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Volumn 10, Issue 3, 2015, Pages

Proteome-wide lysine acetylation in cortical astrocytes and alterations that occur during infection with brain parasite Toxoplasma gondii

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; LYSINE; LYSINE ACETYLTRANSFERASE; LYSINE DEACETYLASE; PROTEOME; UNCLASSIFIED DRUG; NERVE PROTEIN;

EID: 84925424684     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0117966     Document Type: Article
Times cited : (18)

References (99)
  • 1
    • 0037131025 scopus 로고    scopus 로고
    • New insights into neuron-glia communication
    • PMID: 12386325
    • Fields RD, Stevens-Graham B (2002) New insights into neuron-glia communication. Science 298: 556-562. PMID: 12386325
    • (2002) Science , vol.298 , pp. 556-562
    • Fields, R.D.1    Stevens-Graham, B.2
  • 2
    • 79960003831 scopus 로고    scopus 로고
    • Human immunodeficiency virus infection of human astrocytes disrupts blood-brain barrier integrity by a gap junction-dependent mechanism
    • PMID: 21715610
    • Eugenin EA, Clements JE, Zink MC, Berman JW (2011) Human immunodeficiency virus infection of human astrocytes disrupts blood-brain barrier integrity by a gap junction-dependent mechanism. J Neurosci 31: 9456-9465. doi: 10.1523/JNEUROSCI.1460-11.2011 PMID: 21715610
    • (2011) J Neurosci , vol.31 , pp. 9456-9465
    • Eugenin, E.A.1    Clements, J.E.2    Zink, M.C.3    Berman, J.W.4
  • 3
    • 3543008895 scopus 로고    scopus 로고
    • Entry of Listeria monocytogenes into neurons occurs by cell-to-cell spread: An in vitro study
    • PMID: 9712801
    • Dramsi S, Levi S, Triller A, Cossart P (1998) Entry of Listeria monocytogenes into neurons occurs by cell-to-cell spread: an in vitro study. Infect Immun 66: 4461-4468. PMID: 9712801
    • (1998) Infect Immun , vol.66 , pp. 4461-4468
    • Dramsi, S.1    Levi, S.2    Triller, A.3    Cossart, P.4
  • 4
    • 0024391718 scopus 로고
    • An electron microscope and immunohistochemical study of the intracellular location of Toxoplasma tissue cysts within the brains of mice with congenital toxoplasmosis
    • PMID: 2504268
    • Sims TA, Hay J, Talbot IC (1989) An electron microscope and immunohistochemical study of the intracellular location of Toxoplasma tissue cysts within the brains of mice with congenital toxoplasmosis. Br J Exp Pathol 70: 317-325. PMID: 2504268
    • (1989) Br J Exp Pathol , vol.70 , pp. 317-325
    • Sims, T.A.1    Hay, J.2    Talbot, I.C.3
  • 5
    • 0029851770 scopus 로고    scopus 로고
    • Growth and development of Toxoplasma gondii in human neurons and astrocytes
    • PMID: 8939198
    • Halonen SK, Lyman WD, Chiu FC (1996) Growth and development of Toxoplasma gondii in human neurons and astrocytes. J Neuropathol Exp Neurol 55: 1150-1156. PMID: 8939198
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 1150-1156
    • Halonen, S.K.1    Lyman, W.D.2    Chiu, F.C.3
  • 6
    • 2942541583 scopus 로고    scopus 로고
    • Toxoplasmosis
    • PMID: 15194258
    • Montoya JG, Liesenfeld O (2004) Toxoplasmosis. Lancet 363: 1965-1976. PMID: 15194258
    • (2004) Lancet , vol.363 , pp. 1965-1976
    • Montoya, J.G.1    Liesenfeld, O.2
  • 7
    • 26044470703 scopus 로고    scopus 로고
    • Biology and epidemiology of Toxoplasma gondii in man and animals
    • PMID: 16164008
    • Hill DE, Chirukandoth S, Dubey JP (2005) Biology and epidemiology of Toxoplasma gondii in man and animals. Anim Health Res Rev 6: 41-61. PMID: 16164008
    • (2005) Anim Health Res Rev , vol.6 , pp. 41-61
    • Hill, D.E.1    Chirukandoth, S.2    Dubey, J.P.3
  • 8
    • 84859350581 scopus 로고    scopus 로고
    • Mechanisms of Toxoplasma gondii persistence and latency
    • Sullivan WJ Jr, Jeffers V (2012) Mechanisms of Toxoplasma gondii persistence and latency. FEMS microbiology reviews 36: 725-733.
    • (2012) FEMS Microbiology Reviews , vol.36 , pp. 725-733
    • Sullivan, W.J.1    Jeffers, V.2
  • 9
    • 0026675678 scopus 로고
    • Kinetics of cytokine mRNA production in the brains of mice with progressive toxoplasmic encephalitis
    • PMID: 1516621
    • Hunter CA, Roberts CW, Alexander J (1992) Kinetics of cytokine mRNA production in the brains of mice with progressive toxoplasmic encephalitis. Eur J Immunol 22: 2317-2322. PMID: 1516621
    • (1992) Eur J Immunol , vol.22 , pp. 2317-2322
    • Hunter, C.A.1    Roberts, C.W.2    Alexander, J.3
  • 10
    • 0023506773 scopus 로고
    • An ultrastructural study of the early development and tissue cyst formation of Toxoplasma gondii in the brains of mice
    • PMID: 3422976
    • Ferguson DJ, Hutchison WM (1987) An ultrastructural study of the early development and tissue cyst formation of Toxoplasma gondii in the brains of mice. Parasitol Res 73: 483-491. PMID: 3422976
    • (1987) Parasitol Res , vol.73 , pp. 483-491
    • Ferguson, D.J.1    Hutchison, W.M.2
  • 11
    • 0034861021 scopus 로고    scopus 로고
    • Gamma interferon-induced inhibition of Toxoplasma gondii in astrocytes is mediated by IGTP
    • PMID: 11500431
    • Halonen SK, Taylor GA, Weiss LM (2001) Gamma interferon-induced inhibition of Toxoplasma gondii in astrocytes is mediated by IGTP. Infect Immun 69: 5573-5576. PMID: 11500431
    • (2001) Infect Immun , vol.69 , pp. 5573-5576
    • Halonen, S.K.1    Taylor, G.A.2    Weiss, L.M.3
  • 12
    • 19944387923 scopus 로고    scopus 로고
    • Differential effects of interferon-gamma and tumor necrosis factor-alpha on Toxoplasma gondii proliferation in organotypic rat brain slice cultures
    • PMID: 15986605
    • Scheidegger A, Vonlaufen N, Naguleswaran A, Gianinazzi C, Muller N, et al. (2005) Differential effects of interferon-gamma and tumor necrosis factor-alpha on Toxoplasma gondii proliferation in organotypic rat brain slice cultures. J Parasitol 91: 307-315. PMID: 15986605
    • (2005) J Parasitol , vol.91 , pp. 307-315
    • Scheidegger, A.1    Vonlaufen, N.2    Naguleswaran, A.3    Gianinazzi, C.4    Muller, N.5
  • 13
    • 1842454626 scopus 로고    scopus 로고
    • The role of astrocytes in the immunopathogenesis of toxoplasmic encephalitis
    • PMID: 15064118
    • Wilson EH, Hunter CA (2004) The role of astrocytes in the immunopathogenesis of toxoplasmic encephalitis. Int J Parasitol 34: 543-548. PMID: 15064118
    • (2004) Int J Parasitol , vol.34 , pp. 543-548
    • Wilson, E.H.1    Hunter, C.A.2
  • 14
    • 52949085996 scopus 로고    scopus 로고
    • Astrocyte gp130 expression is critical for the control of Toxoplasma encephalitis
    • PMID: 18684959
    • Drogemuller K, Helmuth U, Brunn A, Sakowicz-Burkiewicz M, Gutmann DH, et al. (2008) Astrocyte gp130 expression is critical for the control of Toxoplasma encephalitis. J Immunol 181: 2683-2693. PMID: 18684959
    • (2008) J Immunol , vol.181 , pp. 2683-2693
    • Drogemuller, K.1    Helmuth, U.2    Brunn, A.3    Sakowicz-Burkiewicz, M.4    Gutmann, D.H.5
  • 15
    • 0036942730 scopus 로고    scopus 로고
    • Chemokines are differentially expressed by astrocytes, microglia and inflammatory leukocytes in Toxoplasma encephalitis and critically regulated by interferon-gamma
    • PMID: 11935261
    • Strack A, Asensio VC, Campbell IL, Schluter D, Deckert M (2002) Chemokines are differentially expressed by astrocytes, microglia and inflammatory leukocytes in Toxoplasma encephalitis and critically regulated by interferon-gamma. Acta Neuropathol 103: 458-468. PMID: 11935261
    • (2002) Acta Neuropathol , vol.103 , pp. 458-468
    • Strack, A.1    Asensio, V.C.2    Campbell, I.L.3    Schluter, D.4    Deckert, M.5
  • 16
    • 0035968207 scopus 로고    scopus 로고
    • Microarray analysis reveals previously unknown changes in Toxoplasma gondii-infected human cells
    • PMID: 11294868
    • Blader IJ, Manger ID, Boothroyd JC (2001) Microarray analysis reveals previously unknown changes in Toxoplasma gondii-infected human cells. J Biol Chem 276: 24223-24231. PMID: 11294868
    • (2001) J Biol Chem , vol.276 , pp. 24223-24231
    • Blader, I.J.1    Manger, I.D.2    Boothroyd, J.C.3
  • 17
    • 33846322896 scopus 로고    scopus 로고
    • Toxoplasma co-opts host gene expression by injection of a polymorphic kinase homologue
    • PMID: 17183270
    • Saeij JP, Coller S, Boyle JP, Jerome ME, White MW, et al. (2007) Toxoplasma co-opts host gene expression by injection of a polymorphic kinase homologue. Nature 445: 324-327. PMID: 17183270
    • (2007) Nature , vol.445 , pp. 324-327
    • Saeij, J.P.1    Coller, S.2    Boyle, J.P.3    Jerome, M.E.4    White, M.W.5
  • 18
    • 84892860527 scopus 로고    scopus 로고
    • Transcriptional analysis of murine macrophages infected with different Toxoplasma strains identifies novel regulation of host signaling pathways
    • PMID: 24367253
    • Melo MB, Nguyen QP, Cordeiro C, Hassan MA, Yang N, et al. (2013) Transcriptional analysis of murine macrophages infected with different Toxoplasma strains identifies novel regulation of host signaling pathways. PLoS Pathog 9: e1003779. doi: 10.1371/journal.ppat.1003779 PMID: 24367253
    • (2013) PLoS Pathog , vol.9 , pp. e1003779
    • Melo, M.B.1    Nguyen, Q.P.2    Cordeiro, C.3    Hassan, M.A.4    Yang, N.5
  • 19
    • 39149086727 scopus 로고    scopus 로고
    • Modulation of the host cell proteome by the intracellular apicomplexan parasite Toxoplasma gondii
    • PMID: 17967855
    • Nelson MM, Jones AR, Carmen JC, Sinai AP, Burchmore R, et al. (2008) Modulation of the host cell proteome by the intracellular apicomplexan parasite Toxoplasma gondii. Infect Immun 76: 828-844. PMID: 17967855
    • (2008) Infect Immun , vol.76 , pp. 828-844
    • Nelson, M.M.1    Jones, A.R.2    Carmen, J.C.3    Sinai, A.P.4    Burchmore, R.5
  • 20
    • 83055173136 scopus 로고    scopus 로고
    • Modulation of mouse macrophage proteome induced by Toxoplasma gondii tachyzoites in vivo
    • PMID: 21584632
    • Zhou DH, Yuan ZG, Zhao FR, Li HL, Zhou Y, et al. (2011) Modulation of mouse macrophage proteome induced by Toxoplasma gondii tachyzoites in vivo. Parasitol Res 109: 1637-1646. doi: 10.1007/s00436-011-2435-z PMID: 21584632
    • (2011) Parasitol Res , vol.109 , pp. 1637-1646
    • Zhou, D.H.1    Yuan, Z.G.2    Zhao, F.R.3    Li, H.L.4    Zhou, Y.5
  • 21
    • 84906943632 scopus 로고    scopus 로고
    • Is Lys-N(varepsilon)-acetylation the next big thing in post-translational modifications?
    • PMID: 24866592
    • Rao RS, Thelen JJ, Miernyk JA (2014) Is Lys-N(varepsilon)-acetylation the next big thing in post-translational modifications? Trends Plant Sci 19: 550-553. doi: 10.1016/j.tplants.2014.05.001 PMID: 24866592
    • (2014) Trends Plant Sci , vol.19 , pp. 550-553
    • Rao, R.S.1    Thelen, J.J.2    Miernyk, J.A.3
  • 22
    • 84903712481 scopus 로고    scopus 로고
    • Systematic analysis of the lysine acetylome in Vibrio parahemolyticus
    • PMID: 24874924
    • Pan J, Ye Z, Cheng Z, Peng X, Wen L, et al. (2014) Systematic analysis of the lysine acetylome in Vibrio parahemolyticus. J Proteome Res 13: 3294-3302. doi: 10.1021/pr500133t PMID: 24874924
    • (2014) J Proteome Res , vol.13 , pp. 3294-3302
    • Pan, J.1    Ye, Z.2    Cheng, Z.3    Peng, X.4    Wen, L.5
  • 23
    • 77954013335 scopus 로고    scopus 로고
    • Bacterial protein acetylation: The dawning of a new age
    • PMID: 20487279
    • Hu LI, Lima BP, Wolfe AJ (2010) Bacterial protein acetylation: the dawning of a new age. Molecular microbiology 77: 15-21. doi: 10.1111/j.1365-2958.2010.07204.x PMID: 20487279
    • (2010) Molecular Microbiology , vol.77 , pp. 15-21
    • Hu, L.I.1    Lima, B.P.2    Wolfe, A.J.3
  • 24
    • 79953689290 scopus 로고    scopus 로고
    • Proteins of diverse function and subcellular location are lysine acetylated in Arabidopsis
    • PMID: 21311031
    • Finkemeier I, Laxa M, Miguet L, Howden AJ, Sweetlove LJ (2011) Proteins of diverse function and subcellular location are lysine acetylated in Arabidopsis. Plant physiology 155: 1779-1790. doi: 10.1104/pp.110.171595 PMID: 21311031
    • (2011) Plant Physiology , vol.155 , pp. 1779-1790
    • Finkemeier, I.1    Laxa, M.2    Miguet, L.3    Howden, A.J.4    Sweetlove, L.J.5
  • 25
    • 79953702814 scopus 로고    scopus 로고
    • Lysine acetylation is a widespread protein modification for diverse proteins in Arabidopsis
    • PMID: 21311030
    • Wu X, Oh MH, Schwarz EM, Larue CT, Sivaguru M, et al. (2011) Lysine acetylation is a widespread protein modification for diverse proteins in Arabidopsis. Plant physiology 155: 1769-1778. doi: 10.1104/pp.110.165852 PMID: 21311030
    • (2011) Plant Physiology , vol.155 , pp. 1769-1778
    • Wu, X.1    Oh, M.H.2    Schwarz, E.M.3    Larue, C.T.4    Sivaguru, M.5
  • 26
    • 84898012537 scopus 로고    scopus 로고
    • Acetylation dynamics and stoichiometry in Saccharomyces cerevisiae
    • PMID: 24489116
    • Weinert BT, Iesmantavicius V, Moustafa T, Scholz C, Wagner SA, et al. (2014) Acetylation dynamics and stoichiometry in Saccharomyces cerevisiae. Mol Syst Biol 10: 716. doi: 10.1002/msb.134766 PMID: 24489116
    • (2014) Mol Syst Biol , vol.10 , pp. 716
    • Weinert, B.T.1    Iesmantavicius, V.2    Moustafa, T.3    Scholz, C.4    Wagner, S.A.5
  • 27
    • 79960797509 scopus 로고    scopus 로고
    • Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation
    • PMID: 21791702
    • Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, et al. (2011) Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Science signaling 4: ra48. doi: 10.1126/scisignal.2001902 PMID: 21791702
    • (2011) Science Signaling , vol.4 , pp. ra48
    • Weinert, B.T.1    Wagner, S.A.2    Horn, H.3    Henriksen, P.4    Liu, W.R.5
  • 28
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • PMID: 19608861
    • Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, et al. (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325: 834-840. doi: 10.1126/science.1175371 PMID: 19608861
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5
  • 29
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • PMID: 20167786
    • Zhao S, Xu W, Jiang W, Yu W, Lin Y, et al. (2010) Regulation of cellular metabolism by protein lysine acetylation. Science 327: 1000-1004. doi: 10.1126/science.1179689 PMID: 20167786
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3    Yu, W.4    Lin, Y.5
  • 30
    • 84861689430 scopus 로고    scopus 로고
    • Lysine Acetylation Is Widespread on Proteins of Diverse Function and Localization in the Protozoan Parasite Toxoplasma gondii
    • PMID: 22544907
    • Jeffers V, Sullivan WJ Jr (2012) Lysine Acetylation Is Widespread on Proteins of Diverse Function and Localization in the Protozoan Parasite Toxoplasma gondii. Eukaryot Cell 11: 735-742. doi: 10.1128/EC.00088-12 PMID: 22544907
    • (2012) Eukaryot Cell , vol.11 , pp. 735-742
    • Jeffers, V.1    Sullivan, W.J.2
  • 31
    • 84874879335 scopus 로고    scopus 로고
    • Protein intrinsic disorder in the acetylome of intracellular and extracellular Toxoplasma gondii
    • PMID: 23403842
    • Xue B, Jeffers V, Sullivan WJ, Uversky VN (2013) Protein intrinsic disorder in the acetylome of intracellular and extracellular Toxoplasma gondii. Mol Biosyst 9: 645-657. doi: 10.1039/c3mb25517d PMID: 23403842
    • (2013) Mol Biosyst , vol.9 , pp. 645-657
    • Xue, B.1    Jeffers, V.2    Sullivan, W.J.3    Uversky, V.N.4
  • 32
    • 84881544331 scopus 로고    scopus 로고
    • Extensive lysine acetylation occurs in evolutionarily conserved metabolic pathways and parasite-specific functions during Plasmodium falciparum intraerythrocytic development
    • PMID: 23796209
    • Miao J, Lawrence M, Jeffers V, Zhao F, Parker D, et al. (2013) Extensive lysine acetylation occurs in evolutionarily conserved metabolic pathways and parasite-specific functions during Plasmodium falciparum intraerythrocytic development. Mol Microbiol 89: 660-675. doi: 10.1111/mmi.12303 PMID: 23796209
    • (2013) Mol Microbiol , vol.89 , pp. 660-675
    • Miao, J.1    Lawrence, M.2    Jeffers, V.3    Zhao, F.4    Parker, D.5
  • 33
    • 84877897363 scopus 로고    scopus 로고
    • Loss of calcium/cal-modulin- dependent protein kinase II activity in cortical astrocytes decreases glutamate uptake and induces neurotoxic release of ATP
    • PMID: 23543737
    • Ashpole NM, Chawla AR, Martin MP, Brustovetsky T, Brustovetsky N, et al. (2013) Loss of calcium/cal-modulin- dependent protein kinase II activity in cortical astrocytes decreases glutamate uptake and induces neurotoxic release of ATP. J Biol Chem 288: 14599-14611. doi: 10.1074/jbc.M113.466235 PMID: 23543737
    • (2013) J Biol Chem , vol.288 , pp. 14599-14611
    • Ashpole, N.M.1    Chawla, A.R.2    Martin, M.P.3    Brustovetsky, T.4    Brustovetsky, N.5
  • 34
    • 0028709114 scopus 로고
    • Molecular tools for genetic dissection of the protozoan parasite Toxoplasma gondii
    • PMID: 7707991
    • Roos DS, Donald RG, Morrissette NS, Moulton AL (1994) Molecular tools for genetic dissection of the protozoan parasite Toxoplasma gondii. Methods Cell Biol 45: 27-63. PMID: 7707991
    • (1994) Methods Cell Biol , vol.45 , pp. 27-63
    • Roos, D.S.1    Donald, R.G.2    Morrissette, N.S.3    Moulton, A.L.4
  • 36
    • 84881101018 scopus 로고    scopus 로고
    • Systems-wide analysis of K-Ras, Cdc42, and PAK4 signaling by quantitative phosphoproteomics
    • PMID: 23608596
    • Gnad F, Young A, Zhou W, Lyle K, Ong CC, et al. (2013) Systems-wide analysis of K-Ras, Cdc42, and PAK4 signaling by quantitative phosphoproteomics. Mol Cell Proteomics 12: 2070-2080. doi: 10.1074/mcp.M112.027052 PMID: 23608596
    • (2013) Mol Cell Proteomics , vol.12 , pp. 2070-2080
    • Gnad, F.1    Young, A.2    Zhou, W.3    Lyle, K.4    Ong, C.C.5
  • 37
    • 84861161220 scopus 로고    scopus 로고
    • PTMScan direct: Identification and quantification of peptides from critical signaling proteins by immunoaffinity enrichment coupled with LC-MS/MS
    • PMID: 22322096
    • Stokes MP, Farnsworth CL, Moritz A, Silva JC, Jia X, et al. (2012) PTMScan direct: identification and quantification of peptides from critical signaling proteins by immunoaffinity enrichment coupled with LC-MS/MS. Mol Cell Proteomics 11: 187-201. doi: 10.1074/mcp.M111.015883 PMID: 22322096
    • (2012) Mol Cell Proteomics , vol.11 , pp. 187-201
    • Stokes, M.P.1    Farnsworth, C.L.2    Moritz, A.3    Silva, J.C.4    Jia, X.5
  • 38
    • 84891783174 scopus 로고    scopus 로고
    • Activities at the Universal Protein Resource (UniProt)
    • PMID: 24253303
    • UniProt C (2014) Activities at the Universal Protein Resource (UniProt). Nucleic Acids Res 42: D191-198. doi: 10.1093/nar/gkt1140 PMID: 24253303
    • (2014) Nucleic Acids Res , vol.42 , pp. D191-D198
  • 41
    • 14044252311 scopus 로고    scopus 로고
    • Histone acetylase GCN5 enters the nucleus via importin-alpha in protozoan parasite Toxoplasma gondii
    • PMID: 15591057
    • Bhatti MM, Sullivan WJ Jr (2005) Histone acetylase GCN5 enters the nucleus via importin-alpha in protozoan parasite Toxoplasma gondii. J Biol Chem 280: 5902-5908. PMID: 15591057
    • (2005) J Biol Chem , vol.280 , pp. 5902-5908
    • Bhatti, M.M.1    Sullivan, W.J.2
  • 42
    • 77649189116 scopus 로고    scopus 로고
    • Astrocytes: Biology and pathology
    • PMID: 20012068
    • Sofroniew MV, Vinters HV (2010) Astrocytes: biology and pathology. Acta Neuropathol 119: 7-35. doi: 10.1007/s00401-009-0619-8 PMID: 20012068
    • (2010) Acta Neuropathol , vol.119 , pp. 7-35
    • Sofroniew, M.V.1    Vinters, H.V.2
  • 43
    • 84860530692 scopus 로고    scopus 로고
    • Astrocytes and disease: A neuro-developmental perspective
    • PMID: 22549954
    • Molofsky AV, Krencik R, Ullian EM, Tsai HH, Deneen B, et al. (2012) Astrocytes and disease: a neuro-developmental perspective. Genes Dev 26: 891-907. doi: 10.1101/gad.188326.112 PMID: 22549954
    • (2012) Genes Dev , vol.26 , pp. 891-907
    • Molofsky, A.V.1    Krencik, R.2    Ullian, E.M.3    Tsai, H.H.4    Deneen, B.5
  • 44
    • 20844436280 scopus 로고    scopus 로고
    • Proteome analysis of primary neurons and astrocytes from rat cerebellum
    • PMID: 15952724
    • Yang JW, Rodrigo R, Felipo V, Lubec G (2005) Proteome analysis of primary neurons and astrocytes from rat cerebellum. J Proteome Res 4: 768-788. PMID: 15952724
    • (2005) J Proteome Res , vol.4 , pp. 768-788
    • Yang, J.W.1    Rodrigo, R.2    Felipo, V.3    Lubec, G.4
  • 45
    • 20544433351 scopus 로고    scopus 로고
    • Proteome analysis of mouse primary astrocytes
    • PMID: 15908045
    • Yang JW, Suder P, Silberring J, Lubec G (2005) Proteome analysis of mouse primary astrocytes. Neurochem Int 47: 159-172. PMID: 15908045
    • (2005) Neurochem Int , vol.47 , pp. 159-172
    • Yang, J.W.1    Suder, P.2    Silberring, J.3    Lubec, G.4
  • 46
    • 84883035843 scopus 로고    scopus 로고
    • Angiogenin induces modifications in the astrocyte secretome: Relevance to amyotrophic lateral sclerosis
    • PMID: 23920243
    • Skorupa A, Urbach S, Vigy O, King MA, Chaumont-Dubel S, et al. (2013) Angiogenin induces modifications in the astrocyte secretome: relevance to amyotrophic lateral sclerosis. J Proteomics 91: 274-285. doi: 10.1016/j.jprot.2013.07.028 PMID: 23920243
    • (2013) J Proteomics , vol.91 , pp. 274-285
    • Skorupa, A.1    Urbach, S.2    Vigy, O.3    King, M.A.4    Chaumont-Dubel, S.5
  • 47
    • 84864634069 scopus 로고    scopus 로고
    • Peptidomic analyses of mouse astrocytic cell lines and rat primary cultured astrocytes
    • PMID: 22742998
    • Yin P, Knolhoff AM, Rosenberg HJ, Millet LJ, Gillette MU, et al. (2012) Peptidomic analyses of mouse astrocytic cell lines and rat primary cultured astrocytes. J Proteome Res 11: 3965-3973. doi: 10.1021/pr201066t PMID: 22742998
    • (2012) J Proteome Res , vol.11 , pp. 3965-3973
    • Yin, P.1    Knolhoff, A.M.2    Rosenberg, H.J.3    Millet, L.J.4    Gillette, M.U.5
  • 48
    • 68549133540 scopus 로고    scopus 로고
    • Identification of astrocyte secreted proteins with a combination of shotgun proteomics and bioinformatics
    • PMID: 19469553
    • Dowell JA, Johnson JA, Li L (2009) Identification of astrocyte secreted proteins with a combination of shotgun proteomics and bioinformatics. J Proteome Res 8: 4135-4143. doi: 10.1021/pr900248y PMID: 19469553
    • (2009) J Proteome Res , vol.8 , pp. 4135-4143
    • Dowell, J.A.1    Johnson, J.A.2    Li, L.3
  • 49
    • 77952083750 scopus 로고    scopus 로고
    • Quantitative mass spectrometry-based proteomics reveals the dynamic range of primary mouse astrocyte protein secretion
    • PMID: 20329800
    • Greco TM, Seeholzer SH, Mak A, Spruce L, Ischiropoulos H (2010) Quantitative mass spectrometry-based proteomics reveals the dynamic range of primary mouse astrocyte protein secretion. J Proteome Res 9: 2764-2774. doi: 10.1021/pr100134n PMID: 20329800
    • (2010) J Proteome Res , vol.9 , pp. 2764-2774
    • Greco, T.M.1    Seeholzer, S.H.2    Mak, A.3    Spruce, L.4    Ischiropoulos, H.5
  • 50
    • 84903995739 scopus 로고    scopus 로고
    • Proteomic analysis of mouse astrocytes and their secretome by a combination of FASP and StageTip-based, high pH, reversed-phase fractionation
    • PMID: 24753479
    • Han D, Jin J, Woo J, Min H, Kim Y (2014) Proteomic analysis of mouse astrocytes and their secretome by a combination of FASP and StageTip-based, high pH, reversed-phase fractionation. Proteomics 14: 1604-1609. doi: 10.1002/pmic.201300495 PMID: 24753479
    • (2014) Proteomics , vol.14 , pp. 1604-1609
    • Han, D.1    Jin, J.2    Woo, J.3    Min, H.4    Kim, Y.5
  • 51
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • PMID: 18827828
    • Kazantsev AG, Thompson LM (2008) Therapeutic application of histone deacetylase inhibitors for central nervous system disorders. Nat Rev Drug Discov 7: 854-868. doi: 10.1038/nrd2681 PMID: 18827828
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 854-868
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 52
    • 84883788666 scopus 로고    scopus 로고
    • Epigenetic targeting of histone deacetylase: Therapeutic potential in Parkinson's disease?
    • PMID: 23711791
    • Harrison IF, Dexter DT (2013) Epigenetic targeting of histone deacetylase: therapeutic potential in Parkinson's disease? Pharmacol Ther 140: 34-52. doi: 10.1016/j.pharmthera.2013.05.010 PMID: 23711791
    • (2013) Pharmacol Ther , vol.140 , pp. 34-52
    • Harrison, I.F.1    Dexter, D.T.2
  • 53
    • 84891304904 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of potent and selective class IIa histone deacetylase (HDAC) inhibitors as a potential therapy for Huntington's disease
    • PMID: 24261862
    • Burli RW, Luckhurst CA, Aziz O, Matthews KL, Yates D, et al. (2013) Design, synthesis, and biological evaluation of potent and selective class IIa histone deacetylase (HDAC) inhibitors as a potential therapy for Huntington's disease. J Med Chem 56: 9934-9954. doi: 10.1021/jm4011884 PMID: 24261862
    • (2013) J Med Chem , vol.56 , pp. 9934-9954
    • Burli, R.W.1    Luckhurst, C.A.2    Aziz, O.3    Matthews, K.L.4    Yates, D.5
  • 54
    • 0018403701 scopus 로고
    • Glial fibrillary acidic protein (GFAP): Purification from human fibrillary astrocytoma, development and validation of a radioimmunoassay for GFAP-like immunoactivity
    • PMID: 438840
    • Palfreyman JW, Thomas DG, Ratcliffe JG, Graham DI (1979) Glial fibrillary acidic protein (GFAP): purification from human fibrillary astrocytoma, development and validation of a radioimmunoassay for GFAP-like immunoactivity. J Neurol Sci 41: 101-113. PMID: 438840
    • (1979) J Neurol Sci , vol.41 , pp. 101-113
    • Palfreyman, J.W.1    Thomas, D.G.2    Ratcliffe, J.G.3    Graham, D.I.4
  • 55
    • 0015213652 scopus 로고
    • An acidic protein isolated from fibrous astrocytes
    • PMID: 5113526
    • Eng LF, Vanderhaeghen JJ, Bignami A, Gerstl B (1971) An acidic protein isolated from fibrous astrocytes. Brain Res 28: 351-354. PMID: 5113526
    • (1971) Brain Res , vol.28 , pp. 351-354
    • Eng, L.F.1    Vanderhaeghen, J.J.2    Bignami, A.3    Gerstl, B.4
  • 56
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes: One size doesn't fit all
    • PMID: 17380162
    • Lee KK, Workman JL (2007) Histone acetyltransferase complexes: one size doesn't fit all. Nat Rev Mol Cell Biol 8: 284-295. PMID: 17380162
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 284-295
    • Lee, K.K.1    Workman, J.L.2
  • 57
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specific histone acetylation and deacetylation
    • PMID: 17362198
    • Shahbazian MD, Grunstein M (2007) Functions of site-specific histone acetylation and deacetylation. Annu Rev Biochem 76: 75-100. PMID: 17362198
    • (2007) Annu Rev Biochem , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 58
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • PMID: 16916647
    • Kim SC, Sprung R, Chen Y, Xu Y, Ball H, et al. (2006) Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 23: 607-618. PMID: 16916647
    • (2006) Mol Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3    Xu, Y.4    Ball, H.5
  • 59
    • 84879743246 scopus 로고    scopus 로고
    • The cardiac acetyl-lysine proteome
    • PMID: 23844019
    • Foster DB, Liu T, Rucker J, O'Meally RN, Devine LR, et al. (2013) The cardiac acetyl-lysine proteome. PLoS One 8: e67513. doi: 10.1371/journal.pone.0067513 PMID: 23844019
    • (2013) PLoS One , vol.8 , pp. e67513
    • Foster, D.B.1    Liu, T.2    Rucker, J.3    O'Meally, R.N.4    Devine, L.R.5
  • 60
    • 0034219422 scopus 로고    scopus 로고
    • Modulation of complement component (C3 and factor B) biosynthesis by a histone deacetylase inhibitor in human intestinal epithelial cells
    • PMID: 10851266
    • Andoh A, Fujiyama Y, Shimada M, Bamba T (2000) Modulation of complement component (C3 and factor B) biosynthesis by a histone deacetylase inhibitor in human intestinal epithelial cells. Int J Mol Med 6: 51-54. PMID: 10851266
    • (2000) Int J Mol Med , vol.6 , pp. 51-54
    • Andoh, A.1    Fujiyama, Y.2    Shimada, M.3    Bamba, T.4
  • 61
    • 47349085102 scopus 로고    scopus 로고
    • Osteoactivin, an anabolic factor that regulates osteoblast differentiation and function
    • PMID: 18555216
    • Abdelmagid SM, Barbe MF, Rico MC, Salihoglu S, Arango-Hisijara I, et al. (2008) Osteoactivin, an anabolic factor that regulates osteoblast differentiation and function. Exp Cell Res 314: 2334-2351. doi: 10.1016/j.yexcr.2008.02.006 PMID: 18555216
    • (2008) Exp Cell Res , vol.314 , pp. 2334-2351
    • Abdelmagid, S.M.1    Barbe, M.F.2    Rico, M.C.3    Salihoglu, S.4    Arango-Hisijara, I.5
  • 62
    • 84904860529 scopus 로고    scopus 로고
    • Glycoprotein nonmetastatic melanoma protein B (GPNMB) as a novel neuroprotective factor in cerebral ischemia-reperfusion injury
    • PMID: 25010402
    • Nakano Y, Suzuki Y, Takagi T, Kitashoji A, Ono Y, et al. (2014) Glycoprotein nonmetastatic melanoma protein B (GPNMB) as a novel neuroprotective factor in cerebral ischemia-reperfusion injury. Neuroscience 277: 123-131. doi: 10.1016/j.neuroscience.2014.06.065 PMID: 25010402
    • (2014) Neuroscience , vol.277 , pp. 123-131
    • Nakano, Y.1    Suzuki, Y.2    Takagi, T.3    Kitashoji, A.4    Ono, Y.5
  • 63
    • 2942598149 scopus 로고    scopus 로고
    • PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation
    • PMID: 15174125
    • Hornbeck PV, Chabra I, Kornhauser JM, Skrzypek E, Zhang B (2004) PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation. Proteomics 4: 1551-1561. PMID: 15174125
    • (2004) Proteomics , vol.4 , pp. 1551-1561
    • Hornbeck, P.V.1    Chabra, I.2    Kornhauser, J.M.3    Skrzypek, E.4    Zhang, B.5
  • 64
    • 0023293040 scopus 로고
    • Microtubules containing acetylated alpha-tubulin in mammalian cells in culture
    • PMID: 2879846
    • Piperno G, LeDizet M, Chang XJ (1987) Microtubules containing acetylated alpha-tubulin in mammalian cells in culture. J Cell Biol 104: 289-302. PMID: 2879846
    • (1987) J Cell Biol , vol.104 , pp. 289-302
    • Piperno, G.1    LeDizet, M.2    Chang, X.J.3
  • 65
    • 84906491034 scopus 로고    scopus 로고
    • The tubulin code: Molecular components, readout mechanisms, and functions
    • PMID: 25135932
    • Janke C (2014) The tubulin code: molecular components, readout mechanisms, and functions. J Cell Biol 206: 461-472. doi: 10.1083/jcb.201406055 PMID: 25135932
    • (2014) J Cell Biol , vol.206 , pp. 461-472
    • Janke, C.1
  • 66
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • PMID: 19131956
    • Huang da W, Sherman BT, Lempicki RA (2009) Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 4: 44-57. doi: 10.1038/nprot.2008.211 PMID: 19131956
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Huang Da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 67
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists
    • PMID: 19033363
    • Huang da W, Sherman BT, Lempicki RA (2009) Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res 37: 1-13. doi: 10.1093/nar/gkn923 PMID: 19033363
    • (2009) Nucleic Acids Res , vol.37 , pp. 1-13
    • Huang Da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 68
    • 38149129457 scopus 로고    scopus 로고
    • A transcriptome database for astrocytes, neurons, and oligodendrocytes: A new resource for understanding brain development and function
    • PMID: 18171944
    • Cahoy JD, Emery B, Kaushal A, Foo LC, Zamanian JL, et al. (2008) A transcriptome database for astrocytes, neurons, and oligodendrocytes: a new resource for understanding brain development and function. J Neurosci 28: 264-278. doi: 10.1523/JNEUROSCI.4178-07.2008 PMID: 18171944
    • (2008) J Neurosci , vol.28 , pp. 264-278
    • Cahoy, J.D.1    Emery, B.2    Kaushal, A.3    Foo, L.C.4    Zamanian, J.L.5
  • 69
    • 70350732744 scopus 로고    scopus 로고
    • Improved visualization of protein consensus sequences by iceLogo
    • PMID: 19876014
    • Colaert N, Helsens K, Martens L, Vandekerckhove J, Gevaert K (2009) Improved visualization of protein consensus sequences by iceLogo. Nature methods 6: 786-787. doi: 10.1038/nmeth1109-786 PMID: 19876014
    • (2009) Nature Methods , vol.6 , pp. 786-787
    • Colaert, N.1    Helsens, K.2    Martens, L.3    Vandekerckhove, J.4    Gevaert, K.5
  • 70
    • 84865726581 scopus 로고    scopus 로고
    • Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns
    • PMID: 22902405
    • Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, et al. (2012) Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Cell Rep 2: 419-431. doi: 10.1016/j.celrep.2012.07.006 PMID: 22902405
    • (2012) Cell Rep , vol.2 , pp. 419-431
    • Lundby, A.1    Lage, K.2    Weinert, B.T.3    Bekker-Jensen, D.B.4    Secher, A.5
  • 71
    • 84885618025 scopus 로고    scopus 로고
    • GPNMB enhances bone regeneration by promoting angiogenesis and osteogenesis: Potential role for tissue engineering bone
    • PMID: 23794283
    • Hu X, Zhang P, Xu Z, Chen H, Xie X (2013) GPNMB enhances bone regeneration by promoting angiogenesis and osteogenesis: potential role for tissue engineering bone. J Cell Biochem 114: 2729-2737. doi: 10.1002/jcb.24621 PMID: 23794283
    • (2013) J Cell Biochem , vol.114 , pp. 2729-2737
    • Hu, X.1    Zhang, P.2    Xu, Z.3    Chen, H.4    Xie, X.5
  • 72
    • 38449094315 scopus 로고    scopus 로고
    • Syndecan-4 mediates the coinhibitory function of DC-HIL on T cell activation
    • PMID: 17947650
    • Chung JS, Dougherty I, Cruz PD Jr, Ariizumi K (2007) Syndecan-4 mediates the coinhibitory function of DC-HIL on T cell activation. J Immunol 179: 5778-5784. PMID: 17947650
    • (2007) J Immunol , vol.179 , pp. 5778-5784
    • Chung, J.S.1    Dougherty, I.2    Cruz, P.D.3    Ariizumi, K.4
  • 73
    • 84880109599 scopus 로고    scopus 로고
    • Glycoprotein non-metastatic b (GPNMB): A metastatic mediator and emerging therapeutic target in cancer
    • PMID: 23874106
    • Maric G, Rose AA, Annis MG, Siegel PM (2013) Glycoprotein non-metastatic b (GPNMB): A metastatic mediator and emerging therapeutic target in cancer. Onco Targets Ther 6: 839-852. doi: 10.2147/OTT.S44906 PMID: 23874106
    • (2013) Onco Targets Ther , vol.6 , pp. 839-852
    • Maric, G.1    Rose, A.A.2    Annis, M.G.3    Siegel, P.M.4
  • 74
    • 84866097059 scopus 로고    scopus 로고
    • The potential of GPNMB as novel neuroprotective factor in amyotrophic lateral sclerosis
    • PMID: 22891158
    • Tanaka H, Shimazawa M, Kimura M, Takata M, Tsuruma K, et al. (2012) The potential of GPNMB as novel neuroprotective factor in amyotrophic lateral sclerosis. Sci Rep 2: 573. doi: 10.1038/srep00573 PMID: 22891158
    • (2012) Sci Rep , vol.2 , pp. 573
    • Tanaka, H.1    Shimazawa, M.2    Kimura, M.3    Takata, M.4    Tsuruma, K.5
  • 75
    • 78649747024 scopus 로고    scopus 로고
    • The melanoma-associated transmembrane glycoprotein Gpnmb controls trafficking of cellular debris for degradation and is essential for tissue repair
    • PMID: 20709912
    • Li B, Castano AP, Hudson TE, Nowlin BT, Lin SL, et al. (2010) The melanoma-associated transmembrane glycoprotein Gpnmb controls trafficking of cellular debris for degradation and is essential for tissue repair. FASEB J 24: 4767-4781. doi: 10.1096/fj.10-154757 PMID: 20709912
    • (2010) FASEB J , vol.24 , pp. 4767-4781
    • Li, B.1    Castano, A.P.2    Hudson, T.E.3    Nowlin, B.T.4    Lin, S.L.5
  • 76
    • 84859045769 scopus 로고    scopus 로고
    • Function of the active site lysine autoacetylation in Tip60 catalysis
    • PMID: 22470428
    • Yang C, Wu J, Zheng YG (2012) Function of the active site lysine autoacetylation in Tip60 catalysis. PLoS One 7: e32886. doi: 10.1371/journal.pone.0032886 PMID: 22470428
    • (2012) PLoS One , vol.7 , pp. e32886
    • Yang, C.1    Wu, J.2    Zheng, Y.G.3
  • 77
    • 10044262126 scopus 로고    scopus 로고
    • The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5/PCAF and TIP60
    • PMID: 15572685
    • Patel JH, Du Y, Ard PG, Phillips C, Carella B, et al. (2004) The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5/PCAF and TIP60. Mol Cell Biol 24: 10826-10834. PMID: 15572685
    • (2004) Mol Cell Biol , vol.24 , pp. 10826-10834
    • Patel, J.H.1    Du, Y.2    Ard, P.G.3    Phillips, C.4    Carella, B.5
  • 78
    • 84857473399 scopus 로고    scopus 로고
    • Impaired chromatin remodelling at STAT1-regulated promoters leads to global unresponsiveness of Toxoplasma gondii-infected macrophages to IFN-gamma
    • PMID: 22275866
    • Lang C, Hildebrandt A, Brand F, Opitz L, Dihazi H, et al. (2012) Impaired chromatin remodelling at STAT1-regulated promoters leads to global unresponsiveness of Toxoplasma gondii-infected macrophages to IFN-gamma. PLoS Pathog 8: e1002483. doi: 10.1371/journal.ppat.1002483 PMID: 22275866
    • (2012) PLoS Pathog , vol.8 , pp. e1002483
    • Lang, C.1    Hildebrandt, A.2    Brand, F.3    Opitz, L.4    Dihazi, H.5
  • 79
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • PMID: 16175177
    • Whitesell L, Lindquist SL (2005) HSP90 and the chaperoning of cancer. Nat Rev Cancer 5: 761-772. PMID: 16175177
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 80
    • 84857044092 scopus 로고    scopus 로고
    • Post-translational modifications of Hsp90 and their contributions to chaperone regulation
    • PMID: 21856339
    • Mollapour M, Neckers L (2012) Post-translational modifications of Hsp90 and their contributions to chaperone regulation. Biochim Biophys Acta 1823: 648-655. doi: 10.1016/j.bbamcr.2011.07.018 PMID: 21856339
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 648-655
    • Mollapour, M.1    Neckers, L.2
  • 81
    • 84867103151 scopus 로고    scopus 로고
    • Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues
    • PMID: 22790023
    • Wagner SA, Beli P, Weinert BT, Scholz C, Kelstrup CD, et al. (2012) Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Mol Cell Proteomics 11: 1578-1585. doi: 10.1074/mcp.M112.017905 PMID: 22790023
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1578-1585
    • Wagner, S.A.1    Beli, P.2    Weinert, B.T.3    Scholz, C.4    Kelstrup, C.D.5
  • 82
    • 82455179484 scopus 로고    scopus 로고
    • Systematic and quantitative assessment of the ubiquitin-modified proteome
    • PMID: 21906983
    • Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, et al. (2011) Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell 44: 325-340. doi: 10.1016/j.molcel.2011.08.025 PMID: 21906983
    • (2011) Mol Cell , vol.44 , pp. 325-340
    • Kim, W.1    Bennett, E.J.2    Huttlin, E.L.3    Guo, A.4    Li, J.5
  • 83
    • 0032716145 scopus 로고    scopus 로고
    • The regeneration of reduced glutathione in rat forebrain mitochondria identifies metabolic pathways providing the NADPH required
    • PMID: 10568508
    • Vogel R, Wiesinger H, Hamprecht B, Dringen R (1999) The regeneration of reduced glutathione in rat forebrain mitochondria identifies metabolic pathways providing the NADPH required. Neurosci Lett 275: 97-100. PMID: 10568508
    • (1999) Neurosci Lett , vol.275 , pp. 97-100
    • Vogel, R.1    Wiesinger, H.2    Hamprecht, B.3    Dringen, R.4
  • 84
    • 84875737737 scopus 로고    scopus 로고
    • Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes
    • PMID: 23036594
    • Deponte M (2013) Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes. Biochim Biophys Acta 1830: 3217-3266. doi: 10.1016/j.bbagen.2012.09.018 PMID: 23036594
    • (2013) Biochim Biophys Acta , vol.1830 , pp. 3217-3266
    • Deponte, M.1
  • 85
    • 84859951790 scopus 로고    scopus 로고
    • SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status
    • PMID: 22416140
    • Yu W, Dittenhafer-Reed KE, Denu JM (2012) SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status. J Biol Chem 287: 14078-14086. doi: 10.1074/jbc.M112.355206 PMID: 22416140
    • (2012) J Biol Chem , vol.287 , pp. 14078-14086
    • Yu, W.1    Dittenhafer-Reed, K.E.2    Denu, J.M.3
  • 87
    • 84864389182 scopus 로고    scopus 로고
    • Cellular GCN5 Is a Novel Regulator of Human Adenovirus E1A-Conserved Region 3 Transactivation
    • PMID: 22623781
    • Ablack JN, Cohen M, Thillainadesan G, Fonseca GJ, Pelka P, et al. (2012) Cellular GCN5 Is a Novel Regulator of Human Adenovirus E1A-Conserved Region 3 Transactivation. J Virol 86: 8198-8209. doi: 10.1128/JVI.00289-12 PMID: 22623781
    • (2012) J Virol , vol.86 , pp. 8198-8209
    • Ablack, J.N.1    Cohen, M.2    Thillainadesan, G.3    Fonseca, G.J.4    Pelka, P.5
  • 88
    • 77949449851 scopus 로고    scopus 로고
    • GCN5-dependent acetylation of HIV-1 integrase enhances viral integration
    • PMID: 20226045
    • Terreni M, Valentini P, Liverani V, Gutierrez MI, Di Primio C, et al. (2010) GCN5-dependent acetylation of HIV-1 integrase enhances viral integration. Retrovirology 7: 18. doi: 10.1186/1742-4690-7-18 PMID: 20226045
    • (2010) Retrovirology , vol.7 , pp. 18
    • Terreni, M.1    Valentini, P.2    Liverani, V.3    Gutierrez, M.I.4    Di Primio, C.5
  • 89
    • 23044476198 scopus 로고    scopus 로고
    • HIV-1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic stresses
    • PMID: 16001085
    • Col E, Caron C, Chable-Bessia C, Legube G, Gazzeri S, et al. (2005) HIV-1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic stresses. EMBO J 24: 2634-2645. PMID: 16001085
    • (2005) EMBO J , vol.24 , pp. 2634-2645
    • Col, E.1    Caron, C.2    Chable-Bessia, C.3    Legube, G.4    Gazzeri, S.5
  • 90
    • 61649087854 scopus 로고    scopus 로고
    • Acetylation of the human T-cell leukemia virus type 1 Tax oncoprotein by p300 promotes activation of the NF-kappaB pathway
    • PMID: 19200568
    • Lodewick J, Lamsoul I, Polania A, Lebrun S, Burny A, et al. (2009) Acetylation of the human T-cell leukemia virus type 1 Tax oncoprotein by p300 promotes activation of the NF-kappaB pathway. Virology 386: 68-78. doi: 10.1016/j.virol.2008.12.043 PMID: 19200568
    • (2009) Virology , vol.386 , pp. 68-78
    • Lodewick, J.1    Lamsoul, I.2    Polania, A.3    Lebrun, S.4    Burny, A.5
  • 92
    • 58149235363 scopus 로고    scopus 로고
    • Acetylation of MKP-1 and the control of inflammation
    • PMID: 18922786
    • Chi H, Flavell RA (2008) Acetylation of MKP-1 and the control of inflammation. Science signaling 1: pe44. doi: 10.1126/scisignal.141pe44 PMID: 18922786
    • (2008) Science Signaling , vol.1 , pp. pe44
    • Chi, H.1    Flavell, R.A.2
  • 93
    • 80655129565 scopus 로고    scopus 로고
    • Acetylation is indispensable for p53 antiviral activity
    • PMID: 22033337
    • Munoz-Fontela C, Gonzalez D, Marcos-Villar L, Campagna M, Gallego P, et al. (2011) Acetylation is indispensable for p53 antiviral activity. Cell cycle 10: 3701-3705. doi: 10.4161/cc.10.21.17899 PMID: 22033337
    • (2011) Cell Cycle , vol.10 , pp. 3701-3705
    • Munoz-Fontela, C.1    Gonzalez, D.2    Marcos-Villar, L.3    Campagna, M.4    Gallego, P.5
  • 94
    • 77955945083 scopus 로고    scopus 로고
    • Involvement of TIP60 acetyltransferase in intracellular Salmonella replication
    • PMID: 20796290
    • Wang X, Li D, Qu D, Zhou D (2010) Involvement of TIP60 acetyltransferase in intracellular Salmonella replication. BMC Microbiol 10: 228. doi: 10.1186/1471-2180-10-228 PMID: 20796290
    • (2010) BMC Microbiol , vol.10 , pp. 228
    • Wang, X.1    Li, D.2    Qu, D.3    Zhou, D.4
  • 95
    • 77951451986 scopus 로고    scopus 로고
    • Salmonella typhimurium infection increases p53 acetylation in intestinal epithelial cells
    • PMID: 20224008
    • Wu S, Ye Z, Liu X, Zhao Y, Xia Y, et al. (2010) Salmonella typhimurium infection increases p53 acetylation in intestinal epithelial cells. Am J Physiol Gastrointest Liver Physiol 298: G784-794. doi: 10.1152/ajpgi.00526.2009 PMID: 20224008
    • (2010) Am J Physiol Gastrointest Liver Physiol , vol.298 , pp. G784-G794
    • Wu, S.1    Ye, Z.2    Liu, X.3    Zhao, Y.4    Xia, Y.5
  • 96
    • 77449116892 scopus 로고    scopus 로고
    • Acetylation goes global: The emergence of acetylation biology
    • PMID: 19920250
    • Norris KL, Lee JY, Yao TP (2009) Acetylation goes global: the emergence of acetylation biology. Science signaling 2: pe76. doi: 10.1126/scisignal.297pe76 PMID: 19920250
    • (2009) Science Signaling , vol.2 , pp. pe76
    • Norris, K.L.1    Lee, J.Y.2    Yao, T.P.3
  • 97
    • 84899728474 scopus 로고    scopus 로고
    • Toxoplasma gondii virulence factor ROP18 inhibits the host NF-kappaB pathway by promoting p65 degradation
    • PMID: 24648522
    • Du J, An R, Chen L, Shen Y, Chen Y, et al. (2014) Toxoplasma gondii virulence factor ROP18 inhibits the host NF-kappaB pathway by promoting p65 degradation. J Biol Chem 289: 12578-12592. doi: 10.1074/jbc.M113.544718 PMID: 24648522
    • (2014) J Biol Chem , vol.289 , pp. 12578-12592
    • Du, J.1    An, R.2    Chen, L.3    Shen, Y.4    Chen, Y.5
  • 98
    • 84892910206 scopus 로고    scopus 로고
    • Toxoplasma GRA7 effector increases turnover of immunity-related GTPases and contributes to acute virulence in the mouse
    • PMID: 24390541
    • Alaganan A, Fentress SJ, Tang K, Wang Q, Sibley LD (2014) Toxoplasma GRA7 effector increases turnover of immunity-related GTPases and contributes to acute virulence in the mouse. Proc Natl Acad Sci U S A 111: 1126-1131. doi: 10.1073/pnas.1313501111 PMID: 24390541
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 1126-1131
    • Alaganan, A.1    Fentress, S.J.2    Tang, K.3    Wang, Q.4    Sibley, L.D.5
  • 99
    • 84885444878 scopus 로고    scopus 로고
    • A Toxoplasma dense granule protein, GRA24, modulates the early immune response to infection by promoting a direct and sustained host p38 MAPK activation
    • PMID: 24043761
    • Braun L, Brenier-Pinchart MP, Yogavel M, Curt-Varesano A, Curt-Bertini RL, et al. (2013) A Toxoplasma dense granule protein, GRA24, modulates the early immune response to infection by promoting a direct and sustained host p38 MAPK activation. J Exp Med 210: 2071-2086. doi: 10.1084/jem.20130103 PMID: 24043761
    • (2013) J Exp Med , vol.210 , pp. 2071-2086
    • Braun, L.1    Brenier-Pinchart, M.P.2    Yogavel, M.3    Curt-Varesano, A.4    Curt-Bertini, R.L.5


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