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Volumn 1822, Issue 4, 2012, Pages 607-614

Non-histone lysine acetylated proteins in heart failure

Author keywords

Global screening; Heart failure; Lysine acetylation; Mitochondrial protein; Sirtuin 3

Indexed keywords

ACYL COENZYME A DEHYDROGENASE; CREATINE KINASE; LYSINE; MALATE DEHYDROGENASE; MITOCHONDRIAL ENZYME; NONHISTONE PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PYRUVATE DEHYDROGENASE; SIRTUIN 3;

EID: 84857136130     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2011.11.016     Document Type: Article
Times cited : (63)

References (28)
  • 1
    • 33644837326 scopus 로고    scopus 로고
    • Control of cardiac growth by histone acetylation/deacetylation
    • Backs J., Olson E.N. Control of cardiac growth by histone acetylation/deacetylation. Circ. Res. 2006, 98:15.
    • (2006) Circ. Res. , vol.98 , pp. 15
    • Backs, J.1    Olson, E.N.2
  • 2
    • 79958041601 scopus 로고    scopus 로고
    • The SirT3 divining rod points to oxidative stress
    • Bell E.L., Guarente L. The SirT3 divining rod points to oxidative stress. Mol. Cell 2011, 42:561.
    • (2011) Mol. Cell , vol.42 , pp. 561
    • Bell, E.L.1    Guarente, L.2
  • 5
    • 76349122643 scopus 로고    scopus 로고
    • Protein acetylation in the cardiorenal axis: the promise of histone deacetylase inhibitors
    • Bush E.W., McKinsey T.A. Protein acetylation in the cardiorenal axis: the promise of histone deacetylase inhibitors. Circ. Res. 2010, 106:272.
    • (2010) Circ. Res. , vol.106 , pp. 272
    • Bush, E.W.1    McKinsey, T.A.2
  • 7
    • 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., Jazrawi E., Adcock I.M., Latchman D.S. 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. 2003, 278:6838.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6838
    • Gusterson, R.J.1    Jazrawi, E.2    Adcock, I.M.3    Latchman, D.S.4
  • 8
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • Hallows W.C., Lee S., Denu J.M. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:10230.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 10230
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3
  • 11
    • 0028566018 scopus 로고
    • Transition from compensatory hypertrophy to dilated, failing left ventricles in Dahl salt-sensitive rats
    • Inoko M., Kihara Y., Morii I., Fujiwara H., Sasayama S. Transition from compensatory hypertrophy to dilated, failing left ventricles in Dahl salt-sensitive rats. Am. J. Physiol. 1994, 267:H2471-H2482.
    • (1994) Am. J. Physiol. , vol.267
    • Inoko, M.1    Kihara, Y.2    Morii, I.3    Fujiwara, H.4    Sasayama, S.5
  • 12
    • 29544438797 scopus 로고    scopus 로고
    • Proteomic analysis of organ-specific post-translational lysine-acetylation and -methylation in mice by use of anti-acetyllysine and -methyllysine mouse monoclonal antibodies
    • Iwabata H., Yoshida M., Komatsu Y. Proteomic analysis of organ-specific post-translational lysine-acetylation and -methylation in mice by use of anti-acetyllysine and -methyllysine mouse monoclonal antibodies. Proteomics 2005, 5:4653.
    • (2005) Proteomics , vol.5 , pp. 4653
    • Iwabata, H.1    Yoshida, M.2    Komatsu, Y.3
  • 13
    • 79251588033 scopus 로고    scopus 로고
    • Roles and targets of class I and IIa histone deacetylases in cardiac hypertrophy
    • Kee H.J., Kook H. Roles and targets of class I and IIa histone deacetylases in cardiac hypertrophy. J. Biomed. Biotechnol. 2011, 2011:928326.
    • (2011) J. Biomed. Biotechnol. , vol.2011 , pp. 928326
    • Kee, H.J.1    Kook, H.2
  • 14
    • 78650116597 scopus 로고    scopus 로고
    • Post-translational modifications of mitochondrial outer membrane proteins
    • Kerner J., Lee K., Hoppel C.L. Post-translational modifications of mitochondrial outer membrane proteins. Free Radic. Res. 2011, 45:16.
    • (2011) Free Radic. Res. , vol.45 , pp. 16
    • Kerner, J.1    Lee, K.2    Hoppel, C.L.3
  • 17
    • 58149522335 scopus 로고    scopus 로고
    • Regulation of muscle creatine kinase by phosphorylation in normal and diabetic hearts
    • Lin G., Liu Y., MacLeod K.M. Regulation of muscle creatine kinase by phosphorylation in normal and diabetic hearts. Cell. Mol. Life Sci. 2009, 66:135.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 135
    • Lin, G.1    Liu, Y.2    MacLeod, K.M.3
  • 18
    • 0034845541 scopus 로고    scopus 로고
    • Abnormal cardiac and skeletal muscle mitochondrial function in pacing-induced cardiac failure
    • Marin-Garcia J., Goldenthal M.J., Moe G.W. Abnormal cardiac and skeletal muscle mitochondrial function in pacing-induced cardiac failure. Cardiovasc. Res. 2001, 52:103.
    • (2001) Cardiovasc. Res. , vol.52 , pp. 103
    • Marin-Garcia, J.1    Goldenthal, M.J.2    Moe, G.W.3
  • 19
    • 79959541505 scopus 로고    scopus 로고
    • Acetylation of MnSOD directs enzymatic activity responding to cellular nutrient status or oxidative stress
    • Ozden O., Park S.H., Kim H.S., Jiang H., Coleman M.C., Spitz D.R., Gius D. Acetylation of MnSOD directs enzymatic activity responding to cellular nutrient status or oxidative stress. Aging (Albany, NY) 2011, 3:102.
    • (2011) Aging (Albany, NY) , vol.3 , pp. 102
    • Ozden, O.1    Park, S.H.2    Kim, H.S.3    Jiang, H.4    Coleman, M.C.5    Spitz, D.R.6    Gius, D.7
  • 23
    • 33745889628 scopus 로고    scopus 로고
    • Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
    • Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., Verdin E. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:10224.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 10224
    • Schwer, B.1    Bunkenborg, J.2    Verdin, R.O.3    Andersen, J.S.4    Verdin, E.5
  • 24
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • Spange S., Wagner T., Heinzel T., Kramer O.H. Acetylation of non-histone proteins modulates cellular signalling at multiple levels. Int. J. Biochem. Cell Biol. 2009, 41:185.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 185
    • Spange, S.1    Wagner, T.2    Heinzel, T.3    Kramer, O.H.4
  • 25
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • Starai V.J., Celic I., Cole R.N., Boeke J.D., Escalante-Semerena J.C. Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 2002, 298:2390.
    • (2002) Science , vol.298 , pp. 2390
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 26
    • 70349208608 scopus 로고    scopus 로고
    • Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice
    • Sundaresan N.R., Gupta M., Kim G., Rajamohan S.B., Isbatan A., Gupta M.P. Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. J. Clin. Invest. 2009, 119:2758.
    • (2009) J. Clin. Invest. , vol.119 , pp. 2758
    • Sundaresan, N.R.1    Gupta, M.2    Kim, G.3    Rajamohan, S.B.4    Isbatan, A.5    Gupta, M.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.