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Volumn 86, Issue , 2016, Pages 124-128

The effects of Rpd3 on fly metabolism, health, and longevity

Author keywords

Aging; Dietary restriction; Drosophila melanogaster; dSir2; HDAC; Longevity; rpd3

Indexed keywords

4 PHENYLBUTYRIC ACID; BUTYRIC ACID; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; PROTEIN RPD3; TRICHOSTATIN A; UNCLASSIFIED DRUG; VALPROATE SEMISODIUM; VALPROIC ACID; VORINOSTAT; DROSOPHILA PROTEIN; HISTONE DEACETYLASE 1; RPD3 PROTEIN, DROSOPHILA; SIR2 PROTEIN, DROSOPHILA; SIRTUIN;

EID: 84959526162     PISSN: 05315565     EISSN: 18736815     Source Type: Journal    
DOI: 10.1016/j.exger.2016.02.015     Document Type: Article
Times cited : (5)

References (65)
  • 1
    • 84871695502 scopus 로고    scopus 로고
    • dSir2 in the adult fat body, but not in muscles, regulates life span in a diet-dependent manner
    • Banerjee, K.K., Ayyub, C., Ali, S.Z., Mandot, V., Prasad, N., Kolthur-Seetharam, N.G.U., dSir2 in the adult fat body, but not in muscles, regulates life span in a diet-dependent manner. Cell Rep. 2 (2012), 1485–1491.
    • (2012) Cell Rep. , vol.2 , pp. 1485-1491
    • Banerjee, K.K.1    Ayyub, C.2    Ali, S.Z.3    Mandot, V.4    Prasad, N.5    Kolthur-Seetharam, N.G.U.6
  • 6
    • 28844469898 scopus 로고    scopus 로고
    • Increase in activity during calroie restriction require Sirt1
    • Chen, D., Steele, A.D., Lindquist, S., Guarente, L., Increase in activity during calroie restriction require Sirt1. Science, 310, 2005, 1641.
    • (2005) Science , vol.310 , pp. 1641
    • Chen, D.1    Steele, A.D.2    Lindquist, S.3    Guarente, L.4
  • 8
    • 0029805633 scopus 로고    scopus 로고
    • The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast
    • De Rubertis, F., Kadosh, D., Henchoz, S., Pauli, D., Reuter, G., Struhl, K., Spierer, P., The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast. Nature 384 (1996), 589–591.
    • (1996) Nature , vol.384 , pp. 589-591
    • De Rubertis, F.1    Kadosh, D.2    Henchoz, S.3    Pauli, D.4    Reuter, G.5    Struhl, K.6    Spierer, P.7
  • 10
    • 79952529158 scopus 로고    scopus 로고
    • A circadian rhythm orchestrated by histone deacetylase 3 controls hepatic lipid metabolism
    • Feng, D., Liu, T., Sun, Z., Bugge, A., Mullican, S.E., Alenghat, T., Liu, X.S., Lazar, M.A., A circadian rhythm orchestrated by histone deacetylase 3 controls hepatic lipid metabolism. Science 331 (2011), 1315–1319.
    • (2011) Science , vol.331 , pp. 1315-1319
    • Feng, D.1    Liu, T.2    Sun, Z.3    Bugge, A.4    Mullican, S.E.5    Alenghat, T.6    Liu, X.S.7    Lazar, M.A.8
  • 11
    • 34248523169 scopus 로고    scopus 로고
    • Recovery of learning and memory is associated with chromatin remodelling
    • Fischer, A., Sananbenesi, F., Wang, X., Dobbin, M., Tsai, L.H., Recovery of learning and memory is associated with chromatin remodelling. Nature 447 (2007), 178–182.
    • (2007) Nature , vol.447 , pp. 178-182
    • Fischer, A.1    Sananbenesi, F.2    Wang, X.3    Dobbin, M.4    Tsai, L.H.5
  • 12
    • 52049126629 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors improve learning consolidation in young and in KA-induced-neurodegeneration and SAMP-8-mutant mice
    • Fontan-Lozano, A., Romero-Granados, R., Troncoso, J., Munera, A., Delgado-Garcia, J.M., Carrion, A.M., Histone deacetylase inhibitors improve learning consolidation in young and in KA-induced-neurodegeneration and SAMP-8-mutant mice. Mol. Cell. Neurosci. 39 (2008), 193–201.
    • (2008) Mol. Cell. Neurosci. , vol.39 , pp. 193-201
    • Fontan-Lozano, A.1    Romero-Granados, R.2    Troncoso, J.3    Munera, A.4    Delgado-Garcia, J.M.5    Carrion, A.M.6
  • 14
    • 84958149071 scopus 로고    scopus 로고
    • RPD3 histone deacetylase and nutrition have distinct but interacting effects on Drosophila longevity
    • Frankel, S., Woods, J.K., Ziafazeli, T., Rogina, B., RPD3 histone deacetylase and nutrition have distinct but interacting effects on Drosophila longevity. Aging 7 (2015), 1–18.
    • (2015) Aging , vol.7 , pp. 1-18
    • Frankel, S.1    Woods, J.K.2    Ziafazeli, T.3    Rogina, B.4
  • 15
    • 85001852252 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitors — emerging roles in neuronal memory, learning, synaptic plasticity and neural regeneration
    • Ganai, S.A., Ramadoss, M., Mahadevan, V., Histone deacetylase (HDAC) inhibitors — emerging roles in neuronal memory, learning, synaptic plasticity and neural regeneration. Curr. Neuropharmacol., 5, 2015, 15067.
    • (2015) Curr. Neuropharmacol. , vol.5 , pp. 15067
    • Ganai, S.A.1    Ramadoss, M.2    Mahadevan, V.3
  • 16
    • 66449123586 scopus 로고    scopus 로고
    • Acetylation/deacetylation modulates the stability of DNA replication licensing factor Cdt1
    • Glozak, M.A., Seto, E., Acetylation/deacetylation modulates the stability of DNA replication licensing factor Cdt1. J. Biol. Chem. 284 (2009), 11446–11453.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11446-11453
    • Glozak, M.A.1    Seto, E.2
  • 17
    • 84941425076 scopus 로고    scopus 로고
    • Loss of histone deacetylase Hdac1 disrupts metabolic processes in intestinal epithelial cells
    • Gonneaud, A., Turgeon, N., Boisvert, F.M., Boudreau, F., Asselin, C., Loss of histone deacetylase Hdac1 disrupts metabolic processes in intestinal epithelial cells. FEBS Lett. 589 (2015), 2776–2783.
    • (2015) FEBS Lett. , vol.589 , pp. 2776-2783
    • Gonneaud, A.1    Turgeon, N.2    Boisvert, F.M.3    Boudreau, F.4    Asselin, C.5
  • 19
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p
    • Grozinger, C.M., Hassig, C.A., Schreiber, S.L., Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc. Natl. Acad. Sci. U. S. A. 96 (1999), 4868–4873.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 20
    • 0842325787 scopus 로고    scopus 로고
    • Histone deacetylase is a target of valproic acid-mediated cellular differentiation
    • Gurvich, N., Tsygankova, O.M., Meinkoth, J.L., Klein, P.S., Histone deacetylase is a target of valproic acid-mediated cellular differentiation. Cancer Res. 64 (2004), 1079–1086.
    • (2004) Cancer Res. , vol.64 , pp. 1079-1086
    • Gurvich, N.1    Tsygankova, O.M.2    Meinkoth, J.L.3    Klein, P.S.4
  • 21
    • 84886812954 scopus 로고    scopus 로고
    • The nextus of chromatin regulation and intermediary metabolism
    • Gut, P., Verdin, E., The nextus of chromatin regulation and intermediary metabolism. Nature 502 (2013), 489–498.
    • (2013) Nature , vol.502 , pp. 489-498
    • Gut, P.1    Verdin, E.2
  • 22
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: biological insights and disease relevance
    • Haigis, M.C., Sinclair, D.A., Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5 (2010), 253–295.
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 23
    • 84877648303 scopus 로고    scopus 로고
    • Overexpression of Sir2 in the adult fat body is sufficient to extend lifespan of male and female drosophila
    • Hoffman, J., Romey, R., Fink, C., Yong, L., Roder, T., Overexpression of Sir2 in the adult fat body is sufficient to extend lifespan of male and female drosophila. Aging 4 (2013), 315–327.
    • (2013) Aging , vol.4 , pp. 315-327
    • Hoffman, J.1    Romey, R.2    Fink, C.3    Yong, L.4    Roder, T.5
  • 24
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S., Armstrong, C.M., Kaberlein, M., Guarente, L., Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403 (2000), 795–800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaberlein, M.3    Guarente, L.4
  • 27
    • 0036696982 scopus 로고    scopus 로고
    • Distinct roles of processes modulated by histone deacetylases Rpd3p, Hda1p, and Sir2p in life extension by caloric restriction in yeast
    • Jiang, J.C., Wawryn, J., Shantha Kumara, H.M., Jazwinski, S.M., Distinct roles of processes modulated by histone deacetylases Rpd3p, Hda1p, and Sir2p in life extension by caloric restriction in yeast. Exp. Gerontol. 37 (2002), 1023–1030.
    • (2002) Exp. Gerontol. , vol.37 , pp. 1023-1030
    • Jiang, J.C.1    Wawryn, J.2    Shantha Kumara, H.M.3    Jazwinski, S.M.4
  • 28
    • 0034617261 scopus 로고    scopus 로고
    • Histone deacetylases specifically down-regulate p53-dependent gene activation
    • Juan, L.J., Shia, W.J., Chen, M.H., Yang, W.M., Seto, E., Lin, Y.S., Wu, C.W., Histone deacetylases specifically down-regulate p53-dependent gene activation. J. Biol. Chem. 275 (2000), 20436–20443.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20436-20443
    • Juan, L.J.1    Shia, W.J.2    Chen, M.H.3    Yang, W.M.4    Seto, E.5    Lin, Y.S.6    Wu, C.W.7
  • 29
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein, M., McVey, M., Guerente, L., The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13 (1999), 2570–2580.
    • (1999) Genes Dev. , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guerente, L.3
  • 31
    • 0037154205 scopus 로고    scopus 로고
    • Life span extension in drosophila by feeding a drug
    • Kang, H., Benzer, S., Min, K., Life span extension in drosophila by feeding a drug. Proc. Natl. Acad. Sci. U. S. A. 99 (2002), 838–843.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 838-843
    • Kang, H.1    Benzer, S.2    Min, K.3
  • 32
    • 0030877160 scopus 로고    scopus 로고
    • A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators
    • Kasten, M.M., Dorland, S., Stillman, D.J., A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators. Mol. Cell. Biol. 17 (1997), 4852–4858.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4852-4858
    • Kasten, M.M.1    Dorland, S.2    Stillman, D.J.3
  • 33
    • 79954632599 scopus 로고    scopus 로고
    • Role of TOR signaling in aging and related biological processes in Drosophila melanogaster
    • Katewa, S.D., Kapahi, P., Role of TOR signaling in aging and related biological processes in Drosophila melanogaster. Exp. Gerontol. 46 (2011), 382–390.
    • (2011) Exp. Gerontol. , vol.46 , pp. 382-390
    • Katewa, S.D.1    Kapahi, P.2
  • 34
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • Kazantsev, A.G., Thompson, L.M., Therapeutic application of histone deacetylase inhibitors for central nervous system disorders. Nat. Rev. Drug Discov. 7 (2008), 854–868.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 854-868
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 35
    • 0032831936 scopus 로고    scopus 로고
    • Modulation of life-span by histone deacetylase genes in Saccharomyces cerevisiae
    • Kim, S., Benguria, A., Lai, C.Y., Jazwinski, S.M., Modulation of life-span by histone deacetylase genes in Saccharomyces cerevisiae. Mol. Biol. Cell 10 (1999), 3125–3136.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3125-3136
    • Kim, S.1    Benguria, A.2    Lai, C.Y.3    Jazwinski, S.M.4
  • 36
    • 41949120723 scopus 로고    scopus 로고
    • Liver-specific deletion of histone deacetylase 3 discrupts metabolic transcriptional network
    • Knutson, S.K., Chyla, B.J., Amann, J.M., Bhaskara, S., Huppert, S.S., Hiebert, S.W., Liver-specific deletion of histone deacetylase 3 discrupts metabolic transcriptional network. EMBO J. 27 (2008), 1017–1028.
    • (2008) EMBO J. , vol.27 , pp. 1017-1028
    • Knutson, S.K.1    Chyla, B.J.2    Amann, J.M.3    Bhaskara, S.4    Huppert, S.S.5    Hiebert, S.W.6
  • 37
    • 84943400659 scopus 로고    scopus 로고
    • Heart-specific Rpd3 downregulation enhances cardiac function and longevity
    • Kopp, Z.A., et al. Heart-specific Rpd3 downregulation enhances cardiac function and longevity. Aging 7 (2015), 648–663.
    • (2015) Aging , vol.7 , pp. 648-663
    • Kopp, Z.A.1
  • 38
    • 34047255367 scopus 로고    scopus 로고
    • Valproic acid, a molecular lead to multiple regulatory pathways
    • Kostrouchova, M., Kostrouch, Z., Kostrouchova, M., Valproic acid, a molecular lead to multiple regulatory pathways. Folia Biol. 53 (2007), 37–49.
    • (2007) Folia Biol. , vol.53 , pp. 37-49
    • Kostrouchova, M.1    Kostrouch, Z.2    Kostrouchova, M.3
  • 39
    • 0032582489 scopus 로고    scopus 로고
    • Extended life-span and stress resistance in the Drosophila mutant methuselah
    • Lin, Y.J., Seroude, L., Benzer, S., Extended life-span and stress resistance in the Drosophila mutant methuselah. Science 282 (1998), 943–946.
    • (1998) Science , vol.282 , pp. 943-946
    • Lin, Y.J.1    Seroude, L.2    Benzer, S.3
  • 41
    • 0033535957 scopus 로고    scopus 로고
    • The Rpd3 histone deacetylase is required for segmentation of the Drosophila embryo
    • Mannervik, M., Levine, M., The Rpd3 histone deacetylase is required for segmentation of the Drosophila embryo. Proc. Natl. Acad. Sci. U. S. A. 96 (1999), 6797–6801.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6797-6801
    • Mannervik, M.1    Levine, M.2
  • 42
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug
    • Marks, P.A., Breslow, R., Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug. Nat. Biotechnol. 25 (2007), 84–90.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 43
    • 84872761579 scopus 로고    scopus 로고
    • Chemical regulation of mid- and late-life longevities in Drosophila
    • McDonald, P., Maizi, B.M., Arking, R., Chemical regulation of mid- and late-life longevities in Drosophila. Exp. Gerontol. 48 (2013), 240–249.
    • (2013) Exp. Gerontol. , vol.48 , pp. 240-249
    • McDonald, P.1    Maizi, B.M.2    Arking, R.3
  • 44
    • 84871650811 scopus 로고    scopus 로고
    • Metabolic reprogramming by class i and II histone deacetylases
    • Mihaylova, M.M., Shaw, R.J., Metabolic reprogramming by class i and II histone deacetylases. Trends Endocrinol. Metab. 24 (2012), 48–57.
    • (2012) Trends Endocrinol. Metab. , vol.24 , pp. 48-57
    • Mihaylova, M.M.1    Shaw, R.J.2
  • 45
    • 66049101024 scopus 로고    scopus 로고
    • Histone deacetylase 1 and 2 control the progression of neural precursors to neurons during brain development
    • Montgomery, R.L., Hsieh, J., Barbosa, A.C., Richardson, J.A., Olson, E.N., Histone deacetylase 1 and 2 control the progression of neural precursors to neurons during brain development. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 7876–7881.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 7876-7881
    • Montgomery, R.L.1    Hsieh, J.2    Barbosa, A.C.3    Richardson, J.A.4    Olson, E.N.5
  • 46
    • 0033952282 scopus 로고    scopus 로고
    • Mutational analysis of a histone deacetylase in Drosophila melanogaster: missense mutations suppress gene silencing associated with position effect variegation
    • Mottus, R., Sobel, R.E., Grigliatti, T.A., Mutational analysis of a histone deacetylase in Drosophila melanogaster: missense mutations suppress gene silencing associated with position effect variegation. Genetics 154 (2000), 657–668.
    • (2000) Genetics , vol.154 , pp. 657-668
    • Mottus, R.1    Sobel, R.E.2    Grigliatti, T.A.3
  • 47
    • 53249114029 scopus 로고    scopus 로고
    • Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease
    • Pallos, J., Bodai, L., Lukacsovich, T., Purcell, J.M., Steffan, J.S., Thompson, L.M., Marsh, J.L., Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease. Hum. Mol. Genet. 17 (2008), 3767–3775.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3767-3775
    • Pallos, J.1    Bodai, L.2    Lukacsovich, T.3    Purcell, J.M.4    Steffan, J.S.5    Thompson, L.M.6    Marsh, J.L.7
  • 48
    • 77953589623 scopus 로고    scopus 로고
    • dSir2 mediates the increased spontaneous physical activity in flies on calorie restriction
    • Parashar, V., Rogina, B., dSir2 mediates the increased spontaneous physical activity in flies on calorie restriction. Aging 1 (2009), 529–541.
    • (2009) Aging , vol.1 , pp. 529-541
    • Parashar, V.1    Rogina, B.2
  • 49
    • 0034669165 scopus 로고    scopus 로고
    • Chromosomal localization links the SIN3–RPD3 complex to the regulation of chromatin condensation, histone acetylation and gene expression
    • Pile, L.A., Wassarman, D.A., Chromosomal localization links the SIN3–RPD3 complex to the regulation of chromatin condensation, histone acetylation and gene expression. EMBO J. 19 (2000), 6131–6140.
    • (2000) EMBO J. , vol.19 , pp. 6131-6140
    • Pile, L.A.1    Wassarman, D.A.2
  • 50
    • 0141621080 scopus 로고    scopus 로고
    • The SIN3 deacetylase complex represses genes encoding mitochondrial proteins: implications for the regulation of energy metabolism
    • Pile, L.A., Spellman, P.T., Katzenberger, R.J., Wassarman, D.A., The SIN3 deacetylase complex represses genes encoding mitochondrial proteins: implications for the regulation of energy metabolism. J. Biol. Chem. 278 (2003), 37840–37848.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37840-37848
    • Pile, L.A.1    Spellman, P.T.2    Katzenberger, R.J.3    Wassarman, D.A.4
  • 51
    • 84900481019 scopus 로고    scopus 로고
    • Increased mitochondrial biogenesis preserves intestinal stem cell homeostasis and contributes to longevity in Indy mutant flies
    • Rogers, R.P., Rogina, B., Increased mitochondrial biogenesis preserves intestinal stem cell homeostasis and contributes to longevity in Indy mutant flies. Aging 6 (2014), 335–350.
    • (2014) Aging , vol.6 , pp. 335-350
    • Rogers, R.P.1    Rogina, B.2
  • 52
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • Rogina, B., Helfand, S.L., Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl. Acad. Sci. U. S. A. 101 (2004), 15998–16003.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 53
    • 18744416824 scopus 로고    scopus 로고
    • Longevity regulation by Drosophila Rpd3 deacetylase and caloric restriction
    • Rogina, B., Helfand, S.L., Frankel, S., Longevity regulation by Drosophila Rpd3 deacetylase and caloric restriction. Science, 298, 2002, 1745.
    • (2002) Science , vol.298 , pp. 1745
    • Rogina, B.1    Helfand, S.L.2    Frankel, S.3
  • 54
    • 84921425001 scopus 로고    scopus 로고
    • Erasers of histone acetylations: the histone deacetyase enzymes
    • Seto, E., Yoshida, M., Erasers of histone acetylations: the histone deacetyase enzymes. Cold Spring Harb. Perspect. Biol., 6, 2014, a08713.
    • (2014) Cold Spring Harb. Perspect. Biol. , vol.6 , pp. a08713
    • Seto, E.1    Yoshida, M.2
  • 55
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C.A., Schreiber, S.L., A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272 (1996), 408–411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 56
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum, H.A., Guarente, L., Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410 (2001), 227–230.
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 57
    • 0026060619 scopus 로고
    • RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae
    • Vidal, M., Gaber, R.F., RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae. Mol. Cell. Biol. 11 (1991), 6317–6327.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 6317-6327
    • Vidal, M.1    Gaber, R.F.2
  • 58
    • 0026046959 scopus 로고
    • RPD1 (SIN3/UME4) is required for maximal activation and repression of diverse yeast genes
    • Vidal, M., Strich, R., Esposito, R.E., Gaber, R.F., RPD1 (SIN3/UME4) is required for maximal activation and repression of diverse yeast genes. Mol. Cell. Biol. 11 (1991), 6306–6316.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 6306-6316
    • Vidal, M.1    Strich, R.2    Esposito, R.E.3    Gaber, R.F.4
  • 60
  • 61
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
    • Yang, X.J., Seto, E., The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. Nat. Rev. Mol. Cell Biol. 9 (2008), 206–218.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 206-218
    • Yang, X.J.1    Seto, E.2
  • 62
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YYi is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3
    • Yang, W.M., Inouye, C., Zeng, Y., Bearss, D., Seto, E., Transcriptional repression by YYi is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. Proc. Natl. Acad. Sci. U. S. A. 93 (1996), 12845–12850.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 12845-12850
    • Yang, W.M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 63
    • 12244251445 scopus 로고    scopus 로고
    • Stat3 dimerization regulated by reversible acetylation of a single lysine residue
    • Yuan, Z.L., Guan, Y.J., Chatterjee, D., Chin, Y.E., Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science 307 (2005), 269–273.
    • (2005) Science , vol.307 , pp. 269-273
    • Yuan, Z.L.1    Guan, Y.J.2    Chatterjee, D.3    Chin, Y.E.4
  • 64
    • 15044356553 scopus 로고    scopus 로고
    • Lifespan extension and elevated hsp gene expression in Drosophila caused by histone deacetylase inhibitors
    • Zhao, Y., Sun, H., Lu, J., Li, X., Chen, X., Tao, D., Huang, W., Huang, B., Lifespan extension and elevated hsp gene expression in Drosophila caused by histone deacetylase inhibitors. J. Exp. Biol. 208 (2005), 687–705.
    • (2005) J. Exp. Biol. , vol.208 , pp. 687-705
    • Zhao, Y.1    Sun, H.2    Lu, J.3    Li, X.4    Chen, X.5    Tao, D.6    Huang, W.7    Huang, B.8
  • 65
    • 84864290214 scopus 로고    scopus 로고
    • Histone deacetylation inhibition in pulmonary hypertension: therapeutic potential of valproic acid and suberoylanilide hydroxamic acid
    • Zhao, L., Chen, C.N., Hajji, N., Oliver, E., Cotroneo, E., Wharton, J., Wang, D., Li, M., McKinsey, T.A., Stenmark, K.R., et al. Histone deacetylation inhibition in pulmonary hypertension: therapeutic potential of valproic acid and suberoylanilide hydroxamic acid. Circulation 126 (2012), 455–467.
    • (2012) Circulation , vol.126 , pp. 455-467
    • Zhao, L.1    Chen, C.N.2    Hajji, N.3    Oliver, E.4    Cotroneo, E.5    Wharton, J.6    Wang, D.7    Li, M.8    McKinsey, T.A.9    Stenmark, K.R.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.