Sirtuin‐dependent epigenetic regulation in the maintenance of genome integrity
Open accessAbstract
Sirtuins are a family of deacetylases that target histone and non‐histone proteins and require NAD + as an enzymatic cofactor for their enzymatic activity. This requirement confers sirtuins with the ability to detect changes in metabolism and energy homeostasis and to coordinate cellular responses to maintain genome integrity. Thus, sirtuins are crucial in the crosstalk between environment and genome, and therefore in responses to stress at the cell and organism levels. Sirtuins play a major role in maintaining genome integrity, largely through regulation of epigenetic mechanisms. They target different histone marks, including H4K16Ac, H3K9Ac, H3K56Ac and H3K18Ac, and non‐histone components of the chromatin machinery, such as enzymes and structural proteins. Here we summarize our current view on the link between sirtuins and epigenetics, one that reflects the continual adaptation of the genome to stress.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
MicroRNA-126 inhibits osteosarcoma cells proliferation by targeting Sirt1
Xu, J., Liu, P., Si, M.-J., & Ding, X. (2013) · Tumor Biology · doi:10.1007/s13277-013-0974-x · Cited by 35 · see citing works
RetractedBartel (2004) · doi:10.1016/s0092-8674(04)00045-5 · Cited by 34,714 · see citing works
The C. elegans heterochronic gene lin-4 encodes small RNAs with antisense complementarity to lin-14
Lee, R. C., Feinbaum, R. L., & Ambros, V. (1993) · Cell · doi:10.1016/0092-8674(93)90529-y · Cited by 12,948 · see citing works
The functions of animal microRNAs
Ambros, V. (2004) · Nature · doi:10.1038/nature02871 · Cited by 10,728 · see citing works
Wightman, B., Ha, I., & Ruvkun, G. (1993) · Cell · doi:10.1016/0092-8674(93)90530-4 · Cited by 4,292 · see citing works
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040 · see citing works
Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R. S., & Zhang, Y. (2002) · Science · doi:10.1126/science.1076997 · Cited by 3,775 · see citing works
MicroRNA Targeting Specificity in Mammals: Determinants beyond Seed Pairing
Grimson, A., Farh, K. K.-H., Johnston, W. K., Garrett-Engele, P., Lim, L. P., & Bartel, D. P. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.017 · Cited by 3,766 · see citing works
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 · see citing works
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 · see citing works
Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase
Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750 · see citing works
A microRNA component of the p53 tumour suppressor network
He, L., He, X., Lim, L. P., de Stanchina, E., Xuan, Z., Liang, Y., Xue, W., Zender, L., Magnus, J., Ridzon, D., et al. (2007) · Nature · doi:10.1038/nature05939 · Cited by 2,692 · see citing works
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,653 · see citing works
ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS
Allfrey, V. G., Faulkner, R. D., & Mirsky, A. E. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.5.786 · Cited by 2,649 · see citing works
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559 · see citing works
The Polycomb group protein EZH2 directly controls DNA methylation
Viré, E., Brenner, C., Deplus, R., Blanchon, L., Fraga, M., Didelot, C., Morey, L., Van Eynde, A., Bernard, D., Vanderwinden, J.-M., et al. (2006) · Nature · doi:10.1038/nature04431 · Cited by 2,204 · see citing works
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081 · see citing works
The DNA methyltransferases of mammals
Bestor, T. H. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.16.2395 · Cited by 2,045 · see citing works
Transactivation of miR-34a by p53 broadly influences gene expression and promotes apoptosis
Chang, T.-C., Wentzel, E. A., Kent, O. A., Ramachandran, K., Mullendore, M., Lee, K. H., Feldmann, G., Yamakuchi, M., Ferlito, M., Lowenstein, C. J., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.010 · Cited by 2,010 · see citing works
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 · see citing works
Fraga, M. F., Ballestar, E., Villar‐Garea, A., Boix-Chornet, M., Espada, J., Schotta, G., Bonaldi, T., Haydon, C. E., Ropero, S., Petrie, K. R., et al. (2005) · Nature Genetics · doi:10.1038/ng1531 · Cited by 1,926 · see citing works
Poly(ADP-ribose): novel functions for an old molecule
Schreiber, V., Dantzer, F., Amé, J., & de MURCIA, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1963 · Cited by 1,917 · see citing works
Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions
Shogren‐Knaak, M. A., Ishii, H., Sun, J.-M., Pazin, M. J., Davie, J., & Peterson, C. L. (2006) · Science · doi:10.1126/science.1124000 · Cited by 1,876 · see citing works
Dent, S., Denu, J. M., & Allis, C. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.81 · Cited by 1,844 · see citing works
CBP/p300 in cell growth, transformation, and development
Goodman, R. H., & Smolik, S. (2000) · Genes & Development · doi:10.1101/gad.14.13.1553 · Cited by 1,778 · see citing works
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 · see citing works
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 · see citing works
Functions of Site-Specific Histone Acetylation and Deacetylation
Shahbazian, M. D., & Grunstein, M. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.162114 · Cited by 1,635 · see citing works
Kuzmichev, A., Nishioka, K., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (2002) · Genes & Development · doi:10.1101/gad.1035902 · Cited by 1,596 · see citing works
Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey
Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487 · see citing works
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 · see citing works
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 · see citing works
MicroRNAs to Nanog, Oct4 and Sox2 coding regions modulate embryonic stem cell differentiation
Tay, Y., Zhang, J., Thomson, A. M., Lim, B., & Rigoutsos, I. (2008) · Nature · doi:10.1038/nature07299 · Cited by 1,385 · see citing works
Transcriptional Activation of miR-34a Contributes to p53-Mediated Apoptosis
Raver-Shapira, N., Marciano, E., Meiri, E., Spector, Y., Rosenfeld, N., Moskovits, N. B.-C., Bentwich, Z., & Oren, M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.017 · Cited by 1,352 · see citing works
miR-34a repression of SIRT1 regulates apoptosis
Yamakuchi, M., Ferlito, M., & Lowenstein, C. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801613105 · Cited by 1,344 · see citing works
Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216 · see citing works
Target mRNAs are repressed as efficiently by microRNA-binding sites in the 5′ UTR as in the 3′ UTR
Lytle, J., Yario, T. A., & STEITZ, J. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703820104 · Cited by 1,196 · see citing works
p53-Mediated Activation of miRNA34 Candidate Tumor-Suppressor Genes
Bommer, G. T., Gerin, I., Feng, Y., Kaczorowski, A. J., Kuick, R. D., Love, R. E., Zhai, Y., Giordano, T. J., Qin, Z. S., Moore, B. B., et al. (2007) · Current Biology · doi:10.1016/j.cub.2007.06.068 · Cited by 1,122 · see citing works
SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin
Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111 · see citing works
A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatinPreprint
Schotta, G., Lachner, M., Sarma, K., Ebert, A., Sengupta, R., Reuter, G., Reinberg, D., & Jenuwein, T. (2004) · Genes & Development · doi:10.1101/gad.300704 · Cited by 1,110 · see citing works
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 · see citing works
Kawahara, T. L. A., Michishita, E., Adler, A. S., Damian, M., Berber, E., Lin, M., McCord, R. A., Ongaigui, K. C. L., Boxer, L. D., Chang, H. Y., et al. (2009) · Cell · doi:10.1016/j.cell.2008.10.052 · Cited by 1,090 · see citing works
DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci
Rountree, M. R., Bachman, K. E., & Baylin, S. B. (2000) · Nature Genetics · doi:10.1038/77023 · Cited by 1,056 · see citing works
Lysine Acetylation: Codified Crosstalk with Other Posttranslational Modifications
Yang, X.-J., & Seto, E. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.002 · Cited by 1,006 · see citing works
Kauppinen, A., Suuronen, T., Ojala, J. O., Kaarniranta, K., & Salminen, A. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.06.007 · Cited by 1,001 · see citing works
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 · see citing works
DNA methyltransferase Dnmt1 associates with histone deacetylase activity
Fuks, F., Burgers, W. A., Brehm, A., Hughes‐Davies, L., & Kouzarides, T. (2000) · Nature Genetics · doi:10.1038/71750 · Cited by 988 · see citing works
Tarasov, V., Jung, P., Verdoodt, B., Lodygin, D., Epanchintsev, A., Menssen, A., Meister, G., & Hermeking, H. (2007) · Cell Cycle · doi:10.4161/cc.6.13.4436 · Cited by 922 · see citing works
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 · see citing works
Self-citationCloning and sequencing of a cDNA encoding DNA methyltransferase of mouse cells
Bestor, T. H., Laudano, A. P., Mattaliano, R. J., & Ingram, V. M. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90122-2 · Cited by 913 · see citing works
Tazawa, H., Tsuchiya, N., Izumiya, M., & Nakagama, H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707351104 · Cited by 902 · see citing works
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 · see citing works
Impaired DNA Damage Response, Genome Instability, and Tumorigenesis in SIRT1 Mutant Mice
Wang, R.-H., Sengupta, K., Li, C., Kim, H., Cao, L., Xiao, C., Kim, S., Xu, X., Yin, Z., Chilton, B. S., et al. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.09.001 · Cited by 769 · see citing works
A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM
Sun, Y., Jiang, X., Chen, S., Fernandes, N., & Price, B. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504211102 · Cited by 738 · see citing works
Sirt1 Regulates Insulin Secretion by Repressing UCP2 in Pancreatic β Cells
Bordone, L., Motta, M. C., Picard, F., Robinson, A., Jhala, U. S., Apfeld, J., McDonagh, T., Lemieux, M., McBurney, M., Szilvasi, A., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040031 · Cited by 715 · see citing works
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 · see citing works
SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine
Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., Du, J., Kim, R., Ge, E., Mostoslavsky, R., et al. (2013) · Nature · doi:10.1038/nature12038 · Cited by 697 · see citing works
Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?
Hassa, P. O., Haenni, S. S., Elser, M., & Hottiger, M. O. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00040-05 · Cited by 682 · see citing works
Histone acetylation and deacetylation in yeast
Kurdistani, S. K., & Grunstein, M. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1075 · Cited by 677 · see citing works
miR-33a/b contribute to the regulation of fatty acid metabolism and insulin signaling
Dávalos, A., Goedeke, L., Smibert, P., Ramírez, C. M., Warrier, N. P., Andreo, U., Cirera-Salinas, D., Rayner, K., Suresh, U., Pastor-Pareja, J. C., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102281108 · Cited by 670 · see citing works
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 · see citing works
Self-citationHistone H4 lysine 16 acetylation regulates cellular lifespan
Dang, W., Steffen, K. K., Perry, R., Dorsey, J. A., Johnson, F. B., Shilatifard, A., Kaeberlein, M., Kennedy, B. K., & Berger, S. L. (2009) · Nature · doi:10.1038/nature08085 · Cited by 667 · see citing works
Min, H., Kapoor, A., Fuchs, M. A., Mirshahi, F., Zhou, H., Maher, J. W., Kellum, J. M., Warnick, R., Contos, M. J., & Sanyal, A. J. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.004 · Cited by 653 · see citing works
Vakhrusheva, O., Smolka, C., Gajawada, P., Sawa Kostin, D., Boettger, T., Kubin, T., Braun, T. W., & Bober, E. (2008) · Circulation Research · doi:10.1161/circresaha.107.164558 · Cited by 639 · see citing works
Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription
Ford, E., Voit, R., Liszt, G., Magin, C., Grummt, I., & Guarente, L. (2006) · Genes & Development · doi:10.1101/gad.1399706 · Cited by 629 · see citing works
SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation
Barber, M. F., Michishita-Kioi, E., Xi, Y., Tasselli, L., Kioi, M., Moqtaderi, Z., Tennen, R. I., Paredes, S., Young, N. L., Chen, K., et al. (2012) · Nature · doi:10.1038/nature11043 · Cited by 621 · see citing works
DNMT1 is required to maintain CpG methylation and aberrant gene silencing in human cancer cells
Robert, M., Morin, S., Beaulieu, N., Gauthier, F., Chute, I. C., Barsalou, A., & MacLeod, A. R. (2002) · Nature Genetics · doi:10.1038/ng1068 · Cited by 615 · see citing works
The Mammalian SIR2α Protein Has a Role in Embryogenesis and Gametogenesis
McBurney, M. W., Yang, X., Jardine, K., Hixon, M., Boekelheide, K., Webb, J. R., Lansdorp, P. M., & Lemieux, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.38-54.2003 · Cited by 611 · see citing works
A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
Masumoto, H., Hawke, D. H., Kobayashi, R., & Verreault, A. (2005) · Nature · doi:10.1038/nature03714 · Cited by 595 · see citing works
Sir2 Regulates Skeletal Muscle Differentiation as a Potential Sensor of the Redox State
Fulco, M., Schiltz, R. L., Iezzi, S., King, M. T., Zhao, P., Kashiwaya, Y., Hoffman, E. P., Veech, R. L., & Sartorelli, V. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00226-0 · Cited by 590 · see citing works
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 580 · see citing works
Rane, S., He, M., Sayed, D. H., Vashistha, H., Malhotra, A., Sadoshima, J., Vatner, D. E., Vatner, S. F., & Abdellatif, M. (2009) · Circulation Research · doi:10.1161/circresaha.108.193102 · Cited by 578 · see citing works
Sirtuins: critical regulators at the crossroads between cancer and aging
Saunders, L. R., & Verdin, E. M. (2007) · Oncogene · doi:10.1038/sj.onc.1210616 · Cited by 569 · see citing works
O’Hagan, H. M., Wang, W., Sen, S., Shields, C. E. D., Lee, S. S., Zhang, Y. W., Clements, E. G., Cai, Y., Neste, L. V., Easwaran, H., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.09.012 · Cited by 569 · see citing works
Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair
Bird, A. W., Yu, D. Y., Pray-Grant, M. G., Qiu, Q., Harmon, K. E., Megee, P. C., Grant, P. A., Smith, M. M., & Christman, M. F. (2002) · Nature · doi:10.1038/nature01035 · Cited by 565 · see citing works
Tanner, K. G., Landry, J. W., Sternglanz, R., & Denu, J. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250422697 · Cited by 557 · see citing works
Conformational Dynamics of the Chromatin Fiber in Solution: Determinants, Mechanisms, and Functions
Hansen, J. C. (2002) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.31.101101.140858 · Cited by 556 · see citing works
Methylation of Histone H4 Lysine 20 Controls Recruitment of Crb2 to Sites of DNA Damage
Sanders, S. L., Portoso, M., Mata, J., Bähler, J., Allshire, R. C., & Kouzarides, T. (2004) · Cell · doi:10.1016/j.cell.2004.11.009 · Cited by 545 · see citing works
SIRT2 Maintains Genome Integrity and Suppresses Tumorigenesis through Regulating APC/C Activity
Kim, H., Vassilopoulos, A., Wang, R.-H., Lahusen, T. J., Xiao, Z., Xu, X., Li, C., Veenstra, T. D., Li, B., Yu, H., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.09.004 · Cited by 536 · see citing works
Biochemistry and biology of mammalian DNA methyltransferases
Hermann, A., Gowher, H., & Jeltsch, A. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4201-1 · Cited by 536 · see citing works
Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure.
Poirier, G. G., de MURCIA, G., Jongstra‐Bilen, J., Niedergang, C., & Mandel, P. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.11.3423 · Cited by 516 · see citing works
Role for Human SIRT2 NAD-Dependent Deacetylase Activity in Control of Mitotic Exit in the Cell Cycle
Dryden, S. C., Nahhas, F. A., Nowak, J. E., Goustin, A. S., & Tainsky, M. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.9.3173-3185.2003 · Cited by 500 · see citing works
Akhtar, A., & Becker, P. B. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80431-1 · Cited by 482 · see citing works
MicroRNA 217 Modulates Endothelial Cell Senescence via Silent Information Regulator 1
Menghini, R., Casagrande, V., Cardellini, M., Martelli, E., Terrinoni, A., Amati, F., Vasa‐Nicotera, M., Ippoliti, A., Novelli, G., Melino, G., et al. (2009) · Circulation · doi:10.1161/circulationaha.109.864629 · Cited by 479 · see citing works
Scher, M. B., Vaquero, A., & Reinberg, D. (2007) · Genes & Development · doi:10.1101/gad.1527307 · Cited by 476 · see citing works
Self-citationMiR-34, SIRT1, and p53: The feedback loop
Yamakuchi, M., & Lowenstein, C. J. (2009) · Cell Cycle · doi:10.4161/cc.8.5.7753 · Cited by 468 · see citing works
Schotta, G., Sengupta, R., Kubicek, S., Malin, S., Kauer, M., Callén, E., Celeste, A., Pagani, M., Opravil, S., Rosa-Velázquez, I. A. D. L., et al. (2008) · Genes & Development · doi:10.1101/gad.476008 · Cited by 455 · see citing works
Histone H3 methylation links DNA damage detection to activation of the tumour suppressor Tip60
Sun, Y., Jiang, X., Xu, Y., Ayrapetov, M. K., Moreau, L. A., Whetstine, J. R., & Price, B. D. (2009) · Nature Cell Biology · doi:10.1038/ncb1982 · Cited by 454 · see citing works
Different Ezh2-Containing Complexes Target Methylation of Histone H1 or Nucleosomal Histone H3
Kuzmichev, A., Jenuwein, T., Tempst, P., & Reinberg, D. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00185-6 · Cited by 449 · see citing works
Acetylation of Histone H3 Lysine 56 Regulates Replication-Coupled Nucleosome Assembly
Li, Q., Zhou, H., Wurtele, H., Davies, B., Horazdovsky, B., Verreault, A., & Zhang, Z. (2008) · Cell · doi:10.1016/j.cell.2008.06.018 · Cited by 447 · see citing works
SirT1 Regulates Energy Metabolism and Response to Caloric Restriction in Mice
Boily, G., Seifert, E. L., Bevilacqua, L., He, X. H., Sabourin, G., Estey, C., Moffat, C., Crawford, S., Saliba, S., Jardine, K., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001759 · Cited by 444 · see citing works
SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation.
Vaquero, A., Scher, M., Erdjument-Bromage, H., Tempst, P., Serrano, L., & Reinberg, D. (2007) · Nature · doi:10.1038/nature06268 · Cited by 439 · see citing works
Self-citationChen, C., Carson, J. J., Feser, J., Tamburini, B. A. J., Zabaronick, S., Linger, J. G., & Tyler, J. K. (2008) · Cell · doi:10.1016/j.cell.2008.06.035 · Cited by 426 · see citing works
Kuzmichev, A., Margueron, R., Vaquero, A., Preissner, T. S., Scher, M. B., Kirmizis, A., Ouyang, X., Brockdorff, N., Abate-Shen, C. T., Farnham, P., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409875102 · Cited by 406 · see citing works
Self-citationAcetylation in Histone H3 Globular Domain Regulates Gene Expression in Yeast
Xu, F., Zhang, K., & Grunstein, M. R. (2005) · Cell · doi:10.1016/j.cell.2005.03.011 · Cited by 394 · see citing works
Epigenetic control of rDNA loci in response to intracellular energy status
Murayama, A., Ohmori, K., Fujimura, A., Minami, H., Yasuzawa-Tanaka, K., Kuroda, T., Oie, S., Daitoku, H., Okuwaki, M., Nagata, K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.03.030 · Cited by 394 · see citing works
Inhibition of SIRT1 Reactivates Silenced Cancer Genes without Loss of Promoter DNA Hypermethylation
Pruitt, K., Zinn, R. L., Ohm, J. E., McGarvey, K. M., Kang, S.-H. L., Watkins, D. N., Herman, J. G., & Baylin, S. B. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020040 · Cited by 387 · see citing works
Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6
Michishita, E., McCord, R. A., Boxer, L. D., Barber, M. F., Hong, T., Gozani, O., & Chua, K. F. (2009) · Cell Cycle · doi:10.4161/cc.8.16.9367 · Cited by 384 · see citing works
Heterochromatin Formation in Mammalian Cells
Nielsen, A. L., Oulad‐Abdelghani, M., Ortiz, J. A., Remboutsika, E., Chambon, P., & Losson, R. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00218-0 · Cited by 384 · see citing works
SIRT6 recruits SNF2H to DNA break sites, preventing genomic instability through chromatin remodeling
Toiber, D., Erdel, F., Bouazoune, K., Silberman, D. M., Zhong, L., Mulligan, P., Sebastian, C., Cosentino, C., Martinez-Pastor, B., Giacosa, S., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.018 · Cited by 381 · see citing works
Bouras, T., Fu, M., Sauve, A. A., Wang, F., Quong, A. A., Perkins, N. D., Hay, R. T., Gu, W. J., & Pestell, R. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408748200 · Cited by 354 · see citing works
Regulation of Homologous Recombination by RNF20-Dependent H2B Ubiquitination
Nakamura, K., Kato, A., Kobayashi, J., Yanagihara, H., Sakamoto, S., Oliveira, D. V. N. P., Shimada, M., Tauchi, H., Suzuki, H., Tashiro, S., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.002 · Cited by 351 · see citing works
Genetic Analysis of Histone H4: Essential Role of Lysines Subject to Reversible Acetylation
Megee, P. C., Morgan, B. A., Mittman, B. A., & Smith, M. M. (1990) · Science · doi:10.1126/science.2106160 · Cited by 349 · see citing works
Hino, R., Uozaki, H., Murakami, N., Ushiku, T., Shinozaki‐Ushiku, A., Ishikawa, S., Morikawa, T., Nakaya, T., Sakatani, T., Takada, K., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3070 · Cited by 344 · see citing works
Beck, D. B., Oda, H., Shen, S. S., & Reinberg, D. (2012) · Genes & Development · doi:10.1101/gad.177444.111 · Cited by 343 · see citing works
MicroRNA-34a regulation of endothelial senescence
Ito, T., Yagi, S., & Yamakuchi, M. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.07.012 · Cited by 336 · see citing works
Cohen-Armon, M., Visochek, L., Rozensal, D., Kalal, A., Geistrikh, I., Klein, R., Bendetz-Nezer, S., Yao, Z., & Seger, R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.012 · Cited by 329 · see citing works
The Dual Role of Sirtuins in Cancer
Bosch‐Presegué, L., & Vaquero, A. (2011) · Genes & Cancer · doi:10.1177/1947601911417862 · Cited by 329 · see citing works
Self-citationMethyl-CpG-binding Protein, MeCP2, Is a Target Molecule for Maintenance DNA Methyltransferase, Dnmt1
Kimura, H., & Shiota, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209923200 · Cited by 328 · see citing works
Zhao, T., Li, J., & Chen, A. F. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00192.2010 · Cited by 328 · see citing works
Interphase Nucleo-Cytoplasmic Shuttling and Localization of SIRT2 during Mitosis
North, B. J., & Verdin, E. M. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000784 · Cited by 326 · see citing works
Kim, J. K., Noh, J. H., Jung, K. H., Eun, J. W., Bae, H. J., Kim, M. G., Chang, Y. G., Shen, Q., Park, W. S., Lee, J. Y., et al. (2012) · Hepatology · doi:10.1002/hep.26101 · Cited by 322 · see citing works
Regulation of DNMT1 stability through SET7-mediated lysine methylation in mammalian cells
Estève, P., Chin, H. G., Benner, J. S., Feehery, G. R., Samaranayake, M., Horwitz, G. A., Jacobsen, S. E., & Pradhan, S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810362106 · Cited by 319 · see citing works
Oda, H., Okamoto, I., Murphy, N., Chu, J., Price, S. M., Shen, M. M., Torres-Padilla, M. E., Heard, É., & Reinberg, D. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01768-08 · Cited by 319 · see citing works
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 · see citing works
30 nm Chromatin Fibre Decompaction Requires both H4-K16 Acetylation and Linker Histone Eviction
Robinson, P. J. J., An, W., Routh, A. L., Martino, F., Chapman, L., Roeder, R. G., & Rhodes, D. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.04.050 · Cited by 311 · see citing works
Histone modifications: signalling receptors and potential elements of a heritable epigenetic code
Nightingale, K. P., O’Neill, L. P., & Turner, B. M. (2006) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2006.02.015 · Cited by 311 · see citing works
Rajamohan, S. B., Pillai, V. B., Gupta, M., Sundaresan, N. R., Birukov, K. G., Samant, S. A., Hottiger, M. O., & Gupta, M. P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00121-09 · Cited by 303 · see citing works
Celic, I., Masumoto, H., Griffith, W. P., Meluh, P. B., Cotter, R. J., Boeke, J. D., & Verreault, A. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.023 · Cited by 291 · see citing works
Hashimi, S. T., Fulcher, J. A., Chang, M. H., Gov, L., Wang, S., & Lee, B. (2009) · Blood · doi:10.1182/blood-2008-09-179150 · Cited by 291 · see citing works
MicroRNA-22 Regulates Cardiac Hypertrophy and Remodeling in Response to Stress
Huang, Z., Chen, J., Seok, H., Zhang, Z., Kataoka, M., Hu, X., & Wang, D.-Z. (2013) · Circulation Research · doi:10.1161/circresaha.112.300682 · Cited by 291 · see citing works
Bell, S. D., Botting, C. H., Wardleworth, B. N., Jackson, S. P., & White, M. F. (2002) · Science · doi:10.1126/science.1070506 · Cited by 289 · see citing works
The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells
Tardat, M., Brustel, J., Kirsh, O., Lefevbre, C., Callanan, M. B., Sardet, C., & Julien, E. (2010) · Nature Cell Biology · doi:10.1038/ncb2113 · Cited by 289 · see citing works
miR-22 represses cancer progression by inducing cellular senescence
Xu, D., Takeshita, F., Hino, Y., Fukunaga, S., Kudo, Y., Tamaki, A., Matsunaga, J., Takahashi, R., Takata, T., Shimamoto, A., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201010100 · Cited by 289 · see citing works
Serrano, L., Martínez‐Redondo, P., Marazuela-Duque, A., Vázquez, B. N., Dooley, S., Voigt, P., Beck, D. B., Kane‐Goldsmith, N., Tong, Q., Rabanal, R. M., et al. (2013) · Genes & Development · doi:10.1101/gad.211342.112 · Cited by 282 · see citing works
Self-citationParp‐1 protects homologous recombination from interference by Ku and Ligase IV in vertebrate cells
Hochegger, H., Dejsuphong, D., Fukushima, T., Morrison, C. G., Sonoda, E., Schreiber, V., Zhao, G., Saberi, A., Masutani, M., Adachi, N., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601015 · Cited by 276 · see citing works
Rine, J., Strathern, J. N., Hicks, J. B., & Herskowitz, I. (1979) · Genetics · doi:10.1093/genetics/93.4.877 · Cited by 268 · see citing works
A Role for SIRT2-Dependent Histone H3K18 Deacetylation in Bacterial Infection
Eskandarian, H. A., Impens, F., Nahori, M., Soubigou, G., Coppée, J., Cossart, P., & Hamon, M. A. (2013) · Science · doi:10.1126/science.1238858 · Cited by 268 · see citing works
Eades, G. L., Yao, Y., Yang, M., Zhang, Y., Chumsri, S., & Zhou, Q. Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.229401 · Cited by 263 · see citing works
Functions of poly(ADP-ribose) polymerase in controlling telomere length and chromosomal stability
di Fagagna, F. D., Hande, M. P., Tong, W., Lansdorp, P. M., Wang, Z.-Q., & Jackson, S. P. (1999) · Nature Genetics · doi:10.1038/12680 · Cited by 256 · see citing works
The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability
Yang, B., Zwaans, B. M. M., Eckersdorff, M., & Lombard, D. B. (2009) · Cell Cycle · doi:10.4161/cc.8.16.9329 · Cited by 254 · see citing works
Isolation of microRNA targets by miRNP immunopurification
Easow, G., Teleman, A. A., & Cohen, S. M. (2007) · RNA · doi:10.1261/rna.563707 · Cited by 252 · see citing works
Recht, J., Tsubota, T., Tanny, J. C., Diaz, R. L., Berger, J. M., Zhang, X., Garcia, B. A., Shabanowitz, J., Burlingame, A. L., Hunt, D. F., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601676103 · Cited by 248 · see citing works
Histone H3-K56 acetylation is important for genomic stability in mammals
Yuan, J., Pu, M., Zhang, Z., & Lou, Z. (2009) · Cell Cycle · doi:10.4161/cc.8.11.8620 · Cited by 247 · see citing works
Chromatin and the genome integrity network
Papamichos‐Chronakis, M., & Peterson, C. L. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3345 · Cited by 245 · see citing works
Sorting out functions of sirtuins in cancer
Roth, M., & Chen, W. (2013) · Oncogene · doi:10.1038/onc.2013.120 · Cited by 239 · see citing works
Cell Cycle and Checkpoint Regulation of Histone H3 K56 Acetylation by Hst3 and Hst4
Maas, N. L., Miller, K. M., DeFazio, L. G., & Toczyski, D. P. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.006 · Cited by 237 · see citing works
The Constantly Changing Face of Chromatin
Vaquero, A., Loyola, A., & Reinberg, D. (2003) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2003.14.re4 · Cited by 237 · see citing works
Self-citationSaunders, L. R., Sharma, A., Tawney, J., Nakagawa, M., Okita, K., Yamanaka, S., Willenbring, H., & Verdin, E. M. (2010) · Aging · doi:10.18632/aging.100176 · Cited by 237 · see citing works
Hyland, E. M., Cosgrove, M. S., Molina, H., Wang, D., Pandey, A., Cottee, R. J., & Boeke, J. D. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.22.10060-10070.2005 · Cited by 236 · see citing works
Daujat, S., Zeißler, U., Waldmann, T., Happel, N., & Schneider, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500229200 · Cited by 230 · see citing works
From Sirtuin Biology to Human Diseases: An Update
Sebastián, C., Satterstrom, F. K., Haigis, M. C., & Mostoslavsky, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.402768 · Cited by 228 · see citing works
MicroRNA 132 Regulates Nutritional Stress-Induced Chemokine Production through Repression of SirT1
Strum, J. C., Johnson, J. H., Ward, J. M., Xie, H., Feild, J. A., Hester, A. G., Alford, A., & Waters, K. M. (2009) · Molecular Endocrinology · doi:10.1210/me.2009-0117 · Cited by 226 · see citing works
The histone methyltransferase SET8 is required for S-phase progression
Jørgensen, S., Elvers, I., Trelle, M. B., Menzel, T., Eskildsen, M., Jensen, O. N., Helleday, T., Helin, K., & Sørensen, C. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200706150 · Cited by 225 · see citing works
SIRT1 Deacetylates the DNA Methyltransferase 1 (DNMT1) Protein and Alters Its Activities
Peng, L., Yuan, Z., Ling, H., Fukasawa, K., Robertson, K. D., Olashaw, N., Koomen, J. M., Chen, J., Lane, W. S., & Seto, E. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.06147-11 · Cited by 222 · see citing works
Faiola, F., Liu, X., Lo, S.-Y., Pan, S., Zhang, K., Lymar, E. S., Farina, A. N., & Martinez, E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.23.10220-10234.2005 · Cited by 218 · see citing works
The ACF1 Complex Is Required for DNA Double-Strand Break Repair in Human Cells
Lan, L., Ui, A., Nakajima, S., Hatakeyama, K., Hoshi, M., Watanabe, R., Janicki, S. M., Ogiwara, H., Kohno, T., Kanno, S., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.003 · Cited by 212 · see citing works
Li, N., Muthusamy, S., Liang, R., Sarojini, H., & Wang, E. (2011) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.12.004 · Cited by 211 · see citing works
A SIRT1-LSD1 Corepressor Complex Regulates Notch Target Gene Expression and Development
Mulligan, P., Yang, F., Stefano, L. D., Ji, J., Ouyang, J., Nishikawa, J. L., Toiber, D., Kulkarni, M., Wang, Q., Najafi-Shoushtari, S. H., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.020 · Cited by 211 · see citing works
Downregulation of miR-181a upregulates sirtuin-1 (SIRT1) and improves hepatic insulin sensitivity
Zhou, B., Li, C., Qi, W., Zhang, Y., Zhang, F., Wu, J., Hu, Y., Wu, D., Liu, Y., Yan, T., et al. (2012) · Diabetologia · doi:10.1007/s00125-012-2539-8 · Cited by 209 · see citing works
Egger, G., Jeong, S., Escobar, S. G., Cortez, C. C., Li, T. W. H., Saito, Y., Yoo, C. B., Jones, P. A., & Liang, G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604602103 · Cited by 208 · see citing works
E2F1-inducible microRNA 449a/b suppresses cell proliferation and promotes apoptosis
Lizé, M., Pilarski, S. M., & Dobbelstein, M. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.188 · Cited by 206 · see citing works
Kolthur‐Seetharam, U., Dantzer, F., McBurney, M. W., de MURCIA, G., & Sassone‐Corsi, P. (2006) · Cell Cycle · doi:10.4161/cc.5.8.2690 · Cited by 203 · see citing works
Acetylation of TAFI68, a subunit of TIF‐IB/SL1, activates RNA polymerase I transcription
Muth, V., Nadaud, S., Grummt, I., & Voit, R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1353 · Cited by 201 · see citing works
Tsai, Y.-C., Greco, T. M., Boonmee, A., Miteva, Y., & Cristea, I. M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.a111.015156 · Cited by 198 · see citing works
Poly(ADP-ribosyl)ated chromatin domains: access granted
Rouleau, M., Aubin, R. A., & Poirier, G. G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01080 · Cited by 194 · see citing works
SIRT3 Functions in the Nucleus in the Control of Stress-Related Gene Expression
Iwahara, T., Bonasio, R., Narendra, V. K., & Reinberg, D. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00822-12 · Cited by 192 · see citing works
Karachentsev, D., Sarma, K., Reinberg, D., & Steward, R. (2005) · Genes & Development · doi:10.1101/gad.1263005 · Cited by 191 · see citing works
MicroRNA-195 promotes palmitate-induced apoptosis in cardiomyocytes by down-regulating Sirt1
Zhu, H., Yang, Y., Wang, Y., Li, J., Schiller, P. W., & Peng, T. (2011) · Cardiovascular Research · doi:10.1093/cvr/cvr145 · Cited by 187 · see citing works
miR-34a Regulates Mouse Neural Stem Cell Differentiation
Aranha, M. M., dos Santos, D. M., Solá, S., Steer, C. J., & Rodrigues, C. M. P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021396 · Cited by 185 · see citing works
Dantzer, F., Giraud-Panis, M.-J. E., Jaco, I., Amé, J., Schultz, I., Blasco, M. A., Koering, C.-E., Gilson, É., Murcia, J. M., de MURCIA, G., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.4.1595-1607.2004 · Cited by 185 · see citing works
DNA repair: PARP – another guardian angel?
Jeggo, P. A. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70032-6 · Cited by 181 · see citing works
The Human Rap1 Protein Complex and Modulation of Telomere Length
O’Connor, M. S., Safari, A., Liu, D., Qin, J., & Songyang, Z. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312913200 · Cited by 181 · see citing works
Li, K., Casta, A., Wang, R., Lozada, E., Fan, W., Kane, S. E., Ge, Q., Gu, W. J., Orren, D. K., & Luo, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709707200 · Cited by 177 · see citing works
Han, Y., Liu, Y., Zhang, H., Wang, T., Diao, R., Jiang, Z., Gui, Y., & Cai, Z. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.10.023 · Cited by 176 · see citing works
p300-mediated Acetylation of Histone H3 Lysine 56 Functions in DNA Damage Response in Mammals
Vempati, R. K., Jayani, R. S., Notani, D., Sengupta, A., Galande, S., & Haldar, D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.149393 · Cited by 175 · see citing works
Meder, V., Boeglin, M., de MURCIA, G., & Schreiber, V. (2004) · Journal of Cell Science · doi:10.1242/jcs.01606 · Cited by 171 · see citing works
PR-Set7–dependent lysine methylation ensures genome replication and stability through S phase
Tardat, M., Murr, R., Herceg, Z., Sardet, C., & Julien, E. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200706179 · Cited by 170 · see citing works
Sirt6 Regulates Tnf-Alpha Secretion Through Hydrolysis of Long-Chain Fatty Acyl Lysine
Jiang, H. X., Khan, S., Wang, Y., Charron, G., He, B., Sebastián, C., Du, J., Kim, R., Ge, E. J., Mostoslavsky, R., et al. (2013) · Nature · doi:10.2210/pdb3zg6/pdb · Cited by 169 · see citing works
A Mechanism for Coordinating Chromatin Modification and Preinitiation Complex Assembly
Black, J. C., Choi, J. E., Lombardo, S. R., & Carey, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.07.018 · Cited by 168 · see citing works
Zhou, Q. Y., Agoston, A. T., Atadja, P. W., Nelson, W. G., & Davidson, N. E. (2008) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-0330 · Cited by 167 · see citing works
The SIRT2 Deacetylase Regulates Autoacetylation of p300
Black, J. C., Mosley, A. L., Kitada, T., Washburn, M. P., & Carey, M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.09.018 · Cited by 166 · see citing works
Establishment and Maintenance of DNA Methylation Patterns in Mammals
Chen, T., & Li, E. (2006) · Springer eBooks · doi:10.1007/3-540-31390-7_6 · Cited by 163 · see citing works
MicroRNA-217 Promotes Ethanol-induced Fat Accumulation in Hepatocytes by Down-regulating SIRT1
Yin, H., Hu, M., Zhang, R., Shen, Z., Flatow, L., & You, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.333534 · Cited by 163 · see citing works
Sir2 Deacetylates Histone H3 Lysine 56 to Regulate Telomeric Heterochromatin Structure in Yeast
Xu, F., Zhang, Q., Zhang, K., Xie, W., & Grunstein, M. R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.021 · Cited by 161 · see citing works
Takata, T., & Ishikawa, F. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)03020-6 · Cited by 159 · see citing works
Houston, S. I., McManus, K. J., Adams, M. M., Sims, J. K., Carpenter, P. B., Hendzel, M. J., & Rice, J. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710579200 · Cited by 155 · see citing works
miR-195 regulates SIRT1-mediated changes in diabetic retinopathy
Mortuza, R., Feng, B., & Chakrabarti, S. (2014) · Diabetologia · doi:10.1007/s00125-014-3197-9 · Cited by 153 · see citing works
Zhang, L., Wang, X., & Chen, P. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-290 · Cited by 153 · see citing works
miR-34a contributes to megakaryocytic differentiation of K562 cells independently of p53
Navarro, F., Gutman, D. A., Meire, E., Cáceres, M., Rigoutsos, I., Bentwich, Z., & Lieberman, J. (2009) · Blood · doi:10.1182/blood-2009-02-205062 · Cited by 152 · see citing works
Histone H4 deacetylation facilitates 53BP1 DNA damage signaling and double-strand break repair
Hsiao, K., & Mizzen, C. A. (2013) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjs066 · Cited by 152 · see citing works
MicroRNA-138 and SIRT1 form a mutual negative feedback loop to regulate mammalian axon regenerationPreprint
Liu, C.-M., Wang, R.-Y., Saijilafu, Jiao, Z.-X., Zhang, B.-Y., & Zhou, F. (2013) · Genes & Development · doi:10.1101/gad.209619.112 · Cited by 151 · see citing works
Chromatin state marks cell-type- and gender-specific replication of the Drosophila genomePreprint
Schwaiger, M., Stadler, M. B., Bell, O., Kohler, H., Oakeley, E. J., & Schübeler, D. (2009) · Genes & Development · doi:10.1101/gad.511809 · Cited by 151 · see citing works
SIRT6 in DNA repair, metabolism and ageing
Lombard, D. B., Schwer, B., Alt, F. W., & Mostoslavsky, R. (2008) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2007.01902.x · Cited by 146 · see citing works
Senawong, T., Peterson, V. J., Avram, D., Shepherd, D. M., Frye, R. A., Minucci, S., & Leid, M. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307477200 · Cited by 145 · see citing works
Smeenk, G., Wiegant, W. W., Marteijn, J. A. F., Luijsterburg, M. S., Sroczynski, N., Costelloe, T., Romeijn, R. J., Pastink, A., Mailand, N., Vermeulen, W., et al. (2012) · Journal of Cell Science · doi:10.1242/jcs.109413 · Cited by 145 · see citing works
Predicting and validating microRNA targets.
Lai, E. C. (2004) · Genome biology · doi:10.1186/gb-2004-5-9-115 · Cited by 141 · see citing works
Bosch-Presegué, L., Raurell-Vila, H., Marazuela-Duque, A., Kane-Goldsmith, N., Valle, A., Oliver, J., Serrano, L., & Vaquero, A. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.034 · Cited by 138 · see citing works
Self-citationmiRNA 34a, 100, and 137 modulate differentiation of mouse embryonic stem cells
Tarantino, C., Paolella, G., Cozzuto, L., Minopoli, G., Pastore, L., Parisi, S., & Russo, T. (2010) · The FASEB Journal · doi:10.1096/fj.09-152207 · Cited by 137 · see citing works
Liu, P., & Wilson, M. J. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22993 · Cited by 135 · see citing works
A miR‐34a‐SIRT6 axis in the squamous cell differentiation network
Lefort, K., Brooks, Y., Ostano, P., Cario, M., Calpini, V., Guinea‐Viniegra, J., Albinger‐Hegyi, A., Hoetzenecker, W., Kolfschoten, I., Wagner, E. F., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.156 · Cited by 135 · see citing works
Espada, J., Ballestar, E., Santoro, R., Fraga, M. F., Villar‐Garea, A., Németh, A., Lopez-Serra, L., Ropero, S., Aranda, A., Orozco, H., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm118 · Cited by 134 · see citing works
The Role of SIRT6 Protein in Aging and Reprogramming of Human Induced Pluripotent Stem Cells
Sharma, A. S., Diecke, S., Zhang, W. Y., Lan, F., He, C., Mordwinkin, N. M., Chua, K. F., & Wu, J. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.405928 · Cited by 128 · see citing works
Garcia-Salcedo, J. A., Gijón, P., Nolan, D. P., Tebabi, P., & Pays, E. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg553 · Cited by 127 · see citing works
PARP1 Is a TRF2-associated Poly(ADP-Ribose)Polymerase and Protects Eroded Telomeres
Gomez, M., Wu, J., Schreiber, V., Dunlap, J. R., Dantzer, F., Wang, Y., & Liu, Y. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0672 · Cited by 125 · see citing works
Structure of the SET domain histone lysine methyltransferase Clr4
Min, J., Zhang, X., Cheng, X., Grewal, S. I. S., & Xu, R.-M. (2002) · Nature Structural Biology · doi:10.1038/nsb860 · Cited by 124 · see citing works
Sirtuins in stress response: guardians of the genome
Bosch‐Presegué, L., & Vaquero, A. (2013) · Oncogene · doi:10.1038/onc.2013.344 · Cited by 124 · see citing works
Self-citationSirtuins in neurodegenerative diseases: an update on potential mechanisms
Min, S., Sohn, P., Cho, S.-H., Swanson, R. A., & Gan, L. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00053 · Cited by 123 · see citing works
Sirt2 functions in spindle organization and chromosome alignment in mouse oocyte meiosis
Zhang, L. N., Hou, X., Ma, R., Moley, K. H., Schedi, T., & Wang, Q. (2013) · The FASEB Journal · doi:10.1096/fj.13-244111 · Cited by 122 · see citing works
SIRT4 protein suppresses tumor formation in genetic models of Myc-induced B cell lymphoma
Jeong, S. M., Lee, A., Lee, J., & Haigis, M. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525949 · Cited by 121 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- Strum JC, Johnson JH, Ward J, Xie H, Feild J, Hester A, Alford A & Waters KM (2009) MicroRNA 132 regulates nutritional stress-induced chemokine 1766 FEBS Journal 282 (2015) 1745-1767 ª 2014 FEBS
- Sirtuins and genome stability L. Bosch-Presegu e and A. Vaquero 17424658, 2015, 9, Downloaded from https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.13053 by Readcube (Labtiva Inc.), Wiley Online Library on [08/10/2023]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License production through repression of SirT1. Mol Endocrinol 23, 1876-1884. 234 · DOI
Cited by
Sorted by citations
The world of protein acetylation
Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 799 · see citing works
Penner-Goeke, S., & Binder, E. B. (2019) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2019.21.4/ebinder · Cited by 254 · see citing works
The Substrate Specificity of Sirtuins
Bheda, P., Jing, H., Wolberger, C., & Lin, H. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014537 · Cited by 247 · see citing works
Lei, Y., Wang, J., Wang, D., Li, C., Liu, B., Fang, X., You, J., Guo, M., & Lu, X.-Y. (2020) · Molecular Psychiatry · doi:10.1038/s41380-019-0352-1 · Cited by 131 · see citing works
Corpas, R., Revilla, S., Ursulet, S., Castro, M., Kaliman, P., Petegnief, V., Giménez‐Llort, L., Sarkis, C., Pallàs, M., & Sanfeliu, C. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0087-9 · Cited by 121 · see citing works
Sirt7 promotes adipogenesis in the mouse by inhibiting autocatalytic activation of Sirt1
Fang, J. C., Ianni, A., Smolka, C., Vakhrusheva, O., Nolte, H., Krüger, M., Wietelmann, A., Simonet, N. G., Adrian-Segarra, J. M., Vaquero, A., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706945114 · Cited by 118 · see citing works
Self-citationFunctions and mechanisms of plant histone deacetylases
Chen, X., Ding, A. B., & Zhong, X. (2019) · Science China Life Sciences · doi:10.1007/s11427-019-1587-x · Cited by 119 · see citing works
Liu, X., Cai, S., Zhang, C., Liu, Z., Luo, J., Xing, B., & Du, X. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky777 · Cited by 114 · see citing works
Histone Modifications in Alzheimer’s Disease
Santana, D. A., Smith, M. D. A. C., & Chen, E. (2023) · Genes · doi:10.3390/genes14020347 · Cited by 109 · see citing works
Salminen, A., Kauppinen, A., & Kaarniranta, K. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.03.009 · Cited by 100 · see citing works
Sirtuins and DNA damage repair: SIRT7 comes to play
Vázquez, B. N., Thackray, J. K., & Serrano, L. (2017) · Nucleus · doi:10.1080/19491034.2016.1264552 · Cited by 92 · see citing works
Yang, L., Chen, X., Wang, Z., Sun, Q., Hong, A., Zhang, A., Zhong, X., & Hua, J. (2019) · New Phytologist · doi:10.1111/nph.16380 · Cited by 92 · see citing works
Therapeutic role of sirtuins in neurodegenerative disease and their modulation by polyphenols
Ajami, M., Pazoki–Toroudi, H., Amani, H., Nabavi, S. F., Braidy, N., Vacca, R. A., Atanasov, A. G., MOCAN, A., & Nabavi, S. M. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.11.022 · Cited by 91 · see citing works
Dissecting bipolar disorder complexity through epigenomic approach
Ludwig, B., & Dwivedi, Y. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.123 · Cited by 85 · see citing works
Tang, S., Fang, Y., Huang, G., Xu, X., Padilla‐Banks, E., Fan, W., Xu, Q., Sanderson, S. M., Foley, J. F., Dowdy, S., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796708 · Cited by 78 · see citing works
BST1 regulates nicotinamide riboside metabolism via its glycohydrolase and base-exchange activities
Yaku, K., Palikhe, S., Izumi, H., Yoshida, T., Hikosaka, K., Hayat, F., Karim, M., Iqbal, T., Nitta, Y., Sato, A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27080-3 · Cited by 76 · see citing works
The functional genomic studies of resveratrol in respect to its anti-cancer effects
Huminiecki, Ł., & Horbańczuk, J. O. (2018) · Biotechnology Advances · doi:10.1016/j.biotechadv.2018.02.011 · Cited by 74 · see citing works
SIRT1-dependent epigenetic regulation of H3 and H4 histone acetylation in human breast cancer
Rifai, K. T., Judes, G., Idrissou, M., Daures, M., Bignon, Y., Penault-Llorca, F. M., & Bernard-Gallon, D. J. (2018) · Oncotarget · doi:10.18632/oncotarget.25771 · Cited by 69 · see citing works
PWR/HDA9/ABI4 Complex Epigenetically Regulates ABA Dependent Drought Stress Tolerance in Arabidopsis
Khan, I. U., Ali, A. A., Khan, H. A., Baek, D., Park, J., Lim, C. J., Zareen, S., Jan, M., Lee, S. Y., Pardo, J. M., et al. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.00623 · Cited by 67 · see citing works
Understanding Dietary Intervention-Mediated Epigenetic Modifications in Metabolic Diseases
Asif, S., Morrow, N. M., Mulvihill, E. E., & Kim, K.-H. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.590369 · Cited by 69 · see citing works
The Role of Histone Protein Acetylation in Regulating Endothelial Function
Fang, Z. H., Wang, X., Sun, X., Hu, W., & Miao, Q. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.672447 · Cited by 65 · see citing works
Hekmatimoghaddam, S., Firoozabadi, A. D., Zare‐Khormizi, M. R., & Pourrajab, F. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.10.001 · Cited by 62 · see citing works
Canonical and Noncanonical Actions of Arabidopsis Histone Deacetylases in Ribosomal RNA Processing
Chen, X., Lü, L., Qian, S., Scalf, M., Smith, L. M., & Zhong, X. (2018) · The Plant Cell · doi:10.1105/tpc.17.00626 · Cited by 56 · see citing works
Decoding the Rosetta stone of mitonuclear communication
English, J., Son, J. M., Cardamone, M. D., Lee, C., & Perissi, V. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105161 · Cited by 55 · see citing works
Tabassum, S., Misrani, A. A., Huang, H., Zhang, Z.-Y., Li, Q.-W., & Long, C. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03395-8 · Cited by 55 · see citing works
Tanabe, K., Liu, J., Kato, D., Kurumizaka, H., Yamatsugu, K., Kanai, M., & Kawashima, S. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-21060-2 · Cited by 53 · see citing works
A Molecular Perspective on Sirtuin Activity
Teixeira, C. S. S., Cerqueira, N. M. F. S. A., Gomes, P., & Sousa, S. F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228609 · Cited by 56 · see citing works
Cerbaro, A. F., Rodrigues, V. S. B., Rigotti, M., Branco, C. S., Rech, G., de Oliveira, D. L., & Salvador, M. M. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05401-x · Cited by 54 · see citing works
Bhatiya, M., Pathak, S., Jothimani, G., Duttaroy, A. K., & Banerjee, A. (2023) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-023-00669-w · Cited by 51 · see citing works
Goutham, G., Manikandan, R., Manikandan, B., Raman, T., Chinnasamy, A., Arumugam, M., Setzer, W. N., Daglia, M., Nabavi, S. F., & Nabavi, S. M. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.11.141 · Cited by 45 · see citing works
Sirtuins and their interactions with transcription factors and poly(ADP-ribose) polymerases
Jęśko, H. M., & Strosznajder, R. P. (2016) · Folia Neuropathologica · doi:10.5114/fn.2016.62531 · Cited by 44 · see citing works
Roles of vitamins in stem cells
Godoy-Parejo, C., Deng, C., Zhang, Y., Liu, W., & Chen, G. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03352-6 · Cited by 44 · see citing works
Capsaicin reactivates hMOF in gastric cancer cells and induces cell growth inhibition
Wang, F., Zhao, J., Liu, D., Zhao, T., Lu, Z., Zhu, L., Cao, L., Yang, J., Jin, J., & Cai, Y. (2016) · Cancer Biology & Therapy · doi:10.1080/15384047.2016.1235654 · Cited by 42 · see citing works
Palomer, E., Martín‐Flores, N., Jolly, S., Vargas, P. P., Benvegnù, S., Podpolny, M., Teo, S., Vaher, K., Saito, T., Saido, T. C., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01492-z · Cited by 42 · see citing works
Sirtuins as novel targets in the pathogenesis of airway inflammation in bronchial asthma
Ma, K., Lu, N., Zou, F., & Meng, F. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172670 · Cited by 41 · see citing works
Epigenetic Regulation of Aging and its Rejuvenation
An, Y., Wang, Q., Gao, K., Zhang, C., Ouyang, Y., Li, R., Zhou, M., Wu, T., Zhou, L., Xie, Z., et al. (2025) · MedComm · doi:10.1002/mco2.70369 · Cited by 44 · see citing works
SIRT2 regulates nuclear envelope reassembly through ANKLE2 deacetylation
Kaufmann, T., Kukolj, E., Brachner, A., Beltzung, E., Bruno, M., Kostrhon, S., Opravil, S., Hudecz, O., Mechtler, K., Warren, G., et al. (2016) · Journal of Cell Science · doi:10.1242/jcs.192633 · Cited by 40 · see citing works
The Pleiotropic Function of Human Sirtuins as Modulators of Metabolic Pathways and Viral Infections
Alqarni, M. H., Foudah, A. I., Muharram, M. M., & Labrou, N. E. (2021) · Cells · doi:10.3390/cells10020460 · Cited by 38 · see citing works
NAD+ centric mechanisms and molecular determinants of skeletal muscle disease and aging
Wagner, S., Manickam, R., Brotto, M. A. P., & Tipparaju, S. M. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04408-1 · Cited by 39 · see citing works
Mahon, R. N., & Hafner, R. (2015) · Clinical Infectious Diseases · doi:10.1093/cid/civ621 · Cited by 36 · see citing works
Tanwar, V., Adelstein, J. M., Grimmer, J. A., Youtz, D. J., Katapadi, A., Sugar, B. P., Falvo, M. J., Baer, L. A., Stanford, K. I., & Wold, L. E. (2018) · Journal of the American Heart Association · doi:10.1161/jaha.118.010797 · Cited by 35 · see citing works
Nuclear Sirtuins and the Aging of the Immune System
Gámez-García, A., & Vázquez, B. N. (2021) · Genes · doi:10.3390/genes12121856 · Cited by 33 · see citing works
Chano, T., Avnet, S., Kusuzaki, K., Bonuccelli, G., Sonveaux, P., Rotili, D., Mai, A., & Baldini, N. (2016) · PubMed Central · Cited by 34 · see citing works
Breaking down the Contradictory Roles of Histone Deacetylase SIRT1 in Human Breast Cancer
Rifai, K. T., Idrissou, M., Penault-Llorca, F. M., Bignon, Y., & Bernard-Gallon, D. J. (2018) · Cancers · doi:10.3390/cancers10110409 · Cited by 33 · see citing works
SIRT1 regulates DNA damage signaling through the PP4 phosphatase complex
Rasti, G., Becker, M., Vázquez, B. N., Espinosa‐Alcantud, M., Fernández-Duran, I., Gámez-García, A., Ianni, A., González, J., Bosch‐Presegué, L., Marazuela-Duque, A., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad504 · Cited by 33 · see citing works
Self-citationA positive feedback loop of SIRT1 and miR17HG promotes the repair of DNA double-stranded breaks
Xie, L., Huang, R., Liu, S., Wu, W., Su, A., Li, R., Liu, X. D., Lei, Y., Sun, H., Liu, X., et al. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1641388 · Cited by 32 · see citing works
Farr, G. H., Morris, M., Gómez, A. E., Pham, T. Q., Parker, E. U., Kilroy, E., Said, S., Henry, C. A., & Maves, L. (2020) · Skeletal Muscle · doi:10.1186/s13395-020-00251-4 · Cited by 33 · see citing works
Innate Immune Training Initiates Efferocytosis to Protect against Lung Injury
Kang, Y., Kim, D., Lee, S., Kim, H., Kim, T.-B., Cho, J. A., Lee, T., & Choi, E. Y. (2024) · Advanced Science · doi:10.1002/advs.202308978 · Cited by 31 · see citing works
Li, X., Feng, L., Zhang, C., Wang, J., Wang, S., & Hu, L. (2022) · Science China Life Sciences · doi:10.1007/s11427-021-2096-0 · Cited by 30 · see citing works
SIRT7 promotes chromosome synapsis during prophase I of female meiosis
Vázquez, B. N., Blengini, C. S., Hernandez, Y., Serrano, L., & Schindler, K. (2019) · Chromosoma · doi:10.1007/s00412-019-00713-9 · Cited by 29 · see citing works
Montali, I., Berti, C. C., Morselli, M., Acerbi, G., Barili, V., Pedrazzi, G., Montanini, B., Boni, C., Alfieri, A., Pesci, M., et al. (2023) · Journal of Hepatology · doi:10.1016/j.jhep.2023.02.035 · Cited by 30 · see citing works
Interplay Between Genetic and Epigenetic Mechanisms in Rheumatoid Arthritis
Frank‐Bertoncelj, M., Klein, K., & Gay, S. (2017) · Epigenomics · doi:10.2217/epi-2016-0142 · Cited by 29 · see citing works
Sarikhani, M., Garbern, J. C., Ma, S., Sereda, R., Conde, J., Krähenbühl, G., Escalante, G. O., Ahmed, A., Buenrostro, J. D., & Lee, R. T. (2020) · Stem Cell Reports · doi:10.1016/j.stemcr.2020.06.012 · Cited by 30 · see citing works
Wang, Y., Yang, F., Jiao, F., Chen, Q., Zhang, W., Wang, L.-W., & Gong, Z. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8173016 · Cited by 27 · see citing works
Scientometric Analysis of SIRT6 Studies
Lu, K., Yu, S., Sun, D., Xing, H., An, J., Kong, C., Yu, M., & Zhu, Y. (2018) · Medical Science Monitor · doi:10.12659/msm.913644 · Cited by 26 · see citing works
Could sirtuin activities modify ALS onset and progression?
Tang, B. L. (2017) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0452-2 · Cited by 24 · see citing works
Lactate Metabolism and Satellite Cell Fate
Nalbandian, M., Radak, Z. O., & Takeda, M. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.610983 · Cited by 24 · see citing works
Epigenetic Regulators of White Adipocyte Browning
Nanduri, R. (2021) · Epigenomes · doi:10.3390/epigenomes5010003 · Cited by 23 · see citing works
The circadian clock: a central mediator of cartilage maintenance and osteoarthritis development?
Poulsen, R. C., Hearn, J. I., & Dalbeth, N. (2021) · Rheumatology · doi:10.1093/rheumatology/keab197 · Cited by 22 · see citing works
Liu, C.-L., Zhao, D., Li, J.-J., Liu, S., An, J.-J., Wang, D., Hu, F.-A., Qiu, C.-Y., & Cui, M.-H. (2021) · Neoplasma · doi:10.4149/neo_2021_210623n834 · Cited by 23 · see citing works
Qin, T., Liu, W., Huo, J., Li, L., Zhang, X., Shi, X., Zhou, J., & Wang, C. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.04.032 · Cited by 23 · see citing works
Epigenetic and non-epigenetic mode of SIRT1 action during oocyte meiosis progression
Nevoral, J., Landsmann, L., Štiavnická, M., Hošek, P., Moravec, J., Prokešová, Š., Řimnáčová, H., Koutná, E., Klein, P., Hošková, K., et al. (2019) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-019-0372-3 · Cited by 23 · see citing works
Tantawy, A. H., Meng, X., Marzouk, A. A. E., Fouad, A., Abdelazeem, A. H., Youssif, B. G. M., Jiang, H. X., & Wang, M. (2021) · RSC Advances · doi:10.1039/d1ra04061h · Cited by 21 · see citing works
Zheng, W., Tasselli, L., Li, T., & Chua, K. F. (2021) · Genes · doi:10.3390/genes12091460 · Cited by 21 · see citing works
Sirtuin-dependent metabolic and epigenetic regulation of macrophages during tuberculosis
Zhang, K., Sowers, M. L., Cherryhomes, E., Singh, V. K., Mishra, A., Restrepo, B. I., Khan, A., & Jagannath, C. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1121495 · Cited by 21 · see citing works
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 · see citing works
Chang, Y., He, B., Wang, C., Li, W., Tao, S., Chen, J., Wang, Y., Yang, L., Wu, Y., Wu, Z., et al. (2025) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2025.2491638 · Cited by 23 · see citing works
Epi-drugs as triple-negative breast cancer treatment
Idrissou, M., Sánchez, A., Penault-Llorca, F. M., Bignon, Y., & Bernard-Gallon, D. J. (2020) · Epigenomics · doi:10.2217/epi-2019-0312 · Cited by 20 · see citing works
Multifaced role of protein deacetylase sirtuins in neurodegenerative disease
Gupta, R. V., Ambasta, R. K., & Kumar, P. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.10.047 · Cited by 20 · see citing works
Synthesis of certain benzothieno[3,2-d]pyrimidine derivatives as a selective SIRT2 inhibitors
Khalil, N. A., Ahmed, E., Zaher, A. F., El‐Zoghbi, M. S., & Sobh, E. A. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111926 · Cited by 20 · see citing works
The Fundamental Role of Nutrients for Metabolic Balance and Epigenome Integrity Maintenance
de Souza, A. P., Marinho, V., & Marques, M. R. (2025) · Epigenomes · doi:10.3390/epigenomes9030023 · Cited by 19 · see citing works
Yuan, Y., Xu, L., Zhang, S., Mesalam, A., Lee, K., Liu, H., Joo, M., Idrees, M., & Kong, I. (2019) · Theriogenology · doi:10.1016/j.theriogenology.2019.05.007 · Cited by 19 · see citing works
Simó‐Mirabet, P., Perera, E., Calduch-Giner, J. À., & Pérez‐Sánchez, J. (2020) · Frontiers in Zoology · doi:10.1186/s12983-020-00361-1 · Cited by 17 · see citing works
Barili, V., Vecchi, A. L., Rossi, M., Montali, I., Tiezzi, C., Penna, A., Laccabue, D., Missale, G., Fisicaro, P., & Boni, C. (2021) · Cells · doi:10.3390/cells10102563 · Cited by 18 · see citing works
Histone Modifications and Their Targeting in Lymphoid Malignancies
Fernández-Serrano, M., Winkler, R., Santos, J. C., Pannérer, M.-M. L., Buschbeck, M., & Roué, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010253 · Cited by 14 · see citing works
Identification of novel SIRT1 activators endowed with cardioprotective profile
Flori, L., Petrarolo, G., Brogi, S., Motta, C. L., Testai, L., & Calderone, V. (2021) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2021.105930 · Cited by 15 · see citing works
Zhang, J., Li, Y., Liu, J., Han, F., Shi, J., Wu, G., Wang, K., Shen, K., Zhao, M., Gao, X., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105236 · Cited by 15 · see citing works
Anti-ageing effects of FDA-approved medicines: a focused review
Thanapairoje, K., Junsiritrakhoon, S., Wichaiyo, S., Osman, M. A., & Supharattanasitthi, W. (2023) · Journal of Basic and Clinical Physiology and Pharmacology · doi:10.1515/jbcpp-2022-0242 · Cited by 15 · see citing works
Jafarpour, F., Zadegan, F. G., Ostadhosseini, S., Hajian, M., Kiani‐Esfahani, A., & Nasr‐Esfahani, M. H. (2020) · PLoS ONE · doi:10.1371/journal.pone.0233880 · Cited by 15 · see citing works
Mertsch, S., & Krämer, O. H. (2017) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2017.05.006 · Cited by 14 · see citing works
SIRT1 Synchs Satellite Cell Metabolism with Stem Cell Fate
Díaz‐Ruiz, A., González‐Freire, M., Ferrucci, L., Bernier, M., & de Cabo, R. (2015) · Cell stem cell · doi:10.1016/j.stem.2015.01.006 · Cited by 14 · see citing works
Deciphering the Epigenetic Code in Embryonic and Dental Pulp Stem Cells.
Bayarsaihan, D. (2016) · Europe PMC (PubMed Central) · Cited by 14 · see citing works
Isohookana, J., Haapasaari, K., Soini, Y., & Karihtala, P. (2018) · Anticancer Research · doi:10.21873/anticanres.12474 · Cited by 14 · see citing works
Multifunctional activity-based chemical probes for sirtuins
Sharma, C., Donu, D., Curry, A. M., Barton, E. E., & Cen, Y. (2023) · RSC Advances · doi:10.1039/d3ra02133e · Cited by 13 · see citing works
Substrate-Dependent Sensitivity of SIRT1 to Nicotinamide Inhibition
Rymarchyk, S., Kang, W., & Cen, Y. (2021) · Biomolecules · doi:10.3390/biom11020312 · Cited by 13 · see citing works
Deciphering histone H4 lysine acetylation and methylation via sortase-mediated semisynthesis
Xiao, Y., Zou, K., Yang, J. T., & Wu, M. (2023) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2023.101638 · Cited by 13 · see citing works
Zhang, N., Liu, L., Li, S., Wei, Y., Ren, W., Li, M., Zhao, S., Sun, Z., Yang, X., Ren, Y. N., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2500029122 · Cited by 12 · see citing works
Konada, L., Aricthota, S., Vadla, R., & Haldar, D. (2018) · Scientific Reports · doi:10.1038/s41598-018-26476-4 · Cited by 11 · see citing works
Ghazi, T., Nagiah, S., Dhani, S., & Chuturgoon, A. A. (2020) · Epigenomics · doi:10.2217/epi-2019-0284 · Cited by 11 · see citing works
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 · see citing works
Effects of sirtuins on the riboflavin production in Ashbya gossypii
Kato, T., Azegami, J., Kano, M., Enshasy, H. A. E., & Park, E. Y. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11595-2 · Cited by 9 · see citing works
Nutraceuticals for Promoting Longevity
Pavlović, I., Khateb, S., Milisav, I., & Mahajna, J. A. (2020) · Current Nutraceuticals · doi:10.2174/2665978601666200213121512 · Cited by 8 · see citing works
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 · see citing works
Cai, Q., Li, T., Xiè, J., & Jiāng, D. (2024) · Microbiology Spectrum · doi:10.1128/spectrum.03137-23 · Cited by 6 · see citing works
Das, A., Giri, A. K., & Bhattacharjee, P. (2024) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2024.195007 · Cited by 6 · see citing works
Lee, Y. T., Tan, Y. J., Mok, P. Y., Kaur, G., Sasidharan, S., Falasca, M., & Oon, C. E. (2022) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2022.116039 · Cited by 6 · see citing works
Sgueglia, G., Longobardi, S., Valerio, D., Campitiello, M. R., Colacurci, N., Pietro, C. D., Battaglia, R., D’Hooghe, T. M., Altucci, L., & Dell’Aversana, C. (2023) · Clinical Epigenetics · doi:10.1186/s13148-023-01490-0 · Cited by 7 · see citing works
Zhou, Q., Jiang, N., Dong, Y., & Tian, K. (2023) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2023.110698 · Cited by 5 · see citing works
Liver Diseases: Epigenetic Mechanisms, Oxidative Stress and Use of Alpha-Lipoic Acid
Uskoković, A. S., Dinić, S., Јovanović, J. A., Poznanović, G., Vidaković, M., & Mihailović, M. (2017) · Springer eBooks · doi:10.1007/978-3-319-31143-2_112-1 · Cited by 5 · see citing works
Muñoz‐Cánoves, P., & Croce, L. D. (2015) · FEBS Journal · doi:10.1111/febs.13281 · Cited by 4 · see citing works
- Authors
- Bosch‐Presegué, L., & Vaquero, A.
- Affiliations
- Institut d'Investigació Biomédica de Bellvitge (ES)
- Corresponding author
- Vaquero, Alejandro
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2014-10-13
- Volume
- 282
- Issue
- 9
- Pages
- 1745-1767
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W1976682189
- Cited by
- 132
- References
- 257
- Citations by year
- 2026: 9 · 2025: 7 · 2024: 5 · 2023: 13 · 2022: 10 · 2021: 21 · 2020: 16 · 2019: 14 · 2018: 13 · 2017: 7 · 2016: 13 · 2015: 4
- FWCI
- 0.68
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministerio de Economía y Competitividad (SAF2011-25860)
- Fundació La marato de TV3 (20133810)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- sirtuins, epigenetic regulation, genome stability, histone deacetylation, NAD+, H4K16ac, H3K9ac, H3K18ac, non-histone proteins, stress response, energy homeostasis, chromatin remodeling
- MeSH terms
- Energy Metabolism, Sirtuins, Genomic Instability, Epigenesis, Genetic
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