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Volumn 71, Issue 2, 2012, Pages 263-272

Arabidopsis thaliana histone deacetylase 14 (HDA14) is an α-tubulin deacetylase that associates with PP2A and enriches in the microtubule fraction with the putative histone acetyltransferase ELP3

Author keywords

ELP3; HDA14; histone acetyltransferase; histone deacetylase; PP2A; tubulin

Indexed keywords

ELP3; HDA14; HISTONE ACETYLTRANSFERASES; HISTONE DEACETYLASES; PP2A; TUBULIN;

EID: 84864403917     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2012.04984.x     Document Type: Article
Times cited : (80)

References (51)
  • 1
    • 0033897847 scopus 로고    scopus 로고
    • Inhibition of serine/threonine-specific protein phosphatases causes premature activation of cdc2MsF kinase at G2/M transition and early mitotic microtubule organisation in alfalfa
    • DOI 10.1046/j.1365-313X.2000.00798.x
    • Ayaydin, F., Vissi, E., Meszaros, T., Miskolczi, P., Kovacs, I., Feher, A., Dombradi, V., Erdodi, F., Gergely, P., and, Dudits, D., (2000) Inhibition of serine/threonine-specific protein phosphatases causes premature activation of cdc2MsF kinase at G2/M transition and early mitotic microtubule organisation in alfalfa. Plant J. 23, 85-96. (Pubitemid 30597784)
    • (2000) Plant Journal , vol.23 , Issue.1 , pp. 85-96
    • Ayaydin, F.1    Vissi, E.2    Meszaros, T.3    Miskolczi, P.4    Kovacs, I.5    Feher, A.6    Dombradi, V.7    Erdodi, F.8    Gergely, P.9    Dudits, D.10
  • 2
    • 0031079777 scopus 로고    scopus 로고
    • Inhibitors of protein kinases and phosphatases alter root morphology and disorganize cortical microtubules
    • Baskin, T.I., and, Wilson, J.E., (1997) Inhibitors of protein kinases and phosphatases alter root morphology and disorganize cortical microtubules. Plant Physiol. 113, 493-502. (Pubitemid 27164801)
    • (1997) Plant Physiology , vol.113 , Issue.2 , pp. 493-502
    • Baskin, T.I.1    Wilson, J.E.2
  • 3
    • 38949214828 scopus 로고    scopus 로고
    • Specificity of RCN1-mediated protein phosphatase 2A regulation in meristem organization and stress response in roots
    • DOI 10.1104/pp.107.112995
    • Blakeslee, J.J., Zhou, H.W., Heath, J.T., Skottke, K.R., Barrios, J.A., Liu, S.Y., and, DeLong, A., (2008) Specificity of RCN1-mediated protein phosphatase 2A regulation in meristem organization and stress response in roots. Plant Physiol. 146, 539-553. (Pubitemid 351230783)
    • (2008) Plant Physiology , vol.146 , Issue.2 , pp. 539-553
    • Blakeslee, J.J.1    Zhou, H.-W.2    Heath, J.T.3    Skottke, K.R.4    Rodriguez Barrios, J.A.5    Liu, S.-Y.6    DeLong, A.7
  • 4
    • 77955279255 scopus 로고    scopus 로고
    • The extended PP1 toolkit: Designed to create specificity
    • Bollen, M., Peti, W., Ragusa, M.J., and, Beullens, M., (2010) The extended PP1 toolkit: designed to create specificity. Trends Biochem. Sci. 35, 450-458.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 450-458
    • Bollen, M.1    Peti, W.2    Ragusa, M.J.3    Beullens, M.4
  • 5
    • 0035999371 scopus 로고    scopus 로고
    • The Arabidopsis TONNEAU2 gene encodes a putative novel protein phosphatase 2A regulatory subunit essential for the control of the cortical cytoskeleton
    • DOI 10.1105/tpc.010402
    • Camilleri, C., Azimzadeh, J., Pastuglia, M., Bellini, C., Grandjean, O., and, Bouchez, D., (2002) The Arabidopsis TONNEAU2 gene encodes a putative novel protein phosphatase 2A regulatory subunit essential for the control of the cortical cytoskeleton. Plant Cell, 14, 833-845. (Pubitemid 34519605)
    • (2002) Plant Cell , vol.14 , Issue.4 , pp. 833-845
    • Camilleri, C.1    Azimzadeh, J.2    Pastuglia, M.3    Bellini, C.4    Grandjean, O.5    Bouchez, D.6
  • 7
    • 0033391758 scopus 로고    scopus 로고
    • Effect of water stress on root meristems in woody and herbaceous plants during the first stage of development
    • Chiatante, D., Di Iorio, A., Maiuro, L., and, Scippa, S.G., (1999) Effect of water stress on root meristems in woody and herbaceous plants during the first stage of development. Plant Soil, 217, 159-172. (Pubitemid 30106779)
    • (1999) Plant and Soil , vol.217 , Issue.1-2 , pp. 159-172
    • Chiatante, D.1    Di Iorio, A.2    Maiuro, L.3    Scippa, S.G.4
  • 9
    • 6044241641 scopus 로고    scopus 로고
    • Large-scale identification of tubulin-binding proteins provides insight on subcellular trafficking, metabolic channeling, and signaling in plant cells
    • DOI 10.1074/mcp.M400053-MCP200
    • Chuong, S.D., Good, A.G., Taylor, G.J., Freeman, M.C., Moorhead, G.B., and, Muench, D.G., (2004) Large-scale identification of tubulin-binding proteins provides insight on subcellular trafficking, metabolic channeling, and signaling in plant cells. Mol. Cell. Proteomics, 3, 970-983. (Pubitemid 40361232)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.10 , pp. 970-983
    • Chuong, S.D.X.1    Good, A.G.2    Taylor, G.J.3    Freeman, M.C.4    Moorhead, G.B.G.5    Muench, D.G.6
  • 10
    • 59349089711 scopus 로고    scopus 로고
    • Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin
    • Creppe, C., Malinouskaya, L., Volvert, M.L., et al. (2009) Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin. Cell, 136, 551-564.
    • (2009) Cell , vol.136 , pp. 551-564
    • Creppe, C.1    Malinouskaya, L.2    Volvert, M.L.3
  • 11
    • 33747886506 scopus 로고    scopus 로고
    • Switching the flip: Protein phosphatase roles in signaling pathways
    • DeLong, A., (2006) Switching the flip: protein phosphatase roles in signaling pathways. Curr. Opin. Plant Biol. 9, 470-477.
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 470-477
    • Delong, A.1
  • 12
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • DOI 10.1523/JNEUROSCI.0037-07.2007
    • Dompierre, J.P., Godin, J.D., Charrin, B.C., Cordelieres, F.P., King, S.J., Humbert, S., and, Saudou, F., (2007) Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci. 27, 3571-3583. (Pubitemid 46515140)
    • (2007) Journal of Neuroscience , vol.27 , Issue.13 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelieres, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 13
    • 84964608317 scopus 로고    scopus 로고
    • Taperin (c9orf75), a mutated gene in nonsyndromic deafness, encodes a vertebrate specific, nuclear localized protein phosphatase one alpha (PP1α) docking protein
    • Ferrar, T., Chamousset, D., Nimick, M., DeWever, V., Andersen, J., Trinkle-Mulcahy, L., and, Moorhead, G.B.G., (2012) Taperin (c9orf75), a mutated gene in nonsyndromic deafness, encodes a vertebrate specific, nuclear localized protein phosphatase one alpha (PP1α) docking protein. Biology Open, 1, 128-139.
    • (2012) Biology Open , vol.1 , pp. 128-139
    • Ferrar, T.1    Chamousset, D.2    Nimick, M.3    Dewever, V.4    Andersen, J.5    Trinkle-Mulcahy, L.6    Moorhead, G.B.G.7
  • 14
    • 79953689290 scopus 로고    scopus 로고
    • Proteins of diverse function and subcellular location are lysine acetylated in Arabidopsis
    • Finkemeier, I., Laxa, M., Miguet, L., Howden, A.J., and, Sweetlove, L.J., (2011) Proteins of diverse function and subcellular location are lysine acetylated in Arabidopsis. Plant Physiol. 155, 1779-1790.
    • (2011) Plant Physiol. , vol.155 , pp. 1779-1790
    • Finkemeier, I.1    Laxa, M.2    Miguet, L.3    Howden, A.J.4    Sweetlove, L.J.5
  • 15
    • 34547839586 scopus 로고    scopus 로고
    • Potential role of tubulin acetylation and microtubule-based protein trafficking in familial dysautonomia
    • DOI 10.1111/j.1600-0854.2007.00605.x
    • Gardiner, J., Barton, D., Marc, J., and, Overall, R., (2007) Potential role of tubulin acetylation and microtubule-based protein trafficking in familial dysautonomia. Traffic, 8, 1145-1149. (Pubitemid 47244871)
    • (2007) Traffic , vol.8 , Issue.9 , pp. 1145-1149
    • Gardiner, J.1    Barton, D.2    Marc, J.3    Overall, R.4
  • 16
    • 0032767474 scopus 로고    scopus 로고
    • Acetylated tubulin is found in all microtubule arrays of two species of pine
    • Gilmer, S., Clay, P., MacRae, T.H., and, Fowke, L.C., (1999) Acetylated tubulin is found in all microtubule arrays of two species of pine. Protoplasma, 207, 174-185. (Pubitemid 29334990)
    • (1999) Protoplasma , vol.207 , Issue.3-4 , pp. 174-185
    • Gilmer, S.1    Clay, P.2    MacRae, T.H.3    Fowke, L.C.4
  • 18
    • 39149121834 scopus 로고    scopus 로고
    • Tubulin modifications and their cellular functions
    • Hammond, J.W., Cai, D., and, Verhey, K.J., (2008) Tubulin modifications and their cellular functions. Curr. Opin. Cell Biol. 20, 71-76.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 71-76
    • Hammond, J.W.1    Cai, D.2    Verhey, K.J.3
  • 19
    • 39949083195 scopus 로고    scopus 로고
    • PP2A holoenzyme assembly: In cauda venenum (the sting is in the tail)
    • Janssens, V., Longin, S., and, Goris, J., (2008) PP2A holoenzyme assembly: in cauda venenum (the sting is in the tail). Trends Biochem. Sci. 33, 113-121.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 113-121
    • Janssens, V.1    Longin, S.2    Goris, J.3
  • 20
    • 33645669336 scopus 로고    scopus 로고
    • A chloroplast-localized dual-specificity protein phosphatase in Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-binding domain, which binds the polysaccharide starch
    • Kerk, D., Conley, T.R., Rodriguez, F.A., Tran, H.T., Nimick, M., Muench, D.G., and, Moorhead, G.B., (2006) A chloroplast-localized dual-specificity protein phosphatase in Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-binding domain, which binds the polysaccharide starch. Plant J. 46, 400-413.
    • (2006) Plant J. , vol.46 , pp. 400-413
    • Kerk, D.1    Conley, T.R.2    Rodriguez, F.A.3    Tran, H.T.4    Nimick, M.5    Muench, D.G.6    Moorhead, G.B.7
  • 21
    • 38949205017 scopus 로고    scopus 로고
    • Evolutionary radiation pattern of novel protein phosphatases revealed by analysis of protein data from the completely sequenced genomes of humans, green algae, and higher plants
    • DOI 10.1104/pp.107.111393
    • Kerk, D., Templeton, G., and, Moorhead, G.B., (2008) Evolutionary radiation pattern of novel protein phosphatases revealed by analysis of protein data from the completely sequenced genomes of humans, green algae, and higher plants. Plant Physiol. 146, 351-367. (Pubitemid 351230768)
    • (2008) Plant Physiology , vol.146 , Issue.2 , pp. 351-367
    • Kerk, D.1    Templeton, G.2    Moorhead, G.B.G.3
  • 22
    • 19444382725 scopus 로고    scopus 로고
    • Identification of a novel family of 70 kDa microtubule-associated proteins in Arabidopsis cells
    • DOI 10.1111/j.1365-313X.2005.02393.x
    • Korolev, A.V., Chan, J., Naldrett, M.J., Doonan, J.H., and, Lloyd, C.W., (2005) Identification of a novel family of 70 kDa microtubule-associated proteins in Arabidopsis cells. Plant J. 42, 547-555. (Pubitemid 40722150)
    • (2005) Plant Journal , vol.42 , Issue.4 , pp. 547-555
    • Korolev, A.V.1    Chan, J.2    Naldrett, M.J.3    Doonan, J.H.4    Lloyd, C.W.5
  • 23
    • 0028132006 scopus 로고
    • Purification of type 1 protein (serine/threonine) phosphatases by microcystin-Sepharose affinity chromatography
    • DOI 10.1016/0014-5793(94)01232-6
    • Moorhead, G., MacKintosh, R.W., Morrice, N., Gallagher, T., and, MacKintosh, C., (1994) Purification of type 1 protein (serine/threonine) phosphatases by microcystin-Sepharose affinity chromatography. FEBS Lett. 356, 46-50. (Pubitemid 24374030)
    • (1994) FEBS Letters , vol.356 , Issue.1 , pp. 46-50
    • Moorhead, G.1
  • 26
    • 58249089943 scopus 로고    scopus 로고
    • Evolution of protein phosphatases in plants and animals
    • Moorhead, G.B., De Wever, V., Templeton, G., and, Kerk, D., (2009) Evolution of protein phosphatases in plants and animals. Biochem. J. 417, 401-409.
    • (2009) Biochem. J. , vol.417 , pp. 401-409
    • Moorhead, G.B.1    De Wever, V.2    Templeton, G.3    Kerk, D.4
  • 28
    • 76549105500 scopus 로고    scopus 로고
    • Plant Elongator regulates auxin-related genes during RNA polymerase II transcription elongation
    • Nelissen, H., De Groeve, S., Fleury, D., et al. (2010) Plant Elongator regulates auxin-related genes during RNA polymerase II transcription elongation. Proc. Natl Acad. Sci. USA, 107, 1678-1683.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1678-1683
    • Nelissen, H.1    De Groeve, S.2    Fleury, D.3
  • 29
    • 27344457467 scopus 로고    scopus 로고
    • Crystal structure of a bacterial class 2 histone deacetylase homologue
    • DOI 10.1016/j.jmb.2005.09.065, PII S0022283605011459
    • Nielsen, T.K., Hildmann, C., Dickmanns, A., Schwienhorst, A., and, Ficner, R., (2005) Crystal structure of a bacterial class 2 histone deacetylase homologue. J. Mol. Biol. 354, 107-120. (Pubitemid 41527217)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.1 , pp. 107-120
    • Nielsen, T.K.1    Hildmann, C.2    Dickmanns, A.3    Schwienhorst, A.4    Ficner, R.5
  • 30
    • 77951644400 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis
    • Olsen, J.V., Vermeulen, M., Santamaria, A., et al. (2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. 3, ra3.
    • (2010) Sci. Signal. , vol.3
    • Olsen, J.V.1    Vermeulen, M.2    Santamaria, A.3
  • 31
    • 0036929765 scopus 로고    scopus 로고
    • Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes
    • DOI 10.1093/nar/gkf660
    • Pandey, R., Muller, A., Napoli, C.A., Selinger, D.A., Pikaard, C.S., Richards, E.J., Bender, J., Mount, D.W., and, Jorgensen, R.A., (2002) Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes. Nucleic Acids Res. 30, 5036-5055. (Pubitemid 36033021)
    • (2002) Nucleic Acids Research , vol.30 , Issue.23 , pp. 5036-5055
    • Pandey, R.1    Muller, A.2    Napoli, C.A.3    Selinger, D.A.4    Pikaard, C.S.5    Richards, E.J.6    Bender, J.7    Mount, D.W.8    Jorgensen, R.A.9
  • 32
    • 77949772648 scopus 로고    scopus 로고
    • Changes in the accumulation of alpha- and beta-tubulin during bud development in Vitis vinifera L
    • Parrotta, L., Cai, G., and, Cresti, M., (2010) Changes in the accumulation of alpha- and beta-tubulin during bud development in Vitis vinifera L. Planta, 231, 277-291.
    • (2010) Planta , vol.231 , pp. 277-291
    • Parrotta, L.1    Cai, G.2    Cresti, M.3
  • 33
    • 0022399572 scopus 로고
    • Monoclonal antibodies specific for an acetylated form of α-tubulin recognize the antigen in cilia and flagella from a variety of organisms
    • DOI 10.1083/jcb.101.6.2085
    • Piperno, G., and, Fuller, M.T., (1985) Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms. J. Cell Biol. 101, 2085-2094. (Pubitemid 16169938)
    • (1985) Journal of Cell Biology , vol.101 , Issue.6 , pp. 2085-2094
    • Piperno, G.1    Fuller, M.T.2
  • 34
    • 33750618516 scopus 로고    scopus 로고
    • Microtubule Acetylation Promotes Kinesin-1 Binding and Transport
    • DOI 10.1016/j.cub.2006.09.014, PII S096098220602207X
    • Reed, N.A., Cai, D., Blasius, T.L., Jih, G.T., Meyhofer, E., Gaertig, J., and, Verhey, K.J., (2006) Microtubule acetylation promotes kinesin-1 binding and transport. Curr. Biol. 16, 2166-2172. (Pubitemid 44692098)
    • (2006) Current Biology , vol.16 , Issue.21 , pp. 2166-2172
    • Reed, N.A.1    Cai, D.2    Blasius, T.L.3    Jih, G.T.4    Meyhofer, E.5    Gaertig, J.6    Verhey, K.J.7
  • 35
    • 33745813187 scopus 로고    scopus 로고
    • Reading protein modifications with interaction domains
    • DOI 10.1038/nrm1960, PII NRM1960
    • Seet, B.T., Dikic, I., Zhou, M.M., and, Pawson, T., (2006) Reading protein modifications with interaction domains. Nat. Rev. Mol. Cell Biol. 7, 473-483. (Pubitemid 44036453)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.7 , pp. 473-483
    • Seet, B.T.1    Dikic, I.2    Zhou, M.-M.3    Pawson, T.4
  • 36
    • 0033520355 scopus 로고    scopus 로고
    • Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies
    • Sontag, E., Nunbhakdi-Craig, V., Lee, G., Brandt, R., Kamibayashi, C., Kuret, J., White, C.L. III, Mumby, M.C., and, Bloom, G.S., (1999) Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies. J. Biol. Chem. 274, 25490-25498.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25490-25498
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Brandt, R.4    Kamibayashi, C.5    Kuret, J.6    White Iii, C.L.7    Mumby, M.C.8    Bloom, G.S.9
  • 39
    • 2642511406 scopus 로고    scopus 로고
    • Proteomic characterization of protein phosphatase complexes of the mammalian nucleus
    • DOI 10.1074/mcp.M300115-MCP200
    • Tran, H.T., Ulke, A., Morrice, N., Johannes, C.J., and, Moorhead, G.B., (2004) Proteomic characterization of protein phosphatase complexes of the mammalian nucleus. Mol. Cell. Proteomics, 3, 257-265. (Pubitemid 38714281)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.3 , pp. 257-265
    • Tran, H.T.1    Ulke, A.2    Morrice, N.3    Johannes, C.J.4    Moorhead, G.B.G.5
  • 40
    • 82755162955 scopus 로고    scopus 로고
    • Two ancient bacterial-like PPP family phosphatases from Arabidopsis are highly conserved plant proteins that possess unique properties
    • Uhrig, R.G., and, Moorhead, G.B., (2011) Two ancient bacterial-like PPP family phosphatases from Arabidopsis are highly conserved plant proteins that possess unique properties. Plant Physiol. 157, 1778-1792.
    • (2011) Plant Physiol. , vol.157 , pp. 1778-1792
    • Uhrig, R.G.1    Moorhead, G.B.2
  • 43
    • 0742267787 scopus 로고    scopus 로고
    • Post-translational modifications of α-tubulin in Zea mays L. are highly tissue specific
    • DOI 10.1007/s00425-003-1122-4
    • Wang, W., Vignani, R., Scali, M., Sensi, E., and, Cresti, M., (2004) Post-translational modifications of alpha-tubulin in Zea mays L are highly tissue specific. Planta, 218, 460-465. (Pubitemid 38154260)
    • (2004) Planta , vol.218 , Issue.3 , pp. 460-465
    • Wang, W.1    Vignani, R.2    Scali, M.3    Sensi, E.4    Cresti, M.5
  • 45
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: Codified crosstalk with other posttranslational modifications
    • Yang, X.J., and, Seto, E., (2008) Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol. Cell, 31, 449-461.
    • (2008) Mol. Cell , vol.31 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 46
    • 0033967129 scopus 로고    scopus 로고
    • Protein phosphatases PP1 and PP2A are located in distinct positions in the Chlamydomonas flagellar axoneme
    • Yang, P., Fox, L., Colbran, R.J., and, Sale, W.S., (2000) Protein phosphatases PP1 and PP2A are located in distinct positions in the Chlamydomonas flagellar axoneme. J. Cell Sci. 113 (Pt 1), 91-102. (Pubitemid 30066336)
    • (2000) Journal of Cell Science , vol.113 , Issue.1 , pp. 91-102
    • Yang, P.1    Fox, L.2    Colbran, R.J.3    Sale, W.S.4
  • 47
    • 53349117774 scopus 로고    scopus 로고
    • High-quality binary protein interaction map of the yeast interactome network
    • Yu, H., Braun, P., Yildirim, M.A., et al. (2008) High-quality binary protein interaction map of the yeast interactome network. Science, 322, 104-110.
    • (2008) Science , vol.322 , pp. 104-110
    • Yu, H.1    Braun, P.2    Yildirim, M.A.3
  • 48
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • DOI 10.1093/emboj/cdg115
    • Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S., and, Matthias, P., (2003) HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J. 22, 1168-1179. (Pubitemid 36313600)
    • (2003) EMBO Journal , vol.22 , Issue.5 , pp. 1168-1179
    • Zhang, Y.1    Li, N.2    Caron, C.3    Matthias, G.4    Hess, D.5    Khochbin, S.6    Matthias, P.7
  • 49
    • 40749161986 scopus 로고    scopus 로고
    • Mice lacking histone deacetylase 6 have hyperacetylated tubulin but are viable and develop normally
    • Zhang, Y., Kwon, S., Yamaguchi, T., et al. (2008) Mice lacking histone deacetylase 6 have hyperacetylated tubulin but are viable and develop normally. Mol. Cell. Biol. 28, 1688-1701.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1688-1701
    • Zhang, Y.1    Kwon, S.2    Yamaguchi, T.3
  • 50
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • Zhao, S., Xu, W., Jiang, W., et al. (2010) Regulation of cellular metabolism by protein lysine acetylation. Science, 327, 1000-1004.
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3
  • 51
    • 1542752539 scopus 로고    scopus 로고
    • Disparate roles for the regulatory A subunit isoforrns in arabidopsis protein phosphatase 2A
    • DOI 10.1105/tpc.018994
    • Zhou, H.W., Nussbaumer, C., Chao, Y., and, DeLong, A., (2004) Disparate roles for the regulatory A subunit isoforms in Arabidopsis protein phosphatase 2A. Plant Cell, 16, 709-722. (Pubitemid 38335280)
    • (2004) Plant Cell , vol.16 , Issue.3 , pp. 709-722
    • Zhou, H.-W.1    Nussbaumer, C.2    Chao, Y.3    DeLong, A.4


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