031962486 scopus 로고    scopus 로고
    • Small stress proteins: Chaperones that act as regulators of intracellular redox state and programmed cell death
    • Arrigo A-P. 1998. Small stress proteins: chaperones that act as regulators of intracellular redox state and programmed cell death. J Biol Chem 379:19-26.
    • (1998) J Biol Chem , vol.379 , pp. 19-26
    • Arrigo, A.-P.1
  • 8
    • 0002241311 scopus 로고
    • Expression and function of the low-molecular-weight heat shock proteins
    • Morimoto RI, Tissieres A, Georgopoulos C, editors. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Arrigo A-P, Landry J. 1994. Expression and function of the low-molecular-weight heat shock proteins. In: Morimoto RI, Tissieres A, Georgopoulos C, editors. The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. p 335-373.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 335-373
    • Arrigo, A.-P.1    Landry, J.2
  • 9
    • 0032940072 scopus 로고    scopus 로고
    • Histone deacetylases: Transcriptional repression with SINers and NuRDs
    • Ayer DE. 1999. Histone deacetylases: transcriptional repression with SINers and NuRDs. Trends Cell Biol 9:193-198.
    • (1999) Trends Cell Biol , vol.9 , pp. 193-198
    • Ayer, D.E.1
  • 10
    • 0021436060 scopus 로고
    • Developmental control of the heat shock response in Xenopus
    • Bienz M. 1984a. Developmental control of the heat shock response in Xenopus. Proc Natl Acad Sci USA 81:3138-3142.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3138-3142
    • Bienz, M.1
  • 11
    • 0021526790 scopus 로고
    • Xenopus hsp70 genes are constitutively expressed in injected oocytes
    • Bienz M. 1984b. Xenopus hsp70 genes are constitutively expressed in injected oocytes. EMBO J 3:2477-2483.
    • (1984) EMBO J , vol.3 , pp. 2477-2483
    • Bienz, M.1
  • 12
    • 0033200392 scopus 로고    scopus 로고
    • A functional interaction between the histone deacetylase RPD3 and the corepressor Groucho in Drosophila development
    • Chen G, Fernandez J, Mische S, Courey AJ. 1999. A functional interaction between the histone deacetylase RPD3 and the corepressor Groucho in Drosophila development. Genes Dev 13:2218-2230.
    • (1999) Genes Dev , vol.13 , pp. 2218-2230
    • Chen, G.1    Fernandez, J.2    Mische, S.3    Courey, A.J.4
  • 13
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin J, Przbyla A, MacDonald R, Rutter W. 1979. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18:5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.1    Przbyla, A.2    MacDonald, R.3    Rutter, W.4
  • 14
    • 0030879870 scopus 로고    scopus 로고
    • The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane
    • Cox JS, Chapman RE, Walter P. 1997. The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane. Mol Biol Cell 8:1805-1814.
    • (1997) Mol Biol Cell , vol.8 , pp. 1805-1814
    • Cox, J.S.1    Chapman, R.E.2    Walter, P.3
  • 15
    • 0033609935 scopus 로고    scopus 로고
    • Hepatocytes nuclear factor 3 relieves chromatin-mediated repression of the α-fetoprotein gene
    • Crowe AJ, Sang L, Li KK, Lee KC, Spear BT, Barton MC. 1999. Hepatocytes nuclear factor 3 relieves chromatin-mediated repression of the α-fetoprotein gene. J Biol Chem 274:25113-25120.
    • (1999) J Biol Chem , vol.274 , pp. 25113-25120
    • Crowe, A.J.1    Sang, L.2    Li, K.K.3    Lee, K.C.4    Spear, B.T.5    Barton, M.C.6
  • 16
    • 0033635948 scopus 로고    scopus 로고
    • Multiple stage-dependent roles for histone deacetylases during amphibian embryogenesis: Implications for the involvement of extracellular matrix remodeling
    • Damjanovski S, Sachs LM, Shi Y-B. 2001. Multiple stage-dependent roles for histone deacetylases during amphibian embryogenesis: implications for the involvement of extracellular matrix remodeling. Int J Dev Biol 44:769-776.
    • (2001) Int J Dev Biol , vol.44 , pp. 769-776
    • Damjanovski, S.1    Sachs, L.M.2    Shi, Y.-B.3
  • 17
    • 0035076210 scopus 로고    scopus 로고
    • Histone acetylation at promoters is differentially affected by specific activators and repressors
    • Deckert J, Struhl K. 2001. Histone acetylation at promoters is differentially affected by specific activators and repressors. Mol Cell Biol 21:2726-2735.
    • (2001) Mol Cell Biol , vol.21 , pp. 2726-2735
    • Deckert, J.1    Struhl, K.2
  • 18
    • 0027429520 scopus 로고
    • Chromatin transitions during early Xenopus embryogenesis: Changes in histone H4 acetylation and linker histone type
    • Dimitrov S, Almouzni G, Dasso M, Wolffe AP. 1993. Chromatin transitions during early Xenopus embryogenesis: changes in histone H4 acetylation and linker histone type. Dev Biol 160:214-227.
    • (1993) Dev Biol , vol.160 , pp. 214-227
    • Dimitrov, S.1    Almouzni, G.2    Dasso, M.3    Wolffe, A.P.4
  • 19
    • 0031571667 scopus 로고    scopus 로고
    • Retinoic acid can block differentiation of the myocardium after heart specification
    • Drysdale TA, Patterson KD, Saha M, Krieg PA. 1997. Retinoic acid can block differentiation of the myocardium after heart specification. Dev Biol 188:205-215.
    • (1997) Dev Biol , vol.188 , pp. 205-215
    • Drysdale, T.A.1    Patterson, K.D.2    Saha, M.3    Krieg, P.A.4
  • 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, 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
  • 22
    • 0031922636 scopus 로고    scopus 로고
    • Control of gene expression in Xenopus early development
    • Hair A, Prioleau M-N, Vassetzky Y, Mechali M. 1998. Control of gene expression in Xenopus early development. Dev Genet 22:122-131.
    • (1998) Dev Genet , vol.22 , pp. 122-131
    • Hair, A.1    Prioleau, M.-N.2    Vassetzky, Y.3    Mechali, M.4
  • 23
    • 0026285616 scopus 로고
    • In situ hybridization: An improved whole-mount method for Xenopus embryos
    • Kay, BK, Peng, HB editors. Toronto: Academic Press
    • Harland RM. 1991. In situ hybridization: an improved whole-mount method for Xenopus embryos. In: Kay, BK, Peng, HB editors. Methods in cell biology, Xenopus laevis: practical uses in cell and molecular biology, vol. 36. Toronto: Academic Press. p 685-694.
    • (1991) Methods in Cell Biology, Xenopus laevis: Practical Uses in Cell and Molecular Biology , vol.36 , pp. 685-694
    • Harland, R.M.1
  • 24
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU. 1996. Molecular chaperones in cellular protein folding. Nature 381:571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 25
    • 0027301001 scopus 로고
    • Heat shock gene expression and development. I. An overview of poikilothermic animal developmental systems
    • Heikkila JJ. 1993a. Heat shock gene expression and development. I. An overview of poikilothermic animal developmental systems. Dev Genet 14:1-5.
    • (1993) Dev Genet , vol.14 , pp. 1-5
    • Heikkila, J.J.1
  • 26
    • 0027159965 scopus 로고
    • Heat shock gene expression and development. II. An overview of mammalian and avian developmental systems
    • Heikkila JJ. 1993b. Heat shock gene expression and development. II. An overview of mammalian and avian developmental systems. Dev Genet 14:87-91.
    • (1993) Dev Genet , vol.14 , pp. 87-91
    • Heikkila, J.J.1
  • 27
    • 0021917408 scopus 로고
    • Acquisition of the heat shock response and thermotolerance in Xenopus laevis
    • Heikkila JJ, Kloc M, Bury J, Schultz GA, Browder L. 1985. Acquisition of the heat shock response and thermotolerance in Xenopus laevis. Dev Biol 107:483-489.
    • (1985) Dev Biol , vol.107 , pp. 483-489
    • Heikkila, J.J.1    Kloc, M.2    Bury, J.3    Schultz, G.A.4    Browder, L.5
  • 28
    • 0023243914 scopus 로고
    • Examination of heat shock protein mRNA accumulation in early Xenopus laevis embryos
    • Heikkila JJ, Ovsenek N, Krone PH. 1987. Examination of heat shock protein mRNA accumulation in early Xenopus laevis embryos. Biochem Cell Biol 65:87-94.
    • (1987) Biochem Cell Biol , vol.65 , pp. 87-94
    • Heikkila, J.J.1    Ovsenek, N.2    Krone, P.H.3
  • 29
    • 0030766710 scopus 로고    scopus 로고
    • Heat shock protein gene expression during Xenopus development
    • Heikkila JJ, Ohan N, Tam Y, Ali A. 1997. Heat shock protein gene expression during Xenopus development. Cell Mol Life Sci 53:114-121.
    • (1997) Cell Mol Life Sci , vol.53 , pp. 114-121
    • Heikkila, J.J.1    Ohan, N.2    Tam, Y.3    Ali, A.4
  • 31
    • 0027525970 scopus 로고
    • Studies of the DNA binding properties of histone H4 amino acid terminus: Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 tail to DNA
    • Hong L, Schroth GP, Matthews HR, Yau P, Bradbury EM. 1993. Studies of the DNA binding properties of histone H4 amino acid terminus: thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 tail to DNA. J Biol Chem 268:305-314.
    • (1993) J Biol Chem , vol.268 , pp. 305-314
    • Hong, L.1    Schroth, G.P.2    Matthews, H.R.3    Yau, P.4    Bradbury, E.M.5
  • 32
    • 0030069517 scopus 로고    scopus 로고
    • HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress
    • Huot JF, Houle F, Spitz DR, Landry J. 1996. HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress. Cancer Res 56:273-279.
    • (1996) Cancer Res , vol.56 , pp. 273-279
    • Huot, J.F.1    Houle, F.2    Spitz, D.R.3    Landry, J.4
  • 33
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. 2001. Translating the histone code. Science 293:1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 34
    • 0031865050 scopus 로고    scopus 로고
    • Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo
    • Kadosh D, Struhl K. 1998. Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo. Mol Cell Biol 18:5121-5127.
    • (1998) Mol Cell Biol , vol.18 , pp. 5121-5127
    • Kadosh, D.1    Struhl, K.2
  • 35
    • 0023613813 scopus 로고
    • The events of the midblastula transition in Xenopus are regulated by changes in the cell cycle
    • Kimelman D, Kirschner M, Scherson T. 1987. The events of the midblastula transition in Xenopus are regulated by changes in the cell cycle. Cell 48:399-407.
    • (1987) Cell , vol.48 , pp. 399-407
    • Kimelman, D.1    Kirschner, M.2    Scherson, T.3
  • 36
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides T. 2000. Acetylation: a regulatory modification to rival phosphorylation? EMBO J 19:1176-1179.
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 37
    • 0023911049 scopus 로고
    • Analysis of hsp 30, hsp 70, and ubiquitin gene expression in Xenopus laevis tadpoles
    • Krone PH, Heikkila JJ. 1988. Analysis of hsp 30, hsp 70, and ubiquitin gene expression in Xenopus laevis tadpoles. Development 103:59-67.
    • (1988) Development , vol.103 , pp. 59-67
    • Krone, P.H.1    Heikkila, J.J.2
  • 38
    • 0024411412 scopus 로고
    • Expression of microinjected hsp 70/CAT and hsp 30/CAT chimeric genes in developing Xenopus laevis embryos
    • Krone PH, Heikkila JJ. 1989. Expression of microinjected hsp 70/CAT and hsp 30/CAT chimeric genes in developing Xenopus laevis embryos. Development 106:271-281.
    • (1989) Development , vol.106 , pp. 271-281
    • Krone, P.H.1    Heikkila, J.J.2
  • 39
    • 0026537572 scopus 로고
    • Comparison of the regulatory regions of the Xenopus laevis small heat-shock protein encoding gene family
    • Krone PH, Snow A, Ali A, Pasternak JJ, Heikkila JJ. 1992. Comparison of the regulatory regions of the Xenopus laevis small heat-shock protein encoding gene family. Gene 110:159-166.
    • (1992) Gene , vol.110 , pp. 159-166
    • Krone, P.H.1    Snow, A.2    Ali, A.3    Pasternak, J.J.4    Heikkila, J.J.5
  • 40
    • 0032757495 scopus 로고    scopus 로고
    • Spatial pattern of constitutive and heat shock-induced expression of the small heat shock protein gene family, hsp30, in Xenopus laevis tailbud embryos
    • Lang L, Miskovic D, Fernando P, Heikkila JJ. 1999. Spatial pattern of constitutive and heat shock-induced expression of the small heat shock protein gene family, hsp30, in Xenopus laevis tailbud embryos. Dev Genet 25:365-374.
    • (1999) Dev Genet , vol.25 , pp. 365-374
    • Lang, L.1    Miskovic, D.2    Fernando, P.3    Heikkila, J.J.4
  • 41
    • 0033954189 scopus 로고    scopus 로고
    • Stress-induced, tissue-specific enrichment of hsp70 mRNA accumulation in Xenopus laevis embryos
    • Lang L, Miskovic D, Lo M, Heikkila JJ. 2000. Stress-induced, tissue-specific enrichment of hsp70 mRNA accumulation in Xenopus laevis embryos. Cell Stress Chaperones 5:36-44.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 36-44
    • Lang, L.1    Miskovic, D.2    Lo, M.3    Heikkila, J.J.4
  • 42
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 angstrom resolution
    • Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ. 1997. Crystal structure of the nucleosome core particle at 2.8 angstrom resolution. Nature 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 45
    • 0033050547 scopus 로고    scopus 로고
    • Constitutive and stress-inducible expression of the endoplasmic reticulum heat shock protein 70 gene Family member, immunoglobulin-binding protein (BiP), during Xenopus laevis early development
    • Miskovic D, Heikkila JJ. 1999. Constitutive and stress-inducible expression of the endoplasmic reticulum heat shock protein 70 gene Family member, immunoglobulin-binding protein (BiP), during Xenopus laevis early development. Dev Genet 25:31-39.
    • (1999) Dev Genet , vol.25 , pp. 31-39
    • Miskovic, D.1    Heikkila, J.J.2
  • 46
    • 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 RI. 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
  • 48
    • 0343416249 scopus 로고    scopus 로고
    • Histone deacetylases: Silencers for hire
    • Ng HH, Bird A. 2000. Histone deacetylases: silencers for hire. Trends Biochem Sci 25:121-126.
    • (2000) Trends Biochem Sci , vol.25 , pp. 121-126
    • Ng, H.H.1    Bird, A.2
  • 50
    • 0032525139 scopus 로고    scopus 로고
    • Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin
    • Nightingale KP, Wellinger RE, Sogo JM, Becker PB. 1998. Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin. EMBO J 17:2865-2876.
    • (1998) EMBO J , vol.17 , pp. 2865-2876
    • Nightingale, K.P.1    Wellinger, R.E.2    Sogo, J.M.3    Becker, P.B.4
  • 51
    • 0025151698 scopus 로고
    • DNA sequence-specific binding activity of the heat shock transcription factor is heat-inducible before the midblastula transition of early Xenopus development
    • Ovsenek N, Heikkila JJ. 1990. DNA sequence-specific binding activity of the heat shock transcription factor is heat-inducible before the midblastula transition of early Xenopus development. Development 110:427-433.
    • (1990) Development , vol.110 , pp. 427-433
    • Ovsenek, N.1    Heikkila, J.J.2
  • 52
    • 0027135501 scopus 로고
    • The function of heat shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell DA, Linquist S. 1994. The function of heat shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu Rev Genet 27:437-496.
    • (1994) Annu Rev Genet , vol.27 , pp. 437-496
    • Parsell, D.A.1    Linquist, S.2
  • 53
    • 0035965343 scopus 로고    scopus 로고
    • Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen
    • Pheil CJ, Zhang F, Huang EY, Guenther MG, Lazar MA, Klein PS. 2001. Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J Biol Chem 276:36734-36741.
    • (2001) J Biol Chem , vol.276 , pp. 36734-36741
    • Pheil, C.J.1    Zhang, F.2    Huang, E.Y.3    Guenther, M.G.4    Lazar, M.A.5    Klein, P.S.6
  • 54
    • 0034669165 scopus 로고    scopus 로고
    • Chromosomal localization links the SIN3-RPD3 complex to the regulation of chromatin condensation, histone acetylation and gene expression
    • Pile LA, Wasserman DA. 2000. Chromosomal localization links the SIN3-RPD3 complex to the regulation of chromatin condensation, histone acetylation and gene expression. EMBO J 19:6131-6140.
    • (2000) EMBO J , vol.19 , pp. 6131-6140
    • Pile, L.A.1    Wasserman, D.A.2
  • 55
    • 0035888026 scopus 로고    scopus 로고
    • Chromatin remodeling, measured by a novel real-time polymerase chain reaction assay, across proximal promoter region of the IL-2 gene
    • Rao S, Procko E, Shannon MF. 2001. Chromatin remodeling, measured by a novel real-time polymerase chain reaction assay, across proximal promoter region of the IL-2 gene. J Immunol 167:4494-4503.
    • (2001) J Immunol , vol.167 , pp. 4494-4503
    • Rao, S.1    Procko, E.2    Shannon, M.F.3
  • 56
    • 0032560117 scopus 로고    scopus 로고
    • Transcription repression by Ume6 involves deacetylation of lysine 5 of histone H4 by Rpd3
    • Rundlett SE, Carmen AA, Suka N, Turner BM, Grunstein M. 1998. Transcription repression by Ume6 involves deacetylation of lysine 5 of histone H4 by Rpd3. Nature 392:831-835.
    • (1998) Nature , vol.392 , pp. 831-835
    • Rundlett, S.E.1    Carmen, A.A.2    Suka, N.3    Turner, B.M.4    Grunstein, M.5
  • 57
    • 0035650655 scopus 로고    scopus 로고
    • An essential role of histone deacetylases in postembryonic organ transformations in Xenopus laevis
    • Sachs LM, Amano T, Shi Y-B. 2001. An essential role of histone deacetylases in postembryonic organ transformations in Xenopus laevis. Int J Mol Med 8:595-601.
    • (2001) Int J Mol Med , vol.8 , pp. 595-601
    • Sachs, L.M.1    Amano, T.2    Shi, Y.-B.3
  • 59
    • 0035107064 scopus 로고    scopus 로고
    • Inhibition of histone deacetylation induces constitutive derepression of the β-interferon promoter and confers antiviral activity
    • Shestakova E, Bandu M-T, Doly J, Bonnefoy E. 2001. Inhibition of histone deacetylation induces constitutive derepression of the β-interferon promoter and confers antiviral activity. J Virol 75:3444-3452.
    • (2001) J Virol , vol.75 , pp. 3444-3452
    • Shestakova, E.1    Bandu, M.-T.2    Doly, J.3    Bonnefoy, E.4
  • 60
    • 0032702598 scopus 로고    scopus 로고
    • Role of covalent modifications of histones in regulating gene expression
    • Spencer VA, Davie JR. 1999. Role of covalent modifications of histones in regulating gene expression. Gene 240:1-12.
    • (1999) Gene , vol.240 , pp. 1-12
    • Spencer, V.A.1    Davie, J.R.2
  • 62
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner DE, Berger SL. 2000. Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64:435-459.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 63
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl K. 1998. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev 12:599-606.
    • (1998) Genes Dev , vol.12 , pp. 599-606
    • Struhl, K.1
  • 65
    • 0029558353 scopus 로고
    • Identification of members of the hsp30 small heat shock protein family and characterization of their developmental regulation in heat-shocked Xenopus laevis embryos
    • Tam Y, Heikkila JJ. 1995. Identification of members of the hsp30 small heat shock protein family and characterization of their developmental regulation in heat-shocked Xenopus laevis embryos. Dev Genet 17:331-339.
    • (1995) Dev Genet , vol.17 , pp. 331-339
    • Tam, Y.1    Heikkila, J.J.2
  • 66
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters E, Lee G, Vierling E. 1996. Evolution, structure and function of the small heat shock proteins in plants. J Exp Biol 47:325-338.
    • (1996) J Exp Biol , vol.47 , pp. 325-338
    • Waters, E.1    Lee, G.2    Vierling, E.3
  • 67
    • 0033926403 scopus 로고    scopus 로고
    • Chromatin structural features and targets that regulate transcription
    • Wolffe AP, Guschin D. 2000. Chromatin structural features and targets that regulate transcription. J Struc Biol 129:102-122.
    • (2000) J Struc Biol , vol.129 , pp. 102-122
    • Wolffe, A.P.1    Guschin, D.2
  • 68
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M, Kikima M, Akita M, Beppu T. 1990. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem 265:17174-17179.
    • (1990) J Biol Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kikima, M.2    Akita, M.3    Beppu, T.4


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