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Volumn 110, Issue 4, 2015, Pages 1-20

SIRT3 deficiency impairs mitochondrial and contractile function in the heart

Author keywords

Cardiac function; Energetics; Mitochondria; Sirtuin 3

Indexed keywords

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; MITOCHONDRIAL PROTEIN; PALMITIC ACID; SIRTUIN 3; TRICARBOXYLIC ACID; SIRT3 PROTEIN, MOUSE;

EID: 84929088095     PISSN: 03008428     EISSN: 14351803     Source Type: Journal    
DOI: 10.1007/s00395-015-0493-6     Document Type: Article
Times cited : (166)

References (56)
  • 1
    • 0037315085 scopus 로고    scopus 로고
    • Age-dependent changes in metabolism, contractile function, and ischemic sensitivity in hearts from db/db mice
    • COI: 1:CAS:528:DC%2BD3sXhtFans7c%3D, PID: 12540618
    • Aasum E, Hafstad AD, Severson DL, Larsen TS (2003) Age-dependent changes in metabolism, contractile function, and ischemic sensitivity in hearts from db/db mice. Diabetes 52:434–441. doi:10.2337/diabetes.52.2.434
    • (2003) Diabetes , vol.52 , pp. 434-441
    • Aasum, E.1    Hafstad, A.D.2    Severson, D.L.3    Larsen, T.S.4
  • 2
    • 0033542112 scopus 로고    scopus 로고
    • Cloning and characterization of the 5′ flanking region of the human uncoupling protein 3 (UCP3) gene
    • COI: 1:CAS:528:DyaK1MXjtVersbg%3D, PID: 10329378
    • Acin A, Rodriguez M, Rique H, Canet E, Boutin JA, Galizzi JP (1999) Cloning and characterization of the 5′ flanking region of the human uncoupling protein 3 (UCP3) gene. Biochem Biophys Res Commun 258:278–283. doi:10.1006/bbrc.1999.0530
    • (1999) Biochem Biophys Res Commun , vol.258 , pp. 278-283
    • Acin, A.1    Rodriguez, M.2    Rique, H.3    Canet, E.4    Boutin, J.A.5    Galizzi, J.P.6
  • 3
    • 55749084738 scopus 로고    scopus 로고
    • A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
    • COI: 1:CAS:528:DC%2BD1cXht1SgtrbL, PID: 18794531
    • Ahn BH, Kim HS, Song S, Lee IH, Liu J, Vassilopoulos A, Deng CX, Finkel T (2008) A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proc Natl Acad Sci USA 105:14447–14452. doi:10.1073/pnas.0803790105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14447-14452
    • Ahn, B.H.1    Kim, H.S.2    Song, S.3    Lee, I.H.4    Liu, J.5    Vassilopoulos, A.6    Deng, C.X.7    Finkel, T.8
  • 5
    • 0032489437 scopus 로고    scopus 로고
    • Altered constitutive expression of fatty acid-metabolizing enzymes in mice lacking the peroxisome proliferator-activated receptor alpha (PPARalpha)
    • COI: 1:CAS:528:DyaK1cXhsleis7s%3D, PID: 9488698
    • Aoyama T, Peters JM, Iritani N, Nakajima T, Furihata K, Hashimoto T, Gonzalez FJ (1998) Altered constitutive expression of fatty acid-metabolizing enzymes in mice lacking the peroxisome proliferator-activated receptor alpha (PPARalpha). J Biol Chem 273:5678–5684. doi:10.1074/jbc.273.10.5678
    • (1998) J Biol Chem , vol.273 , pp. 5678-5684
    • Aoyama, T.1    Peters, J.M.2    Iritani, N.3    Nakajima, T.4    Furihata, K.5    Hashimoto, T.6    Gonzalez, F.J.7
  • 6
    • 67650232210 scopus 로고    scopus 로고
    • Loss of cardioprotection with ageing
    • COI: 1:CAS:528:DC%2BD1MXnvVOkt7o%3D, PID: 19176601
    • Boengler K, Schulz R, Heusch G (2009) Loss of cardioprotection with ageing. Cardiovasc Res 83:247–261. doi:10.1093/cvr/cvp033
    • (2009) Cardiovasc Res , vol.83 , pp. 247-261
    • Boengler, K.1    Schulz, R.2    Heusch, G.3
  • 7
    • 34548848059 scopus 로고    scopus 로고
    • Mitochondrial energetics in the heart in obesity related diabetes: direct evidence for increased uncoupled respiration and activation of uncoupling proteins
    • COI: 1:CAS:528:DC%2BD2sXhtFygt7%2FE, PID: 17623815
    • Boudina S, Sena S, Theobald H, Sheng X, Wright JJ, Hu XX, Aziz S, Johnson JI, Bugger H, Zaha VG, Abel ED (2007) Mitochondrial energetics in the heart in obesity related diabetes: direct evidence for increased uncoupled respiration and activation of uncoupling proteins. Diabetes 56:2457–2466. doi:10.2337/db07-0481
    • (2007) Diabetes , vol.56 , pp. 2457-2466
    • Boudina, S.1    Sena, S.2    Theobald, H.3    Sheng, X.4    Wright, J.J.5    Hu, X.X.6    Aziz, S.7    Johnson, J.I.8    Bugger, H.9    Zaha, V.G.10    Abel, E.D.11
  • 8
    • 77956572071 scopus 로고    scopus 로고
    • Mitochondria in the diabetic heart
    • COI: 1:CAS:528:DC%2BC3cXhtlShsb7P, PID: 20639213
    • Bugger H, Abel ED (2010) Mitochondria in the diabetic heart. Cardiovasc Res 88:229–240. doi:10.1093/cvr/cvq239
    • (2010) Cardiovasc Res , vol.88 , pp. 229-240
    • Bugger, H.1    Abel, E.D.2
  • 9
    • 38949135755 scopus 로고    scopus 로고
    • Molecular mechanisms for myocardial mitochondrial dysfunction in the metabolic syndrome
    • COI: 1:CAS:528:DC%2BD1cXksVCqsQ%3D%3D
    • Bugger H, Abel ED (2008) Molecular mechanisms for myocardial mitochondrial dysfunction in the metabolic syndrome. Clin Sci (Lond) 114:195–210. doi:10.1042/CS20070166
    • (2008) Clin Sci (Lond) , vol.114 , pp. 195-210
    • Bugger, H.1    Abel, E.D.2
  • 10
    • 58149330628 scopus 로고    scopus 로고
    • Type 1 diabetic akita mouse hearts are insulin sensitive but manifest structurally abnormal mitochondria that remain coupled despite increased uncoupling protein 3
    • COI: 1:CAS:528:DC%2BD1MXhsleju7k%3D, PID: 18678617
    • Bugger H, Boudina S, Hu XX, Tuinei J, Zaha VG, Theobald HA, Yun UJ, McQueen AP, Wayment B, Litwin SE, Abel ED (2008) Type 1 diabetic akita mouse hearts are insulin sensitive but manifest structurally abnormal mitochondria that remain coupled despite increased uncoupling protein 3. Diabetes 57:2924–2932. doi:10.2337/db08-0079
    • (2008) Diabetes , vol.57 , pp. 2924-2932
    • Bugger, H.1    Boudina, S.2    Hu, X.X.3    Tuinei, J.4    Zaha, V.G.5    Theobald, H.A.6    Yun, U.J.7    McQueen, A.P.8    Wayment, B.9    Litwin, S.E.10    Abel, E.D.11
  • 11
    • 70349134016 scopus 로고    scopus 로고
    • Tissue-specific remodeling of the mitochondrial proteome in type 1 diabetic akita mice
    • COI: 1:CAS:528:DC%2BD1MXhtFChsbnI, PID: 19542201
    • Bugger H, Chen D, Riehle C, Soto J, Theobald HA, Hu XX, Ganesan B, Weimer BC, Abel ED (2009) Tissue-specific remodeling of the mitochondrial proteome in type 1 diabetic akita mice. Diabetes 58:1986–1997. doi:10.2337/db09-0259
    • (2009) Diabetes , vol.58 , pp. 1986-1997
    • Bugger, H.1    Chen, D.2    Riehle, C.3    Soto, J.4    Theobald, H.A.5    Hu, X.X.6    Ganesan, B.7    Weimer, B.C.8    Abel, E.D.9
  • 13
    • 75349111140 scopus 로고    scopus 로고
    • Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria
    • COI: 1:CAS:528:DC%2BD1MXhsFOgtb3O, PID: 20000467
    • Cimen H, Han MJ, Yang Y, Tong Q, Koc H, Koc EC (2010) Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria. Biochemistry 49:304–311. doi:10.1021/bi901627u
    • (2010) Biochemistry , vol.49 , pp. 304-311
    • Cimen, H.1    Han, M.J.2    Yang, Y.3    Tong, Q.4    Koc, H.5    Koc, E.C.6
  • 15
    • 33745237201 scopus 로고    scopus 로고
    • Metabolite profiling in Arabidopsis
    • COI: 1:CAS:528:DC%2BD28XjtlWmu7c%3D, PID: 16739598
    • Fiehn O (2006) Metabolite profiling in Arabidopsis. Methods Mol Biol 323:439–447. doi:10.1385/1-59745-003-0:439
    • (2006) Methods Mol Biol , vol.323 , pp. 439-447
    • Fiehn, O.1
  • 16
    • 0031011211 scopus 로고    scopus 로고
    • A mouse model for mitochondrial myopathy and cardiomyopathy resulting from a deficiency in the heart/muscle isoform of the adenine nucleotide translocator
    • COI: 1:CAS:528:DyaK2sXktFCrtL4%3D, PID: 9207786
    • Graham BH, Waymire KG, Cottrell B, Trounce IA, MacGregor GR, Wallace DC (1997) A mouse model for mitochondrial myopathy and cardiomyopathy resulting from a deficiency in the heart/muscle isoform of the adenine nucleotide translocator. Nat Genet 16:226–234. doi:10.1038/ng0797-226
    • (1997) Nat Genet , vol.16 , pp. 226-234
    • Graham, B.H.1    Waymire, K.G.2    Cottrell, B.3    Trounce, I.A.4    MacGregor, G.R.5    Wallace, D.C.6
  • 17
    • 84857136130 scopus 로고    scopus 로고
    • Non-histone lysine acetylated proteins in heart failure
    • COI: 1:CAS:528:DC%2BC38Xjt1yjtro%3D, PID: 22155497
    • Grillon JM, Johnson KR, Kotlo K, Danziger RS (2012) Non-histone lysine acetylated proteins in heart failure. Biochim Biophys Acta 1822:607–614. doi:10.1016/j.bbadis.2011.11.016
    • (2012) Biochim Biophys Acta , vol.1822 , pp. 607-614
    • Grillon, J.M.1    Johnson, K.R.2    Kotlo, K.3    Danziger, R.S.4
  • 18
    • 79952266729 scopus 로고    scopus 로고
    • Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy
    • COI: 1:CAS:528:DC%2BC3MXhtVSisrg%3D, (100252 [pii])
    • Hafner AV, Dai J, Gomes AP, Xiao CY, Palmeira CM, Rosenzweig A, Sinclair DA (2010) Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy. Aging (Albany NY) 2:914–923 (100252 [pii])
    • (2010) Aging (Albany NY) , vol.2 , pp. 914-923
    • Hafner, A.V.1    Dai, J.2    Gomes, A.P.3    Xiao, C.Y.4    Palmeira, C.M.5    Rosenzweig, A.6    Sinclair, D.A.7
  • 21
    • 70149095672 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyltransferase regulates cell survival through NAD+ synthesis in cardiac myocytes
    • COI: 1:CAS:528:DC%2BD1MXhtVekt7%2FF, PID: 19661458
    • Hsu CP, Oka S, Shao D, Hariharan N, Sadoshima J (2009) Nicotinamide phosphoribosyltransferase regulates cell survival through NAD+ synthesis in cardiac myocytes. Circ Res 105:481–491. doi:10.1161/CIRCRESAHA.109.203703
    • (2009) Circ Res , vol.105 , pp. 481-491
    • Hsu, C.P.1    Oka, S.2    Shao, D.3    Hariharan, N.4    Sadoshima, J.5
  • 22
    • 84893843597 scopus 로고    scopus 로고
    • Metabolomic changes in Caenorhabditis elegans lifespan mutants as evident from GC-EI-MS and GC-APCI-TOF-MS profiling
    • COI: 1:CAS:528:DC%2BC2cXivVektLo%3D
    • Jaeger C, Tellström V, Zurek G, König S, Eimer S, Kammerer B (2014) Metabolomic changes in Caenorhabditis elegans lifespan mutants as evident from GC-EI-MS and GC-APCI-TOF-MS profiling. Metabolomics 10:859–876. doi:10.1007/s11306-014-0637-y
    • (2014) Metabolomics , vol.10 , pp. 859-876
    • Jaeger, C.1    Tellström, V.2    Zurek, G.3    König, S.4    Eimer, S.5    Kammerer, B.6
  • 25
    • 25444458591 scopus 로고    scopus 로고
    • Preferable anesthetic conditions for echocardiographic determination of murine cardiac function
    • COI: 1:CAS:528:DC%2BD2MXhtVOqsrvM, PID: 16177543
    • Kawahara Y, Tanonaka K, Daicho T, Nawa M, Oikawa R, Nasa Y, Takeo S (2005) Preferable anesthetic conditions for echocardiographic determination of murine cardiac function. J Pharmacol Sci 99:95–104. doi:10.1254/jphs.FP0050343
    • (2005) J Pharmacol Sci , vol.99 , pp. 95-104
    • Kawahara, Y.1    Tanonaka, K.2    Daicho, T.3    Nawa, M.4    Oikawa, R.5    Nasa, Y.6    Takeo, S.7
  • 26
    • 0842307483 scopus 로고    scopus 로고
    • The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
    • COI: 1:CAS:528:DC%2BD2cXntFWitQ%3D%3D, PID: 14749836
    • Kokoszka JE, Waymire KG, Levy SE, Sligh JE, Cai J, Jones DP, MacGregor GR, Wallace DC (2004) The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore. Nature 427:461–465. doi:10.1038/nature02229
    • (2004) Nature , vol.427 , pp. 461-465
    • Kokoszka, J.E.1    Waymire, K.G.2    Levy, S.E.3    Sligh, J.E.4    Cai, J.5    Jones, D.P.6    MacGregor, G.R.7    Wallace, D.C.8
  • 27
    • 0025374115 scopus 로고
    • An acyl-coenzyme A dehydrogenase assay utilizing the ferricenium ion
    • COI: 1:CAS:528:DyaK3cXitlWlsbY%3D, PID: 2363500
    • Lehman TC, Hale DE, Bhala A, Thorpe C (1990) An acyl-coenzyme A dehydrogenase assay utilizing the ferricenium ion. Anal Biochem 186:280–284
    • (1990) Anal Biochem , vol.186 , pp. 280-284
    • Lehman, T.C.1    Hale, D.E.2    Bhala, A.3    Thorpe, C.4
  • 29
    • 84922031813 scopus 로고    scopus 로고
    • Prolonged fasting identifies heat shock protein 10 as a Sirtuin 3 substrate: elucidating a new mechanism linking mitochondrial protein acetylation to fatty acid oxidation enzyme folding and function
    • COI: 1:CAS:528:DC%2BC2MXhsVCqtL0%3D, PID: 25505263
    • Lu Z, Chen Y, Aponte AM, Battaglia V, Gucek M, Sack MN (2015) Prolonged fasting identifies heat shock protein 10 as a Sirtuin 3 substrate: elucidating a new mechanism linking mitochondrial protein acetylation to fatty acid oxidation enzyme folding and function. J Biol Chem 290:2466–2476. doi:10.1074/jbc.M114.606228
    • (2015) J Biol Chem , vol.290 , pp. 2466-2476
    • Lu, Z.1    Chen, Y.2    Aponte, A.M.3    Battaglia, V.4    Gucek, M.5    Sack, M.N.6
  • 30
    • 0038308820 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in heart failure
    • (author reply 2299)
    • Marin-Garcia J (2003) Mitochondrial dysfunction in heart failure. J Am Coll Cardiol 41:229. doi:10.1016/S0735-1097(03)00494-7(author reply 2299)
    • (2003) J Am Coll Cardiol , vol.41 , pp. 229
    • Marin-Garcia, J.1
  • 31
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: insights into their biological function
    • COI: 1:CAS:528:DC%2BD2sXks1ansr4%3D, PID: 17447894
    • Michan S, Sinclair D (2007) Sirtuins in mammals: insights into their biological function. Biochem J 404:1–13. doi:10.1042/BJ20070140
    • (2007) Biochem J , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 32
    • 42749085693 scopus 로고    scopus 로고
    • Increased mitochondrial uncoupling proteins, respiratory uncoupling and decreased efficiency in the chronically infarcted rat heart
    • COI: 1:CAS:528:DC%2BD1cXmsVOqsL8%3D, PID: 18328500
    • Murray AJ, Cole MA, Lygate CA, Carr CA, Stuckey DJ, Little SE, Neubauer S, Clarke K (2008) Increased mitochondrial uncoupling proteins, respiratory uncoupling and decreased efficiency in the chronically infarcted rat heart. J Mol Cell Cardiol 44:694–700. doi:10.1016/j.yjmcc.2008.01.008
    • (2008) J Mol Cell Cardiol , vol.44 , pp. 694-700
    • Murray, A.J.1    Cole, M.A.2    Lygate, C.A.3    Carr, C.A.4    Stuckey, D.J.5    Little, S.E.6    Neubauer, S.7    Clarke, K.8
  • 33
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • COI: 1:CAS:528:DC%2BD1MXlvFamsL8%3D, PID: 19410549
    • Nakagawa T, Lomb DJ, Haigis MC, Guarente L (2009) SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137:560–570. doi:10.1016/j.cell.2009.02.026
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.J.2    Haigis, M.C.3    Guarente, L.4
  • 34
    • 78651386544 scopus 로고    scopus 로고
    • Adenine nucleotide translocase 1 deficiency results in dilated cardiomyopathy with defects in myocardial mechanics, histopathological alterations, and activation of apoptosis
    • PID: 21232697
    • Narula N, Zaragoza MV, Sengupta PP, Li P, Haider N, Verjans J, Waymire K, Vannan M, Wallace DC (2011) Adenine nucleotide translocase 1 deficiency results in dilated cardiomyopathy with defects in myocardial mechanics, histopathological alterations, and activation of apoptosis. JACC Cardiovasc Imaging 4:1–10. doi:10.1016/j.jcmg.2010.06.018
    • (2011) JACC Cardiovasc Imaging , vol.4 , pp. 1-10
    • Narula, N.1    Zaragoza, M.V.2    Sengupta, P.P.3    Li, P.4    Haider, N.5    Verjans, J.6    Waymire, K.7    Vannan, M.8    Wallace, D.C.9
  • 35
    • 84878396502 scopus 로고    scopus 로고
    • Myocardial energetics in heart failure
    • PID: 23740216
    • Nickel A, Loffler J, Maack C (2013) Myocardial energetics in heart failure. Basic Res Cardiol 108:358. doi:10.1007/s00395-013-0358-9
    • (2013) Basic Res Cardiol , vol.108 , pp. 358
    • Nickel, A.1    Loffler, J.2    Maack, C.3
  • 36
    • 2942564591 scopus 로고    scopus 로고
    • Sirtuins: Sir2-related NAD-dependent protein deacetylases
    • PID: 15128440
    • North BJ, Verdin E (2004) Sirtuins: Sir2-related NAD-dependent protein deacetylases. Genome Biol 5:224. doi:10.1186/gb-2004-5-5-224
    • (2004) Genome Biol , vol.5 , pp. 224
    • North, B.J.1    Verdin, E.2
  • 37
    • 0037019589 scopus 로고    scopus 로고
    • Pharmacologic inhibition of poly(adenosine diphosphate-ribose) polymerase may represent a novel therapeutic approach in chronic heart failure
    • COI: 1:CAS:528:DC%2BD38Xns1Omsbw%3D, PID: 12225730
    • Pacher P, Liaudet L, Mabley J, Komjati K, Szabo C (2002) Pharmacologic inhibition of poly(adenosine diphosphate-ribose) polymerase may represent a novel therapeutic approach in chronic heart failure. J Am Coll Cardiol 40:1006–1016. doi:10.1016/S0735-1097(02)02062-4
    • (2002) J Am Coll Cardiol , vol.40 , pp. 1006-1016
    • Pacher, P.1    Liaudet, L.2    Mabley, J.3    Komjati, K.4    Szabo, C.5
  • 38
    • 84861415338 scopus 로고    scopus 로고
    • Direct renin inhibition exerts an anti-hypertrophic effect associated with improved mitochondrial function in post-infarction heart failure in diabetic rats
    • COI: 1:CAS:528:DC%2BC38XnslKns7s%3D, PID: 22613984
    • Parodi-Rullan R, Barreto-Torres G, Ruiz L, Casasnovas J, Javadov S (2012) Direct renin inhibition exerts an anti-hypertrophic effect associated with improved mitochondrial function in post-infarction heart failure in diabetic rats. Cell Physiol Biochem 29:841–850. doi:10.1159/000178526
    • (2012) Cell Physiol Biochem , vol.29 , pp. 841-850
    • Parodi-Rullan, R.1    Barreto-Torres, G.2    Ruiz, L.3    Casasnovas, J.4    Javadov, S.5
  • 40
    • 30044443515 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1-dependent cardiac myocyte cell death during heart failure is mediated by NAD+ depletion and reduced Sir2alpha deacetylase activity
    • COI: 1:CAS:528:DC%2BD2MXhtlCmsbzJ, PID: 16207712
    • Pillai JB, Isbatan A, Imai S, Gupta MP (2005) Poly(ADP-ribose) polymerase-1-dependent cardiac myocyte cell death during heart failure is mediated by NAD+ depletion and reduced Sir2alpha deacetylase activity. J Biol Chem 280:43121–43130. doi:10.1074/jbc.M506162200
    • (2005) J Biol Chem , vol.280 , pp. 43121-43130
    • Pillai, J.B.1    Isbatan, A.2    Imai, S.3    Gupta, M.P.4
  • 43
    • 50149103440 scopus 로고    scopus 로고
    • Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
    • COI: 1:CAS:528:DC%2BD1cXhtVKisb7I, PID: 18680753
    • Schlicker C, Gertz M, Papatheodorou P, Kachholz B, Becker CF, Steegborn C (2008) Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. J Mol Biol 382:790–801. doi:10.1016/j.jmb.2008.07.048
    • (2008) J Mol Biol , vol.382 , pp. 790-801
    • Schlicker, C.1    Gertz, M.2    Papatheodorou, P.3    Kachholz, B.4    Becker, C.F.5    Steegborn, C.6
  • 44
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • COI: 1:CAS:528:DC%2BD2MXivV2kt7s%3D, PID: 15653680
    • Shi T, Wang F, Stieren E, Tong Q (2005) SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J Biol Chem 280:13560–13567. doi:10.1074/jbc.M414670200
    • (2005) J Biol Chem , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 45
    • 84920157343 scopus 로고    scopus 로고
    • O-GlcNAc signaling in cancer metabolism and epigenetics
    • COI: 1:CAS:528:DC%2BC2cXotVaqsbo%3D, PID: 24769077
    • Singh JP, Zhang K, Wu J, Yang X (2015) O-GlcNAc signaling in cancer metabolism and epigenetics. Cancer Lett 356:244–250. doi:10.1016/j.canlet.2014.04.014
    • (2015) Cancer Lett , vol.356 , pp. 244-250
    • Singh, J.P.1    Zhang, K.2    Wu, J.3    Yang, X.4
  • 46
    • 21244492310 scopus 로고    scopus 로고
    • Myocardial substrate metabolism in the normal and failing heart
    • COI: 1:CAS:528:DC%2BD2MXmsFylsr0%3D, PID: 15987803
    • Stanley WC, Recchia FA, Lopaschuk GD (2005) Myocardial substrate metabolism in the normal and failing heart. Physiol Rev 85:1093–1129. doi:10.1152/physrev.00006.2004
    • (2005) Physiol Rev , vol.85 , pp. 1093-1129
    • Stanley, W.C.1    Recchia, F.A.2    Lopaschuk, G.D.3
  • 47
    • 0026718789 scopus 로고
    • Differential expression of adenine nucleotide translocator isoforms in mammalian tissues and during muscle cell differentiation
    • COI: 1:CAS:528:DyaK38Xlt1ymuro%3D, PID: 1378836
    • Stepien G, Torroni A, Chung AB, Hodge JA, Wallace DC (1992) Differential expression of adenine nucleotide translocator isoforms in mammalian tissues and during muscle cell differentiation. J Biol Chem 267:14592–14597
    • (1992) J Biol Chem , vol.267 , pp. 14592-14597
    • Stepien, G.1    Torroni, A.2    Chung, A.B.3    Hodge, J.A.4    Wallace, D.C.5
  • 48
    • 70349208608 scopus 로고    scopus 로고
    • Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice
    • COI: 1:CAS:528:DC%2BD1MXhtFWgs7%2FN, PID: 19652361
    • Sundaresan NR, Gupta M, Kim G, Rajamohan SB, Isbatan A, Gupta MP (2009) Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. J Clin Invest. 119:2758–2771. doi:10.1172/JCI39162
    • (2009) J Clin Invest. , vol.119 , pp. 2758-2771
    • Sundaresan, N.R.1    Gupta, M.2    Kim, G.3    Rajamohan, S.B.4    Isbatan, A.5    Gupta, M.P.6
  • 49
    • 53549105529 scopus 로고    scopus 로고
    • SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70
    • COI: 1:CAS:528:DC%2BD1cXht1Cit7fE, PID: 18710944
    • Sundaresan NR, Samant SA, Pillai VB, Rajamohan SB, Gupta MP (2008) SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70. Mol Cell Biol 28:6384–6401. doi:10.1128/MCB.00426-08
    • (2008) Mol Cell Biol , vol.28 , pp. 6384-6401
    • Sundaresan, N.R.1    Samant, S.A.2    Pillai, V.B.3    Rajamohan, S.B.4    Gupta, M.P.5
  • 50
    • 0037109183 scopus 로고    scopus 로고
    • Switching metabolic genes to build a better heart
    • PID: 12379570
    • Taegtmeyer H (2002) Switching metabolic genes to build a better heart. Circulation 106:2043–2045. doi:10.1161/01.CIR.0000036760.42319.3F
    • (2002) Circulation , vol.106 , pp. 2043-2045
    • Taegtmeyer, H.1
  • 51
    • 84861338375 scopus 로고    scopus 로고
    • Emerging beneficial roles of sirtuins in heart failure
    • PID: 22622703
    • Tanno M, Kuno A, Horio Y, Miura T (2012) Emerging beneficial roles of sirtuins in heart failure. Basic Res Cardiol 107:273. doi:10.1007/s00395-012-0273-5
    • (2012) Basic Res Cardiol , vol.107 , pp. 273
    • Tanno, M.1    Kuno, A.2    Horio, Y.3    Miura, T.4
  • 54
    • 14344266084 scopus 로고    scopus 로고
    • Poly(ADP-Ribose) polymerase promotes cardiac remodeling, contractile failure, and translocation of apoptosis-inducing factor in a murine experimental model of aortic banding and heart failure
    • COI: 1:CAS:528:DC%2BD2MXitVOhtbg%3D, PID: 15523000
    • Xiao CY, Chen M, Zsengeller Z, Li H, Kiss L, Kollai M, Szabo C (2005) Poly(ADP-Ribose) polymerase promotes cardiac remodeling, contractile failure, and translocation of apoptosis-inducing factor in a murine experimental model of aortic banding and heart failure. J Pharmacol Exp Ther 312:891–898. doi:10.1124/jpet.104.077164
    • (2005) J Pharmacol Exp Ther , vol.312 , pp. 891-898
    • Xiao, C.Y.1    Chen, M.2    Zsengeller, Z.3    Li, H.4    Kiss, L.5    Kollai, M.6    Szabo, C.7
  • 55
    • 61649089277 scopus 로고    scopus 로고
    • Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli
    • COI: 1:CAS:528:DC%2BD1MXitV2lu7o%3D, PID: 18723842
    • Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009) Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics 8:215–225. doi:10.1074/mcp.M800187-MCP200
    • (2009) Mol Cell Proteomics , vol.8 , pp. 215-225
    • Zhang, J.1    Sprung, R.2    Pei, J.3    Tan, X.4    Kim, S.5    Zhu, H.6    Liu, C.F.7    Grishin, N.V.8    Zhao, Y.9


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