The role of sirtuins in cellular homeostasis

Mammalian Sirtuins: Biological Insights and Disease Relevance

Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085

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

NAD+ Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the Nucleus

Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648

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

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

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

SIRT1 and other sirtuins in metabolism

Chang, H.-C., & Guarente, L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.12.001 · Cited by 1,157

The sirtuin SIRT6 regulates lifespan in male mice

Kanfi, Y., Naiman, S., Amir, G., Peshti, V., Zinman, G., Nahum, L., Bar-Joseph, Z., & Cohen, H. Y. (2012) · Nature · doi:10.1038/nature10815 · Cited by 1,059

The many faces of insulin-like peptide signalling in the brain

Fernandez, A. M., & Torres-Alemán, I. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3209 · Cited by 872

Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes

Pandey, R. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf660 · Cited by 783

Biomimetic Molecular Clamp Nanopores for Simultaneous Quantifications of NAD + and NADH

Liu, X., Feng, W., Yao, F., Zhang, J., Rauf, A., Chen, T., Shi, X., Qiao, X., Ma, L., Yu, S., et al. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c00986 · Cited by 16

Association of sirtuins (SIRT1-7) with lung and intestinal diseases

Chen, Y., Zhou, D., Feng, Y., Li, B., Cui, Y., Chen, G., & Li, N. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04462-9 · Cited by 16

Role of epigenetics in corneal health and disease

Sood, S., Tiwari, A., Sangwan, J., Vohra, M., Sinha, N. R., Tripathi, R., Sangwan, V., & Mohan, R. R. (2024) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2024.101318 · Cited by 15

SIRT1 Deacetylates SC35 and Suppresses Its Function in Tau Exon 10 Inclusion

Yin, X., Jiang, X., Wang, J., Qian, S., Liu, F., & Qian, W. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170418 · Cited by 15

The possible role of sirtuins in male reproduction

Loganathan, C., Kannan, A., Panneerselvam, A., Mariajoseph-Antony, L. F., Kumar, S. A., Kumarasamy, A., & Prahalathan, C. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04116-2 · Cited by 14

Mitochondria and Epigenetic Regulation: Bidirectional Crosstalk and Emerging Mitochondria-Targeted Degron Tools

Xu, Y., Jian, X., Shi, L., Shock, L. S., Chen, L., Chow, L. T., & Wang, H. (2026) · Cells · doi:10.3390/cells15020095 · Cited by 13

The Role of Sirtuins in Osteogenic Differentiation of Vascular Smooth Muscle Cells and Vascular Calcification

Wang, S., & Hu, S. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.894692 · Cited by 13

Effect of acute cold exposure on cardiac mitochondrial function: role of sirtuins

Mohan, M. S., Aswani, S. S., Aparna, N. S., Boban, P. T., Sudhakaran, P. R., & Saja, K. (2023) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04656-1 · Cited by 13

The Role of NAD+ in Metabolic Regulation of Adipose Tissue: Implications for Obesity-Induced Insulin Resistance

Ruskovska, T., & Bernlohr, D. (2023) · Biomedicines · doi:10.3390/biomedicines11092560 · Cited by 13

Molecular Challenges and Opportunities in Climate Change-Induced Kidney Diseases

Ceron, E. L., Pherez-Farah, A., Krishnan‐Sivadoss, I., & Guerrero-Beltrán, C. E. (2024) · Biomolecules · doi:10.3390/biom14030251 · Cited by 13

Cuscuta chinensis flavonoids alleviate ovarian damage in offspring female mice induced by BPA exposure during pregnancy by regulating the central carbon metabolism pathway

Zhao, Q., Liu, Y., Chuo, Y., Wang, X., Jiao, Y., Shi, W., & Bao, Y. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.116253 · Cited by 14

Natural Compounds and PCL Nanofibers: A Novel Tool to Counteract Stem Cell Senescence

Bellu, E., Cruciani, S., Garroni, G., Balzano, F., Satta, R. R., Montesu, M. A., Fadda, A., Mulas, M., Sarais, G., Bandiera, P., et al. (2021) · Cells · doi:10.3390/cells10061415 · Cited by 13

Hyperbaric oxygen via mediating SIRT1‐induced deacetylation of HMGB1 improved cReperfusion inj/reperfusion injury

Zhao, P., Xu, S., Huang, Z., Jiang, G., Deng, P., & Zhang, Y. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15458 · Cited by 13

Neurotrophic fragments as therapeutic alternatives to ameliorate brain aging

Treviño, S., Flores, I., & Díaz, A. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.331867 · Cited by 13

Axonal mRNA localization and local translation in neurodegenerative disease

Li, H., Wang, Y., Zhang, Y., Shen, M., Li, H.-Y., Yu, Z., & Chen, G. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.308074 · Cited by 12

The Association between Clusterin Sialylation Degree and Levels of Oxidative–Antioxidant Balance Markers in Seminal Plasmas and Blood Sera of Male Partners with Abnormal Sperm Parameters

Janiszewska, E., Kokot, I., Kmieciak, A., Stelmasiak, Z., Gilowska, I., Faúndez, R., & Kratz, E. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810598 · Cited by 12

Epigenetic Regulation by Dietary Restriction: Part II.

Ng, G. Y.-Q., Fann, D. Y., Jo, D., Sobey, C. G., & Arumugam, T. V. (2019) · PubMed · Cited by 12

The Wnt–NAD+ axis in cancer, aging, and tissue regeneration

Lamprecht, J., Sanad, S. M., Kusumbe, A. P., & Habib, S. J. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.07.006 · Cited by 14

Oral administration of crocin-loaded solid lipid nanoparticles inhibits neuroinflammation in a rat model of epileptic seizures by activating SIRT1 expression

Kakebaraei, S., Gholami, M., Nasta, T. Z., Arkan, E., Bahrehmand, F., Fakhri, S., & Jalili, C. (2024) · Research in Pharmaceutical Sciences · doi:10.4103/rps.rps_68_24 · Cited by 11

Dietary fatty acids as nutritional modulators of sirtuins: a systematic review

Caldas, A. P. S., Rocha, D. M. U. P., Bressan, J., & Hermsdorff, H. H. M. (2020) · Nutrition Reviews · doi:10.1093/nutrit/nuaa007 · Cited by 11

The enigmatic role of SIRT2 in the cardiovascular system: Deciphering its protective and detrimental actions to unlock new avenues for therapeutic intervention

Alhasaniah, A. H., Alissa, M., Elsaid, F. G., Alsugoor, M. H., Alqahtani, M. S., Alessa, A., Jambi, K., Albakri, G. S., Albaqami, F. M. K., & Bennett, E. (2024) · Current Problems in Cardiology · doi:10.1016/j.cpcardiol.2024.102929 · Cited by 10

Alzheimer’s Disease: A Review of Molecular Mechanisms and Therapeutic Implications by Targeting Sirtuins, Caspases, and GSK-3

Pandya, K., Roul, K., Tripathi, A., Belemkar, S., Sinha, A., Erol, M., & Kumar, D. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00207 · Cited by 11

PEP-1-SIRT2-induced matrix metalloproteinase-1 and -13 modulates type II collagen expression via ERK signaling in rabbit articular chondrocytes

Eo, S.-H., Choi, S. Y., & Kim, S. J. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.09.024 · Cited by 10

Molecular and functional characteristics of megakaryocytes and platelets in aging

Esparza, O., Higa, K. C., & Davizon‐Castillo, P. (2020) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000601 · Cited by 11

Combined Inhibition of Specific Sirtuins as a Potential Strategy to Inhibit Melanoma Growth

Singh, C. K., Panackal, J. E., Siddiqui, S., Ahmad, N., & Nihal, M. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.591972 · Cited by 10

Relationship between an indel mutation within the SIRT4 gene and growth traits in Chinese cattle

Zhang, Q., Jin, Y., Jiang, F., Cheng, H., Wang, Y., Lan, X., & Song, E. (2019) · Animal Biotechnology · doi:10.1080/10495398.2018.1520716 · Cited by 10

Sirtuins as Players in the Signal Transduction of Citrus Flavonoids

Lombardo, G. E., Russo, C., Maugeri, A., & Navarra, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25041956 · Cited by 9

Assay technologies facilitating drug discovery for ADP‐ribosyl writers, readers and erasers

Glumoff, T., Sowa, S. T., & Lehtiö, L. (2021) · BioEssays · doi:10.1002/bies.202100240 · Cited by 9

Characterization and mutational analysis of a nicotinamide mononucleotide deamidase from Agrobacterium tumefaciens showing high thermal stability and catalytic efficiency

Martínez-Moñino, A. B., Perez, R. Z., García-Saura, A. G., Gil-Ortiz, F., Pérez‐Gilabert, M., & Sánchez‐Ferrer, Á. (2017) · PLoS ONE · doi:10.1371/journal.pone.0174759 · Cited by 9

Sirtuins in Brain and Neurodegenerative Disease

Szegő, É. M., Outeiro, T. F., & Kazantsev, A. G. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00013-7 · Cited by 9

Age-related epigenetic drift deregulates SIRT6 expression and affects its downstream genes in human peripheral blood mononuclear cells

Owczarz, M., Połosak, J., Domaszewska-Szostek, A., Kołodziej, P., Kuryłowicz, A., & Puzianowska‐Kuźnicka, M. (2020) · Epigenetics · doi:10.1080/15592294.2020.1780081 · Cited by 10

SIRT1 and thrombosis

Bettiol, A., Urban, M. L., Emmi, G., Galora, S., Argento, F. R., Fini, E., Borghi, S., Bagni, G., Mattioli, I., Prisco, D., et al. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1325002 · Cited by 9

DeepSIRT: A deep neural network for identification of sirtuin targets and their subcellular localizations

Shah, S. M. A., Taju, S. W., Dlamini, B. B., & Ou, Y. (2021) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2021.107514 · Cited by 8

Potential Application of Plant-Derived Compounds in Multiple Sclerosis Management

Woodfin, S., Hall, S., Ramerth, A., Chapple, B. E., Fausnacht, D. W., Moore, W., Alkhalidy, H., & Liu, D. (2024) · Nutrients · doi:10.3390/nu16172996 · Cited by 8

SIRT5-mediated GLS and GDH desuccinylation attenuates the autophagy of bovine mammary epithelial cells induced by ammonia

Yang, H., Gao, S., Lu, G., He, J., Dong, J., Zhang, X., Liu, L., Zhong, K., Zha, G., Han, L., et al. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111570 · Cited by 7

The role of SIRT1 in the development of gastrointestinal tumors

Zhang, Y., Zhou, X., Zhai, J., Ma, J., & Zhang, S. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1606530 · 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

Knockdown of Quinolinate Phosphoribosyltransferase Results in Decreased Salicylic Acid-Mediated Pathogen Resistance in Arabidopsis thaliana

Li, S., Ding, H., Deng, Y., & Zhang, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168484 · Cited by 7

Browning of Adipose Tissue and Sirtuin Involvement

Favero, G., Krajčíková, K., Bonomini, F., Rodella, L. F., Tomečková, V., & Rezzani, R. (2018) · InTech eBooks · doi:10.5772/intechopen.74760 · Cited by 7

Far from Inert: Membrane Lipids Possess Intrinsic Reactivity That Has Consequences for Cell Biology

Sanderson, J. M. (2020) · BioEssays · doi:10.1002/bies.201900147 · Cited by 7

Trichomes and naphthoquinones protect Streptocarpus dunnii Hook.f. against environmental stresses

Hook, I., Sheridan, H., & Reid, C. (2018) · South African Journal of Botany · doi:10.1016/j.sajb.2018.09.016 · Cited by 7

Advances of SIRT4 in cancer metabolism and therapy

Yue, X., Shi, Y., & Luo, Q. (2023) · Pediatric Discovery · doi:10.1002/pdi3.17 · Cited by 6

A Novel Pro-Inflammatory Mechanosensing Pathway Orchestrated by the Disintegrin Metalloproteinase ADAM15 in Synovial Fibroblasts

Janczi, T., Meier, F. M. P., Fehrl, Y., Kinne, R. W., Böhm, B. B., & Burkhardt, H. (2021) · Cells · doi:10.3390/cells10102705 · Cited by 6

Implications of altered sirtuins in metabolic regulation and oral cancer

Xu, Q., Xin, Y., Wang, H., Sun, Y., Chen, C., & Zhang, J. (2023) · PeerJ · doi:10.7717/peerj.14752 · Cited by 6

Future Demands Concerning the Epigenetic Relevance of Melatonin and the Circadian System in Gerontology

Hardeland, R. (2017) · Journal of Geriatric Medicine and Gerontology · doi:10.23937/2469-5858/1510036 · 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

Unraveling the Role of AtSRT2 in Energy Metabolism, Stress Responses, and Gene Expression during Osmotic Stress in Arabidopsis thaliana

Obrecht, A., & Paneque, M. (2024) · Plants · doi:10.3390/plants13050711 · Cited by 5

The curious case of mitochondrial sirtuin in rewiring breast cancer metabolism: Mr Hyde or Dr Jekyll?

Tharayil, J. S., Kandettu, A., & Chakrabarty, S. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167691 · Cited by 5

Redox state and the sirtuin deacetylases are major factors that regulate the acetylation status of the stress protein NQO1

Siegel, D. M., Harris, P. S., Michel, C. R., de Cabo, R., Fritz, K. S., & Ross, D. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1015642 · Cited by 5

Detection of InDel variations within seven candidate genes and their associations with phenotypic traits in three cattle breeds

Peng, K., Zhang, G., Yu, T. Y., Cao, Y., Yu, Y., Chen, H., Lei, C., Lan, X., & Zhao, Y. (2019) · Animal Biotechnology · doi:10.1080/10495398.2019.1620258 · Cited by 5

Downregulation of forkhead box O1 (FOXO1) acetylation ameliorates cognitive dysfunction by inhibiting endoplasmic reticulum stress‐regulated neuronal apoptosis in APP/PS1 transgenic mice

Zhang, N., Zhao, Z., Chen, X., Yao, H., Zhu, M., Ma, S., Wang, H., Yin, X., Zhou, Y., Zheng, C., et al. (2025) · Neuroprotection/Neuroprotection (Chichester, England. Print) · doi:10.1002/nep3.66 · Cited by 4

Aberrant Caspase Activation in Laminin-α2-Deficient Human Myogenic Cells is Mediated by p53 and Sirtuin Activity

Yoon, S., Beermann, M. L., Yu, B., Shao, D., Bachschmid, M. M., & Miller, J. B. (2017) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-170262 · Cited by 4

Comments on the history of medical–biological studies of aging, the birth of scientific gerontology

Robert, L., & Labat‐Robert, J. (2016) · Current Research in Translational Medicine · doi:10.1016/j.retram.2016.08.004 · Cited by 4

Sirtuins as mediators and targets of arsenic toxicity: unraveling signaling pathway crosstalk

El-Mahrouk, S. R., & El‐Kadi, A. O. S. (2025) · Archives of Toxicology · doi:10.1007/s00204-025-04158-1 · Cited by 3

Supplementation of Nicotinic Acid and Its Derivatives Up-Regulates Cellular NAD+ Level Rather than Nicotinamide Derivatives in Cultured Normal Human Epidermal Keratinocytes

Oyama, T., Yamamoto, T., Kameda, T., Kamiya, T., Abe, H., Abe, T., & Tanuma, S. (2024) · Life · doi:10.3390/life14030413 · Cited by 4

Novel incubation‐free approaches to determine phytoplankton net primary productivity, growth, and biomass based on flow cytometry and quantification of ATP and NAD(H)

Jones, B., Halsey, K. H., & Behrenfeld, M. J. (2017) · Limnology and Oceanography Methods · doi:10.1002/lom3.10213 · Cited by 3

Possible Therapeutic Potential of Flavonoids and Phenolic Acids from Honey in Age-Related Neurodegenerative Diseases Via Targeting NAD+ Degradation

Khan, A., Alshahrani, S., Arafah, A. M., Qamar, W., Shoaib, A., Wali, A. F., Amin, I., Alqahtani, S. S., & Rehman, M. U. (2020) · Springer eBooks · doi:10.1007/978-981-15-7305-7_2 · Cited by 3

Summa of Erasers of Histone Acetylation with Special Emphasis on Classical Histone Deacetylases (HDACs)

Ganai, S. A. (2020) · Springer eBooks · doi:10.1007/978-981-15-8179-3_3 · Cited by 3

Combined Metformin and Baricitinib Therapy Attenuates Inflammation in STZ ‐Induced Diabetic Rats via AMPK / JAK – STAT Pathway Crosstalk

Allahyari, M., Marjani, A., Jazi, M. S., & Jahanshahi, M. (2025) · Endocrinology Diabetes & Metabolism · doi:10.1002/edm2.70101 · Cited by 3

SIRT3 attenuates AGEs-induced senescence in human granulosa cells through enhancing mitophagy

Li, S., Tang, M., Zhu, S., Zhang, Z., Cao, Y., & Xue, R. (2026) · Cell Biology and Toxicology · doi:10.1007/s10565-026-10138-7 · Cited by 2

Decreased sirtuin 4 levels promote cellular proliferation and invasion in papillary thyroid carcinoma

Lee, H., Hah, Y., Cheon, S. Y., Won, S. J., Yim, C. D., Ryu, S., Lee, S. J., Seo, J., & Park, J. J. (2024) · European Thyroid Journal · doi:10.1530/etj-24-0079 · Cited by 2

Bioluminescence assay of lysine deacylase sirtuin activity

Scoyk, A. V., Antelope, O., Franzini, A., Ayer, D. E., Peterson, R. T., Pomicter, A. D., Owen, S. C., & Deininger, M. W. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.10.006 · Cited by 3

TFAP2B governs the regulation of SIRT1 to inhibit osteoclast-induced bone destruction

Wen, L., Zeng, X., Lin, Z., Chen, P., Zhao, D., & Zeng, X. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151410 · Cited by 2

Solanesol Mediated SIRT-1 Activation Prevents Neurobehavioral and Neurochemical Defects in Ouabain-Induced Experimental Model of Bipolar Disorder in RatsPreprint

Rajkhowa, B., Mehan, S., Sethi, P., Bhalla, S., Prajapati, A., Kumar, S., Alshammari, A., Alharbi, M., Alsuhaymi, N., Alghamdi, A., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-1060160/v1 · Cited by 2

Sirtuin 3, a mitochondrial metabolic enzyme, links the mitochondrial function to neurophysiology in depression

Chen, C.-Y., Wang, Y., Liu, L., & Zhang, Y. (2025) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2025.111563 · Cited by 1

Resveratrol: From biochemical mechanisms to therapeutic and industrial potential

MERHAN, O., & Kocamaz, D. (2026) · Studies in natural products chemistry · doi:10.1016/b978-0-443-51074-8.00008-5 · Cited by 1

Atrial Cardiomyopathy-associated Arrhythmia and the Impact of Sirtuin Signaling Pathway: A Narrative Review

Lee, W., Fang, H., Chen, H., Lin, Y.-S., Chen, M., & Liu, P. Y. (2025) · Current Vascular Pharmacology · doi:10.2174/0115701611336403250122100104 · Cited by 1

Solanesol Mediated SIRT-1 Signaling Activation Prevents Neurobehavioral and Neurochemical Defects in Ouabain-induced Experimental Model of Bipolar Disorder in RatsPreprint

Rajkhowa, B., & Mehan, S. (2021) · Research Square · doi:10.21203/rs.3.rs-735926/v1 · Cited by 1

MicroRNA-9 represses sirtuin 1 (SIRT1) in human keratinocytes

Farrer, D., Jc, R., & Ross, K. (2016) · Liverpool John Moores University · doi:10.21276/sb.2016.2.9.2

Sirtuin 7 Promotes Mesenchymal to Epithelial Transition by β-Catenin Redistribution and Stabilization

Kiran, S., Kiran, M., & Ramakrishna, G. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00740

Design of Mitochondrial Targeting Peptide-based SIRT1 Activators

Ma, C. (2021) · TSpace (University of Toronto)

Immunometabolism and Organ Transplantation

Domínguez-Amorocho, O. A., de Lima, J., & Câmara, N. O. S. (2021) · Springer eBooks · doi:10.1007/978-3-030-86684-6_13

Sirtuins

Zwergel, C., Tomaselli, D., & Mai, A. (2021) · Springer eBooks · doi:10.1007/978-3-030-57401-7_10044

PRMT5 regulates the NAD-SIRT1-p53 signal axis by affecting the methylation of CD38 at R58 to promote malignant tumor cell proliferationPreprint

Zhou, Y., Liang, L., Yue, C., Li, W., Gao, M., Zeng, F., He, J., He, Z., Jin, X., Liao, Q., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1376204/v1

Sirtuins

Zwergel, C., Tomaselli, D., & Mai, A. (2021) · Springer eBooks · doi:10.1007/978-3-030-21573-6_10044-1

Papel da Sirtuina 1 na ativação e diferenciação das células T CD4>sup<+>/sup< em um modelo murino de obesidade e transplante

Domínguez-Amorocho, O. A. (2022) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.42.2022.tde-16052022-092324

Peer Review #3 of "Implications of altered sirtuins in metabolic regulation and oral cancer (v0.2)"

(2023) · PeerJ · doi:10.7287/peerj.14752v0.2/reviews/3

Peer Review #3 of "Implications of altered sirtuins in metabolic regulation and oral cancer (v0.1)"

(2023) · PeerJ · doi:10.7287/peerj.14752v0.1/reviews/3

Peer Review #1 of "Implications of altered sirtuins in metabolic regulation and oral cancer (v0.1)"

(2023) · PeerJ · doi:10.7287/peerj.14752v0.1/reviews/1

Peer Review #2 of "Implications of altered sirtuins in metabolic regulation and oral cancer (v0.1)"

(2023) · PeerJ · doi:10.7287/peerj.14752v0.1/reviews/2

Peer Review #2 of "Implications of altered sirtuins in metabolic regulation and oral cancer (v0.2)"

(2023) · PeerJ · doi:10.7287/peerj.14752v0.2/reviews/2

Evaluating the Effect of Resveratrol on SIRT1 with Different Peptide Substrates

Hur, Y. (2023) · doi:10.31979/etd.f9mw-4y9r

Mitochondria in Endothelial Dysfunction and The Relation to Cardiovascular Disease

Poznyak, A. V., Khotina, V. A., Sukhorukov, V. N., Sobenin, I. A., Popov, M. A., Postnov, A. Y., & Orekhov, A. A. N. (2024) · Journal of Angiotherapy · doi:10.25163/angiotherapy.859557

SIRT5-mediated GLS and GDH desuccinylation attenuates autophagy in MAC-T cells induced by ammoniaPreprint

Yang, H., Gao, S., Lu, G., He, J., Dong, J., Zhang, X., Liu, L., Zhong, K., Zha, G., Han, L., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.26.609685

Bioinformatics-based analysis of nicotinamide adenine dinucleotide metabolism-related genes to predict immune status and prognosis for head and neck squamous cell carcinoma patients

Guan, Z., Gu, X., & Zheng, L. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1609175

Sirtuin expression in skin fibroblasts: pharmacomodulatory effect of quercetin

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