메뉴 건너뛰기




Volumn 5 JUL, Issue , 2014, Pages

Metabolism leaves its mark on the powerhouse: Recent progress in post-translational modifications of lysine in mitochondria

Author keywords

Acetylation; Butyrylation; Crotonylation; Glutarylation; Heart; Malonylation; Propionylation; Sirt3; Sirt5; Sirtuin; Succinylation

Indexed keywords

CYCLOPHILIN D; DICARBOXYLIC ACID; LYSINE; MANGANESE SUPEROXIDE DISMUTASE; MITOCHONDRIAL PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; PYRUVATE DEHYDROGENASE COMPLEX; SIRTUIN 3; SIRTUIN 4; SIRTUIN 5; SUCCINATE DEHYDROGENASE (UBIQUINONE);

EID: 84907327882     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00301     Document Type: Review
Times cited : (74)

References (134)
  • 2
    • 84892575903 scopus 로고    scopus 로고
    • Redox regulation of mitochondrial function with emphasis on cysteine oxidation reactions
    • Mailloux, R. J., Jin, X., and Willmore, W. G. (2014) Redox regulation of mitochondrial function with emphasis on cysteine oxidation reactions. Redox Biology 2, 123-139
    • (2014) Redox Biology , vol.2 , pp. 123-139
    • Mailloux, R.J.1    Jin, X.2    Willmore, W.G.3
  • 3
    • 81955165133 scopus 로고    scopus 로고
    • Mitochondrial protein phosphorylation as a regulatory modality: implications for mitochondrial dysfunction in heart failure
    • (Greenwich, Conn.)
    • O'Rourke, B., Van Eyk, J. E., and Foster, D. B. (2011) Mitochondrial protein phosphorylation as a regulatory modality: implications for mitochondrial dysfunction in heart failure. Congestive heart failure (Greenwich, Conn.) 17, 269-282
    • (2011) Congestive heart failure , vol.17 , pp. 269-282
    • O'Rourke, B.1    Van Eyk, J.E.2    Foster, D.B.3
  • 4
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey, V., Faulkner, R., and Mirsky, A. E. (1964) Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proceedings of the National Academy of Sciences, U. S. A. 51, 786-794
    • (1964) Proceedings of the National Academy of Sciences, U.S.A. , vol.51 , pp. 786-794
    • Allfrey, V.1    Faulkner, R.2    Mirsky, A.E.3
  • 5
    • 0014409959 scopus 로고
    • Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone.
    • Gershey, E. L., Vidali, G., and Allfrey, V. G. (1968) Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone. The Journal of biological chemistry 243, 5018-5022
    • (1968) The Journal of biological chemistry , vol.243 , pp. 5018-5022
    • Gershey, E.L.1    Vidali, G.2    Allfrey, V.G.3
  • 10
    • 84873343462 scopus 로고    scopus 로고
    • Comprehensive profiling of protein lysine acetylation in Escherichia coli
    • Zhang, K., Zheng, S., Yang, J. S., Chen, Y., and Cheng, Z. (2013) Comprehensive profiling of protein lysine acetylation in Escherichia coli. Journal of proteome research 12, 844-851
    • (2013) Journal of proteome research , vol.12 , pp. 844-851
    • Zhang, K.1    Zheng, S.2    Yang, J.S.3    Chen, Y.4    Cheng, Z.5
  • 11
    • 3242788065 scopus 로고    scopus 로고
    • Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica
    • Starai, V. J., and Escalante-Semerena, J. C. (2004) Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica. Journal of molecular biology 340, 1005-1012
    • (2004) Journal of molecular biology , vol.340 , pp. 1005-1012
    • Starai, V.J.1    Escalante-Semerena, J.C.2
  • 12
    • 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., and Escalante-Semerena, J. C. (2002) Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 298, 2390-2392
    • (2002) Science , vol.298 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 15
    • 84878629096 scopus 로고    scopus 로고
    • The acetylproteome of Gram-positive model bacterium Bacillus subtilis
    • Kim, D., Yu, B. J., Kim, J. A., Lee, Y. J., Choi, S. G., Kang, S., and Pan, J. G. (2013) The acetylproteome of Gram-positive model bacterium Bacillus subtilis. Proteomics 13, 1726-1736
    • (2013) Proteomics , vol.13 , pp. 1726-1736
    • Kim, D.1    Yu, B.J.2    Kim, J.A.3    Lee, Y.J.4    Choi, S.G.5    Kang, S.6    Pan, J.G.7
  • 17
    • 79954582107 scopus 로고    scopus 로고
    • Control of protein function by reversible Nvarepsilon-lysine acetylation in bacteria
    • Thao, S., and Escalante-Semerena, J. C. (2011) Control of protein function by reversible Nvarepsilon-lysine acetylation in bacteria. Current opinion in microbiology 14, 200-204
    • (2011) Current opinion in microbiology , vol.14 , pp. 200-204
    • Thao, S.1    Escalante-Semerena, J.C.2
  • 20
    • 84885155285 scopus 로고    scopus 로고
    • Widespread and enzyme-independent Nepsilon-acetylation and Nepsilon-succinylation of proteins in the chemical conditions of the mitochondrial matrix
    • Wagner, G. R., and Payne, R. M. (2013) Widespread and enzyme-independent Nepsilon-acetylation and Nepsilon-succinylation of proteins in the chemical conditions of the mitochondrial matrix. The Journal of biological chemistry 288, 29036-29045
    • (2013) The Journal of biological chemistry , vol.288 , pp. 29036-29045
    • Wagner, G.R.1    Payne, R.M.2
  • 21
    • 84871107379 scopus 로고    scopus 로고
    • Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease
    • Newman, J. C., He, W., and Verdin, E. (2012) Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease. The Journal of biological chemistry 287, 42436-42443
    • (2012) The Journal of biological chemistry , vol.287 , pp. 42436-42443
    • Newman, J.C.1    He, W.2    Verdin, E.3
  • 22
    • 84860192261 scopus 로고    scopus 로고
    • Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1
    • Scott, I., Webster, B. R., Li, J. H., and Sack, M. N. (2012) Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1. The Biochemical journal 443, 655-661
    • (2012) The Biochemical journal , vol.443 , pp. 655-661
    • Scott, I.1    Webster, B.R.2    Li, J.H.3    Sack, M.N.4
  • 23
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins--emerging roles in physiology, aging, and calorie restriction
    • Haigis, M. C., and Guarente, L. P. (2006) Mammalian sirtuins--emerging roles in physiology, aging, and calorie restriction. Genes & development 20, 2913-2921
    • (2006) Genes & development , vol.20 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 24
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • Schwer, B., North, B. J., Frye, R. A., Ott, M., and Verdin, E. (2002) The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. The Journal of cell biology 158, 647-657
    • (2002) The Journal of cell biology , vol.158 , pp. 647-657
    • Schwer, B.1    North, B.J.2    Frye, R.A.3    Ott, M.4    Verdin, E.5
  • 25
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., and Horikawa, I. (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Molecular biology of the cell 16, 4623-4635
    • (2005) Molecular biology of the cell , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 26
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi, T., Wang, F., Stieren, E., and Tong, Q. (2005) SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. The Journal of biological chemistry 280, 13560-13567
    • (2005) The Journal of biological chemistry , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 31
    • 65249091951 scopus 로고    scopus 로고
    • Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogues and 32P-NAD
    • Du, J., Jiang, H., and Lin, H. (2009) Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogues and 32P-NAD. Biochemistry 48, 2878-2890
    • (2009) Biochemistry , vol.48 , pp. 2878-2890
    • Du, J.1    Jiang, H.2    Lin, H.3
  • 50
    • 79959906869 scopus 로고    scopus 로고
    • Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase
    • Jiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., Xiong, Y., Guan, K. L., and Zhao, S. (2011) Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase. Molecular cell 43, 33-44
    • (2011) Molecular cell , vol.43 , pp. 33-44
    • Jiang, W.1    Wang, S.2    Xiao, M.3    Lin, Y.4    Zhou, L.5    Lei, Q.6    Xiong, Y.7    Guan, K.L.8    Zhao, S.9
  • 55
    • 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., and Gupta, M. P. (2009) Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. The Journal of clinical investigation 119, 2758-2771
    • (2009) The Journal of clinical investigation , 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
  • 56
    • 79952266729 scopus 로고    scopus 로고
    • Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy
    • Hafner, A. V., Dai, J., Gomes, A. P., Xiao, C. Y., Palmeira, C. M., Rosenzweig, A., and Sinclair, D. A. (2010) Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy. Aging 2, 914-923
    • (2010) Aging , 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
  • 57
    • 78651468722 scopus 로고    scopus 로고
    • Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction
    • Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., and Prolla, T. A. (2010) Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction. Cell 143, 802-812
    • (2010) Cell , vol.143 , pp. 802-812
    • Someya, S.1    Yu, W.2    Hallows, W.C.3    Xu, J.4    Vann, J.M.5    Leeuwenburgh, C.6    Tanokura, M.7    Denu, J.M.8    Prolla, T.A.9
  • 58
    • 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
    • Sundaresan, N. R., Samant, S. A., Pillai, V. B., Rajamohan, S. B., and Gupta, M. P. (2008) SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70. Molecular and cellular biology 28, 6384-6401
    • (2008) Molecular and cellular biology , 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
  • 62
    • 78649521247 scopus 로고    scopus 로고
    • Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
    • Qiu, X., Brown, K., Hirschey, M. D., Verdin, E., and Chen, D. (2010) Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell metabolism 12, 662-667
    • (2010) Cell metabolism , vol.12 , pp. 662-667
    • Qiu, X.1    Brown, K.2    Hirschey, M.D.3    Verdin, E.4    Chen, D.5
  • 63
    • 79957979314 scopus 로고    scopus 로고
    • Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
    • Chen, Y., Zhang, J., Lin, Y., Lei, Q., Guan, K. L., Zhao, S., and Xiong, Y. (2011) Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS. EMBO reports 12, 534-541
    • (2011) EMBO reports , vol.12 , pp. 534-541
    • Chen, Y.1    Zhang, J.2    Lin, Y.3    Lei, Q.4    Guan, K.L.5    Zhao, S.6    Xiong, Y.7
  • 66
    • 79551470041 scopus 로고    scopus 로고
    • Lysine deacetylation in ischaemic preconditioning: the role of SIRT1
    • Nadtochiy, S. M., Redman, E., Rahman, I., and Brookes, P. S. (2011) Lysine deacetylation in ischaemic preconditioning: the role of SIRT1. Cardiovascular research 89, 643-649
    • (2011) Cardiovascular research , vol.89 , pp. 643-649
    • Nadtochiy, S.M.1    Redman, E.2    Rahman, I.3    Brookes, P.S.4
  • 68
    • 84870907221 scopus 로고    scopus 로고
    • Metabolic inflexibility and protein lysine acetylation in heart mitochondria of a chronic model of type 1 diabetes
    • Vadvalkar, S. S., Baily, C. N., Matsuzaki, S., West, M., Tesiram, Y. A., and Humphries, K. M. (2013) Metabolic inflexibility and protein lysine acetylation in heart mitochondria of a chronic model of type 1 diabetes. The Biochemical journal 449, 253-261
    • (2013) The Biochemical journal , vol.449 , pp. 253-261
    • Vadvalkar, S.S.1    Baily, C.N.2    Matsuzaki, S.3    West, M.4    Tesiram, Y.A.5    Humphries, K.M.6
  • 69
    • 84872308934 scopus 로고    scopus 로고
    • SIRT3 protects cardiomyocytes from oxidative stress-mediated cell death by activating NF-kappaB
    • Chen, C. J., Fu, Y. C., Yu, W., and Wang, W. (2013) SIRT3 protects cardiomyocytes from oxidative stress-mediated cell death by activating NF-kappaB. Biochemical and biophysical research communications 430, 798-803
    • (2013) Biochemical and biophysical research communications , vol.430 , pp. 798-803
    • Chen, C.J.1    Fu, Y.C.2    Yu, W.3    Wang, W.4
  • 70
    • 71549116704 scopus 로고    scopus 로고
    • Mitochondria in the elderly: Is acetylcarnitine a rejuvenator?
    • Rosca, M. G., Lemieux, H., and Hoppel, C. L. (2009) Mitochondria in the elderly: Is acetylcarnitine a rejuvenator? Advanced drug delivery reviews 61, 1332-1342
    • (2009) Advanced drug delivery reviews , vol.61 , pp. 1332-1342
    • Rosca, M.G.1    Lemieux, H.2    Hoppel, C.L.3
  • 71
    • 77951176793 scopus 로고    scopus 로고
    • Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria
    • Shulga, N., Wilson-Smith, R., and Pastorino, J. G. (2010) Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria. Journal of cell science 123, 894-902
    • (2010) Journal of cell science , vol.123 , pp. 894-902
    • Shulga, N.1    Wilson-Smith, R.2    Pastorino, J.G.3
  • 75
    • 84860003699 scopus 로고    scopus 로고
    • Friedreich's ataxia reveals a mechanism for coordinate regulation of oxidative metabolism via feedback inhibition of the SIRT3 deacetylase
    • Wagner, G. R., Pride, P. M., Babbey, C. M., and Payne, R. M. (2012) Friedreich's ataxia reveals a mechanism for coordinate regulation of oxidative metabolism via feedback inhibition of the SIRT3 deacetylase. Human molecular genetics 21, 2688-2697
    • (2012) Human molecular genetics , vol.21 , pp. 2688-2697
    • Wagner, G.R.1    Pride, P.M.2    Babbey, C.M.3    Payne, R.M.4
  • 77
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio, H., Simon, D., Cossee, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P., and Koenig, M. (2001) Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nature genetics 27, 181-186
    • (2001) Nature genetics , vol.27 , pp. 181-186
    • Puccio, H.1    Simon, D.2    Cossee, M.3    Criqui-Filipe, P.4    Tiziano, F.5    Melki, J.6    Hindelang, C.7    Matyas, R.8    Rustin, P.9    Koenig, M.10
  • 79
    • 78650516004 scopus 로고    scopus 로고
    • Identification of lysine succinylation as a new post-translational modification
    • Zhang, Z., Tan, M., Xie, Z., Dai, L., Chen, Y., and Zhao, Y. (2011) Identification of lysine succinylation as a new post-translational modification. Nature chemical biology 7, 58-63
    • (2011) Nature chemical biology , vol.7 , pp. 58-63
    • Zhang, Z.1    Tan, M.2    Xie, Z.3    Dai, L.4    Chen, Y.5    Zhao, Y.6
  • 81
    • 84883307077 scopus 로고    scopus 로고
    • Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation
    • Weinert, B. T., Scholz, C., Wagner, S. A., Iesmantavicius, V., Su, D., Daniel, J. A., and Choudhary, C. (2013) Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell reports 4, 842-851
    • (2013) Cell reports , vol.4 , pp. 842-851
    • Weinert, B.T.1    Scholz, C.2    Wagner, S.A.3    Iesmantavicius, V.4    Su, D.5    Daniel, J.A.6    Choudhary, C.7
  • 82
    • 1542298916 scopus 로고    scopus 로고
    • Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli
    • Zhao, K., Chai, X., and Marmorstein, R. (2004) Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli. Journal of molecular biology 337, 731-741
    • (2004) Journal of molecular biology , vol.337 , pp. 731-741
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3
  • 87
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • Nakagawa, T., Lomb, D. J., Haigis, M. C., and Guarente, L. (2009) SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137, 560-570
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.J.2    Haigis, M.C.3    Guarente, L.4
  • 93
    • 84884473738 scopus 로고    scopus 로고
    • Ethanol metabolism modifies hepatic protein acylation in mice
    • Fritz, K. S., Green, M. F., Petersen, D. R., and Hirschey, M. D. (2013) Ethanol metabolism modifies hepatic protein acylation in mice. PloS one 8, e75868
    • (2013) PloS one , vol.8
    • Fritz, K.S.1    Green, M.F.2    Petersen, D.R.3    Hirschey, M.D.4
  • 96
    • 84861530755 scopus 로고    scopus 로고
    • Proteomic analysis of mitochondrial proteins in cardiomyocytes from rats subjected to intermittent hypoxia
    • Zhu, W. Z., Wu, X. F., Zhang, Y., and Zhou, Z. N. (2012) Proteomic analysis of mitochondrial proteins in cardiomyocytes from rats subjected to intermittent hypoxia. European journal of applied physiology 112, 1037-1046
    • (2012) European journal of applied physiology , vol.112 , pp. 1037-1046
    • Zhu, W.Z.1    Wu, X.F.2    Zhang, Y.3    Zhou, Z.N.4
  • 98
    • 84907331239 scopus 로고
    • The degradation of l-lysine in guinea pig liver homogenate; formation of alpha-aminoadipic acid
    • Borsook, H., Deasy, C. L., and et al. (1948) The degradation of l-lysine in guinea pig liver homogenate; formation of alpha-aminoadipic acid. The Journal of biological chemistry 176, 1383-1393
    • (1948) The Journal of biological chemistry , vol.176 , pp. 1383-1393
    • Borsook, H.1    Deasy, C.L.2
  • 99
    • 84907338246 scopus 로고
    • The degradation of alpha-aminoadipic acid in guinea pig liver homogenate
    • Borsook, H., Deasy, C. L., and et al. (1948) The degradation of alpha-aminoadipic acid in guinea pig liver homogenate. The Journal of biological chemistry 176, 1395-1400
    • (1948) The Journal of biological chemistry , vol.176 , pp. 1395-1400
    • Borsook, H.1    Deasy, C.L.2
  • 103
    • 0040820804 scopus 로고
    • Studies on the fatty acid oxidizing system of animal tissues. III. Butyryl coenzyme A dehydrogenase.
    • Green, D. E., Mii, S., Mahler, H. R., and Bock, R. M. (1954) Studies on the fatty acid oxidizing system of animal tissues. III. Butyryl coenzyme A dehydrogenase. The Journal of biological chemistry 206, 1-12
    • (1954) The Journal of biological chemistry , vol.206 , pp. 1-12
    • Green, D.E.1    Mii, S.2    Mahler, H.R.3    Bock, R.M.4
  • 104
    • 0022980720 scopus 로고
    • The purification and characterization of glutaryl-coenzyme A dehydrogenase from porcine and human liver
    • Lenich, A. C., and Goodman, S. I. (1986) The purification and characterization of glutaryl-coenzyme A dehydrogenase from porcine and human liver. The Journal of biological chemistry 261, 4090-4096
    • (1986) The Journal of biological chemistry , vol.261 , pp. 4090-4096
    • Lenich, A.C.1    Goodman, S.I.2
  • 105
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer, R. K., Jungermann, K., and Decker, K. (1977) Energy conservation in chemotrophic anaerobic bacteria. Bacteriological reviews 41, 100-180
    • (1977) Bacteriological reviews , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 110
    • 70450277232 scopus 로고    scopus 로고
    • Identification and characterization of propionylation at histone H3 lysine 23 in mammalian cells
    • Liu, B., Lin, Y., Darwanto, A., Song, X., Xu, G., and Zhang, K. (2009) Identification and characterization of propionylation at histone H3 lysine 23 in mammalian cells. The Journal of biological chemistry 284, 32288-32295
    • (2009) The Journal of biological chemistry , vol.284 , pp. 32288-32295
    • Liu, B.1    Lin, Y.2    Darwanto, A.3    Song, X.4    Xu, G.5    Zhang, K.6
  • 113
    • 37549067781 scopus 로고    scopus 로고
    • Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases
    • Smith, B. C., and Denu, J. M. (2007) Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases. The Journal of biological chemistry 282, 37256-37265
    • (2007) The Journal of biological chemistry , vol.282 , pp. 37256-37265
    • Smith, B.C.1    Denu, J.M.2
  • 114
    • 84886686038 scopus 로고    scopus 로고
    • Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins
    • Feldman, J. L., Baeza, J., and Denu, J. M. (2013) Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins. The Journal of biological chemistry 288, 31350-31356
    • (2013) The Journal of biological chemistry , vol.288 , pp. 31350-31356
    • Feldman, J.L.1    Baeza, J.2    Denu, J.M.3
  • 115
    • 84861665777 scopus 로고    scopus 로고
    • Identification of combinatorial patterns of post-translational modifications on individual histones in the mouse brain
    • Tweedie-Cullen, R. Y., Brunner, A. M., Grossmann, J., Mohanna, S., Sichau, D., Nanni, P., Panse, C., and Mansuy, I. M. (2012) Identification of combinatorial patterns of post-translational modifications on individual histones in the mouse brain. PloS one 7, e36980
    • (2012) PloS one , vol.7
    • Tweedie-Cullen, R.Y.1    Brunner, A.M.2    Grossmann, J.3    Mohanna, S.4    Sichau, D.5    Nanni, P.6    Panse, C.7    Mansuy, I.M.8
  • 117
    • 84862271824 scopus 로고    scopus 로고
    • Substrates for efficient fluorometric screening employing the NAD-dependent sirtuin 5 lysine deacylase (KDAC) enzyme
    • Madsen, A. S., and Olsen, C. A. (2012) Substrates for efficient fluorometric screening employing the NAD-dependent sirtuin 5 lysine deacylase (KDAC) enzyme. Journal of medicinal chemistry 55, 5582-5590
    • (2012) Journal of medicinal chemistry , vol.55 , pp. 5582-5590
    • Madsen, A.S.1    Olsen, C.A.2
  • 118
    • 0029791410 scopus 로고    scopus 로고
    • Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket
    • Engel, C. K., Mathieu, M., Zeelen, J. P., Hiltunen, J. K., and Wierenga, R. K. (1996) Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket. The EMBO journal 15, 5135-5145
    • (1996) The EMBO journal , vol.15 , pp. 5135-5145
    • Engel, C.K.1    Mathieu, M.2    Zeelen, J.P.3    Hiltunen, J.K.4    Wierenga, R.K.5
  • 119
    • 0017350345 scopus 로고
    • Purification and properties of pig heart crotonase and the presence of short chain and long chain enoyl coenzyme A hydratases in pig and guinea pig tissues
    • Fong, J. C., and Schulz, H. (1977) Purification and properties of pig heart crotonase and the presence of short chain and long chain enoyl coenzyme A hydratases in pig and guinea pig tissues. The Journal of biological chemistry 252, 542-547
    • (1977) The Journal of biological chemistry , vol.252 , pp. 542-547
    • Fong, J.C.1    Schulz, H.2
  • 120
    • 0016239547 scopus 로고
    • Long chain enoyl coenzyme A hydratase from pig heart
    • Schulz, H. (1974) Long chain enoyl coenzyme A hydratase from pig heart. The Journal of biological chemistry 249, 2704-2709
    • (1974) The Journal of biological chemistry , vol.249 , pp. 2704-2709
    • Schulz, H.1
  • 121
    • 0015523407 scopus 로고
    • Enoyl coenzyme A hydratase (crotonase). Catalytic properties of crotonase and its possible regulatory role in fatty acid oxidation.
    • Waterson, R. M., and Hill, R. L. (1972) Enoyl coenzyme A hydratase (crotonase). Catalytic properties of crotonase and its possible regulatory role in fatty acid oxidation. The Journal of biological chemistry 247, 5258-5265
    • (1972) The Journal of biological chemistry , vol.247 , pp. 5258-5265
    • Waterson, R.M.1    Hill, R.L.2
  • 123
    • 40949099577 scopus 로고    scopus 로고
    • Genetically encoding N(epsilon)-acetyllysine in recombinant proteins
    • Neumann, H., Peak-Chew, S. Y., and Chin, J. W. (2008) Genetically encoding N(epsilon)-acetyllysine in recombinant proteins. Nature chemical biology 4, 232-234
    • (2008) Nature chemical biology , vol.4 , pp. 232-234
    • Neumann, H.1    Peak-Chew, S.Y.2    Chin, J.W.3
  • 126
    • 80053920774 scopus 로고    scopus 로고
    • Nicotinamide mononucleotide, a key NAD(+) intermediate, treats the pathophysiology of diet- and age-induced diabetes in mice
    • Yoshino, J., Mills, K. F., Yoon, M. J., and Imai, S. (2011) Nicotinamide mononucleotide, a key NAD(+) intermediate, treats the pathophysiology of diet- and age-induced diabetes in mice. Cell metabolism 14, 528-536
    • (2011) Cell metabolism , vol.14 , pp. 528-536
    • Yoshino, J.1    Mills, K.F.2    Yoon, M.J.3    Imai, S.4
  • 127
    • 84859951790 scopus 로고    scopus 로고
    • SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status
    • Yu, W., Dittenhafer-Reed, K. E., and Denu, J. M. (2012) SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status. The Journal of biological chemistry 287, 14078-14086
    • (2012) The Journal of biological chemistry , vol.287 , pp. 14078-14086
    • Yu, W.1    Dittenhafer-Reed, K.E.2    Denu, J.M.3
  • 128
    • 84870880080 scopus 로고    scopus 로고
    • Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3
    • Sol, E. M., Wagner, S. A., Weinert, B. T., Kumar, A., Kim, H. S., Deng, C. X., and Choudhary, C. (2012) Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3. PloS one 7, e50545
    • (2012) PloS one , vol.7
    • Sol, E.M.1    Wagner, S.A.2    Weinert, B.T.3    Kumar, A.4    Kim, H.S.5    Deng, C.X.6    Choudhary, C.7
  • 129
    • 67649395959 scopus 로고    scopus 로고
    • Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals
    • Yu, W., Lin, Y., Yao, J., Huang, W., Lei, Q., Xiong, Y., Zhao, S., and Guan, K. L. (2009) Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals. The Journal of biological chemistry 284, 13669-13675
    • (2009) The Journal of biological chemistry , vol.284 , pp. 13669-13675
    • Yu, W.1    Lin, Y.2    Yao, J.3    Huang, W.4    Lei, Q.5    Xiong, Y.6    Zhao, S.7    Guan, K.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.