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Volumn 31, Issue 11, 2011, Pages 2349-2363

Acetylation of a conserved lysine residue in the ATP binding pocket of p38 augments its kinase activity during hypertrophy of cardiomyocytes

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; HISTONE ACETYLTRANSFERASE PCAF; HISTONE DEACETYLASE 3; LYSINE; MITOGEN ACTIVATED PROTEIN KINASE P38;

EID: 79958033203     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01205-10     Document Type: Article
Times cited : (53)

References (59)
  • 1
    • 0242515803 scopus 로고    scopus 로고
    • What determines the intracellular ATP concentration
    • Ataullakhanov, F. I., and V. M. Vitvitsky. 2002. What determines the intracellular ATP concentration. Biosci. Rep. 22:501-511.
    • (2002) Biosci. Rep. , vol.22 , pp. 501-511
    • Ataullakhanov, F.I.1    Vitvitsky, V.M.2
  • 2
    • 85034938067 scopus 로고
    • Mitochondrial transmembrane ion distribution during anoxia
    • Aw, T. Y., B. S. Andersson, and D. P. Jones. 1987. Mitochondrial transmembrane ion distribution during anoxia. Am. J. Physiol. 252:C356-C361.
    • (1987) Am. J. Physiol. , vol.252
    • Aw, T.Y.1    Andersson, B.S.2    Jones, D.P.3
  • 3
    • 34249793710 scopus 로고    scopus 로고
    • Reversible acetylation of non histone proteins: role in cellular function and disease
    • Batta, K., C. Das, S. Gadad, J. Shandilya, and T. Kundu. 2007. Reversible acetylation of non histone proteins: role in cellular function and disease. Subcell. Biochem. 41:193-212.
    • (2007) Subcell. Biochem. , vol.41 , pp. 193-212
    • Batta, K.1    Das, C.2    Gadad, S.3    Shandilya, J.4    Kundu, T.5
  • 4
    • 0041660960 scopus 로고    scopus 로고
    • Mechanism of p38 MAP kinase activation in vivo
    • Brancho, D., et al. 2003. Mechanism of p38 MAP kinase activation in vivo. Genes Dev. 17:1969-1978.
    • (2003) Genes Dev , vol.17 , pp. 1969-1978
    • Brancho, D.1
  • 5
    • 58949098466 scopus 로고    scopus 로고
    • Organochlorine-mediated potentiation of the general coactivator p300 through p38 mitogen-activated protein kinase
    • Bratton, M. R., et al. 2009. Organochlorine-mediated potentiation of the general coactivator p300 through p38 mitogen-activated protein kinase. Carcinogenesis. 30:106-113.
    • (2009) Carcinogenesis , vol.30 , pp. 106-113
    • Bratton, M.R.1
  • 6
    • 0034383952 scopus 로고    scopus 로고
    • The MEK1-ERK1/2 signaling pathway promotes compensated cardiac hypertrophy in transgenic mice
    • Bueno, O. F., et al. 2000. The MEK1-ERK1/2 signaling pathway promotes compensated cardiac hypertrophy in transgenic mice. EMBO J. 19:6341-6350.
    • (2000) EMBO J , vol.19 , pp. 6341-6350
    • Bueno, O.F.1
  • 7
    • 0033485261 scopus 로고    scopus 로고
    • Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation
    • Bulavin, D. V., et al. 1999. Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation. EMBO J. 18:6845-6854.
    • (1999) EMBO J , vol.18 , pp. 6845-6854
    • Bulavin, D.V.1
  • 8
    • 0033179153 scopus 로고    scopus 로고
    • Activation of c-Jun N-terminal kinases and p38-mitogen-activated protein kinases in human heart failure secondary to ischaemic heart disease
    • Cook, S. A., P. H. Sugden, and A. Clerk. 1999. Activation of c-Jun N-terminal kinases and p38-mitogen-activated protein kinases in human heart failure secondary to ischaemic heart disease. J. Mol. Cell. Cardiol. 31:1429-1434.
    • (1999) J. Mol. Cell. Cardiol. , vol.31 , pp. 1429-1434
    • Cook, S.A.1    Sugden, P.H.2    Clerk, A.3
  • 9
    • 10844286471 scopus 로고    scopus 로고
    • Phosphorylation of estrogen receptor alpha blocks its acetylation and regulates estrogen sensitivity
    • Cui, Y., et al. 2004. Phosphorylation of estrogen receptor alpha blocks its acetylation and regulates estrogen sensitivity. Cancer Res. 64:9199-9208.
    • (2004) Cancer Res , vol.64 , pp. 9199-9208
    • Cui, Y.1
  • 10
    • 73949098573 scopus 로고    scopus 로고
    • Selective control of gene expression by CDK9 in human cells
    • Garriga, J., Xie, H., Obradovic, Z., and Graña, X. 2010. Selective control of gene expression by CDK9 in human cells. J. Cell. Physiol. 222:200-208.
    • (2010) J. Cell. Physiol. , vol.222 , pp. 200-208
    • Garriga, J.1    Xie, H.2    Obradovic, Z.3    Graña, X.4
  • 11
    • 0037083375 scopus 로고    scopus 로고
    • MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha
    • Ge, B., et al. 2002. MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha. Science. 295:1291-1294.
    • (2002) Science , vol.295 , pp. 1291-1294
    • Ge, B.1
  • 13
    • 0032557678 scopus 로고    scopus 로고
    • Induction of cyclooxygenase-2 by the activated MEKK1-SEK1/MKK4-p38 mitogen-activated protein kinase pathway
    • Guan, Z., S. Y. Buckman, A. P. Pentland, D. J. Templeton, and A. R. Morrison. 1998. Induction of cyclooxygenase-2 by the activated MEKK1-SEK1/MKK4-p38 mitogen-activated protein kinase pathway. J. Biol. Chem. 273:12901-12908.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12901-12908
    • Guan, Z.1    Buckman, S.Y.2    Pentland, A.P.3    Templeton, D.J.4    Morrison, A.R.5
  • 14
    • 0033539882 scopus 로고    scopus 로고
    • Identification of two distinct regions of p38 MAPK required for substrate binding and phosphorylation
    • Gum, R. J., and P. R. Young. 1999. Identification of two distinct regions of p38 MAPK required for substrate binding and phosphorylation. Biochem. Biophys. Res. Commun. 266:284-289.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 284-289
    • Gum, R.J.1    Young, P.R.2
  • 15
    • 67650095388 scopus 로고    scopus 로고
    • Abnormal energetics and ATP depletion in pressure-overload mouse hearts: in vivo high-energy phosphate concentration measures by noninvasive magnetic resonance
    • Gupta, A., V. P. Chacko, and R. G. Weiss. 2009. Abnormal energetics and ATP depletion in pressure-overload mouse hearts: in vivo high-energy phosphate concentration measures by noninvasive magnetic resonance. Am. J. Physiol. Heart Circ. Physiol. 297:H59-64.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297
    • Gupta, A.1    Chacko, V.P.2    Weiss, R.G.3
  • 16
    • 0037169542 scopus 로고    scopus 로고
    • The transcriptional co-activators CBP and p300 are activated via phenylephrine through the p42/p44 MAPK cascade
    • Gusterson, R., et al. 2002. The transcriptional co-activators CBP and p300 are activated via phenylephrine through the p42/p44 MAPK cascade. J. Biol. Chem. 277:2517-2524.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2517-2524
    • Gusterson, R.1
  • 17
    • 0037470133 scopus 로고    scopus 로고
    • The transcriptional co-activators CREB-binding protein (CBP) and p300 play a critical role in cardiac hypertrophy that is dependent on their histone acetyltransferase activity
    • Gusterson, R. J., E. Jazrawi, I. M. Adcock, and D. S. Latchman. 2003. The transcriptional co-activators CREB-binding protein (CBP) and p300 play a critical role in cardiac hypertrophy that is dependent on their histone acetyltransferase activity. J. Biol. Chem. 278:6838-6847.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6838-6847
    • Gusterson, R.J.1    Jazrawi, E.2    Adcock, I.M.3    Latchman, D.S.4
  • 18
    • 0030894683 scopus 로고    scopus 로고
    • Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation
    • Han, J., Y. Jiang, Z. Li, V. V. Kravchenko, and R. J. Ulevitch. 1997. Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation. Nature. 386:296-299.
    • (1997) Nature , vol.386 , pp. 296-299
    • Han, J.1    Jiang, Y.2    Li, Z.3    Kravchenko, V.V.4    Ulevitch, R.J.5
  • 19
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han, J., J. D. Lee, L. Bibbs, and R. J. Ulevitch. 1994. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science. 265:808-811.
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 20
    • 0036731380 scopus 로고    scopus 로고
    • Constitutive p38HOG mitogen-activated protein kinase activation induces permanent cell cycle arrest and senescence
    • Haq, R., et al. 2002. Constitutive p38HOG mitogen-activated protein kinase activation induces permanent cell cycle arrest and senescence. Cancer Res. 62:5076-5082.
    • (2002) Cancer Res , vol.62 , pp. 5076-5082
    • Haq, R.1
  • 21
    • 0035814747 scopus 로고    scopus 로고
    • Differential activation of signal transduction pathways in human hearts with hypertrophy versus advanced heart failure
    • Haq, S., et al. 2001. Differential activation of signal transduction pathways in human hearts with hypertrophy versus advanced heart failure. Circulation. 103:670-677.
    • (2001) Circulation , vol.103 , pp. 670-677
    • Haq, S.1
  • 22
    • 9444228220 scopus 로고    scopus 로고
    • Inhibition of p38 MAP kinase- and RICK/NFkappaB-signaling suppresses inflammatory bowel disease
    • Hollenbach, E., et al. 2004. Inhibition of p38 MAP kinase- and RICK/NFkappaB-signaling suppresses inflammatory bowel disease. FASEB J. 18: 1550-1552.
    • (2004) FASEB J , vol.18 , pp. 1550-1552
    • Hollenbach, E.1
  • 23
    • 0034660614 scopus 로고    scopus 로고
    • p38 protects human melanoma cells from UV-induced apoptosis through down-regulation of NF-kappaB activity and Fas expression
    • Ivanov, V. N., and Z. Ronai. 2000. p38 protects human melanoma cells from UV-induced apoptosis through down-regulation of NF-kappaB activity and Fas expression. Oncogene. 19:3003-3012.
    • (2000) Oncogene , vol.19 , pp. 3003-3012
    • Ivanov, V.N.1    Ronai, Z.2
  • 24
    • 27144541891 scopus 로고    scopus 로고
    • Chemical genetic engineering of G protein-coupled receptor kinase 2
    • Kenski, D. M., C. Zhang, M. von Zastrow, and K. M. Shokat. 2005. Chemical genetic engineering of G protein-coupled receptor kinase 2. J. Biol. Chem. 280:35051-35061.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35051-35061
    • Kenski, D.M.1    Zhang, C.2    von Zastrow, M.3    Shokat, K.M.4
  • 25
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: a regulatory modification to rival phosphorylation?
    • Kouzarides, T. 2000. Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 19:1176-1179.
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 26
    • 15444357764 scopus 로고    scopus 로고
    • Mechanical stretch induces hypertrophic responses in cardiac myocytes of angiotensin II type 1a receptor knockout mice
    • Kudoh, S., et al. 1998. Mechanical stretch induces hypertrophic responses in cardiac myocytes of angiotensin II type 1a receptor knockout mice. J. Biol. Chem. 273:24037-24043.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24037-24043
    • Kudoh, S.1
  • 27
    • 14944371448 scopus 로고    scopus 로고
    • Alpha-adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes is mediated via thioredoxin-1-sensitive oxidative modification of thiols on Ras
    • Kuster, G. M., et al. 2005. Alpha-adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes is mediated via thioredoxin-1-sensitive oxidative modification of thiols on Ras. Circulation. 111:1192-1198.
    • (2005) Circulation , vol.111 , pp. 1192-1198
    • Kuster, G.M.1
  • 28
    • 55549096745 scopus 로고    scopus 로고
    • SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1
    • Lan, F., J. M. Cacicedo, N. Ruderman, and Y. Ido. 2008. SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. J. Biol. Chem. 283:27628-27635.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27628-27635
    • Lan, F.1    Cacicedo, J.M.2    Ruderman, N.3    Ido, Y.4
  • 29
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis
    • Leist, M., B. Single, A. F. Castoldi, S. Kuhnle, and P. Nicotera. 1997. Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis. J. Exp. Med. 185:1481-1486.
    • (1997) J. Exp. Med. , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3    Kuhnle, S.4    Nicotera, P.5
  • 30
    • 0344924887 scopus 로고    scopus 로고
    • Redefining the roles of p38 and JNK signaling in cardiac hypertrophy: dichotomy between cultured myocytes and animal models
    • Liang, Q., and J. D. Molkentin. 2003. Redefining the roles of p38 and JNK signaling in cardiac hypertrophy: dichotomy between cultured myocytes and animal models. J. Mol. Cell. Cardiol. 35:1385-1394.
    • (2003) J. Mol. Cell. Cardiol. , vol.35 , pp. 1385-1394
    • Liang, Q.1    Molkentin, J.D.2
  • 31
    • 0035834071 scopus 로고    scopus 로고
    • The in vivo role of p38 MAP kinases in cardiac remodeling and restrictive cardiomyopathy
    • Liao, P., et al. 2001. The in vivo role of p38 MAP kinases in cardiac remodeling and restrictive cardiomyopathy. Proc. Natl. Acad. Sci. U. S. A. 98: 12283-12288.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 12283-12288
    • Liao, P.1
  • 32
    • 17644389201 scopus 로고    scopus 로고
    • Myocyte enhancer factor 2 acetylation by p300 enhances its DNA binding activity, transcriptional activity, and myogenic differentiation
    • Ma, K., J. K. L. Chan, G. Zhu, and Z. Wu. 2005. Myocyte enhancer factor 2 acetylation by p300 enhances its DNA binding activity, transcriptional activity, and myogenic differentiation. Mol. Cell. Biol. 25:3575-3582.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3575-3582
    • Ma, K.1    Chan, J.K.L.2    Zhu, G.3    Wu, Z.4
  • 33
    • 85047695408 scopus 로고    scopus 로고
    • Phosphorylation of forkhead transcription factors by erythropoietin and stem cell factor prevents acetylation and their interaction with coactivator p300 in erythroid progenitor cells
    • Mahmud, D. L., et al. 2002. Phosphorylation of forkhead transcription factors by erythropoietin and stem cell factor prevents acetylation and their interaction with coactivator p300 in erythroid progenitor cells. Oncogene. 21:1556-1562.
    • (2002) Oncogene , vol.21 , pp. 1556-1562
    • Mahmud, D.L.1
  • 34
    • 75349091958 scopus 로고    scopus 로고
    • The transcriptional co-activator PCAF regulates cdk2 activity
    • Mateo, F., et al. 2009. The transcriptional co-activator PCAF regulates cdk2 activity. Nucleic Acids Res. 37:7072-7084.
    • (2009) Nucleic Acids Res , vol.37 , pp. 7072-7084
    • Mateo, F.1
  • 35
    • 1442278553 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-mediated activation of p38 is dependent upon Src and RAFTK//Pyk2
    • McMullen, M., R. Keller, M. Sussman, and K. Pumiglia. 2004. Vascular endothelial growth factor-mediated activation of p38 is dependent upon Src and RAFTK//Pyk2. Oncogene. 23:1275-1282.
    • (2004) Oncogene , vol.23 , pp. 1275-1282
    • McMullen, M.1    Keller, R.2    Sussman, M.3    Pumiglia, K.4
  • 36
    • 22344458207 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase (MAPK) is a key mediator in glucocorticoid-induced apoptosis of lymphoid cells: correlation between p38 MAPK activation and site-specific phosphorylation of the human glucocorticoid receptor at serine 211
    • Miller, A. L., et al. 2005. p38 mitogen-activated protein kinase (MAPK) is a key mediator in glucocorticoid-induced apoptosis of lymphoid cells: correlation between p38 MAPK activation and site-specific phosphorylation of the human glucocorticoid receptor at serine 211. Mol. Endocrinol. 19:1569-1583.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 1569-1583
    • Miller, A.L.1
  • 37
    • 0030760725 scopus 로고    scopus 로고
    • Involvement of stress-activated protein kinase and p38/RK mitogen-activated protein kinase signaling pathways in the enhanced phosphorylation of initiation factor 4E in NIH 3T3 cells
    • Morley,1; S. J., and L. McKendrick. 1997. Involvement of stress-activated protein kinase and p38/RK mitogen-activated protein kinase signaling pathways in the enhanced phosphorylation of initiation factor 4E in NIH 3T3 cells. J. Biol. Chem. 272:17887-17893.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17887-17893
    • Morley, S.J.1    McKendrick, L.2
  • 38
    • 33744457909 scopus 로고    scopus 로고
    • Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation
    • Mukherjee, S., et al. 2006. Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. Science. 312:1211-1214.
    • (2006) Science , vol.312 , pp. 1211-1214
    • Mukherjee, S.1
  • 39
    • 10044261073 scopus 로고    scopus 로고
    • p38 alpha mitogen-activated protein kinase plays a critical role in cardiomyocyte survival but not in cardiac hypertrophic growth in response to pressure overload
    • Nishida, K., et al. 2004. p38 alpha mitogen-activated protein kinase plays a critical role in cardiomyocyte survival but not in cardiac hypertrophic growth in response to pressure overload. Mol. Cell. Biol. 24:10611-10620.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10611-10620
    • Nishida, K.1
  • 40
    • 1542613386 scopus 로고    scopus 로고
    • Stress-activated MAP kinases in cardiac remodeling and heart failure: new insights from transgenic studies
    • Petrich, B. G., and Y. Wang. 2004. Stress-activated MAP kinases in cardiac remodeling and heart failure: new insights from transgenic studies. Trends Cardiovasc. Med. 14:50-55.
    • (2004) Trends Cardiovasc. Med. , vol.14 , pp. 50-55
    • Petrich, B.G.1    Wang, Y.2
  • 41
    • 77449120223 scopus 로고    scopus 로고
    • Exogenous NAD blocks cardiac hypertrophic response via activation of the SIRT3-LKB1-AMP-activated kinase pathway
    • Pillai, V. B., et al. 2010. Exogenous NAD blocks cardiac hypertrophic response via activation of the SIRT3-LKB1-AMP-activated kinase pathway. J. Biol. Chem. 285:3133-3144.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3133-3144
    • Pillai, V.B.1
  • 42
    • 0028935270 scopus 로고
    • Pro- inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine
    • Raingeaud, J. L., et al. 1995. Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem. 270:7420-7426.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7420-7426
    • Raingeaud, J.L.1
  • 43
    • 67651210858 scopus 로고    scopus 로고
    • SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1
    • Rajamohan, S. B., et al. 2009. SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1. Mol. Cell. Biol. 29:4116-4129.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 4116-4129
    • Rajamohan, S.B.1
  • 44
    • 0037412181 scopus 로고    scopus 로고
    • A conformational analysis of Walker motif A [GXXXXGKT (S)] in nucleotide-binding and other proteins
    • Ramakrishnan, C., V. S. Dani, and T. Ramasarma. 2002. A conformational analysis of Walker motif A [GXXXXGKT (S)] in nucleotide-binding and other proteins. Protein Eng. 15:783-798.
    • (2002) Protein Eng , vol.15 , pp. 783-798
    • Ramakrishnan, C.1    Dani, V.S.2    Ramasarma, T.3
  • 45
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse, J., et al. 1994. A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell. 78:1027-1037.
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1
  • 46
    • 41149145576 scopus 로고    scopus 로고
    • Acetylation of conserved lysines in the catalytic core of cyclin-dependent kinase 9 inhibits kinase activity and regulates transcription
    • Sabò, A., M. Lusic, A. Cereseto, and M. Giacca. 2008. Acetylation of conserved lysines in the catalytic core of cyclin-dependent kinase 9 inhibits kinase activity and regulates transcription. Mol. Cell. Biol. 28:2201-2212.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 2201-2212
    • Sabò, A.1    Lusic, M.2    Cereseto, A.3    Giacca, M.4
  • 47
    • 38449119486 scopus 로고    scopus 로고
    • MAPK p38 regulates transcriptional activity of NF-kappaB in primary human astrocytes via acetylation of p65
    • Saha, R. N., M. Jana, and K. Pahan. 2007. MAPK p38 regulates transcriptional activity of NF-kappaB in primary human astrocytes via acetylation of p65. J. Immunol. 179:7101-7109.
    • (2007) J. Immunol. , vol.179 , pp. 7101-7109
    • Saha, R.N.1    Jana, M.2    Pahan, K.3
  • 48
    • 0032530486 scopus 로고    scopus 로고
    • DNA damage activates p53 through a phosphorylation-acetylation cascade
    • Sakaguchi, K., et al. 1998. DNA damage activates p53 through a phosphorylation-acetylation cascade. Genes Dev. 12:2831-2841.
    • (1998) Genes Dev , vol.12 , pp. 2831-2841
    • Sakaguchi, K.1
  • 49
    • 0036545584 scopus 로고    scopus 로고
    • Role of oxidative stress in myocardial hypertrophy and failure
    • Sawyer, D. B., et al. 2002. Role of oxidative stress in myocardial hypertrophy and failure. J. Mol. Cell. Cardiol. 34:379-388.
    • (2002) J. Mol. Cell. Cardiol. , vol.34 , pp. 379-388
    • Sawyer, D.B.1
  • 50
    • 70349208608 scopus 로고    scopus 로고
    • Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice
    • Sundaresan, N. R., et al. 2009. Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. J. Clin. Invest. 119:2758-2771.
    • (2009) J. Clin. Invest. , vol.119 , pp. 2758-2771
    • Sundaresan, N.R.1
  • 51
    • 0032562716 scopus 로고    scopus 로고
    • Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest
    • Takenaka, K., T. Moriguchi, and E. Nishida. 1998. Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest. Science. 280:599-602.
    • (1998) Science , vol.280 , pp. 599-602
    • Takenaka, K.1    Moriguchi, T.2    Nishida, E.3
  • 52
    • 33846418746 scopus 로고    scopus 로고
    • Role of oxidative stress in cardiac hypertrophy and remodeling
    • Takimoto, E., and D. A. Kass. 2007. Role of oxidative stress in cardiac hypertrophy and remodeling. Hypertension. 49:241-248.
    • (2007) Hypertension , vol.49 , pp. 241-248
    • Takimoto, E.1    Kass, D.A.2
  • 53
    • 55549099609 scopus 로고    scopus 로고
    • Transgenic overexpression of Hdac3 in the heart produces increased postnatal cardiac myocyte proliferation but does not induce hypertrophy
    • Trivedi, C. M., M. M. Lu, Q. Wang, and J. A. Epstein. 2008. Transgenic overexpression of Hdac3 in the heart produces increased postnatal cardiac myocyte proliferation but does not induce hypertrophy. J. Biol. Chem. 283: 26484-26489.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26484-26489
    • Trivedi, C.M.1    Lu, M.M.2    Wang, Q.3    Epstein, J.A.4
  • 54
    • 15744385061 scopus 로고    scopus 로고
    • Activation of Stat3 sequencespecific DNA binding and transcription by p300/CREB-binding proteinmediated acetylation
    • Wang, R., P. Cherukuri, and J. Luo. 2005. Activation of Stat3 sequencespecific DNA binding and transcription by p300/CREB-binding proteinmediated acetylation. J. Biol. Chem. 280:11528-11534.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11528-11534
    • Wang, R.1    Cherukuri, P.2    Luo, J.3
  • 55
    • 0029938805 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP kinase
    • Wang, X.-Z., and D. Ron. 1996. Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP kinase. Science. 272:1347-1349.
    • (1996) Science , vol.272 , pp. 1347-1349
    • Wang, X.-Z.1    Ron, D.2
  • 56
    • 33750223130 scopus 로고    scopus 로고
    • Nitration of p38 MAPK in the placenta: association of nitration with reduced catalytic activity of p38 MAPK in pre-eclampsia
    • Webster, R. P., D. Brockman, and L. Myatt. 2006. Nitration of p38 MAPK in the placenta: association of nitration with reduced catalytic activity of p38 MAPK in pre-eclampsia. Mol. Hum. Reprod. 12:677-685.
    • (2006) Mol. Hum. Reprod. , vol.12 , pp. 677-685
    • Webster, R.P.1    Brockman, D.2    Myatt, L.3
  • 57
    • 0038302887 scopus 로고    scopus 로고
    • Cardiac p300 is involved in myocyte growth with decompensated heart failure
    • Yanazume, T., et al. 2003. Cardiac p300 is involved in myocyte growth with decompensated heart failure. Mol. Cell. Biol. 23:3593-3606.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3593-3606
    • Yanazume, T.1
  • 58
    • 2942594784 scopus 로고    scopus 로고
    • Activation of the growth-differentiation factor 11 gene by the histone deacetylase (HDAC) inhibitor trichostatin A and repression by HDAC3
    • Zhang, X., et al. 2004. Activation of the growth-differentiation factor 11 gene by the histone deacetylase (HDAC) inhibitor trichostatin A and repression by HDAC3. Mol. Cell. Biol. 24:5106-5118.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5106-5118
    • Zhang, X.1
  • 59
    • 0032953307 scopus 로고    scopus 로고
    • Regulation of the MEF2 family of transcription factors by p38
    • Zhao, M., et al. 1999. Regulation of the MEF2 family of transcription factors by p38. Mol. Cell. Biol. 19:21-30.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 21-30
    • Zhao, M.1


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