Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase

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

Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase

Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239

The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms

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Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ

Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943

Sirtuin activators mimic caloric restriction and delay ageing in metazoans

Wood, J. G., Rogina, B., Lavu, S., Howitz, K., Helfand, S. L., Tatar, M., & Sinclair, D. (2004) · Nature · doi:10.1038/nature02789 · Cited by 1,868

Requirement of NAD and SIR2 for Life-Span Extension by Calorie Restriction in Saccharomyces cerevisiae

Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775

Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans

Tissenbaum, H. A., & Guarente, L. (2001) · Nature · doi:10.1038/35065638 · Cited by 1,603

The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase

North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542

The Sir2 Family of Protein Deacetylases

Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,497

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

Sirtuins and Neurodegeneration

Dönmez, G. (2017) · Journal of Neurology and Neuromedicine · doi:10.29245/2572.942x/2017/1.1168 · Cited by 11

Impacts on Sirtuin Function and Bioavailability of the Dietary Bioactive Compound Dihydrocoumarin

Jacobi, J. L., Yang, B. H., Li, X., Menze, A. K., Laurentz, S., Janle, E. M., Ferruzzi, M. G., McCabe, G. P., Chapple, C. C. S., & Kirchmaier, A. L. (2016) · PLoS ONE · doi:10.1371/journal.pone.0149207 · Cited by 11

PARP: a transferase by any other name

Till, S., Diamantara, K., & Ladurner, A. G. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1208-1243 · Cited by 11

Milp-hyperbox classification for structure-based drug design in the discovery of small molecule inhibitors of SIRTUIN6

Tardu, M., Rahim, F., Kavaklı, İ. H., & Türkay, M. (2015) · RAIRO - Operations Research · doi:10.1051/ro/2015042 · Cited by 11

Sirtuin 6 promotes eosinophil differentiation by activating GATA‐1 transcription factor

Bang, I. H., Park, D., Lee, Y., Cho, H., Park, B., & Bae, E. J. (2021) · Aging Cell · doi:10.1111/acel.13418 · Cited by 9

Role of the Substrate Specificity-Defining Residues of Human SIRT5 in Modulating the Structural Stability and Inhibitory Features of the Enzyme

Yu, J., Haldar, M., Mallik, S., & Srivastava, D. K. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152467 · Cited by 9

An optimized desuccinylase activity assay reveals a difference in desuccinylation activity between proliferative and differentiated cells

Yuan, T., Keijer, J., Guo, A. H., Lombard, D. B., & de Boer, V. C. J. (2020) · Scientific Reports · doi:10.1038/s41598-020-72833-7 · Cited by 9

Role of APD-Ribosylation in Bone Health and Disease

Wang, C., & Mbalaviele, G. (2019) · Cells · doi:10.3390/cells8101201 · Cited by 9

Sirtuins—Novel Regulators of Epigenetic Alterations in Airway Inflammation

Wu, S., & Liu, H. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.862577 · Cited by 8

Understanding the catalytic abilities of class IV sirtuin OsSRT1 and its linkage to the DNA repair system under stress conditions

Mitra, N., & Dey, S. (2022) · Plant Science · doi:10.1016/j.plantsci.2022.111398 · Cited by 8

Nutraceuticals for Promoting Longevity

Pavlović, I., Khateb, S., Milisav, I., & Mahajna, J. A. (2020) · Current Nutraceuticals · doi:10.2174/2665978601666200213121512 · Cited by 8

Pharmacological manipulations of CNS sirtuins: Potential effects on metabolic homeostasis

Ramadori, G., & Coppari, R. (2010) · Pharmacological Research · doi:10.1016/j.phrs.2010.02.002 · Cited by 8

Nicotinamide adenine dinucleotide: An essential factor in preserving hearing in cisplatin-induced ototoxicity

Kim, H., Oh, G., Shen, A., Lee, S., Khadka, D., Pandit, A., Shim, H., Yang, S., Cho, E. Y., Song, J., et al. (2015) · Hearing Research · doi:10.1016/j.heares.2015.04.002 · Cited by 9

The role of microRNAs in modulating sirtuin 1 expression

Tsai, K., Chen, L.-H., Chen, Y., Kao, C.-L., Chen, L., & Chiou, S. (2011) · Journal of Clinical Gerontology and Geriatrics · doi:10.1016/j.jcgg.2011.06.004 · Cited by 8

Involvement of Sirtuins in Life-Span and Aging Related Diseases

Mahlknecht, U., & Zschoernig, B. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-1704-0_16 · Cited by 7

Role of N-terminus in function and dynamics of sirtuin 7: an in silico study

Hałasa, M., Bartuzi, D., Cieślak, D., Kaczor, A. A., Miziak, P. A., Stepulak, A., & Matosiuk, D. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1600585 · Cited by 7

SIRT6 mediates multidimensional modulation to maintain organism homeostasis

Yang, Y., Zhu, M. L., Liang, J., Wang, H., Sun, D., Li, H., & Chen, L. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30791 · Cited by 7

Sirtuin 6 Is a Critical Epigenetic Regulator of Cancer

Raghu, S., Prabhashankar, A. B., Shivanaiah, B., Tripathi, E., & Sundaresan, N. R. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-07634-3_10 · Cited by 7

Molecular integrative study on interaction domains of nuclear factor erythroid 2-related factor 2 with sirtuin 6

Fu, W., Xiao, Z., Chen, Y., Pei, J., Sun, Y., Zhang, Z., Wu, H., Pei, Y., Wei, S., Wang, Y., et al. (2023) · Biochimie · doi:10.1016/j.biochi.2023.03.002 · Cited by 8

Molecular and functional characterization of sirt4 and sirt6 in Megalobrama amblycephala under high glucose metabolism

Lin, S., Teng, L.-Z., Lin, Y., Miao, L., Ge, X., Hao, J.-Y., Huang, X., & Liu, B. (2019) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2019.01.010 · Cited by 7

The Enzymatic Activities of Sirtuins

Lin, H. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00004-6 · Cited by 6

Sirtuiny – enzymy o wielokierunkowej aktywności katalitycznej

Kratz, E. M., Sołkiewicz, K., Kaczmarek, A., & Piwowar, A. (2021) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.5604/01.3001.0014.7866 · Cited by 6

Gene-Diet Interaction between SIRT6 and Soybean Intake for Different Levels of Pulse Wave Velocity

Sun, K., Xiang, X., Li, N., Huang, S., Qin, X., Wu, Y., Tang, X., Gao, P., Li, J., Wu, T., et al. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160714338 · Cited by 6

Tailored SirReal-type inhibitors enhance SIRT2 inhibition through ligand stabilization and disruption of NAD + co-factor binding

Wirawan, R., Frei, M., Heider, A., Papenkordt, N., Friedrich, F., Wein, T., Jung, M., Groll, M., Huber, E. M., & Bracher, F. (2025) · RSC Medicinal Chemistry · doi:10.1039/d5md00144g · Cited by 5

PKCδ Regulates Chromatin Remodeling and DNA Repair through SIRT6

Affandi, T., Haas, A., Ohm, A. M., Wright, G. M., Black, J. C., & Reyland, M. E. (2023) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-23-0493 · Cited by 5

2-(Diarylalkyl)aminobenzothiazole derivatives induce autophagy and apoptotic death through SIRT inhibition and P53 activation In MCF7 breast cancer cells

Venkateswarlu, K., Kumar, D., Kalavagunta, P. K., Bhukya, B., Tangutur, A. D., & Nayak, P. K. (2025) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2025.108395 · Cited by 6

Anoxia Rapidly Induces Changes in Expression of a Large and Diverse Set of Genes in Endothelial Cells

Antonelli, A., Scarpa, E. S., Bruzzone, S., Astigiano, C., Piacente, F., Bruschi, M., Fraternale, A., Buduo, C. A. D., Balduini, A., & Magnani, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065157 · Cited by 5

Advances in natural small molecules on pretranslational regulation of gluconeogenesis

Wu, X., & Chen, S. (2023) · Drug Development Research · doi:10.1002/ddr.22053 · Cited by 5

Effect of quercetin on the protein-substrate interactions in SIRT6: Insight from MD simulations

Zhang, H., Zhang, J., & Zhang, H. (2024) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2024.108778 · Cited by 6

Small Molecule Modulators of Sirtuin Activity

Alcain, F. J., Minor, R. K., Villalba, J. M., & de Cabo, R. (2010) · Springer eBooks · doi:10.1007/978-90-481-3999-6_10 · Cited by 5

Papel pleiotrópico y homeostático de las Sirtuinas en la función biológica humana.

Hernández-Bedolla, M. A., Barajas‐Espinosa, A. R., Ochoa‐Cortés, F., Alonso, D. E. A., Hernández, A. H., Ostoa, Z. B., & Salguero, I. G. D. (2020) · Ciencias Huasteca Boletín Científico de la Escuela Superior de Huejutla · doi:10.29057/esh.v8i16.5721 · Cited by 5

Mono-ADP-Ribosylation of Heterotrimeric G Proteins

Girolamo, M. D., & Corda, D. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00204-7 · Cited by 5

Cloning, chromosomal characterization and FISH mapping of the NAD+-dependent histone deacetylase gene sirtuin 5 in the mouse

Voelter‐Mahlknecht, S., & Mahlknecht, U. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1939 · Cited by 5

Sirtuins – universal regulators of cell function

Кайдашев, І. П. (2012) · Biopolymers and Cell · doi:10.7124/bc.000033 · Cited by 5

Cellular mechanisms promoting cachexia and how they are opposed by sirtuins

Samant, S. A., Pillai, V. B., & Gupta, M. P. (2018) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2018-0479 · Cited by 5

Structural basis of SIRT2 pre-catalysis NAD + binding dynamics and mechanism

Zhang, N., Pow, K. C., Chen, L., & Hao, Q. (2025) · RSC Chemical Biology · doi:10.1039/d5cb00169b · Cited by 4

Resveratrol Alleviated Oxidative Damage of Bovine Mammary Epithelial Cells via Activating SIRT5-IDH2 Axis

Yang, H., Liu, L., Zhang, X., Gao, S., Li, A., Dong, J., Lu, G., Yang, Q., Liu, X., Sun, S., et al. (2025) · Antioxidants · doi:10.3390/antiox14101171 · Cited by 4

Potential roles of the sirtuins in promoting longevity for larger Argopecten scallops

Zhao, Y., Ning, J., Wang, Y., Liu, G., Xu, X. S., Wang, C., & Lu, X. (2025) · Marine Life Science & Technology · doi:10.1007/s42995-024-00269-3 · Cited by 4

DNA stimulates the deacetylase SIRT6 to mono-ADP-ribosylate proteins with histidine repeats

Pederson, N. J., & Diehl, K. L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108532 · Cited by 8

Immunocell-array for Molecular Dissection of Multiple Signaling Pathways in Mammalian Cells

Zanardi, A., Giorgetti, L., Botrugno, O. A., Minucci, S., Milani, P., Pelicci, P. G., & Carbone, R. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t600051-mcp200 · Cited by 4

Respected Sir(2): magic target for diabetes.

Nerurkar, P. V., & Nerurkar, V. R. (2008) · PubMed · Cited by 4

Roles for Sirtuins in Cardiovascular Biology

Stein, A., Giblin, W., Guo, A. H., & Lombard, D. B. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00012-5 · Cited by 4

Investigation of Mitochondrial ADP-Ribosylation Via Immunofluorescence

Hopp, A.-K., & Hottiger, M. O. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1266-8_12 · Cited by 4

DNA stimulates SIRT6 to mono-ADP-ribosylate proteins within histidine repeatsPreprint

Pederson, N. J., & Diehl, K. L. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.31.606047 · Cited by 4

Lead Optimization: Synthesis and Biological Evaluation of Griseofulvin Derivatives as Novel SIRT6 Activators

Zorko, T., Kogovšek, J., Ciber, L., Ostojić, I., Maraš, N., Novinec, M., & Štefane, B. (2026) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5c00690 · Cited by 3

Sirt6 ablation in the liver causes fatty liver that increases cancer risk by upregulating Serpina12

Li, L., Zeng, J., Zhang, X., Feng, Y., Lei, J. H., Xu, X., Chen, Q., & Deng, C. (2024) · EMBO Reports · doi:10.1038/s44319-024-00071-3 · Cited by 4

SIRT1-FOXOs signaling pathway: A potential target for attenuating cardiomyopathy

Lu, C., Gao, C., Wei, J., Dong, D. F., & Sun, M. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111409 · Cited by 3

SIRT6 modulates lesion microenvironment in LPC induced demyelination by targeting astrocytic CHI3L1

Du, J., Yin, Y., Wu, D., Diao, C., Zhao, T., Peng, F., Li, N., Wang, D., Shi, J., Wang, L., et al. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03241-1 · Cited by 4

Sirtuins and Aging

Pukhalskaia, A. E., Kvetnoy, I. M., Linkova, N. S., Diatlova, A., Gutop, E. O., Kozlov, K. L., & Paltsev, M. A. (2023) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-023-01379-8 · Cited by 3

The Chemopreventive Effect of Ginsenoside Compound K Is Regulated by PARP-1 Hyperactivation, Which Is Promoted by p62-Dependent SIRT6 Degradation

Kim, S. H., Ki, S. H., Hyeong, S.-W., & Oh, S. (2025) · Nutrients · doi:10.3390/nu17030539 · Cited by 3

Epigenetic Reprogramming of the Glucose Metabolic Pathways by the Chromatin Effectors During Cancer

Mondal, P., Tiwary, N., Sengupta, A., Dhang, S., Roy, S., & Das, C. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-07634-3_9 · Cited by 3

[Dacron and polytetrafluoroethylene aorto-bifemoral grafts].

Davidovic, L. B., Lotina, S. I., Kostic, D. M., Cinara, I., Cvetkovic, S. D., Stojanović, P. L., Velimirović, L. B., Markovic, D. M., Pejkić, S., & Pavlović, G. (1997) · PubMed · Cited by 3

Nicotinamide adenine dinucleotide+ metabolism biomarkers in malignant gliomas

Lucena-Cacace, A., Jiménez-García, M. P., & Verdugo-Sivianes, E. (2016) · Cancer translational medicine · doi:10.4103/2395-3977.196912 · Cited by 3

Correction: Over Expression of Wild Type or a Catalytically Dead Mutant of SIRTUIN 6 Does Not Influence NFκB Responses

Grimley, R. L., Polyakova, O., Vamathevan, J. J., McKenary, J., Hayes, B. J., Patel, C., Smith, J. L., Bridges, A. M., Fosberry, A. P., Bhardwaja, A., et al. (2012) · PLoS ONE · doi:10.1371/annotation/9c1a5765-6471-401f-bc74-a916c8ead46f · Cited by 3

Role of SIRT7 in Prostate Cancer Progression: New Insight Into Potential Therapeutic Target

Zhang, J., Liu, C., Luo, W., & Sun, B. (2025) · Cancer Medicine · doi:10.1002/cam4.70786 · Cited by 2

The Expanding Landscape of ADP-Ribosylation: Protein, DNA, RNA, and Mitochondrial Regulation

Sin, Y.-C., & Zhao, L. (2026) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6c00176 · Cited by 2

Acetyl-CoA and acetylation in biology and disease

Puglielli, L., Rigby, M. J., & Fernandez-Fuente, G. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95582-9.00009-7 · Cited by 2

Hepatic SIRT6 protects against cholestatic liver disease primarily via inhibiting bile acid synthesis

Zhang, W., Wang, J., Yang, L., Shao, Y., Peng, H., Jiang, L., & Sheng, L. (2024) · Journal of Biomedical Research · doi:10.7555/jbr.38.20240172 · Cited by 3

Structural Insights Into centSIRT6: Bioinformatic Analysis of N308K and A313S Substitution Effects

Lagunas‐Rangel, F. A. (2025) · Bioinformatics and Biology Insights · doi:10.1177/11779322251339698 · Cited by 2

Sirtuin-Dependent Metabolic Control and Its Role in the Aging Process

Calvo, S. S.-C., Navas, P., & López‐Lluch, G. (2012) · InTech eBooks · doi:10.5772/35702 · Cited by 2

Epigenetic Mechanisms of Sirtuins in Dermatology

Lo, A., Serravallo, M., & Jagdeo, J. R. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800957-4.00008-4 · Cited by 3

Dual role of sirtuins in cancer

Torrens‐Mas, M., & Roca, P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822467-0.00011-5 · Cited by 2

Sirtuins and next generation hallmarks of cancer: cellular energetics and tumor promoting inflammation

Kleszcz, R., & Baer‐Dubowska, W. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822467-0.00005-x · Cited by 2

Sirtuin functions in the brain: From physiological to pathological aspects

Shao, J., Zhang, T., Liu, T., Quan, Y., Fan, L., Liu, J., Yang, X. Y., Xie, Q. R., & Xia, W. (2014) · Journal of Shanghai Jiaotong University (Science) · doi:10.1007/s12204-014-1562-y · Cited by 2

Molecular cloning, expression and subcellular distribution of an alternative splice variant of the porcine Sirt2 gene

Liu, B., Liu, F., Bai, L., Li, Y., & Yang, G. (2009) · Molecular Biology Reports · doi:10.1007/s11033-009-9858-y · Cited by 2

Sirtuins and Aging

Dong, Y., & Zou, S. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0639-7_5 · Cited by 2

The bifunctional roles of sirtuins and their therapeutic potential in cancer

Lee, Y. T., Tan, Y. J., Mok, P. Y., Subramaniam, A. V., & Oon, C. E. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822467-0.00009-7 · Cited by 2

To eat or not to eat – Anti‐ageing effects of energy restriction

Neves, D., Martins, M. J., Passos, E., & Tomada, I. (2015) · Wiley eBooks · doi:10.1002/9781118823408.ch2 · Cited by 2

SirT7 auto-ADP-ribosylation regulates glucose starvation response through macroH2A1.1Preprint

Simonet, N. G., Thackray, J. K., Vázquez, B. N., Ianni, A., Espinosa‐Alcantud, M., Morales‐Sanfrutos, J., Hurtado-Bagès, S., Sabidó, E., Buschbeck, M., Tischfield, J. A., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/719559 · Cited by 2

Immunoprecipitation Using Mono-ADP-Ribosylation-Specific Antibodies

Dauben, H., & Matić, I. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2891-1_9 · Cited by 1

Modulations of SIRTUINs and Management of Brain Disorders

Shekhar, S. K., Siddiqui, S. A., & Rai, G. (2023) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815040197123010006 · Cited by 1

Pyruvate kinase is post-translationally regulated by sirtuin 2 in Aedes aegypti mosquitoes

Petchampai, N., Isoe, J., Balaraman, P., Oscherwitz, M. E., Carter, B. H., Sánchez, C. G., & Scaraffia, P. Y. (2023) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2023.104015 · Cited by 1

Sirt6 prevents the age-related decline of H 2 S through the control of one-carbon metabolism

Touitou, N., Nahum, L., Feldman-Trabelsi, S., Avivi, M. Y., Aon, M. A., Naiman, S., Rathaus, M., Gertler, A. A., Roichman, A., Dvir, L. B., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2514084122 · Cited by 1

Histidine and tyrosine residues are targets for SIRT6 ADP-ribosylation activity

Rack, J. G. M., Prokhorova, E. A., Lauro, R., Kopasz, A. G., Baretić, D., Raggiaschi, R., Mutabdzija, J., Filippov, D. V., Timinszky, G., Leidecker, O., et al. (2026) · Open Biology · doi:10.1098/rsob.250181 · Cited by 1

Folic acid alleviates endothelial dysfunction caused by T2DM-induced ferroptosis by activating the SIRT6/NRF2/GPX4 signaling pathway

Hong, L., Lou, X., Zha, Y., Fu, X., Che, T., Qiao, S., Wang, C., & An, J. (2026) · Food & Function · doi:10.1039/d5fo04381f · Cited by 1

Context-informed subgraph foundation models enable interpretable protein-function prediction

Zhou, Z., Rao, J., Zhang, Z., Ma, R., Yang, J., & Zheng, S. (2026) · Cell Systems · doi:10.1016/j.cels.2026.101535 · Cited by 1

Beyond deacetylation: crosstalk mechanisms and context-dependent regulation of sirtuin non-classical enzymatic functions in disease

Ma, Y., Chen, J., Song, R., & Yu, X. (2026) · Molecular Medicine · doi:10.1186/s10020-026-01503-7 · Cited by 1

Molecular Mechanisms of Cardiovascular Aging

Meiliana, A., & Wijaya, A. (2013) · The Indonesian Biomedical Journal · doi:10.18585/inabj.v5i3.64 · Cited by 1

Assessing the Histone Deacetylase Activity of SIRT6 in Primary Murine Hepatocytes via Proximity Ligation Assay

Wolf, K., & Strand, S. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6527-4_11 · Cited by 1

Diverse Roles for SIRT6 in Mammalian Healthspan and Longevity

Zwaans, B. M. M., Giblin, W., & Lombard, D. B. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_7 · Cited by 1

Silent Information Regulator 2 from Trypanosoma cruzi Is a Potential Target to Infection Control

Gaspar, L., Smith, T., Moretti, N. S., Schenkman, S., & Cordeiro‐da‐Silva, A. (2018) · InTech eBooks · doi:10.5772/intechopen.77030 · Cited by 1

A sirtuin 6 activator in the pipeline: New perspectives in depressive disorder treatment

Carolina, D. O. P. A., Mendonça, D. S. G. A., Barros José, C., & Schroeder, B. G. R. (2024) · Open Journal of Proteomics and Genomics · doi:10.17352/ojpg.000013

The Role of Sirtuin-2 in Tubular Forming Activity of Human Umbilical Vein Endothelial Cells

Jung, S. Y., Kim, C. M., Kim, D. Y., Lee, D. H., Lee, K. S., & Kwon, S. (2013) · Journal of Life Science · doi:10.5352/jls.2013.23.1.131 · Cited by 1

Sirtuins and stem cell maintenance, proliferation, and differentiation

Denu, R. A., & Hematti, P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814118-2.00003-3 · Cited by 1

NAD‐Dependent Deacetylases as Therapeutic Targets

Li, H., Simon, J. A., & Bedalov, A. (2009) · Methods and principles in medicinal chemistry · doi:10.1002/9783527627073.ch10 · Cited by 1

Functional analysis of mitochondrial sirtuins in C. elegans and mammalian cells

Wirth, M. (2011) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3229 · Cited by 1

CELLULAR NAD STATUS AS A REGULATOR OF SKIN PHOTODAMAGE

Benavente, C. A. (2007) · UA Campus Repository (The University of Arizona) · Cited by 1

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Epigenetic Mouse Models

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Neh1 and Neh3 domains of nuclear factor erythroid 2-related factor 2 mediate its binding to NAD-dependent protein deacetylase sirtuin-6Preprint

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© 2004 BioMed Central Ltd Summary

North, B. J., & Verdin, E. (2004)

Sirtuins: Sir2-related NAD-dependent protein deacetylases.

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