Cited by 439Genomics and Chromatin DynamicsEpigenetics and DNA MethylationNuclear Structure and Function

The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.

SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation.

Vaquero, Alejandro, Scher, Michael, Erdjument-Bromage, Hediye, Tempst, Paul, Serrano, Lourdes, Reinberg, Danny·2007·Nature

DOI 10.1038/nature06268

Open this paper in CoChat — free account

Abstract

In contrast to stably repressive, constitutive heterochromatin and stably active, euchromatin, facultative heterochromatin has the capacity to alternate between repressive and activated states of transcription. As such, it is an instructive source to understand the molecular basis for changes in chromatin structure that correlate with transcriptional status. Sirtuin 1 (SIRT1) and suppressor of variegation 3-9 homologue 1 (SUV39H1) are amongst the enzymes responsible for chromatin modulations associated with facultative heterochromatin formation. SUV39H1 is the principal enzyme responsible for the accumulation of histone H3 containing a tri-methyl group at its lysine 9 position (H3K9me3) in regions of heterochromatin. SIRT1 is an NAD+-dependent deacetylase that targets histone H4 at lysine 16 (refs 3 and 4), and through an unknown mechanism facilitates increased levels of H3K9me3 (ref. 3). Here we show that the mammalian histone methyltransferase SUV39H1 is itself targeted by the histone deacetylase SIRT1 and that SUV39H1 activity is regulated by acetylation at lysine residue 266 in its catalytic SET domain. SIRT1 interacts directly with, recruits and deacetylates SUV39H1, and these activities independently contribute to elevated levels of SUV39H1 activity resulting in increased levels of the H3K9me3 modification. Loss of SIRT1 greatly affects SUV39H1-dependent H3K9me3 and impairs localization of heterochromatin protein 1. These findings demonstrate a functional link between the heterochromatin-related histone methyltransferase SUV39H1 and the histone deacetylase SIRT1.

Integrity signals

Registry

Crossref · 10.1038/nature06268

Cites

17 of 17 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845
Loss of the Suv39h Histone Methyltransferases Impairs Mammalian Heterochromatin and Genome Stability
Peters, A. H. F. M., O'Carroll, D., Scherthan, H., Mechtler, K., Sauer, S., Schöfer, C., Weipoltshammer, K., Pagani, M., Lachner, M., Kohlmaier, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00542-6 · Cited by 1,766
G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesisPreprint
Tachibana, M., Sugimoto, K., Nozaki, M., Ueda, J., Ohta, T., Ohki, M., Fukuda, M., Takeda, N., Niida, H., Kato, H., et al. (2002) · Genes & Development · doi:10.1101/gad.989402 · Cited by 1,294
Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
Cheng, H.-L., Mostoslavsky, R., Saito, S., Manis, J. P., Gu, Y., Patel, P., Bronson, R., Appella, E., Alt, F. W., & Chua, K. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934713100 · Cited by 1,095
Inhibition of Silencing and Accelerated Aging by Nicotinamide, a Putative Negative Regulator of Yeast Sir2 and Human SIRT1
Bitterman, K. J., Anderson, R. M., Cohen, H. Y., Latorre-Esteves, M., & Sinclair, D. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205670200 · Cited by 1,002
Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin.
Vaquero, A., Scher, M., Lee, D., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.031 · Cited by 916
Self-citation
The biochemistry of sirtuins
Sauve, A. A., Wolberger, C., Schramm, V. L., & Boeke, J. D. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133500 · Cited by 763
SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosisPreprint
Vaquero, A., Scher, M. B., Lee, D. H., Sutton, A., Cheng, H.-L., Alt, F. W., Serrano, L., Sternglanz, R., & Reinberg, D. (2006) · Genes & Development · doi:10.1101/gad.1412706 · Cited by 670
Self-citation
PR-Set7 Is a Nucleosome-Specific Methyltransferase that Modifies Lysine 20 of Histone H4 and Is Associated with Silent Chromatin
Nishioka, K., Rice, J. C., Sarma, K., Erdjument‐Bromage, H., Werner, J. K., Wang, Y., Chuikov, S., Valenzuela, P., Tempst, P., Steward, R., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00548-8 · Cited by 595
Self-citation

Flagged first, then by citations

Show all 17 references

Sorted by citations

Items 301–400 of 438

Histone proteoform analysis reveals epigenetic changes in adult mouse brown adipose tissue in response to cold stress
Taylor, B. C., Steinthal, L. H., Dias, M., Yalamanchili, H. K., Ochsner, S. A., Zapata, G. E., Mehta, N. R., McKenna, N. J., Young, N. L., & Nuotio-Antar, A. M. (2024) · Epigenetics & Chromatin · doi:10.1186/s13072-024-00536-8 · Cited by 12
Targeting neuronal epigenomes for brain rejuvenation
Zocher, S. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00148-8 · Cited by 13
ERRα and ERRγ coordinate expression of genes associated with Alzheimer’s disease, inhibiting DKK1 to suppress tau phosphorylation
Sato, K., Takayama, K., Saito, Y., & Inoue, S. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2406854121 · Cited by 13
Embedding the Future of Regenerative Medicine into the Open Epigenomic Landscape of Pluripotent Human Embryonic Stem Cells.
Parsons, X. H. (2013) · Annual Research & Review in Biology · Cited by 12
Perfecting DNA double-strand break repair on transcribed chromatin
Tan, X. Y., & Huen, M. S. Y. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190094 · Cited by 11
Expression of the tumor suppressor gene hypermethylated in cancer 1 in laryngeal carcinoma
Markowski, J., Sieroń, A. L., Kasperczyk, K., Ciupińska-Kajor, M., Auguściak-Duma, A., & Likus, W. (2015) · Oncology Letters · doi:10.3892/ol.2015.2983 · Cited by 12
SUV39H1 is a novel biomarker targeting oxidative phosphorylation in hepatitis B virus-associated hepatocellular carcinoma
Zhang, Y., Lao, W., Yang, K., Kong, X., Li, Y., Yu, X., Wang, X., Liu, Y., Li, Z., Deng, Y., et al. (2023) · BMC Cancer · doi:10.1186/s12885-023-11633-4 · Cited by 11
Restoration of mitochondrial function alleviates trigeminal neuropathic pain in mice
Yang, J., Xie, S., Guo, J., Zhou, Y., Yang, Y., Sun, Z., Cai, P., Zhang, C., Jiang, S., Cao, X., et al. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.11.011 · Cited by 12
Pan-cancer analysis of super-enhancer-induced LINC00862 and validation as a SIRT1-promoting factor in cervical cancer and gastric cancer
Liu, S., Wang, Z., Hu, L., Ye, C., Zhang, X., Zhu, Z., Li, J., & Shen, Q. (2024) · Translational Oncology · doi:10.1016/j.tranon.2024.101982 · Cited by 11
Fusaric Acid-Induced Epigenetic Modulation of Hepatic H3K9me3 Triggers Apoptosis in Vitro and in Vivo
Ghazi, T., Nagiah, S., Dhani, S., & Chuturgoon, A. A. (2020) · Epigenomics · doi:10.2217/epi-2019-0284 · Cited by 11
Dephosphorylation of p53 Ser 392 Enhances Trimethylation of Histone H3 Lys 9 via SUV39h1 Stabilization in CK2 Downregulation-Mediated Senescence.
Park, J., & Bae, Y. (2019) · PubMed Central · doi:10.14348/molcells.2019.0018 · Cited by 10
Spatiotemporal dynamics of SIRT 1, 2 and 3 during in vitro maturation of bovine oocytes
Ferreira, A. F., Machado-Simões, J., Soares, M., Sousa, A. P., Ramalho‐Santos, J., & Almeida‐Santos, T. (2022) · Theriogenology · doi:10.1016/j.theriogenology.2022.04.004 · Cited by 10
Role of sirtuins in epigenetic regulation and aging control
Samoilova, E. M., Romanov, S. E., Chudakova, D. A., & Laktionov, P. P. (2024) · Vavilov Journal of Genetics and Breeding · doi:10.18699/vjgb-24-26 · Cited by 10
Acetylome Analysis Identifies SIRT1 Targets in mRNA-Processing and Chromatin-Remodeling in Mouse Liver
Kim, S.-Y., Sim, C. K., Tang, H. R., Han, W., Zhang, K., & Xu, F. (2015) · PLoS ONE · doi:10.1371/journal.pone.0140619 · Cited by 11
A model of dynamic stability of H3K9me3 heterochromatin to explain the resistance to reprogramming of differentiated cells
Jehanno, C., Flouriot, G., Goff, P. L., & Michel, D. (2016) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2016.11.006 · Cited by 11
Stem cell aging in adult progeria
Cheung, H., Pei, D., & Chan, W. (2015) · Cell Regeneration · doi:10.1186/s13619-015-0021-z · Cited by 10
Nicotinamide treatment reduces the levels of histone H3K4 trimethylation in the promoter of the mper1 circadian clock gene and blocks the ability of dexamethasone to induce the acute response
Xydous, M., Sekeri‐Pataryas, K. E., Prombona, A., & Sourlingas, T. G. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.03.001 · Cited by 10
The odyssey of cGAS: From cytosol to nucleus
Hao, W., Li, W., Wang, L., & Li, S. (2023) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2023.09.004 · Cited by 11
Mangiferin protects mesenchymal stem cells against DNA damage and cellular aging via SIRT1 activation
Lim, G. M., & Cho, G.-W. (2025) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2025.112038 · Cited by 9
Gasotransmitters in Gametogenesis and Early Development: Holy Trinity for Assisted Reproductive Technology—A Review
Nevoral, J., Bodart, J., & Petr, J. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1730750 · Cited by 10
Reversible modulation of SIRT1 activity in a mouse strain
Clark-Knowles, K. V., He, X., Jardine, K. E., Coulombe, J., Dewar‐Darch, D., Caron, A. Z., Gray, D. A., & McBurney, M. W. (2017) · PLoS ONE · doi:10.1371/journal.pone.0173002 · Cited by 9
Role of SIRT1 in Epigenetics
Wang, Z. A., Hsu, W. W., & Liu, W. R. (2019) · Springer eBooks · doi:10.1007/978-3-319-55530-0_1 · Cited by 9
Sirtuinsandneuropeptide ydownregulation in Flinders Sensitive Line rat model of depression
Stiernborg, M., Efstathopoulos, P., Lennartsson, A., Lavebratt, C., & Mathé, A. A. (2021) · Acta Neuropsychiatrica · doi:10.1017/neu.2021.36 · Cited by 9
Efficacy of resveratrol in male urogenital tract dysfunctions: an evaluation of pre-clinical data
Calmasini, F., Silva, F., Alexandre, E., & Antunes, E. (2021) · Nutrition Research Reviews · doi:10.1017/s0954422421000354 · Cited by 9
Metabolic energy sensors as targets for designing host-directed therapies for tuberculosis
Cheng, C. Y., Böhme, J., & Singhal, A. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.4mr0617-226r · Cited by 9
Expression and significance of Sirt1 in renal allografts at the early stage of chronic renal allograft dysfunction
Xia, Y. Y., Deng, J., Zhou, Q., Shao, X., Yang, X., Sha, M., & Zou, H. (2018) · Transplant Immunology · doi:10.1016/j.trim.2018.02.006 · Cited by 9
Histone lysine methylation modifiers controlled by protein stability
Park, S., Cho, J. H., Kim, J., & Kim, J. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01329-5 · Cited by 9
Heterochromatic hues of transcription—the diverse roles of noncoding transcripts from constitutive heterochromatin
Saha, P., & Mishra, R. K. (2019) · FEBS Journal · doi:10.1111/febs.15104 · Cited by 8
Role of the Histone Acetyl Transferase MOF and the Histone Deacetylase Sirtuins in Regulation of H4K16ac During DNA Damage Repair and Metabolic Programming: Implications in Cancer and Aging
Pandita, T. K., Hunt, C. R., Singh, V., Adhikary, S., Pandita, S., Roy, S., Ramos, K. S., & Das, C. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-07634-3_4 · Cited by 7
Sensitivity of pituitary gonadotropes to hyperglycemia leads to epigenetic aberrations and reduced follicle‐stimulating hormone levels
Feldman, A., Saleh, A., Pnueli, L., Qiao, S., Shlomi, T., Boehm, U., & Melamed, P. (2018) · The FASEB Journal · doi:10.1096/fj.201800943r · Cited by 6
Genetic Architecture of Depression: Where Do We Stand Now?
Ünal‐Aydın, P., Aydın, O., & Arslan, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-33-6044-0_12 · Cited by 7
An indel in the Suv39h1 gene is associated with resistance to iridovirus in the Asian seabass
Sun, F., Wen, Y., Wang, L., & Yue, G. H. (2020) · Aquaculture · doi:10.1016/j.aquaculture.2020.735611 · Cited by 7
Redox-sensitive epigenetic activation of SUV39H1 contributes to liver ischemia-reperfusion injury
Li, Z., Li, J., Wu, M., Li, Z., Zhou, J., Lu, Y., Xu, Y., Qin, L., & Fan, Z. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103414 · Cited by 6
Small Changes, Big Effects: Chromatin Goes Aging
Lazarus, A., Banerjee, K. K., & Kolthur‐Seetharam, U. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-4525-4_8 · Cited by 6
Retroviral proteomics and interactomes: intricate balances of cell survival and viral replication
Duyne, R. V., Kehn‐Hall, K., Klase, Z. A., Easley, R., Heydarian, M., Saifuddin, M., Wu, W., & Kashanchi, F. (2008) · Expert Review of Proteomics · doi:10.1586/14789450.5.3.507 · Cited by 6
Role for tyrosine phosphorylation of SUV39H1 histone methyltransferase in enhanced trimethylation of histone H3K9 via neuregulin-1/ErbB4 nuclear signaling
Nakajo, H., Ishibashi, K., Aoyama, K., Kubota, S., Hasegawa, H., Yamaguchi, N., & Yamaguchi, N. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.02.130 · Cited by 6
Epigenetic Regulation by Retinoids
Vieira, A. V. (2011) · doi:10.1002/9780470959824.ch14 · Cited by 6
Histone modification cross-talk: analytical tools and molecular mechanisms
Jiang, J., DuBois-Coyne, S. E., Nam, E., Whedon, S. D., Lee, K., & Cole, P. A. (2026) · Biochemical Journal · doi:10.1042/bcj20250115 · Cited by 5
Black carrot extract protects against hepatic injury through epigenetic modifications
Kitano, A., Norikura, T., Matsui‐Yuasa, I., Shimakawa, H., Kamezawa, M., & Kojima‐Yuasa, A. (2022) · Journal of Food Biochemistry · doi:10.1111/jfbc.14292 · Cited by 5
Sirtuin Modulation as Novel Neuroprotective Strategy for Alzheimer’s Disease
Polito, L., Biella, G., & Albani, D. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803690-7.00008-9 · Cited by 5
Cellular regulation and stability of DNA replication forks in eukaryotic cells
Li, X., Wang, L., Liu, X., Zheng, Z., & Kong, D. (2022) · DNA repair · doi:10.1016/j.dnarep.2022.103418 · Cited by 4
Inhibiting BDNF Signaling Upregulates Hippocampal H3K9me3 in a Manner Dependent On In Vitro Aging and Oxidative Stress
Ionescu-Tucker, A., Tong, L., Berchtold, N. C., & Cotman, C. W. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.796087 · Cited by 4
TIP60 recruits SUV39H1 to chromatin to maintain heterochromatin genome stability and resist hydrogen peroxide-induced cytotoxicity
Tu, B., Bao, Y., Tang, M., Zhu, Q., Lu, X., Wang, H., Hou, T., Zhao, Y., Zhang, P., & Zhu, W. (2020) · Genome Instability & Disease · doi:10.1007/s42764-020-00025-8 · Cited by 4
Mitochondrial dysfunction in Parkinson’s disease: a possible target for neuroprotection
Gleave, J. A., Perri, P. D., & Nash, J. E. (2014) · Frontiers in Biology · doi:10.1007/s11515-014-1337-8 · Cited by 5
Epigenome Modification and Ubiquitin‐Dependent Proteolysis During Pronuclear Development of the Mammalian Zygote: Animal Models to Study Pronuclear Development
Nevoral, J., & Šutovský, P. (2017) · Wiley eBooks · doi:10.1002/9781118881286.ch17 · Cited by 5
Nucleocytoplasmic shuttling of sirtuin 1 regulates histone modifications and transcriptional events during early porcine embryonic development
Lee, S., Lu, Q., Zhan, C., Kim, J.-D., Lee, G.-H., Sim, J.-M., Song, H.-J., & Cui, X. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149016 · Cited by 3
The p53 R181C mutation accumulates through impaired deacetylation by Sirt1 and facilitates tumor development
Wang, E., Cao, L., 郭文栋, Dong, X., Zhang, W., Zhang, X., Wang, Z., Chen, X., Li, A., Zou, Y., et al. (2026) · Communications Biology · doi:10.1038/s42003-025-09465-y · Cited by 3
SIRT7 links H3K36ac epigenetic regulation with genome maintenance in the mouse testis
Guitart-Solanes, A., Romero, M., Gámez-García, A., Fernández-Duran, I., Niedenberger, B. A., Madrid-Sandín, C., Spears, N., Roig, I., Geyer, C. B., Vaquero, A., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-72540-3 · Cited by 3
Self-citation
The transposon-driven evolutionary origin and basis of histone deacetylase functions and limitations in disease prevention
Peek, G. W., & Tollefsbol, T. O. (2011) · Clinical Epigenetics · doi:10.1007/s13148-011-0020-z · Cited by 3
Rola sirtuin w naprawie DNA
Kciuk, M., & Kontek, R. (2020) · Postępy Biochemii · doi:10.18388/pb.2020_319 · 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
The Biological Function of Genome Organization
Yang, X., Zhu, H., Liu, Y., Wang, J., Song, Y., Liao, S., & Dong, P. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26189058 · Cited by 3
A metabolism-chromatin axis promotes differential ribosomal RNA transcription in the human malaria parasite
Couble, J., Vignolini, T., Doré, G. R. G., Mussgnug, S., Lombard, B., Richard, M., Loew, D., Büttner, M., Dueñas-Sánchez, R., Poschet, G., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-67522-w · Cited by 5
Cell Type‐Specific Loss of SIRT1 in Central Amygdala Leads to Depression‐Like Behaviors by Altering Neuronal Excitability in Mice
Huang, H., Ding, X., Lin, Y., Hu, W., Zhou, C.-R., Chen, T., Zhou, Y., Dong, W., Zhou, C., & Wu, Y. (2026) · Acta Physiologica · doi:10.1111/apha.70176 · Cited by 2
Arginine methylation-dependent stabilization of SUV39H1 promotes breast cancer growth
Zhao, W., Wang, G., Wang, P., Ma, B., Liu, B., Fu, Y., Tang, Y., Duan, X., Zhou, K., Zhang, J., et al. (2026) · Oncogene · doi:10.1038/s41388-026-03712-0 · Cited by 2
H3K9 trimethylation homeostasis: mechanisms, crosstalk, and cancer relevance
Zhou, L., Wu, Y., & Kang, T. (2026) · Trends in Cell Biology · doi:10.1016/j.tcb.2026.02.002 · Cited by 2
Optogenetic Animal Models of Depression: From Mice to Men
Arslan, A., Ünal‐Aydın, P., Dogan, T., & Aydın, O. (2022) · Neuromethods · doi:10.1007/978-1-0716-2083-0_8 · Cited by 2
Nicotinamide Mononucleotide Alleviates Aging Defects in Hutchinson–Gilford Progeria Syndrome
Xu, Y., Wu, M., Fan, Y., Zhang, J. Y., Xue, D., Zhang, M., Shao, R., Cai, L., Liao, X., Zhang, L., et al. (2025) · The FASEB Journal · doi:10.1096/fj.202500469rr · Cited by 2
[The role of DNA methylation and histone modifications in structural maintainance of heterochromatin domains (chromocenters)].
Golyshev, S. A., Vikhreva, P. N., Sheval, E. V., Kir'ianov, G. I., & Poliakov, V. I. (2008) · PubMed · Cited by 2
Interplay between histone deacetylase SIR-2, linker histone H1 and histone methyltransferases in heterochromatin formation
Wirth, M., & Jedrusik, M. A. (2009) · Epigenetics · doi:10.4161/epi.4.6.9710 · Cited by 2
The Emerging Role of Sirtuin 1,-3 and -4 in Glucose and Lipid Metabolism and in Diabetes Mellitus
Akbaş, E. M. (2014) · Journal of Molecular and Genetic Medicine · doi:10.4172/1747-0862.s1-018 · Cited by 3
Aging in COPD and Idiopathic Pulmonary Fibrosis
Sánchez, C. G. (2015) · Springer eBooks · doi:10.1007/978-3-319-23246-1_15 · Cited by 2
Epigenetics of physiological and premature aging
Ghosh, S., & Zhou, Z. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-799958-6.00014-7 · Cited by 4
Protein Lysine Acylation: Abundance, Dynamics and Function
Pougovkina, O., & de Boer, V. C. J. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_3 · 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
Epigenetic role of sirtuins in neurodegenerative brain disorders
Khanna, A., Anamika, A., & Trigun, S. K. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814118-2.00009-4 · Cited by 3
Sirtuins and Mammalian Aging
Sharman, E. H. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-602-3_5 · Cited by 2
Modulating SIRT1 activity variously affects thymic lymphoma development in mice
Clark-Knowles, K. V., Dewar‐Darch, D., Jardine, K. E., Coulombe, J., Daneshmand, M., He, X., & McBurney, M. W. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.07.043 · Cited by 2
Epigenetics of Aging and Age-Related Disorders
Sidler, C. L., Kovalchuk, O., & Kovalchuk, I. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813939-4.00036-x · Cited by 2
A metabolism-chromatin axis promotes ribosome heterogeneity in the human malaria parasitePreprint
Couble, J., Vignolini, T., Doré, G. R. G., Lombard, B., Richard, M., Loew, D., Büttner, M., Dueñas-Sánchez, R., Poschet, G., Bryant, J. M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.22.644534 · Cited by 2
Myosin inhibition enhances cardiomyocyte cell cycle activity through SIRT1-NFAT-mediated H3K9me3 modification
Jiang, R., Chen, J., Pei, L., Huang, S., Feng, M., Ouyang, Z., Yuan, M., Zhu, Y., Yao, S., He, F., et al. (2025) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2025.151504 · Cited by 1
Imperatorin ameliorates metabolic dysfunction‐associated fatty liver disease through modulating Suv39h1/Fabps/Cept1 signalling pathway
Sun, Y., Wang, C., Wang, Y., Hao, R., Liu, L., Jin, Y., & Sun, H. (2025) · British Journal of Pharmacology · doi:10.1111/bph.70210 · Cited by 1
Stem cells as an essential mediator of the exercise–tumorigenesis link
Zhuang, X., Wong, E. S. W., Tammela, T., & Jones, L. W. (2026) · Nature reviews. Cancer · doi:10.1038/s41568-026-00933-z · Cited by 2
Epigenetic regulation of vertebrate limb development: from field specification to tissue morphogenesis
Lira, C. M. V.-D., Galván-Hernández, C. I., Chimal‐Monroy, J., & Marín‐Llera, J. C. (2026) · Epigenetics · doi:10.1080/15592294.2026.2695477 · Cited by 1
SIRT1 and Inflammaging in Chronic Obstructive Pulmonary Disease
Hwang, J., Sundar, I. K., Yao, H., & Rahman, I. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-397803-5.00015-0 · Cited by 1
SIRT1 as a key factor for histone code establishment in early embryo, from a perspective of assisted reproduction
Nevoral, J., Šutovský, P., Zámostná, K., Petelák, A., Hošková, K., Žalmanová, T., & Petr, J. (2015) · Slovak Journal of Animal Science · Cited by 1
Biogenic gold nanoparticles as antibrain cancer agents
Dhahi, R. M., & Hamil, M. H. (2022) · AIP conference proceedings · doi:10.1063/5.0092700 · Cited by 1
Role of DNA methylation and histone modifications in structural maintenance of heterochromatin domains (chromocenters)
Golyshev, S., Vichreva, P. N., Sheval, E. V., Kiryanov, G., & Polyakov, V. (2008) · Cell and Tissue Biology · doi:10.1134/s1990519x08060059 · Cited by 3
CHROMO domain readers: A rainbow of opportunities
Sun, X. S., Shrestha, P., & Mills, A. A. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-823376-4.00009-4 · 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
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
Chromatin Structure in Senescent Cells
Richards, H. W., & Medrano, E. E. (2009) · Springer eBooks · doi:10.1007/978-1-4419-1075-2_6 · Cited by 1
The Function and Regulation of Senescent Stromal-Derived Osteopontin
Pazolli, E. (2010) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7x34vgs
A Potential Tumor Suppressive Role of SIRT1 in Cancer
Kabra, N. (2010) · Digital Commons - University of South Florida (University of South Florida)
Novel functions of the MOZ double PHD finger domain
Deeves, S. E. (2012) · Nottingham ePrints (University of Nottingham)
Second German-Catalan workshop on epigenetics & cancer
Gonzalez, B., Forcales, S. V., & Perucho, M. (2015) · Epigenetics · doi:10.1080/15592294.2015.1023499
Sirtuins as Potential Drug Targets for Metabolic Diseases
Tong, Q. (2011) · Wiley eBooks · doi:10.1002/9780470910016.ch15
Regulació de l'heterocromatina constitutiva en condicions normals i d'estrès: Paper de SirT1 i d'HP1
Raurell‐Vila, H. (2014) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)
Quiescence induces epigenetic changes in bovine fibroblasts and improves their reprogramming into cloned embryos
Kallingappa, P. K. (2013) · Research Commons (University of Waikato)
Harnessing gene repression to inhibit leukemia
Harte, P. J., & Ernst, P. (2015) · Nature Medicine · doi:10.1038/nm.3834
Emerging Roles of the Sirtuin Family
Athie-Cuervo, A. (2011) · doi:10.7916/d8x354ft
Epigenetic modifications in caloric restriction associated with longevity: A review of evidence
Zand, H., & Sedaghat, F. (2015)
Functional impact of microRNA-34a on stem cell differentiation towards smooth muscle cell
Yu, X. (2014)
Aus dem Adolf-Butenandt-Institut für Biochemie der
Greiner, D. (2008)
Def-eating senescence?
Maulucci, G., & Pani, G. (2012)
Age-related epigenetic changes at base excision repair genes and their modulation by dietary restriction in mice
Gorniak, J. (2015)
Spatio-Temporal Control of Cellular and Organismal Physiology by Sirtuins
Deota, S., Shukla, N., & Kolthur‐Seetharam, U. (2017) · Journal of the Indian Institute of Science · doi:10.1007/s41745-016-0018-9
A Role for Sirtuins in Maintaining Mammalian Lifespan and Healthspan
Giblin, W. (2017) · Deep Blue (University of Michigan)
The Molecular Basis of Histone Methylation
Sun, L., & Fang, J. (2017) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-319-59786-7_6

Authors: Vaquero, A., Scher, M., Erdjument-Bromage, H., Tempst, P., Serrano, L., & Reinberg, D.
Affiliations: Howard Hughes Medical Institute (US)
Memorial Sloan Kettering Cancer Center (US)
Rutgers, The State University of New Jersey (US)
Corresponding author: Reinberg, Danny
ORCID: Vaquero, Alejandro
Tempst, Paul
Serrano, Lourdes
Reinberg, Danny
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2007-11-15
Volume: 450
Issue: 7168
Pages: 440-444
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature06268
OpenAlex: W2012147370
Cited by: 439
References: 17
Citations by year: 2026: 17 · 2025: 17 · 2024: 22 · 2023: 11 · 2022: 24 · 2021: 20 · 2020: 23 · 2019: 20 · 2018: 24 · 2017: 32 · 2016: 16 · 2015: 29 · 2014: 24 · 2013: 36 · 2012: 32
FWCI: 8.07
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: SIRT1, SUV39H1, facultative heterochromatin, heterochromatin formation, histone deacetylase, histone methyltransferase, H3K9me3, HP1, chromatin regulation, transcriptional repression
MeSH terms: Histone Methyltransferases, Acetylation, Amino Acid Sequence, Animals, Cell Line, Fibroblasts, HeLa Cells, Heterochromatin, Histones, Humans, Methyltransferases, Molecular Sequence Data, Niacinamide, Protein Binding, Histone-Lysine N-Methyltransferase, Protein Methyltransferases, Repressor Proteins, Sirtuins, Chromatin Assembly and Disassembly, Mice, Sirtuin 1

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks