SIRT4 is a lysine deacylase that controls leucine metabolism and insulin secretion

Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega

Sievers, F., Wilm, A., Dineen, D., Gibson, T., Karplus, K., Li, W.-Z., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,576 · see citing works

FastTree 2 – Approximately Maximum-Likelihood Trees for Large Alignments

Price, M. N., Dehal, P. S., & Arkin, A. P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009490 · Cited by 14,894 · see citing works

CHARMM: The biomolecular simulation program

Brooks, B. R., Brooks, C. L., MacKerell, A. D., Nilsson, L., Petrella, R. J., Roux, B., Won, Y., Archontis, G., Bartels, C., Boresch, S., et al. (2009) · Journal of Computational Chemistry · doi:10.1002/jcc.21287 · Cited by 8,994 · see citing works

Pfam: the protein families database

Finn, R. D., Bateman, A., Clements, J., Coggill, P., Eberhardt, R. Y., Eddy, S. R., Heger, A., Hetherington, K., Holm, L., Mistry, J., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gkt1223 · Cited by 6,148 · see citing works

Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510 · see citing works

2016 update of the PRIDE database and its related tools

Vizcaíno, J. A., Csordás, A., del‐Toro, N., Dianes, J. A., Griss, J., Lavidas, I., Mayer, G., Pérez‐Riverol, Y., Reisinger, F., Ternent, T., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1145 · Cited by 3,466 · see citing works

A branched-chain amino acid-related metabolic signature that differentiates obese and lean humans and contributes to insulin resistance

Newgard, C. B., An, J., Bain, J. R., Muehlbauer, M. J., Stevens, R. D., Lien, L. F., Haqq, A. M., Shah, S. H., Arlotto, M., Slentz, C. A., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.02.002 · Cited by 3,165 · see citing works

HMDB 3.0—The Human Metabolome Database in 2013

Wishart, D. S., Jewison, T., Guo, A. C., Wilson, M., Knox, C., Liu, Y., Djoumbou-Feunang, Y., Mandal, R., Aziat, F., Dong, E., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1065 · Cited by 2,845 · see citing works

Sirtuins as regulators of metabolism and healthspan

Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works

Protein Structure Modeling with MODELLER

Eswar, N., Eramian, D., Webb, B., Shen, M., & Šali, A. (2008) · Methods in molecular biology · doi:10.1007/978-1-60327-058-8_8 · Cited by 1,781 · see citing works

Genomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6

Mostoslavsky, R., Chua, K. F., Lombard, D. B., Pang, W. W., Fischer, M. R., Gellon, L., Liu, P., Mostoslavsky, G., Franco, S., Murphy, M. M., et al. (2006) · Cell · doi:10.1016/j.cell.2005.11.044 · Cited by 1,637 · see citing works

PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse

Hornbeck, P. V., Kornhauser, J. M., Tkachev, S., Zhang, B., Skrzypek, E., Murray, B. W., Latham, V. M., & Sullivan, M. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1122 · Cited by 1,636 · see citing works

The PredictProtein server

Rost, B., Yachdav, G., & Liu, J. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh377 · Cited by 1,462 · see citing works

Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase

Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429 · see citing works

Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins

Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409 · see citing works

PROMALS3D: a tool for multiple protein sequence and structure alignments

Pei, J., Kim, B., & Grishin, N. V. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn072 · Cited by 1,269 · see citing works

Organelle isolation: functional mitochondria from mouse liver, muscle and cultured filroblasts

Frezza, C., Cipolat, S., & Scorrano, L. (2007) · Nature Protocols · doi:10.1038/nprot.2006.478 · Cited by 1,188 · see citing works

SIRT4 Inhibits Glutamate Dehydrogenase and Opposes the Effects of Calorie Restriction in Pancreatic β Cells

Haigis, M. C., Mostoslavsky, R., Haigis, K. M., Fahie, K., Christodoulou, D. C., Murphy, A. J., Valenzuela, D. M., Yancopoulos, G. D., Karow, M., Blander, G., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.057 · Cited by 1,162 · see citing works

COBALT: constraint-based alignment tool for multiple protein sequences

Papadopoulos, J. S., & Agarwala, R. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm076 · Cited by 1,130 · see citing works

SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin

Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111 · see citing works

Interplay between lipids and branched-chain amino acids in development of insulin resistance

Newgard, C. B. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.01.024 · Cited by 1,080 · see citing works

Lysine glutarylation is a protein posttranslational modification regulated by SIRT5

Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.014 · Cited by 844 · see citing works

2016 update of the PRIDE database and its related tools

Vizcaíno, J. A., Csordás, A., del‐Toro, N., Dianes, J. A., Griss, J., Lavidas, I., Mayer, G., Pérez‐Riverol, Y., Reisinger, F., Ternent, T., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw880 · Cited by 806 · see citing works

Amino Acid Metabolism in Man

Felig, P. (1975) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.44.070175.004441 · Cited by 789 · see citing works

SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle

Nakagawa, T., Lomb, D. J., Haigis, M. C., & Guarente, L. (2009) · Cell · doi:10.1016/j.cell.2009.02.026 · Cited by 787 · see citing works

The first identification of lysine malonylation substrates and its regulatory enzyme

Peng, C., Lu, Z., Xie, Z., Cheng, Z., Chen, Y., Tan, M., Luo, H., Zhang, Y., He, W., Yang, K., et al. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.012658 · Cited by 751 · see citing works

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. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603968103 · Cited by 705 · see citing works

SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine

Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., Du, J., Kim, R., Ge, E., Mostoslavsky, R., et al. (2013) · Nature · doi:10.1038/nature12038 · Cited by 697 · see citing works

Activation of the Protein Deacetylase SIRT6 by Long-chain Fatty Acids and Widespread Deacylation by Mammalian Sirtuins

Feldman, J. L., Baeza, J., & Denu, J. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.511261 · Cited by 637 · cited 7× · see citing works

Performance comparison of generalized born and Poisson methods in the calculation of electrostatic solvation energies for protein structures

Feig, M., Onufriev, A. V., Lee, M. S., Im, W., Case, D. A., & Brooks, C. L. (2003) · Journal of Computational Chemistry · doi:10.1002/jcc.10378 · Cited by 628 · see citing works

The mTORC1 Pathway Stimulates Glutamine Metabolism and Cell Proliferation by Repressing SIRT4

Csibi, A., Fendt, S.-M., Li, C., Poulogiannis, G., Choo, A. Y., Chapski, D. J., Jeong, S. M., Dempsey, J. M., Parkhitko, A., Morrison, T., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.023 · Cited by 586 · see citing works

Branched-chain amino acid supplementation promotes survival and supports cardiac and skeletal muscle mitochondrial biogenesis in middle-aged mice

D'Antona, G., Ragni, M., Cardile, A., Tedesco, L., Dossena, M., Bruttini, F., Caliaro, F., Corsetti, G., Bottinelli, R., Carruba, M. O., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.08.016 · Cited by 568 · see citing works

Widespread and Enzyme-independent Nϵ-Acetylation and Nϵ-Succinylation of Proteins in the Chemical Conditions of the Mitochondrial Matrix*

Wagner, G. R., & Payne, R. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.486753 · Cited by 490 · see citing works

Association of a Peripheral Blood Metabolic Profile With Coronary Artery Disease and Risk of Subsequent Cardiovascular Events

Shah, S. H., Bain, J. R., Muehlbauer, M. J., Stevens, R. D., Crosslin, D. R., Haynes, C. S., Dungan, J., Newby, L. K., Hauser, E. R., Ginsburg, G. S., et al. (2010) · Circulation Cardiovascular Genetics · doi:10.1161/circgenetics.109.852814 · Cited by 468 · see citing works

SIRT4 Has Tumor-Suppressive Activity and Regulates the Cellular Metabolic Response to DNA Damage by Inhibiting Mitochondrial Glutamine Metabolism

Jeong, S. M., Xiao, C., Finley, L. W. S., Lahusen, T., Souza, A. L., Pierce, K., Li, Y.-H., Wang, X., Laurent, G., German, N. J., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.024 · Cited by 445 · see citing works

Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity

Mathias, R. A., Greco, T. M., Oberstein, A., Budayeva, H. G., Chakrabarti, R., Rowland, E. A., Kang, Y., Shenk, T., & Cristea, I. M. (2014) · Cell · doi:10.1016/j.cell.2014.11.046 · Cited by 430 · see citing works

Regulation of Insulin Secretion by SIRT4, a Mitochondrial ADP-ribosyltransferase

Ahuja, N., Schwer, B., Carobbio, S., Waltregny, D., North, B. J., Castronovo, V., Maechler, P., & Verdin, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705488200 · Cited by 422 · see citing works

SIRT4 Coordinates the Balance between Lipid Synthesis and Catabolism by Repressing Malonyl CoA Decarboxylase

Laurent, G., German, N. J., Saha, A. K., de Boer, V. C. J., Davies, M. N., Koves, T. R., Dephoure, N., Fischer, F. F., Boanca, G., Vaitheesvaran, B., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.012 · Cited by 394 · see citing works

An Enzymatic Activity in the Yeast Sir2 Protein that Is Essential for Gene Silencing

Tanny, J. C., Dowd, G. J., Huang, J., Hilz, H., & Moazed, D. (1999) · Cell · doi:10.1016/s0092-8674(00)81671-2 · Cited by 391 · see citing works

L-leucine and a nonmetabolized analogue activate pancreatic islet glutamate dehydrogenase

Sener, A., & Malaisse, W. J. (1980) · Nature · doi:10.1038/288187a0 · Cited by 354 · see citing works

Crystal Structure of a SIR2 Homolog–NAD Complex

Min, J., Landry, J. W., Sternglanz, R., & Xu, R.-M. (2001) · Cell · doi:10.1016/s0092-8674(01)00317-8 · Cited by 326 · see citing works

SIRT4 Regulates Fatty Acid Oxidation and Mitochondrial Gene Expression in Liver and Muscle Cells

Nasrin, N., Wu, X.-P., Fortier, E., Feng, Y., Bare, O., Chen, S., Ren, X., Wu, Z., Streeper, R. S., & Bordone, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.124164 · Cited by 323 · see citing works

Nonenzymatic Protein Acylation as a Carbon Stress Regulated by Sirtuin Deacylases

Wagner, G. R., & Hirschey, M. D. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.027 · Cited by 319 · see citing works

A Fluorogenic Histone Deacetylase Assay Well Suited for High-Throughput Activity Screening

Wegener, D., Wirsching, F., Riester, D., & Schwienhorst, A. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00305-8 · Cited by 283 · see citing works

Structural Basis of Inhibition of the Human NAD+-Dependent Deacetylase SIRT5 by Suramin

Schuetz, A., Min, J., Antoshenko, T., Wang, C.-L., Allali‐Hassani, A., Dong, A., Loppnau, P., Vedadi, M., Bochkarev, A. V., Sternglanz, R., et al. (2007) · Structure · doi:10.1016/j.str.2007.02.002 · Cited by 264 · see citing works

The International Mouse Phenotyping Consortium Web Portal, a unified point of access for knockout mice and related phenotyping data

Koscielny, G., Yaikhom, G., Iyer, V., Meehan, T. F., Morgan, H., Atienza-Herrero, J., Blake, A., Chen, C.-K., Easty, R., Fenza, A. D., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt977 · Cited by 262 · see citing works

A Class of Reactive Acyl-CoA Species Reveals the Non-enzymatic Origins of Protein Acylation

Wagner, G. R., Bhatt, D. P., O’Connell, T. M., Thompson, J. W., Dubois, L. G., Backos, D. S., Yang, H., Mitchell, G. A., Ilkayeva, O. R., Stevens, R. D., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.03.006 · Cited by 258 · see citing works

The PredictProtein server

Rost, B. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg508 · Cited by 247 · see citing works

The sirtuin family’s role in aging and age-associated pathologies

Hall, J. A., Dominy, J. E., Lee, Y., & Puigserver, P. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64094 · Cited by 235 · see citing works

Crystal Structures of Human SIRT3 Displaying Substrate-induced Conformational Changes

Jin, L., Wei, W., Jiang, Y., Peng, H., Cai, J., Mao, C., Dai, H., Choy, W., Bemis, J. E., Jirousek, M. R., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014928 · Cited by 208 · see citing works

Sirtuin/Sir2 Phylogeny, Evolutionary Considerations and Structural Conservation

Greiss, S., & Gartner, A. (2009) · Molecules and Cells · doi:10.1007/s10059-009-0169-x · Cited by 207 · see citing works

Investigating the ADP-ribosyltransferase Activity of Sirtuins with NAD Analogues and 32 P-NAD

Du, J., Jiang, H. X., & Lin, H. (2009) · Biochemistry · doi:10.1021/bi802093g · Cited by 166 · see citing works

SIRT4 regulates ATP homeostasis and mediates a retrograde signaling via AMPK

Ho, L., Titus, A. S., Banerjee, K. K., George, S., Lin, W., Deota, S., Saha, A. K., Nakamura, K., Gut, P., Verdin, E. M., et al. (2013) · Aging · doi:10.18632/aging.100616 · Cited by 160 · see citing works

Regulation of Leucine-stimulated Insulin Secretion and Glutamine Metabolism in Isolated Rat Islets

Li, C., Najafi, H., Daikhin, Y., Nissim, I. B., Collins, H. W., Yudkoff, M., Matschinsky, F. M., & Stanley, C. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210577200 · Cited by 158 · see citing works

SIRT4 Represses Peroxisome Proliferator-Activated Receptor α Activity To Suppress Hepatic Fat Oxidation

Laurent, G., de Boer, V. C. J., Finley, L. W. S., Sweeney, M. O., Lu, H., Schug, T. T., Cen, Y., Jeong, S. M., Li, X., Sauve, A. A., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00087-13 · Cited by 154 · see citing works

Tumour-suppressive function of SIRT4 in human colorectal cancer

Miyo, M., Yamamoto, H., Konno, M., Colvin, H. S., Nishida, N., Koseki, J., Kawamoto, K., Ogawa, H., Hamabe, A., Uemura, M., et al. (2015) · British Journal of Cancer · doi:10.1038/bjc.2015.226 · Cited by 151 · see citing works

Branched-chain amino acid catabolism is a conserved regulator of physiological ageing

Mansfeld, J., Urban, N., Priebe, S., Groth, M., Frahm, C., Hartmann, N., Gebauer, J., Ravichandran, M., Dommaschk, A., Schmeisser, S., et al. (2015) · Nature Communications · doi:10.1038/ncomms10043 · Cited by 149 · see citing works

TCF1 links GIPR signaling to the control of beta cell function and survival

Campbell, J. E., Ussher, J. R., Mulvihill, E. E., Kolic, J., Baggio, L. L., Cao, X., Liu, Y., Lamont, B. J., Morii, T., Streutker, C. J., et al. (2016) · Nature Medicine · doi:10.1038/nm.3997 · Cited by 142 · see citing works

Hyperinsulinemia in pre-weaning diabetes (db) mice

Coleman, D. L., & Hummel, K. P. (1974) · Diabetologia · doi:10.1007/bf01221993 · Cited by 141 · see citing works

Branched-Chain Amino Acid Catabolism in Exercise and Liver Disease

Shimomura, Y., Honda, T., Shiraki, M., Murakami, T., Sato, J., Kobayashi, H., Mawatari, K., Obayashi, M., & Harris, R. A. (2006) · Journal of Nutrition · doi:10.1093/jn/136.1.250s · Cited by 128 · see citing works

SIRT4 protein suppresses tumor formation in genetic models of Myc-induced B cell lymphoma

Jeong, S. M., Lee, A., Lee, J., & Haigis, M. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525949 · Cited by 121 · see citing works

Impaired Adiponectin Signaling Contributes to Disturbed Catabolism of Branched-Chain Amino Acids in Diabetic Mice

Lian, K., Du, C., Liu, Y., Zhu, D., Yan, W., Zhang, H., Hong, Z., Liu, P., Zhang, L., Pei, H., et al. (2014) · Diabetes · doi:10.2337/db14-0312 · Cited by 119 · see citing works

Identification of mitochondrial branched chain aminotransferase and its isoforms in rat tissues.

Hutson, S. M., Wallin, R., & Hall, T. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49589-6 · Cited by 117 · see citing works

Characterization and prediction of residues determining protein functional specificity

Capra, J. A., & Singh, M. (2008) · Bioinformatics · doi:10.1093/bioinformatics/btn214 · Cited by 117 · see citing works

Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADH

Madsen, A. S., Andersen, C. D., Daoud, M., Anderson, K. A., Laursen, J. S., Chakladar, S., Huynh, F. K., Colaço, A. R., Backos, D. S., Fristrup, P., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.668699 · Cited by 110 · see citing works

Representative Proteomes: A Stable, Scalable and Unbiased Proteome Set for Sequence Analysis and Functional Annotation

Chen, C., Natale, D. A., Finn, R. D., Huang, H., Zhang, J., Wu, C. H., & Mazumder, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018910 · Cited by 101 · see citing works

SnapShot: Mammalian Sirtuins

Anderson, K. A., Green, M. F., Huynh, F. K., Wagner, G. R., & Hirschey, M. D. (2014) · Cell · doi:10.1016/j.cell.2014.10.045 · Cited by 100 · see citing works

Old Enzymes, New Tricks: Sirtuins Are NAD+-Dependent De-acylases

Hirschey, M. D. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.10.006 · Cited by 99 · see citing works

In situ assay of the intramitochondrial enzymes: use of alamethicin for permeabilization of mitochondria

Gostimskaya, I. S., Grivennikova, V. G., Zharova, T. V., Bakeeva, L. E., & Vinogradov, A. D. (2003) · Analytical Biochemistry · doi:10.1016/s0003-2697(02)00534-1 · Cited by 98 · see citing works

Hyperinsulinemia Precedes Insulin Resistance in Mice Lacking Pancreatic β-Cell Leptin Signaling

Gray, S. L., Donald, C., Jetha, A., Covey, S. D., & Kieffer, T. J. (2010) · Endocrinology · doi:10.1210/en.2010-0102 · Cited by 92 · see citing works

Proteomics Profiling of Madin-Darby Canine Kidney Plasma Membranes Reveals Wnt-5a Involvement during Oncogenic H-Ras/TGF-β-mediated Epithelial-Mesenchymal Transition

Chen, Y. S., Mathias, R. A., Mathivanan, S., Kapp, E. A., Moritz, R. L., Zhu, H., & Simpson, R. J. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.001131 · Cited by 89 · see citing works

Fluorescence assay of SIRT protein deacetylases using an acetylated peptide substrate and a secondary trypsin reaction

Marcotte, P. A., Richardson, P. R., Guo, J., Barrett, L. W., Xu, N., Gunasekera, A. H., & Glaser, K. B. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.05.039 · Cited by 82 · see citing works

Substrates for Efficient Fluorometric Screening Employing the NAD-Dependent Sirtuin 5 Lysine Deacylase (KDAC) Enzyme

Madsen, A. S., & Olsen, C. A. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300526r · Cited by 73 · see citing works

The Complex Mechanism of Glutamate Dehydrogenase in Insulin Secretion

Fahien, L. A., & MacDonald, M. J. (2011) · Diabetes · doi:10.2337/db10-1150 · Cited by 61 · see citing works

Transamination Is Required for α-Ketoisocaproate but Not Leucine to Stimulate Insulin Secretion*

Zhou, Y., Jetton, T. L., Goshorn, S., Lynch, C. J., & She, P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.136846 · Cited by 59 · see citing works

Identification of 3-methylglutarylcarnitine. A new diagnostic metabolite of 3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency.

Roe, C. R., Millington, D. S., & Maltby, D. A. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112446 · Cited by 56 · see citing works

An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase

Huang, C., Ge, P., Zhou, Z. H., & Tong, L. (2011) · Nature · doi:10.1038/nature10691 · Cited by 54 · see citing works

Evolution of Glutamate Dehydrogenase Regulation of Insulin Homeostasis Is an Example of Molecular Exaptation

Allen, A., Kwagh, J., Fang, J., Stanley, C. A., & Smith, T. J. (2004) · Biochemistry · doi:10.1021/bi048817i · Cited by 50 · see citing works

Measurement of Mammalian Histone Deacetylase Activity

Verdin, E. M., Dequiedt, F., Fischle, W., Frye, R. A., Marshall, B. L., & North, B. J. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)77010-4 · Cited by 44 · see citing works

Stereoselective synthesis of the macrocycle segment of verrucarin J

White, J. D., Carter, J. P., & Kezar, H. S. (1982) · The Journal of Organic Chemistry · doi:10.1021/jo00345a005 · Cited by 39 · see citing works

Chronic hyperinsulinemia reduces insulin sensitivity and metabolic functions of brown adipocyte

Rajan, S., Shankar, K., Beg, M., Varshney, S., Gupta, A., Srivastava, A., Kumar, D., Mishra, R. K., Hussain, Z., Gayen, J. R., et al. (2016) · Journal of Endocrinology · doi:10.1530/joe-16-0099 · Cited by 38 · see citing works

Metabotyping ofCaenorhabditis elegansand their Culture Media Revealed Unique Metabolic Phenotypes Associated to Amino Acid Deficiency and Insulin-Like Signaling

Martin, F., Spanier, B., Collino, S., Montoliu, I., Kolmeder, C. A., Giesbertz, P., Affolter, M., Kussmann, M., Daniel, H., Kochhar, S., et al. (2011) · Journal of Proteome Research · doi:10.1021/pr100703a · Cited by 36 · see citing works

ADP-regenerating enzyme systems in mitochondria of guinea pig myometrium and heart

Clark, J. F., Kuznetsov, A. V., & Radda, G. K. (1997) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1997.272.2.c399 · Cited by 25 · see citing works

Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals interact with pyruvate carboxylase and other acetylated biotin-dependent carboxylases

Wirth, M., Karaca, S., Wenzel, D., Ho, L., Tishkoff, D. X., Lombard, D. B., Verdin, E. M., Urlaub, H., Jedrusik, M. A., & Fischle, W. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.02.002 · Cited by 22 · see citing works

Effects of diazoxide on insulin secretion and metabolic efficiency in the db/db mouse

Lee, S. (1981) · Life Sciences · doi:10.1016/0024-3205(81)90354-4 · Cited by 6 · see citing works

Detecting Sirtuin-Catalyzed Deacylation Reactions Using 32P-Labeled NAD and Thin-Layer Chromatography

Zhu, A. Y., Su, X., & Lin, H. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-637-5_12 · Cited by 3 · see citing works

Functions and mechanisms of non-histone protein acetylation

Narita, T., Weinert, B. T., & Choudhary, C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0081-3 · Cited by 1,232 · see citing works

NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential

Xie, N., Zhang, L., Gao, W. Q., Huang, C., Huber, P., Zhou, X., Li, C. L., Shen, G., & Zou, B. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00311-7 · Cited by 1,076 · see citing works

Modulation of cellular processes by histone and non-histone protein acetylation

Shvedunova, M., & Akhtar, A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00441-y · Cited by 975 · see citing works

The Role of Sirtuins in Antioxidant and Redox Signaling

Singh, C. K., Chhabra, G., Ndiaye, M. A., Garcia‐Peterson, L. M., Mack, N. J., & Ahmad, N. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7290 · Cited by 812 · see citing works

Branched Chain Amino Acids

Neinast, M. D., Murashige, D., & Arany, Z. P. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114455 · Cited by 727 · see citing works

Lipoic acid metabolism and mitochondrial redox regulation

Solmonson, A., & DeBerardinis, R. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000259 · Cited by 492 · see citing works

Sirtuins and NAD + in the Development and Treatment of Metabolic and Cardiovascular Diseases

Kane, A. E., & Sinclair, D. A. (2018) · Circulation Research · doi:10.1161/circresaha.118.312498 · Cited by 490 · see citing works

Sirtuin activators and inhibitors: Promises, achievements, and challenges

Dai, H., Sinclair, D. A., Ellis, J. L., & Steegborn, C. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.03.004 · Cited by 463 · see citing works

The Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy

Guo, L., Tian, Y., & Zhu, W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576946 · Cited by 358 · see citing works

Sirtuins in Renal Health and Disease

Morigi, M., Perico, L., & Benigni, A. (2018) · Journal of the American Society of Nephrology · doi:10.1681/asn.2017111218 · Cited by 359 · see citing works

The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications

Carrico, C., Meyer, J. G., He, W., Gibson, B. W., & Verdin, E. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.01.016 · Cited by 331 · see citing works

Functions of the sirtuin deacylase SIRT5 in normal physiology and pathobiology

Kumar, S., & Lombard, D. B. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1458071 · Cited by 264 · see citing works

Branched-chain Amino Acids: Catabolism in Skeletal Muscle and Implications for Muscle and Whole-body Metabolism

Mann, G., Mora, S., Madu, G., & Adegoke, O. A. J. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.702826 · Cited by 271 · see citing works

A Class of Reactive Acyl-CoA Species Reveals the Non-enzymatic Origins of Protein Acylation

Wagner, G. R., Bhatt, D. P., O’Connell, T. M., Thompson, J. W., Dubois, L. G., Backos, D. S., Yang, H., Mitchell, G. A., Ilkayeva, O. R., Stevens, R. D., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.03.006 · Cited by 258 · see citing works

Mitochondrial sirtuins, metabolism, and aging

Ji, Z., Liu, G., & Qu, J. T. (2021) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2021.11.005 · Cited by 246 · see citing works

p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis

Huang, H., Tang, S., Ji, M. H., Tang, Z., Shimada, M., Liu, X., Qi, S., Locasale, J. W., Roeder, R. G., Zhao, Y., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.04.011 · Cited by 221 · see citing works

Enzyme promiscuity drives branched-chain fatty acid synthesis in adipose tissues

Wallace, M., Green, C. R., Roberts, L. S., Lee, Y. M., McCarville, J. L., Sánchez-Gurmaches, J., Meurs, N., Gengatharan, J. M., Hover, J. D., Phillips, S. A., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0132-2 · Cited by 207 · see citing works

Metabolic control by sirtuins and other enzymes that sense NAD+, NADH, or their ratio

Anderson, K. A., Madsen, A. S., Olsen, C. A., & Hirschey, M. D. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.09.005 · Cited by 210 · see citing works

NAD+ biosynthesis, aging, and disease

Johnson, S., & Imai, S. (2018) · F1000Research · doi:10.12688/f1000research.12120.1 · Cited by 178 · see citing works

Mitohormesis and metabolic health: The interplay between ROS, cAMP and sirtuins

Palmeira, C. M., Teodoro, J. S., Amorim, J. A., Steegborn, C., Sinclair, D. A., & Rolo, A. P. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.07.017 · Cited by 159 · see citing works

UHRF1 promotes aerobic glycolysis and proliferation via suppression of SIRT4 in pancreatic cancer

Hu, Q., Qin, Y., Ji, S., Xu, W., Liu, W., Sun, Q., Zhang, Z., Liu, M., Ni, Q., Yu, X., et al. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.03.024 · Cited by 158 · see citing works

SIRT4 interacts with OPA1 and regulates mitochondrial quality control and mitophagy

Lang, A., Anand, R., Altinoluk-Hambüchen, S., Ezzahoini, H., Stefanski, A., Iram, A., Bergmann, L., Urbach, J., Böhler, P., Hänsel, J., et al. (2017) · Aging · doi:10.18632/aging.101307 · Cited by 145 · see citing works

Histone deacetylase 11 is an ε-N-Myristoyllysine hydrolase

Moreno-Yruela, C., Galleano, I., Madsen, A. S., & Olsen, C. A. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.04.007 · Cited by 149 · see citing works

Sirtuins and Insulin Resistance

Zhou, S., Tang, X., & Chen, H. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00748 · Cited by 143 · see citing works

Emerging Roles for SIRT5 in Metabolism and Cancer

Bringman, L. R., Guo, A. H., Lyssiotis, C. A., & Lombard, D. B. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7264 · Cited by 140 · see citing works

The Roles of Mitochondrial SIRT4 in Cellular Metabolism

Min, Z., Gao, J., & Yu, Y. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00783 · Cited by 134 · see citing works

Molecular basis for hierarchical histone de-β-hydroxybutyrylation by SIRT3

Zhang, X., Cao, R., Niu, J., Yang, S., Ma, H., Zhao, S., & Li, H. (2019) · Cell Discovery · doi:10.1038/s41421-019-0103-0 · Cited by 124 · see citing works

The roles of sirtuins family in cell metabolism during tumor development

Zhu, S., Dong, Z., Ke, X., Hou, J., Zhao, E., Zhang, K., Wang, F., Yang, L., Xiang, Z., & Cui, H. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.11.003 · Cited by 113 · see citing works

Sirtuin 5 is required for mouse survival in response to cardiac pressure overload

Hershberger, K. A., Abraham, D., Martin, A. S., Mao, L., Liu, J., Gu, H., Locasale, J. W., & Hirschey, M. D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.809897 · Cited by 105 · see citing works

Sirtuins, resveratrol and the intertwining cellular pathways connecting them

Ungurianu, A., Zanfirescu, A., & Margina, D. M. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101936 · Cited by 113 · see citing works

Human Sirtuin Regulators: The “Success” Stories

Curry, A. M., White, D. S., Donu, D., & Cen, Y. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.752117 · Cited by 105 · see citing works

Crystal structures of the mitochondrial deacylase Sirtuin 4 reveal isoform-specific acyl recognition and regulation features

Pannek, M., Simic, Z., Fuszard, M. A., Meleshin, M., Rotili, D., Mai, A., Schutkowski, M., & Steegborn, C. (2017) · Nature Communications · doi:10.1038/s41467-017-01701-2 · Cited by 102 · see citing works

Dietary Modulation of the Epigenome

Ideraabdullah, F., & Zeisel, S. H. (2018) · Physiological Reviews · doi:10.1152/physrev.00010.2017 · Cited by 98 · see citing works

SIRT3 deficiency-induced mitochondrial dysfunction and inflammasome formation in the brain

Tyagi, A., Nguyen, C. U., Chong, T., Michel, C. R., Fritz, K. S., Reisdorph, N. A., Knaub, L. A., Reusch, J. E. B., & Pugazhenthi, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-35890-7 · Cited by 96 · see citing works

Roles of Mitochondrial Sirtuins in Mitochondrial Function, Redox Homeostasis, Insulin Resistance and Type 2 Diabetes

Wang, C., & Wei, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155266 · Cited by 95 · see citing works

Sirtuins as Important Factors in Pathological States and the Role of Their Molecular Activity Modulators

Kratz, E. M., Sołkiewicz, K., Kubis-Kubiak, A., & Piwowar, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020630 · Cited by 93 · see citing works

Anti-HIV Drug Elvitegravir Suppresses Cancer Metastasis via Increased Proteasomal Degradation of m6A Methyltransferase METTL3

Liao, L., He, Y., Li, S.-J., Zhang, G.-G., Yu, W., Yang, J., Huang, Z., Zheng, C., He, Q., Li, Y., et al. (2022) · Cancer Research · doi:10.1158/0008-5472.can-21-4124 · Cited by 94 · see citing works

Matrix Redox Physiology Governs the Regulation of Plant Mitochondrial Metabolism through Posttranslational Protein Modifications

Møller, I. M., Igamberdiev, A. U., Bykova, N. V., Finkemeier, I., Rasmusson, A. G., & Schwarzländer, M. (2020) · The Plant Cell · doi:10.1105/tpc.19.00535 · Cited by 89 · see citing works

Contribution of Oxidative Stress and Impaired Biogenesis of Pancreatic β-Cells to Type 2 Diabetes

Ježek, P., Jabůrek, M., & Plecitá‐Hlavatá, L. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7656 · Cited by 88 · see citing works

The CD38 glycohydrolase and the NAD sink: implications for pathological conditions

Zeidler, J. D., Hogan, K. A., Agorrody, G., Peclat, T., Kashyap, S., Kanamori, K. S., Gomez, L. S., Mazdeh, D. Z., Warner, G. M., Thompson, K. L., et al. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00451.2021 · Cited by 90 · see citing works

Sirtuins in atherosclerosis: guardians of healthspan and therapeutic targets

Grootaert, M. O. J., & Bennett, M. R. (2022) · Nature Reviews Cardiology · doi:10.1038/s41569-022-00685-x · Cited by 88 · see citing works

Epigenetic regulation in cancer therapy: From mechanisms to clinical advances

Tao, L., Zhou, Y., Luo, Y., Qiu, J., Xiao, Y., Zou, J., Zhang, Y., Liu, X., Yang, X., Gou, K., et al. (2024) · MedComm – Oncology · doi:10.1002/mog2.59 · Cited by 93 · see citing works

Mitochondrial Sirtuins in cardiometabolic diseases

Tang, X., Chen, X., Chen, H., & Liu, D. (2017) · Clinical Science · doi:10.1042/cs20160685 · Cited by 87 · see citing works

SIRT5 deacylates metabolism-related proteins and attenuates hepatic steatosis in ob/ob mice

Du, Y., Hu, H., Qu, S., Wang, J., Hua, C., Zhang, J., Wei, P., He, X., Hao, J., Liu, P., et al. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.09.037 · Cited by 87 · see citing works

Ketogenic diet-produced β-hydroxybutyric acid accumulates brain GABA and increases GABA/glutamate ratio to inhibit epilepsy

Qiao, Y.-N., Li, L., Hu, S.-H., Yang, Y.-X., Ma, Z., Huang, L., An, Y., Yuan, Y., Lin, Y., Xu, W., et al. (2024) · Cell Discovery · doi:10.1038/s41421-023-00636-x · Cited by 86 · see citing works

Chiral Posttranslational Modification to Lysine ε-Amino Groups

Moreno-Yruela, C., Bæk, M., Monda, F., & Olsen, C. A. (2022) · Accounts of Chemical Research · doi:10.1021/acs.accounts.2c00115 · Cited by 85 · see citing works

Sirt4 is a mitochondrial regulator of metabolism and lifespan in Drosophila melanogaster

Wood, J. G., Schwer, B., Wickremesinghe, P. C., Hartnett, D. A., Burhenn, L., Garcia, M., Li, M., Verdin, E. M., & Helfand, S. L. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1720673115 · Cited by 83 · see citing works

Sirt4: A Multifaceted Enzyme at the Crossroads of Mitochondrial Metabolism and Cancer

Tomaselli, D., Steegborn, C., Mai, A., & Rotili, D. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00474 · Cited by 80 · see citing works

Mitochondrial Function, Metabolic Regulation, and Human Disease Viewed through the Prism of Sirtuin 4 (SIRT4) Functions

Betsinger, C. N., & Cristea, I. M. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00086 · Cited by 80 · see citing works

Sirtuins in Metabolic and Epigenetic Regulation of Stem Cells

Fang, Y., Tang, S., & Li, X. (2019) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2018.12.002 · Cited by 77 · see citing works

Mechanism‐Based Inhibitors of the Human Sirtuin 5 Deacylase: Structure–Activity Relationship, Biostructural, and Kinetic Insight

Rajabi, N., Auth, M., Troelsen, K. R., Pannek, M., Bhatt, D. P., Fontenas, M., Hirschey, M. D., Steegborn, C., Madsen, A. S., & Olsen, C. A. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201709050 · Cited by 75 · see citing works

Uncoupling mechanism and redox regulation of mitochondrial uncoupling protein 1 (UCP1)

Ježek, P., Jabůrek, M., & Porter, R. K. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.11.007 · Cited by 74 · see citing works

Mitochondrial Sirtuins in Reproduction

Emidio, G. D., Falone, S., Artini, P. G., Amicarelli, F., D’Alessandro, A. M., & Tatone, C. (2021) · Antioxidants · doi:10.3390/antiox10071047 · Cited by 74 · see citing works

The Role of Sirtuins in Kidney Diseases

Hong, Y. A., Kim, J. E., Jo, M.-J., & Ko, G.-J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186686 · Cited by 73 · see citing works

Mitochondrial dysfunction and beneficial effects of mitochondria-targeted small peptide SS-31 in Diabetes Mellitus and Alzheimer’s disease

Ding, X.-W., Robinson, M., Li, R., Aldhowayan, H., Geetha, T., & Babu, J. R. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105783 · Cited by 73 · see citing works

A global view of the human post-translational modification landscape

Kitamura, N., & Galligan, J. J. (2023) · Biochemical Journal · doi:10.1042/bcj20220251 · Cited by 70 · see citing works

Emerging Roles of SIRT5 in Metabolism, Cancer, and SARS-CoV-2 Infection

Fabbrizi, E., Fiorentino, F., Carafa, V., Altucci, L., Mai, A., & Rotili, D. (2023) · Cells · doi:10.3390/cells12060852 · Cited by 75 · see citing works

Keeping the balance in NAD metabolism

Strømland, Ø., Niere, M., Nikiforov, A. A., VanLinden, M. R., Heiland, I., & Ziegler, M. (2019) · Biochemical Society Transactions · doi:10.1042/bst20180417 · Cited by 72 · see citing works

Updates on the epigenetic roles of sirtuins

Kosciuk, T., Wang, M., Hong, J. Y., & Lin, H. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.01.023 · Cited by 70 · see citing works

Extranuclear Sirtuins and Metabolic Stress

Elkhwanky, M., & Hakkola, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7270 · Cited by 67 · see citing works

Therapeutic Potential and Activity Modulation of the Protein Lysine Deacylase Sirtuin 5

Fiorentino, F., Castiello, C., Mai, A., & Rotili, D. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00687 · Cited by 69 · see citing works

The multiple facets of acetyl-CoA metabolism: Energetics, biosynthesis, regulation, acylation and inborn errors

Wang, Y., Yang, H., Geerts, C., Fürtös, A., Waters, P. J., Cyr, D., Wang, S., & Mitchell, G. A. (2022) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2022.106966 · Cited by 73 · see citing works

The sirtuin family in cancer

Costa‐Machado, L. F., & Fernández-Marcos, P. J. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1634953 · Cited by 66 · see citing works

SIRT4 is an early regulator of branched-chain amino acid catabolism that promotes adipogenesis

Zaganjor, E., Yoon, H., Spinelli, J. B., Nunn, E. R., Laurent, G., Keskinidis, P., Sivaloganathan, S., Joshi, S., Notarangelo, G., Mulei, S., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109345 · Cited by 67 · see citing works

SIRT4 and Its Roles in Energy and Redox Metabolism in Health, Disease and During Exercise

Han, Y., Zhou, S., Coetzee, S., & Chen, A. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01006 · Cited by 69 · see citing works

Targeting glutamine metabolism in hepatic stellate cells alleviates liver fibrosis

Yin, X.-C., Peng, J., Gu, L.-H., Liu, Y., Li, X., Wu, J.-H., Xu, B., Zhuge, Y., & Zhang, F. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05409-0 · Cited by 62 · see citing works

Sirtuin 4 activates autophagy and inhibits tumorigenesis by upregulating the p53 signaling pathway

Li, J., Zhan, H., Ren, Y., Feng, M., Wang, Q., Jiao, Q., Wang, Y., Liu, X., Zhang, S., Du, L., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01063-3 · Cited by 64 · see citing works

Sirtuins at the Crossroads between Mitochondrial Quality Control and Neurodegenerative Diseases: Structure, Regulation, Modifications, and Modulators

Xu, H. M., Liu, Y., Li, L.-S., & Liu, Y. (2023) · Aging and Disease · doi:10.14336/ad.2022.1123 · Cited by 66 · see citing works

Mitochondrial Reactive Oxygen Species, Insulin Resistance, and Nrf2-Mediated Oxidative Stress Response—Toward an Actionable Strategy for Anti-Aging

Kasai, S., Kokubu, D., Mizukami, H., & Itoh, K. (2023) · Biomolecules · doi:10.3390/biom13101544 · Cited by 73 · see citing works

SIRT4 is the last puzzle of mitochondrial sirtuins

Li, Y., Zhou, Y., Wang, F., Chen, X., Wang, C., Wang, J., Liu, T., Li, Y., & He, B. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.07.031 · Cited by 63 · see citing works

The balance between NAD+ biosynthesis and consumption in ageing

Strømland, Ø., Diab, J., Ferrario, E., Sverkeli, L. J., & Ziegler, M. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111569 · Cited by 63 · see citing works

The Emerging Role of HDACs: Pathology and Therapeutic Targets in Diabetes Mellitus

Dewanjee, S., Vallamkondu, J., Kalra, R. S., Chakraborty, P., Gangopadhyay, M., Sahu, R., Medala, V. K., John, A. A., Reddy, P. H., Feo, V. D., et al. (2021) · Cells · doi:10.3390/cells10061340 · Cited by 61 · see citing works

Metabolic sensing and control in mitochondria

Liu, Y., & Birsoy, K. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.016 · Cited by 64 · see citing works

Reactive Acyl-CoA Species Modify Proteins and Induce Carbon Stress

Trub, A. G., & Hirschey, M. D. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.02.002 · Cited by 59 · see citing works

Circulating Branched Chain Amino Acids and Cardiometabolic Disease

Fine, K. S., Wilkins, J. T., & Sawicki, K. T. (2024) · Journal of the American Heart Association · doi:10.1161/jaha.123.031617 · Cited by 60 · see citing works

Advances in the Development of Therapeutics for Cytomegalovirus Infections

Acosta, E. P., Bowlin, T. L., Brooks, J., Chiang, L. W., Hussein, I. T. M., Kimberlin, D. W., Kauvar, L. M., Leavitt, R. Y., Prichard, M. N., & Whitley, R. J. (2019) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiz493 · Cited by 60 · see citing works

Current Trends in Sirtuin Activator and Inhibitor Development

Bursch, K. L., Goetz, C. J., & Smith, B. C. (2024) · Molecules · doi:10.3390/molecules29051185 · Cited by 59 · see citing works

NAD(H) in mitochondrial energy transduction: implications for health and disease

Walker, M. A., & Tian, R. (2018) · Current Opinion in Physiology · doi:10.1016/j.cophys.2018.03.011 · Cited by 58 · see citing works

Molecular and cellular regulatory roles of sirtuin protein

Pande, S., & Raisuddin, S. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2070722 · Cited by 58 · see citing works

Sirtuin Modulators: Past, Present, and Future Perspectives

Fiorentino, F., Mautone, N., Menna, M., D’Acunzo, F., Mai, A., & Rotili, D. (2022) · Future Medicinal Chemistry · doi:10.4155/fmc-2022-0031 · Cited by 56 · see citing works

Histone Deacetylases: Molecular Mechanisms and Therapeutic Implications for Muscular Dystrophies

Sandonà, M., Cavioli, G., Renzini, A., Cedola, A., Gigli, G., Coletti, D., McKinsey, T. A., Moresi, V., & Saccone, V. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054306 · Cited by 57 · see citing works

LC–MS/MS-based quantitative study of the acyl group- and site-selectivity of human sirtuins to acylated nucleosomes

Tanabe, K., Liu, J., Kato, D., Kurumizaka, H., Yamatsugu, K., Kanai, M., & Kawashima, S. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-21060-2 · Cited by 53 · see citing works

A Molecular Perspective on Sirtuin Activity

Teixeira, C. S. S., Cerqueira, N. M. F. S. A., Gomes, P., & Sousa, S. F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228609 · Cited by 56 · see citing works

The Mystery of Extramitochondrial Proteins Lysine Succinylation

Chinopoulos, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116085 · Cited by 42 · see citing works

3-Methylglutaric acid in energy metabolism

Jones, D. E., Perez, L., & Ryan, R. O. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.11.006 · Cited by 54 · see citing works

Targeting Sirtuins: Substrate Specificity and Inhibitor Design

Rajabi, N., Galleano, I., Madsen, A. S., & Olsen, C. A. (2018) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.11.003 · Cited by 52 · see citing works

Sirtuin-4 (SIRT4), a therapeutic target with oncogenic and tumor-suppressive activity in cancer

Huang, G., & Zhu, G. (2018) · OncoTargets and Therapy · doi:10.2147/ott.s157724 · Cited by 52 · see citing works

Ustilaginoidea virens modulates lysine 2‐hydroxyisobutyrylation in rice flowers during infection

Chen, X., Xu, Q., Duan, Y., Liu, H., Chen, X., Huang, J., Luo, C., Zhou, D., & Zheng, L. (2021) · Journal of Integrative Plant Biology · doi:10.1111/jipb.13149 · Cited by 51 · see citing works

Cellular and molecular biology of sirtuins in cardiovascular disease

Liu, Y., Wen, R., Liu, C., Zhang, T., & Yang, N. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114931 · Cited by 53 · see citing works

Imbalance of Lysine Acetylation Contributes to the Pathogenesis of Parkinson’s Disease

Wang, R., Sun, H., Wang, G., & Ren, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197182 · Cited by 50 · see citing works

Diabetic retinopathy, oxidative stress, and sirtuins: an in depth look in enzymatic patterns and new therapeutic horizons

Nebbioso, M., Lambìase, A., Armentano, M., Tucciarone, G., Sacchetti, M., Greco, A., & Alisi, L. (2021) · Survey of Ophthalmology · doi:10.1016/j.survophthal.2021.04.003 · Cited by 50 · see citing works

Pathways of Non-enzymatic Lysine Acylation

Baldensperger, T., & Glomb, M. A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.664553 · Cited by 45 · see citing works

Emerging Roles of SIRT3 in Cardiac Metabolism

Murugasamy, K., Munjal, A., & Sundaresan, N. R. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.850340 · Cited by 48 · see citing works

Temporal dynamics of liver mitochondrial protein acetylation and succinylation and metabolites due to high fat diet and/or excess glucose or fructose

Meyer, J. G., Softic, S., Basisty, N., Rardin, M. J., Verdin, E. M., Gibson, B. W., Ilkayeva, O., Newgard, C. B., Kahn, C. R., & Schilling, B. (2018) · PLoS ONE · doi:10.1371/journal.pone.0208973 · Cited by 49 · see citing works

Roles of sirtuin family members in chronic obstructive pulmonary disease

Zhang, X.-Y., Li, W., Zhang, J., Li, C., Zhang, J., & Lv, X. (2022) · Respiratory Research · doi:10.1186/s12931-022-01986-y · Cited by 46 · see citing works

Epigenetic Remodeling in Obesity-Related Vascular Disease

Masi, S., Ambrosini, S., Mohammed, S. A., Sciarretta, S., Lüscher, T. F., Paneni, F., & Costantino, S. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8040 · Cited by 46 · see citing works

Role of Sirtuins in Tumor Angiogenesis

Edatt, L., Poyyakkara, A., Raji, G. R., Ramachandran, V., Shankar, S. S., & Kumar, V. B. S. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2019.01516 · Cited by 43 · see citing works

Anabolic SIRT4 Exerts Retrograde Control over TORC1 Signaling by Glutamine Sparing in the Mitochondria

Shaw, E., Talwadekar, M., Rashida, Z., Mohan, N., Acharya, A., Khatri, S., Laxman, S., & Kolthur‐Seetharam, U. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00212-19 · Cited by 42 · see citing works

Potent and Selective Inhibitors of Human Sirtuin 5

Kalbas, D., Liebscher, S., Nowak, T., Meleshin, M., Pannek, M., Popp, C., Alhalabi, Z., Bordusa, F., Sippl, W., Steegborn, C., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01648 · Cited by 42 · see citing works

Continuous Activity Assay for HDAC11 Enabling Reevaluation of HDAC Inhibitors

Kutil, Z., Mikešová, J., Zessin, M., Meleshin, M., Nováková, Z., Alquicer, G., Kozikowski, A. P., Sippl, W., Bařinka, C., & Schutkowski, M. (2019) · ACS Omega · doi:10.1021/acsomega.9b02808 · Cited by 40 · see citing works

Sirtuin 4 controls leucine metabolism and insulin secretion by reversing effects of reactive metabolites

Huynh, F. K., Anderson, K. A., Stuart, J. D., Lin, Z., & Hirschey, M. D. (2018) · The FASEB Journal · doi:10.1096/fasebj.2018.32.1_supplement.670.23

The Roles of Mitochondrial SIRT4 in Cellular Metabolism

Min, Z., Gao, J., & Yu, Y. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00783 · Cited by 134 · see citing works

Loss of sirtuin 4 leads to elevated glucose‐ and leucine‐stimulated insulin levels and accelerated age‐induced insulin resistance in multiple murine genetic backgrounds

Huynh, F. K., Hu, X., Lin, Z., Johnson, J. D., & Hirschey, M. D. (2017) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-017-0069-8 · Cited by 24 · see citing works

Sirtuin 4 regulates nutrient-stimulated insulin secretion by modulating GLP-1 secretion

Penney, M. C., Do, E., Luong, A., & Huynh, F. K. (2024) · Physiology · doi:10.1152/physiol.2024.39.s1.1724

SIRT4 Is a Regulator of Insulin Secretion

Zaganjor, E., Vyas, S., & Haigis, M. C. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.06.002 · Cited by 35 · see citing works