Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling

UCSF Chimera—A visualization system for exploratory research and analysis

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Oxidants, oxidative stress and the biology of ageing

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Aging: a theory based on free radical and radiation chemistry

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AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity

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A Mitochondrial Paradigm of Metabolic and Degenerative Diseases, Aging, and Cancer: A Dawn for Evolutionary Medicine

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Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1

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Mammalian Sirtuins: Biological Insights and Disease Relevance

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A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology

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Regulation of cellular metabolism by protein lysine acetylation

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SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation

Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687

Subcellular Localization and Mitotic Interactome Analyses Identify SIRT4 as a Centrosomally Localized and Microtubule Associated Protein

Bergmann, L., Lang, A., Bross, C., Altinoluk-Hambüchen, S., Fey, I., Overbeck, N., Stefanski, A., Wiek, C., Kefalas, A., Verhülsdonk, P., et al. (2020) · Cells · doi:10.3390/cells9091950 · Cited by 32

H2S donor molecules against cold ischemia-reperfusion injury in preclinical models of solid organ transplantation

Dugbartey, G. J., Juriasingani, S., Zhang, M. Y., & Şener, A. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105842 · Cited by 33

AMP-Activated Kinase (AMPK) Activation by AICAR in Human White Adipocytes Derived from Pericardial White Adipose Tissue Stem Cells Induces a Partial Beige-Like Phenotype

Abdul-Rahman, O., Kristóf, E., Doan‐Xuan, Q., Vida, A., Nagy, L., Horváth, A., Simon, J., Maros, T., Szentkirályi, I., Palotás, L., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0157644 · Cited by 32

Impaired hepatic mitochondrial function during early lactation in dairy cows: Association with protein lysine acetylation

García-Roche, M., Casal, A., Mattiauda, D. A., Ceriani, M., Jasinsky, A., Mastrogiovanni, M., Trostchansky, A., Carriquiry, M., Cassina, A., & Quijano, C. (2019) · PLoS ONE · doi:10.1371/journal.pone.0213780 · Cited by 31

Ambient fine particulate matter exposure perturbed circadian rhythm and oscillations of lipid metabolism in adipose tissues

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The protective effects of 17-β estradiol and SIRT1 against cardiac hypertrophy: a review

Hajializadeh, Z., & Khaksari, M. (2021) · Heart Failure Reviews · doi:10.1007/s10741-021-10171-0 · Cited by 30

Mechanism of Rhein-Induced Apoptosis in Rat Primary Hepatocytes: Beneficial Effect of Cyclosporine A

Panigrahi, G., Yadav, A., Srivastava, A., Tripathi, A., Raisuddin, S., & Das, M. (2015) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5b00063 · Cited by 31

SirT3 regulates diabetogenic effects caused by arsenic: An implication for mitochondrial complex II modification

Rezaei, M., Keshtzar, E., Khodayar, M. J., & Javadipour, M. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2018.10.025 · Cited by 31

TREM2 Ameliorates Lipopolysaccharide-Induced Oxidative Stress Response and Neuroinflammation by Promoting Sirtuin3 in BV2 Cells

Li, H., Liu, F., Jiang, W., Wang, K., Cao, X., Zou, J., Zhou, Y., Li, Z., Liu, S., Cui, X., et al. (2022) · Neurotoxicity Research · doi:10.1007/s12640-021-00459-2 · Cited by 29

The acute hepatotoxicity of tacrine explained by1H NMR based metabolomic profiling

Lou, Y.-H., Wang, J., Dong, G., Guo, P.-P., Wei, D., Xie, S., Yang, M., & Kong, L. (2015) · Toxicology Research · doi:10.1039/c5tx00096c · Cited by 30

Resveratrol Stimulates Cortisol Biosynthesis by Activating SIRT-Dependent Deacetylation of P450scc

Li, D., Dammer, E. B., & Sewer, M. B. (2012) · Endocrinology · doi:10.1210/en.2011-2088 · Cited by 30

Inhibition of NAD+-dependent histone deacetylases (sirtuins) causes growth arrest and activates both apoptosis and autophagy in the pathogenic protozoanTrypanosoma cruzi

Veiga-Santos, P., Reignault, L. C., Huber, K., Bracher, F., de Souza, W., & de Carvalho, T. M. U. (2014) · Parasitology · doi:10.1017/s0031182013001704 · Cited by 30

The plasticizer BBP selectively inhibits epigenetic regulator sirtuin during differentiation of C3H10T1/2 stem cell line

Zhang, J., & Choudhury, M. (2016) · Toxicology in Vitro · doi:10.1016/j.tiv.2016.11.016 · Cited by 30

Overexpression of SIRT1 prevents hypoxia-induced apoptosis in osteoblast cells

Zhou, L., Wang, S. I., Moon, Y. J., Kim, K. M., Lee, K. B., Park, B., Jang, K. Y., & Kim, J. R. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.6917 · Cited by 30

Estrogen modulates vascular smooth muscle cell function through downregulation of SIRT1

Lee, C.-H., Su, S., Chiang, C., Chien, C., Hsu, C., Yu, T.-Y., Huang, S., Shieh, Y., Kao, H.-W., Tsai, C., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.22546 · Cited by 30

Cellular and Mitochondrial NAD Homeostasis in Health and Disease

Waddell, J., Khatoon, R., & Kristián, T. (2023) · Cells · doi:10.3390/cells12091329 · Cited by 33

Mitochondria in Alzheimer’s Disease and Diabetes-Associated Neurodegeneration: License to Heal!

Cardoso, S., Correia, S. C., Carvalho, C., & Moreira, P. I. (2017) · Handbook of experimental pharmacology · doi:10.1007/164_2017_3 · Cited by 29

Mitochondrial Sirtuins in Skin and Skin Cancers

Su, S., Ndiaye, M. A., Singh, C. K., & Ahmad, N. (2020) · Photochemistry and Photobiology · doi:10.1111/php.13254 · Cited by 29

BCL2 Interacting Protein 3-like/NIX-mediated Mitophagy Plays an Important Role in the Process of Age-related Hearing Loss

Kim, Y. J., Choo, O., Lee, J.-S., Jang, J. H., Woo, H. G., & Choung, Y. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.12.005 · Cited by 30

Nutraceutical based SIRT3 activators as therapeutic targets in Alzheimer's disease

Govindarajulu, M., Ramesh, S., Neel, L. T., Fabbrini, M., Buabeid, M. A., Fujihashi, A., Dwyer, D., Lynd, T. O., Shah, K., Mohanakumar, K. P., et al. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.104958 · Cited by 31

Friend or Foe? Mitochondria as a Pharmacological Target in Cancer Treatment

Dickerson, T., Jauregui, C. E., & Teng, Y. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0110 · Cited by 28

Synergistic impact of endurance training and intermittent hypobaric hypoxia on cardiac function and mitochondrial energetic and signaling

Magalhães, J., Falcão‐Pires, I., Gonçalves, I. O., Lumini‐Oliveira, J., Marques‐Aleixo, I., Passos, E., Rocha‐Rodrigues, S., Machado, N. G., Moreira, A. C., Miranda‐Silva, D., et al. (2013) · International Journal of Cardiology · doi:10.1016/j.ijcard.2013.08.001 · Cited by 28

Aging Biology in the Kidney

Bitzer, M., & Wiggins, J. E. (2015) · Advances in Chronic Kidney Disease · doi:10.1053/j.ackd.2015.11.005 · Cited by 30

Remote ischemic preconditioning protects against spinal cord ischemia–reperfusion injury in mice by activating NMDAR/AMPK/PGC-1α/SIRT3 signaling

Gu, C., Kong, F., Zeng, J., Geng, X., Sun, Y., & Chen, X. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-00999-4 · Cited by 27

Targeting Mitochondrial Sirtuins in Age-Related Neurodegenerative Diseases and Fibrosis

Xiao, H., Xie, Y., Xi, K., Xie, J., Liu, M., Zhang, Y., Cheng, Z., Wang, W., Guo, B., & Wu, S. (2023) · Aging and Disease · doi:10.14336/ad.2023.0203 · Cited by 29

SIRT1 confers protection against ischemia/reperfusion injury in cardiomyocytes via regulation of uncoupling protein 2 expression

Deng, M., Wang, D., He, S., Xu, R., & Xie, Y. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7452 · Cited by 27

Exercise mitigates diclofenac‐induced liver mitochondrial dysfunction

Alves, E. S., Marques‐Aleixo, I., Coxito, P. M., Balça, M. M., Rizo‐Roca, D., Rocha‐Rodrigues, S., Martins, S., Torrella, J. R., Oliveira, P. J., Moreno, A. J., et al. (2014) · European Journal of Clinical Investigation · doi:10.1111/eci.12285 · Cited by 26

Over-expression of the Sirt3 sirtuin Protects neuronally differentiated PC12 Cells from degeneration induced by oxidative stress and trophic withdrawal

Shulyakova, N., Sidorova‐Darmos, E., Fong, J., Zhang, G., Mills, L. R., & Eubanks, J. H. (2014) · Brain Research · doi:10.1016/j.brainres.2014.08.066 · Cited by 26

Interplay between NAD+ and acetyl‑CoA metabolism in ischemia-induced mitochondrial pathophysiology

Klimova, N., Long, A., Scafidi, S., & Kristián, T. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.09.025 · Cited by 26

Antioxidant Modulation of mTOR and Sirtuin Pathways in Age-Related Neurodegenerative Diseases

Abdullah, A., Murshid, N. M., & Makpol, S. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02083-1 · Cited by 29

Roles of SIRT3 in cardiovascular and neurodegenerative diseases

Cheng, Y., Zhao, A., Li, Y., Li, C., Miao, X., Yang, W., & Wang, Y. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102654 · Cited by 25

Sirtuins in Multiple Sclerosis: The crossroad of neurodegeneration, autoimmunity and metabolism

Foolad, F., Khodagholi, F., & Javan, M. (2019) · Multiple Sclerosis and Related Disorders · doi:10.1016/j.msard.2019.06.004 · Cited by 26

A mechanism-based potent sirtuin inhibitor containing Nε-thiocarbamoyl-lysine (TuAcK)

Hirsch, B. M., Hao, Y., Li, X., Wesdemiotis, C., Wang, Z., & Zheng, W. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.06.069 · Cited by 25

Effect of Resveratrol on Sirtuins, OPA1, and Fis1 Expression in Adult Zebrafish Retina

Sheng, W., Lu, Y., Feng, M., Wang, N., Liu, Z.-Z., Han, Y., Wang, H.-T., Zou, S., Xu, H. A., & Zhang, X. (2018) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.18-24539 · Cited by 25

Renal Protective Effects of Early Continuous Venovenous Hemofiltration in Rhabdomyolysis: Improved Renal Mitochondrial Dysfunction and Inhibited Apoptosis

Tang, W., Chen, Z., Wu, W., Qiu, H., Bo, H., Zhang, L., & Fu, P. (2013) · Artificial Organs · doi:10.1111/j.1525-1594.2012.01574.x · Cited by 25

Protein acetylation mechanisms in the regulation of insulin and insulin-like growth factor 1 signalling

Pirola, L., Zerzaihi, O., Vidal, H., & Solari, F. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.05.011 · Cited by 26

SIRT3 is a novel prognostic biomarker for esophageal squamous cell carcinoma

Yan, S., Han, X., Han, P., Chen, H.-M., Huang, L., & Li, Y. (2014) · Medical Oncology · doi:10.1007/s12032-014-0103-8 · Cited by 24

Neuroinflammation and Mitochondrial Dysfunction in the Pathogenesis of Alzheimer?s Disease: Modulation by Coriolus Versicolor (Yun-Zhi) Nutritional Mushroom

Calabrese, V. (2017) · Journal of Neurology and Neuromedicine · doi:10.29245/2572.942x/2017/2.942x/2017/1.1088 · Cited by 24

A direct role for hepatitis B virus X protein in inducing mitochondrial membrane permeabilization

Lee, H., Cho, Y. Y., Lee, G. Y., You, D., Yoo, Y. D., & Kim, Y. J. (2017) · Journal of Viral Hepatitis · doi:10.1111/jvh.12831 · Cited by 24

Deoxynivalenol downregulates NRF2-induced cytoprotective response in human hepatocellular carcinoma (HepG2) cells

Ndlovu, S. S., Nagiah, S., Abdul, N. S., Ghazi, T., & Chuturgoon, A. A. (2021) · Toxicon · doi:10.1016/j.toxicon.2021.01.017 · Cited by 24

Bioactive peptide apelin rescues acute kidney injury by protecting the function of renal tubular mitochondria

Guan, Y., Diao, Z.-L., Huang, H., Zheng, J., Zhang, Q., Wang, L., & Liu, W. (2021) · Amino Acids · doi:10.1007/s00726-021-03028-1 · Cited by 24

The mTOR/PGC-1α/SIRT3 Pathway Drives Reductive Glutamine Metabolism to Reduce Oxidative Stress Caused by ISKNV in CPB Cells

Fu, X., Li, K., Niu, Y., Lin, Q., Liang, H., Luo, X., Liu, L., & Li, N. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.02310-21 · Cited by 24

Mitochondrial metabolic reprogramming by SIRT3 regulation ameliorates drug resistance in renal cell carcinoma

Gu, Y.-R., Kim, J., Na, J. C., & Han, W. K. (2022) · PLoS ONE · doi:10.1371/journal.pone.0269432 · Cited by 26

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

Post-translational modification by acetylation regulates the mitochondrial carnitine/acylcarnitine transport protein

Giangregorio, N., Tonazzi, A., Console, L., & Indiveri, C. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2881-0 · Cited by 24

Knockout of SIRT4 decreases chemosensitivity to 5‑FU in colorectal cancer cells

Zhu, Y., Wang, G., Li, X., Wang, T., Weng, M., & Zhang, Y. (2018) · Oncology Letters · doi:10.3892/ol.2018.8850 · Cited by 24

Sirt3 is dispensable for oocyte quality and female fertility in lean and obese mice

Iljas, J. D., & Homer, H. A. (2020) · The FASEB Journal · doi:10.1096/fj.202000153r · Cited by 24

Integrated or Independent Actions of Metformin in Target Tissues Underlying Its Current Use and New Possible Applications in the Endocrine and Metabolic Disorder Area

Tulipano, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313068 · Cited by 26

Mitochondrial sirtuins – a new therapeutic target for repair and protection in multiple sclerosis

Rice, C. M., Sun, M., Kemp, K. C., Gray, E., Wilkins, A., & Scolding, N. J. (2012) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2012.08150.x · Cited by 25

Bioenergetic shift and actin cytoskeleton remodelling as acute vascular adaptive mechanisms to angiotensin II in murine retina and ophthalmic artery

Perumal, N., Straßburger, L., Herzog, D. P., Müller, M. B., Pfeiffer, N., Grus, F. H., & Manicam, C. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101597 · Cited by 23

Genetic Reduction of Mitochondria Complex I Subunits is Protective against Cisplatin-Induced Neurotoxicity inDrosophila

Groen, C. M., Podratz, J. L., Pathoulas, J., Staff, N. P., & Windebank, A. J. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.1479-20.2021 · Cited by 25

FUS Mutation Causes Disordered Lipid Metabolism in Skeletal Muscle Associated with ALS

Zhou, B., Zheng, Y., Li, X., Dong, H., Yu, J., Zou, Y., Zhu, M., Yu, Y., Fang, X., Zhou, M., et al. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03048-2 · Cited by 23

Succinate-Directed Approaches for Warburg Effect-Targeted Cancer Management, an Alternative to Current Treatments?

Casas-Benito, A., Martínez-Herrero, S., & Martínez, A. (2023) · Cancers · doi:10.3390/cancers15102862 · Cited by 26

Outcomes of hypothalamic oxytocin neuron-driven cardioprotection after acute myocardial infarction

Schunke, K. J., Rodriguez, J., Dyavanapalli, J., Schloen, J., Wang, X., Escobar, J. B., Kowalik, G., Cheung, E. C., Ribeiro, C., Russo, R., et al. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-01013-1 · Cited by 26

Is the peroxisome proliferator-activated receptor gamma a putative target for epilepsy treatment? Current evidence and future perspectives

Senn, L., Costa, A., Avallone, R., Socała, K., Właź, P., & Biagini, G. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108316 · Cited by 23

Sirtuins (SIRTs) As a Novel Target in Gastric Cancer

Poniewierska-Baran, A., Warias, P., & Zgutka, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315119 · Cited by 22

Mitochondrial impairment, decreased sirtuin activity and protein acetylation in dorsal root ganglia in Friedreich Ataxia models

Sanz‐Alcázar, A., Britti, E., Delaspre, F., Medina‐Carbonero, M., Pazos-Gil, M., Tamarit, J., Ros, J., & Cabiscol, E. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05064-4 · Cited by 21

USEFULNESS OF Β-HYDROXY-Β-METHYLBUTYRATE (HMB) SUPPLEMENTATION IN DIFFERENT SPORTS: AN UPDATE AND PRACTICAL IMPLICATIONS.

Albert, F. J., Morente-Sánchez, J., Ortega, F. B., Castillo, M. J., & Gutiérrez, Á. (2015) · PubMed · doi:10.3305/nh.2015.32.1.9101 · Cited by 23

Characterizing Sirtuin 3 Deacetylase Affinity for Aldehyde Dehydrogenase 2

Harris, P. S., Gomez, J., Backos, D. S., & Fritz, K. S. (2017) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6b00315 · Cited by 22

Isosteviol sodium protects the cardiomyocyte response associated with the SIRT1/PGC‐1α pathway

Mei, Y., Liu, B., Su, H., Zhang, H., Liu, F., Ke, Q., Sun, X., & Tan, W. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15715 · Cited by 21

Potential relationship between Sirt3 and autophagy in ovarian cancer (Review)

Shi, Y., He, R., Yu, Y., He, Y., Zhan, L., & Wei, B. (2020) · Oncology Letters · doi:10.3892/ol.2020.12023 · Cited by 21

Patulin triggers NRF2-mediated survival mechanisms in kidney cells

Pillay, Y., Phulukdaree, A., Nagiah, S., & Chuturgoon, A. A. (2015) · Toxicon · doi:10.1016/j.toxicon.2015.03.004 · Cited by 21

Endurance training and chronic intermittent hypoxia modulate in vitro salicylate-induced hepatic mitochondrial dysfunction

Ascensão, A. A. M. R., Gonçalves, I. O., Lumini‐Oliveira, J., Marques‐Aleixo, I., Passos, E., Rocha‐Rodrigues, S., Machado, N. G., Moreira, A. C., Oliveira, P. J., Torrella, J. R., et al. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.10.007 · Cited by 21

Grape seed proanthocyanidins prevent H 2 O 2 ‐induced mitochondrial dysfunction and apoptosis via SIRT 1 activation in embryonic kidney cells

Rigotti, M., Cerbaro, A. F., Silva, I. D. R., Agostini, F., Branco, C. S., Moura, S., & Salvador, M. M. (2020) · Journal of Food Biochemistry · doi:10.1111/jfbc.13147 · Cited by 21

Theaflavin 3, 3 ′‐Digallate Delays Ovarian Aging by Improving Oocyte Quality and Regulating Granulosa Cell Function

He, J. H., Yao, G., He, Q., Zhang, T., Fan, H., Bai, Y., Zhang, J., Yang, G., Xu, Z., Hu, J., et al. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/7064179 · Cited by 20

Soy isoflavones administered to rats from weaning until sexual maturity affect ovarian follicle development by inducing apoptosis

Wang, W., Sun, Y., Liu, J., Li, Y., Li, H., Xiao, S., Weng, S., & Zhang, W. (2014) · Food and Chemical Toxicology · doi:10.1016/j.fct.2014.07.010 · Cited by 20

Effects of nutrient restriction and arginine treatment on oxidative stress in the ovarian tissue of ewes during the luteal phase

Guo, Y., Nie, H., Xu, C., Zhang, G., Sun, L., Zhang, T., Wang, Z., Xu, F., You, P., & Wang, F. (2018) · Theriogenology · doi:10.1016/j.theriogenology.2018.02.016 · Cited by 22

Effect of breed on the expression of Sirtuins (Sirt1-7) and antioxidant capacity in porcine brain

Ren, Y., Shan, T., Zhu, L., Wu, T., Guo, J., & Wang, Y. (2013) · animal · doi:10.1017/s175173111300164x · Cited by 19

Cooperative effects of SIRT1 and SIRT2 on APP acetylation

Li, N., Bai, N., Zhao, X., Cheng, R., Wu, X., Jiang, B., Li, X., Xue, M., Xu, H., Guo, Q., et al. (2023) · Aging Cell · doi:10.1111/acel.13967 · Cited by 19

Dietary fat supplementation relieves cold temperature-induced energy stress through AMPK-mediated mitochondrial homeostasis in pigs

He, W., Liu, X., Feng, Y., Ding, H., Sun, H., Li, Z., & Shi, B. (2024) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-024-01014-7 · Cited by 22

Dual modifying of MAVS at lysine 7 by SIRT3-catalyzed deacetylation and SIRT5-catalyzed desuccinylation orchestrates antiviral innate immunity

Liu, X., Zhu, C., Jia, S., Deng, H., Tang, J., Sun, X., Zeng, X., Chen, X., Wang, Z., Liu, W., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2314201121 · Cited by 20

An Update on Lysine Deacylases Targeting the Expanding “Acylome”

Olsen, C. A. (2013) · ChemMedChem · doi:10.1002/cmdc.201300421 · Cited by 20

Importance of Riboflavin Kinase in the Pathogenesis of Stroke

Zou, Y., Zhang, X., Su, F., & Liu, X. (2012) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2012.00379.x · Cited by 19

A sirtuin activator and an anti-inflammatory molecule—multifaceted roles of adjudin and its potential applications for aging-related diseases

Xia, W., & Geng, K. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.07.020 · Cited by 19

Transcriptome Profiling Reveals a Novel Mechanism of Antiviral Immunity Upon Sacbrood Virus Infection in Honey Bee Larvae (Apis cerana)

Guo, Y., Zhang, Z., Zhuang, M., Wang, L., Li, K., Yao, J., Yang, H., Huang, J., Hao, Y., Fan, Y., et al. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.615893 · Cited by 19

Regulation of the mitogen-activated protein kinase kinase (MEK)-1 by NAD+-dependent deacetylases

Yeung, F., Ramsey, C. S., Popko-Ścibor, A. E., Allison, D. F., Gray, L., Shin, M., Kumar, M., Li, D., McCubrey, J. A., & Mayo, M. W. (2014) · Oncogene · doi:10.1038/onc.2014.39 · Cited by 17

Influence of anaerobic and aerobic exercise on age-related pathways in skeletal muscle

Navas‐Enamorado, I., Bernier, M., Brea‐Calvo, G., & de Cabo, R. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.04.005 · Cited by 21

Competitive regulation by transcription factors and DNA methylation in the bovine SIRT5 promoter: Roles of E2F4 and KLF6

Hong, J., Wang, X., Mei, C., & Zan, L. (2018) · Gene · doi:10.1016/j.gene.2018.10.052 · Cited by 18

Understanding oocyte ageing: can we influence the process as clinicians?

Homer, H. A. (2021) · Current Opinion in Obstetrics & Gynecology · doi:10.1097/gco.0000000000000708 · Cited by 18

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The Pan-Sirtuin Inhibitor MC2494 Regulates Mitochondrial Function in a Leukemia Cell Line

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Intermittent fasting along with hydroalcoholic extract of Centella-asiatica ameliorates sub-acute hypoxia-induced ischemic stroke in adult zebrafish

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Comprehensive transcriptome-based characterization of differentially expressed genes involved in microsporogenesis of radish CMS line and its maintainer

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Mitochondrial Adaptations in Aged Skeletal Muscle: Effect of Exercise Training

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Alterations on growth and cell organization of Giardia intestinalis trophozoites after treatment with KH-TFMDI, a novel class III histone deacetylase inhibitor

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Distinctive Features of Orbital Adipose Tissue (OAT) in Graves’ Orbitopathy

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Hsa_circRNA_0045861 promotes renal injury in ureteropelvic junction obstruction via the microRNA-181d-5p/sirtuin 1 signaling axis

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lncRNA TUG1 as Potential Novel Biomarker for Prognosis of Cardiovascular Diseases

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Reactive Oxygen Species: Friends and Foes of Signal Transduction

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