SIRT6 Recruits SNF2H to DNA Break Sites, Preventing Genomic Instability through Chromatin Remodeling

The DNA Damage Response: Making It Safe to Play with Knives

Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368

Playing the End Game: DNA Double-Strand Break Repair Pathway Choice

Chapman, J. R., Taylor, M. R. G., & Boulton, S. J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.029 · Cited by 1,728

53BP1 Inhibits Homologous Recombination in Brca1-Deficient Cells by Blocking Resection of DNA Breaks

Bunting, S. F., Callén, E., Wong, N., Chen, H.-T., Polato, F., Gunn, A., Bothmer, A., Feldhahn, N., Fernandez-Capetillo, O., Cao, L., et al. (2010) · Cell · doi:10.1016/j.cell.2010.03.012 · Cited by 1,671

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

Recent progress in the biology and physiology of sirtuins

Finkel, T., Deng, C., & Mostoslavsky, R. (2009) · Nature · doi:10.1038/nature08197 · Cited by 1,506

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 Histone Deacetylase Sirt6 Regulates Glucose Homeostasis via Hif1α

Zhong, L., D'Urso, A., Toiber, D., Sebastian, C., Henry, R. E., Vadysirisack, D. D., Guimaraes, A., Marinelli, B., Wikstrom, J. D., Nir, T., et al. (2010) · Cell · doi:10.1016/j.cell.2009.12.041 · Cited by 1,001

SIRT6 Promotes DNA Repair Under Stress by Activating PARP1

Mao, Z., Hine, C., Tian, X., Van Meter, M., Au, M., Vaidya, A., Seluanov, A., & Gorbunova, V. (2011) · Science · doi:10.1126/science.1202723 · Cited by 867

CBP/p300-mediated acetylation of histone H3 on lysine 56

Das, C., Lucia, M. S., Hansen, K. C., & Tyler, J. K. (2009) · Nature · doi:10.1038/nature07861 · Cited by 698

Sirtuins and the prevention of immunosenescence

Lasigliè, D. (2021) · Vitamins and hormones · doi:10.1016/bs.vh.2020.12.011 · Cited by 5

Association between SIRT6 Methylation and Human Longevity in a Chinese Population

Tang, X. A., Wei, Y., Wang, J., Chen, S., Cai, J., Tang, J., Xu, X., Long, B., Yu, G., Zhang, Z., et al. (2020) · Public Health Genomics · doi:10.1159/000508832 · Cited by 4

Inhibition of Sirt6 suppresses tumor growth by inducing G1/S phase arrest in renal cancer cells.

Ding, Y., Wu, S., Huo, Y., Chen, X., Chai, L., Wang, Y., Wang, X., Zhu, G., & Jiang, W. (2019) · Europe PMC (PubMed Central) · Cited by 4

Efeito Cardioprotetor da Suplementação Materna com Resveratrol sobre a Toxicidade Induzida por Doxorrubicina em Cardiomiócitos de Neonatos

Brito, V. B., Nascimento, L. V. M., Moura, D. J., & Saffi, J. (2021) · Arquivos Brasileiros de Cardiologia · doi:10.36660/abc.20200752 · 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

ZDHHC20-mediated S-palmitoylation of KAP1/TRIM28 promotes DNA damage repair

Liu, Z., Wang, H., Han, Y., Chen, Y., Wang, Y., Zhang, S., Mo, Y., Wang, C., Xiao, M., & Xu, B. (2025) · Oncogene · doi:10.1038/s41388-025-03604-9 · Cited by 3

Ginsenoside Rg5 mitigates tenocyte death via SIRT6/autophagy-dependent signaling in an aging model

Lim, D. S., Ahn, S. H., Cho, W., Gwon, H. J., Ko, J. H., Pyo, M. K., El‐Aty, A. M. A., Hong, S. A., Shin, J. W., Jeong, J. H., et al. (2025) · Journal of Ginseng Research · doi:10.1016/j.jgr.2025.11.009 · Cited by 3

Mammalian MutY Homolog (MYH or MUTYH) is Critical for Telomere Integrity under Oxidative Stress

Gupta, A., Hwang, B., Benyamien-Roufaeil, D. S., Jain, S., Liu, S., Gonzales, R., Brown, R. A., Zalzman, M., & Lu, A.-L. (2022) · OBM Geriatrics · doi:10.21926/obm.geriatr.2202196 · Cited by 3

Potential biomarkers of early diagnosis of Alzheimer’s disease

Bogolepova, A. N., Makhnovich, E. V., Коваленко, Е. А., & Osinovskaya, N. A. (2022) · S S Korsakov Journal of Neurology and Psychiatry · doi:10.17116/jnevro20221220917 · Cited by 3

The Impact of NAD Bioavailability on DNA Double-Strand Break Repair Capacity in Human Dermal Fibroblasts after Ionizing Radiation

Svetlova, M., Solovjeva, L., Kropotov, A., & Nikiforov, A. A. (2023) · Cells · doi:10.3390/cells12111518 · Cited by 3

Sirtuins and Their Implications in the Physiopathology of Gestational Diabetes Mellitus

Zgutka, K., Tkacz, M., Grabowska, M., Mikołajek-Bedner, W., & Tarnowski, M. (2025) · Pharmaceuticals · doi:10.3390/ph18010041 · Cited by 5

Rola sirtuin w naprawie DNA

Kciuk, M., & Kontek, R. (2020) · Postępy Biochemii · doi:10.18388/pb.2020_319 · Cited by 3

Nuclear translocation of p19INK4d in response to oxidative DNA damage promotes chromatin relaxation

Sonzogni, S. V., Ogara, M. F., Castillo, D., Sirkin, P. F., Radicella, J. P., & Cánepa, E. T. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-014-2205-1 · Cited by 3

Quercetin activates the SIRT6-Nrf2 axis during oxidative stress, modulating ageing-associated markers in healthy menPreprint

Juan, C. G., Briški, N. Š., Volpe-Zanutto, F., Matchett, K., & Davison, G. W. (2025) · medRxiv · doi:10.1101/2025.10.31.25338366 · Cited by 4

Mechanisms of the Antiproliferative Effects of SIRT6 Inhibition in Melanoma: A Multi-Omics Analysis

Aldrete, K. B. A., Waseem, D., Garcia‐Peterson, L. M., Ndiaye, M. A., Nam, J. H., & Ahmad, N. (2026) · Cancers · doi:10.3390/cancers18040590 · Cited by 2

SIRT6 Regulates Protein Synthesis and Folding Through Nucleolar Remodeling

Stein, D., Gallrein, C., Portillo, M., Kaluski‐Kopach, S., García-Venzor, A., Lachberg, Y., Eremenko, E., Smirnov, D., Dror, S., Einav, M., et al. (2026) · Aging Cell · doi:10.1111/acel.70384 · Cited by 7

The BRCA1-A complex restricts replication fork reversal-dependent DNA repair in ATM deficient cells

Datta, A., Jackson, J., Morozov, Y. I., Qiu, J., Vindigni, A., & Greenberg, R. A. (2026) · Nature Communications · doi:10.1038/s41467-026-75271-7 · Cited by 2

Characterization and implementation of a miniature X-ray system for live cell microscopy

Prajapati, S., Locatelli, M., Sawyer, C., Holmes, J., Bonin, K., Black, P., & Vidi, P. (2021) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2021.111772 · 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

The Controversy Around Sirtuins and Their Functions in Aging

Sun, Y., & Dang, W. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-801816-3.00017-0 · Cited by 2

Multitasking Roles of the Mammalian Deacetylase SIRT6

Hassanieh, S., & Mostoslavsky, R. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00009-5 · Cited by 2

A sirtuin's role in preventing senescence by protecting ribosomal DNA

Etchegaray, J., & Mostoslavsky, R. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.h118.004040 · Cited by 2

Deacetylation of a deacetylase drives the DNA damage response

Ng, R., & Huen, M. S. Y. (2020) · Genome Instability & Disease · doi:10.1007/s42764-020-00018-7 · Cited by 2

SIRT6 activation rescues the age-related decline in DNA damage repair in primary human chondrocytesPreprint

Copp, M. E., Shine, J., Brown, H. L., Nimmala, K. R., Chubinskaya, S., Collins, J. A., Loeser, R. F., & Diekman, B. O. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.27.530205 · Cited by 2

SIRT6 regulates protein synthesis and folding through nucleolar remodelingPreprint

Toiber, D., Stein, D., Portillo, M., Kaluski-Kopatch, S., Stein, D., Lachberg, Y., Eremenko, E., Smirnov, D., Einav, M., Khrameeva, E. E., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4215918/v1 · Cited by 2

Manipulating PARK7/DJ-1 Levels by Genotoxic Stress Alters Noncoding RNAs and Cellular Homeostasis

Zohar, K., Zoubi, H. O., Goldberg, M., Eliyahu, T., & Michal Linial, B. (2025) · Cells · doi:10.3390/cells14231860 · 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

Critical role of Sirtuin 6 (SIRT6) in osteoarthritis chondrocytes: the interaction among various biological processes

Ding, N., He, Z., & Yang, Q. (2026) · Annals of Medicine · doi:10.1080/07853890.2026.2638000 · Cited by 1

Targeting Sirtuin Signaling in Parkinson’s Disease and Neurodegeneration: Molecular Insights and Translational Potential

Kumari, S., Singh, H., Kamiya, A., & Taliyan, R. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06062-w · Cited by 2

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

Sirtuins as Regulators of Cardiac Hypertrophy and Heart Failure

Samant, S. A., & Gupta, M. P. (2016) · Cardiac and vascular biology · doi:10.1007/978-3-319-41457-7_11 · Cited by 1

Molecular characterization and expression pattern analysis of Sirtuin family genes in the eastern honeybee, Apis cerana

Ma, Q., Chen, S., Ma, Z., Li, D.-F., Dang, X., Xu, J.-S., & Zhou, Z. (2024) · Discover Life · doi:10.1007/s11084-024-09660-7 · Cited by 2

Computational analysis of congenital heart disease associated SNPs: unveiling their impact on the gene regulatory system

Vashisht, S., Parisi, C., & Winata, C. L. (2025) · BMC Genomics · doi:10.1186/s12864-025-11232-6 · Cited by 2

Vector semantics of multidomain protein architectures

Cui, X., Xiao, Y., Stolzer, M., & Durand, D. (2026) · Bioinformatics Advances · doi:10.1093/bioadv/vbag037 · Cited by 2

Epigenetics of Cisplatin Resistance

Gray, S. G. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800206-3.00026-4 · Cited by 1

Sirtuins and Stress Response in Skin Cancer, Aging, and Barrier Function

He, Y. (2016) · Springer eBooks · doi:10.1007/978-3-319-43157-4_12 · Cited by 1

Research progress of Sirtuins in DNA damage repair

QinXian, L. I. U., Guo, W., Tang, M., Wang, H., & Zhu, W. (2017) · Scientia Sinica Vitae · doi:10.1360/n052016-00332 · Cited by 1

DNA damage, sirtuins, and epigenetic marks

Alves-Fernandes, D. K., & Jasiulionis, M. G. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91081-1.00016-9 · Cited by 1

Epigenetics of cisplatin resistance

Baird, A., & Gray, S. G. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-91367-6.00026-x · Cited by 1

Nonhomologous DNA End Joining in Mammalian Cells

Ray, U., & Raghavan, S. C. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00101-2 · Cited by 1

The Divergent 3D Genome Landscapes of Aging and Neurodegenerative mouse modelsPreprint

Kashuk, E., Smirnov, D., Eremenko, E., Tsitrina, A. A., Kriukov, D. V., Golova, A., Kaluski-Kopatch, S., Khrameeva, E. E., & Toiber, D. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.10.687599 · Cited by 1

The catalytic activity of sirtuins in physiology and disease from the epigenetic point of view

Albani, D., & Forloni, G. (2014) · Epigenetics of Degenerative Diseases · doi:10.2478/end-2014-0001

Facilitating repair

David, R. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3652

The Role of Sirtuin 6 in Maintaining Vascular Integrity

Leung, S. Z. (2016) · Scholarship@Western (Western University)

Ligand Binding and Catalysis in Selected Sirtuin Isozymes

Yu, J. (2016) · NDSU Repository (North Dakota State University)

Variation, Modification, and Reorganization of Broken Chromatin

Humphrey, T. C., Downs, J. A., & Chambers, A. L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802389-1.00011-3 · Cited by 1

The Circadian Clock and the Aging Process

Hui, K. Y., & Ripperger, J. A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811353-0.00075-0

CHD6 and the oxidative stress-induced DNA damage response

Moore, S. (2018) · Libraries and Cultural Resources (University of Calgary) · doi:10.11575/prism/32051

Insights into Cellular Stress Revealed by SIRT7

Liu, Y. (2014) · eScholarship (California Digital Library)

Synergy between SIRT1 and SIRT6 helps recognize DNA breaks and potentiate the DNA damage response and repairPreprint

Meng, F., Qian, M., Peng, B., Wang, X., Peng, L., Zheng, K., Liu, Z., Tang, X., Zhang, S., Sun, S., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.01.930172

Neutralizing Gatad2a-Chd4-Mbd3 Axis within the NuRD Complex Facilitates Deterministic Induction of Naive PluripotencyPreprint

Mor, N., Rais, Y., Peles, S., Sheban, D., Aguilera-Castrejon, A., Zviran, A., Elinger, D., Viukov, S. V., Geula, S., Krupalnik, V., et al. (2018) · SSRN Electronic Journal · doi:10.2139/ssrn.3155556

Sirtuin signaling in hematologic malignancies

Denu, R. A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822467-0.00012-7

SIRT6 Regulates Telomere Movement in the Presence and Absence of Oxidative DamagePreprint

Gao, Y. D., Chen, X., Leger, B. S., Ma, H., Xu, J., Spagnol, S. T., Dahl, K. N., Levine, A. S., Liu, Y., & Lan, L. (2018) · SSRN Electronic Journal · doi:10.2139/ssrn.3155782

Chromatin remodeling in the UV-induced DNA damage response

Aydın, Ö. Z. (2014) · RePub (Erasmus University Rotterdam)

Nuclear NAD + homeostasis is essential for naive and chemoresistant BRCA1/2 -deficient tumor survivalPreprint

Musiani, D., Yücel, H., Sourd, L., Marangoni, E., & Ceccaldi, R. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.09.471907

Introduction

Ghosh, S. (2019) · Springer theses · doi:10.1007/978-981-32-9267-3_1

SENP1 Knockdown Suppresses Tumor Progression in Lung Adenocarcinoma by Regulating AAR Genes ExpressionPreprint

Cheng, H., Li, R., Wang, F., Yu, X., Wang, F., Gao, Y., Mu, J., & He, J. (2020) · doi:10.21203/rs.3.rs-26420/v1

Faculty Opinions recommendation of SIRT6 Is Responsible for More Efficient DNA Double-Strand Break Repair in Long-Lived Species.

Kapahi, P. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.735571855.793559381

The interplay between DNA damage and epigenetics in cancer

Challis, D., & Brettingham‐Moore, K. H. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91081-1.00015-7

Applications of bioinformatics and machine learning in the analysis of proteomics data

Li, B. (2023) · Utrecht University Repository (Utrecht University) · doi:10.33540/1818

Potential Biomarkers for Early Diagnosis of Alzheimer’s Disease and Primary Open-Angle Glaucoma

Bogolepova, A. N., Makhnovich, E. V., Коваленко, Е. А., & Osinovskaya, N. A. (2023) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-023-01449-x

Additional file 1 of Sirt6 enhances macrophage lipophagy and improves lipid metabolism disorder by regulating the Wnt1/β-catenin pathway in atherosclerosis

Wang, T., Cheng, Z., Zhao, R., Cheng, J., Ren, H., Zhang, P., Liu, P., Hao, Q., Zhang, Q., Yu, X., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24186212

Genes as Genome Stabilizers in Pluripotent Stem Cells

Karmakar, A., Augustine, A. B. H. R., & Thummer, R. P. (2025) · Advances in experimental medicine and biology · doi:10.1007/5584_2025_853

Sirtuins as a Double-Edged Sword in Cancer: From Molecular Mechanisms to Therapeutic Opportunities

Sima, N., Bosch‐Presegué, L., & Vaquero, A. (2014) · Springer eBooks · doi:10.1007/978-94-017-9421-3_5

Additional file 4 of Sirt6 enhances macrophage lipophagy and improves lipid metabolism disorder by regulating the Wnt1/β-catenin pathway in atherosclerosis

Wang, T., Cheng, Z., Zhao, R., Cheng, J., Ren, H., Zhang, P., Liu, P., Hao, Q., Zhang, Q., Yu, X., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24186221

Additional file 2 of Sirt6 enhances macrophage lipophagy and improves lipid metabolism disorder by regulating the Wnt1/β-catenin pathway in atherosclerosis

Wang, T., Cheng, Z., Zhao, R., Cheng, J., Ren, H., Zhang, P., Liu, P., Hao, Q., Zhang, Q., Yu, X., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24186215

Additional file 3 of Sirt6 enhances macrophage lipophagy and improves lipid metabolism disorder by regulating the Wnt1/β-catenin pathway in atherosclerosis

Wang, T., Cheng, Z., Zhao, R., Cheng, J., Ren, H., Zhang, P., Liu, P., Hao, Q., Zhang, Q., Yu, X., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24186218

Molecular drivers of ageing and emerging longevity therapies

Dhinakaran, M. L., Murugesu, S., & Srinivasan, D. K. (2026) · Exploration of Drug Science · doi:10.37349/eds.2026.1008152

Novel small-molecule positive allosteric modulator 1 with blood-brain barrier penetration activity exerts anti-cellular senescence effects via the PAC1-R/YY1/SIRT6 pathway

Su, W., Xiao, L., Tang, S., Zheng, X., Zhang, Y., & Yu, R. (2026) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2026032

Double strand break repair within constitutive heterochromatin

Tsouroula, A. (2017) · theses.fr (ABES) · doi:10.70675/6345eaa6z96c3z47bdz8b53zab2527ff8785

Analyse de données et modèle pour l'étude de la chromatine, des G-quadruplexes et de la réparation de l'ADN

Rocher, V. (2021) · theses.fr (ABES) · doi:10.70675/217850a9z3e46z4daazadc6zb1bce2ccfe54

Caractérisation de la dynamique de l'ADN-glycosylase OGG1 et de résidus responsables de son interaction avec l'ADN en cellules vivantes

D’Augustin, O. (2022) · theses.fr (ABES) · doi:10.70675/26791ff9zc628z4081zaf62zab7c02c91558

Stiffness-dependent alveolar type II cell senescence in idiopathic pulmonary fibrosis

Lin, C.-R., Woranam, K., Hayek, H., Jeger, J., Karim, L., Kośmider, B., Kaminski, R., Schultz, C. W., Bolla, S., Marchetti, N., et al. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02881-5

GSDME acts as an epigenetic modifier to promote melanoma development via centriole biogenesis regulator PLK4

Du, J., Yang, Y., Zhao, M., Zhang, H., Li, X., Qu, D., Wang, J., Wang, X., Yi, X., Ma, J. X., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01767-w

Targeting SIRT6 epigenetically restrains neutrophil hyperplasia and enhances chemotherapeutic efficacy

Wang, L., Wu, X., Wang, P., Zhang, M., Li, L., Huang, Z., Mao, Y., Chen, H., Wen, Q., Liu, W., et al. (2026) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2026.06.020

Long-lived mammals contain more phosphorylation sites in the SIRT6 C-terminus that enhance PARP1 interaction and resistance to oxidative stress

Gigas, J., Meadow, M. E., Guo, J., Lan, C., Hillpot, E. C., Martinez, J. C., Tombline, G., Bellomio, P. M., Rivera-Almodóvar, V., Welle, K. A., et al. (2026) · GeroScience · doi:10.1007/s11357-026-02389-3

SIRT6 signaling as an underexplored mechanistic node in nanoformulation‐based neuroinflammation therapy for Alzheimer's disease

Mancy, A. S. (2026) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.70305

PRMT5 lactylation mediates SIRT6-dependent DNA damage and senescence in benzene-induced hematotoxicity

Sun, R., Xu, K., Li, X., Huang, J., Wang, D., Pu, Y., & Zhang, J. (2026) · Food and Chemical Toxicology · doi:10.1016/j.fct.2026.116343

Pro-Longevity Role of SIRT6 to Promote Life Span and Delay Ageing – An Integrated Review Towards Healthy Ageing

Dhar, P., Srigunan, V., & Moodithaya, S. S. (2026) · Journal of Health and Allied Sciences NU · doi:10.25259/jhasnu_57_2026

ISWI/CHRAC orchestrates sequential chromatin-remodeling activities by mobilizing DNA polymerase ε for homologous recombination

Qian, J., Tanaka, K., Yasui, A., & Ui, A. (2026) · Communications Biology · doi:10.1038/s42003-026-10862-0

Chromatin Modifications Orchestrate DNA Repair Pathway Choice: Epigenetics Strategies for Enhancing CRISPR –Cas9‐Mediated Knock‐In Efficiency

Chen, X., Qin, S., Yang, C., Xing, Z., Liu, C., Zhang, X., Wu, X., Li, X., Gong, Y., & Liu, Z. (2026) · Cell Proliferation · doi:10.1111/cpr.70285

Variation, modification, and reorganization of broken chromatin

Humphrey, T. C., Downs, J. A., & Chambers, A. L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-443-19001-8.00014-3

BindingDB Entry 50010551: An overview of Sirtuins as potential therapeutic target: Structure, function and modulators.

BindingDB (2021) · UC San Diego · doi:10.7270/q2w380vz

BindingDB Entry 50018259: Emerging Therapeutic Potential of SIRT6 Modulators.

BindingDB (2024) · UC San Diego · doi:10.7270/q2mw2nb8

Facilitating repair

David, R. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3652

SIRT6 coordinates with CHD4 to promote chromatin relaxation and DNA repair

Hou, T., Cao, Z., Zhang, J., Tang, M., Tian, Y., Li, Y., Lu, X., Chen, Y., Wang, H., Wei, F., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa006 · Cited by 96

SIRT6 stabilizes DNA-dependent protein kinase at chromatin for DNA double-strand break repair

McCord, R. A., Michishita, E., Hong, T., Berber, E., Boxer, L. D., Kusumoto, R., Guan, S., Shi, X., Gozani, O., Burlingame, A. L., et al. (2009) · Aging · doi:10.18632/aging.100011 · Cited by 313

Chapter 22. Emerging Roles of Sirtuins in Chromatin Regulation and DNA Repair via their NAD+-dependent Activities

Rodriguez, Y., & Wilson, S. H. (2020) · Chemical biology · doi:10.1039/9781839162541-00152 · Cited by 1

Synergy between SIRT1 and SIRT6 helps recognize DNA breaks and potentiates the DNA damage response and repair in humans and mice

Meng, F., Qian, M., Peng, B., Peng, L., Wang, X., ZHENG, K. C., Liu, Z., Tang, X., Zhang, S., Sun, S., et al. (2020) · eLife · doi:10.7554/elife.55828 · Cited by 83