The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases

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

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

Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity

Frye, R. A. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0897 · Cited by 809 · see citing works

Transcriptional silencing in yeast is associated with reduced nucleosome acetylation.Preprint

Braunstein, M., Rose, A. B., Holmes, S. G., Allis, C. D., & Broach, J. R. (1993) · Genes & Development · doi:10.1101/gad.7.4.592 · Cited by 792 · see citing works

Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast

Hecht, A., Laroche, T., Strahl‐Bolsinger, S., Gasser, S. M., & Grunstein, M. R. (1995) · Cell · doi:10.1016/0092-8674(95)90512-x · Cited by 780 · see citing works

Exit from Mitosis Is Triggered by Tem1-Dependent Release of the Protein Phosphatase Cdc14 from Nucleolar RENT Complex

Shou, W., Seol, J. H., Shevchenko, A., Baskerville, C., Moazed, D., Chen, Z. W. S., Jang, J., Shevchenko, A., Charbonneau, H., & Deshaies, R. J. (1999) · Cell · doi:10.1016/s0092-8674(00)80733-3 · Cited by 702 · see citing works

The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability.Preprint

Brachmann, C. B., Sherman, J. M., Devine, S. E., Cameron, E. E., Pillus, L., & Boeke, J. D. (1995) · Genes & Development · doi:10.1101/gad.9.23.2888 · Cited by 605 · see citing works

Structure and Utilization of Tubulin Isotypes

Sullivan, K. F. (1988) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.04.110188.003351 · Cited by 478 · see citing works

NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM‐related cofactor Tra1p

Allard, S., Utley, R. T., Savard, J., Clarke, A. S., Grant, P. A., Brandl, C. J., Pillus, L., Workman, J. L., & Côté, J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.18.5108 · Cited by 460 · see citing works

The Major Cytoplasmic Histone Acetyltransferase in Yeast: Links to Chromatin Replication and Histone Metabolism

Parthun, M. R., Widom, J., & Gottschling, D. E. (1996) · Cell · doi:10.1016/s0092-8674(00)81325-2 · Cited by 440 · see citing works

An Enzymatic Activity in the Yeast Sir2 Protein that Is Essential for Gene Silencing

Tanny, J. C., Dowd, G. J., Huang, J., Hilz, H., & Moazed, D. (1999) · Cell · doi:10.1016/s0092-8674(00)81671-2 · Cited by 391 · see citing works

Net1, a Sir2-Associated Nucleolar Protein Required for rDNA Silencing and Nucleolar Integrity

Straight, A. F., Shou, W., Dowd, G. J., Turck, C. W., Deshaies, R. J., Johnson, A. D., & Moazed, D. (1999) · Cell · doi:10.1016/s0092-8674(00)80734-5 · Cited by 389 · see citing works

Identification of a Gene Encoding a Yeast Histone H4 Acetyltransferase

Kleff, S., Andrulis, E. D., Anderson, C. W., & Sternglanz, R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.42.24674 · Cited by 353 · see citing works

Acetylation of MyoD Directed by PCAF Is Necessary for the Execution of the Muscle Program

Sartorelli, V., Puri, P., Hamamori, Y., Ogryzko, V. V., Chung, G., Nakatani, Y., Wang, J. Y. J., & Kedes, L. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80383-4 · Cited by 353 · see citing works

Esa1p Is an Essential Histone Acetyltransferase Required for Cell Cycle Progression

Clarke, A. S., Lowell, J. E., Jacobson, S. J., & Pillus, L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2515 · Cited by 347 · see citing works

Histones of Drosophila Embryos

Alfageme, C. R., Zweidler, A., Mahowald, A. P., & Cohen, L. H. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42534-9 · Cited by 336 · see citing works

ESA1 is a histone acetyltransferase that is essential for growth in yeast

Smith, E. R., Eisen, A., Gu, W., Sattah, M., Pannuti, A., Zhou, J., Cook, R. G., Lucchesi, J. C., & Allis, C. D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3561 · Cited by 322 · see citing works

A Role for Histone Acetylation in the Developmental Regulation of V(D)J Recombination

McMurry, M. T., & Krangel, M. S. (2000) · Science · doi:10.1126/science.287.5452.495 · Cited by 288 · see citing works

Silencing and Heritable Domains of Gene Expression

Loo, S., & Rine, J. (1995) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cb.11.110195.002511 · Cited by 195 · see citing works

Diverse and dynamic functions of the Sir silencing complex

Guarente, L. (1999) · Nature Genetics · doi:10.1038/15458 · Cited by 154 · see citing works

CobB, a New Member of the SIR2 Family of Eucaryotic Regulatory Proteins, Is Required to Compensate for the Lack of Nicotinate Mononucleotide:5,6-Dimethylbenzimidazole Phosphoribosyltransferase Activity in cobT Mutants during Cobalamin Biosynthesis in Salmonella typhimurium LT2

Tsang, A. W., & Escalante‐Semerena, J. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.31788 · Cited by 148 · see citing works

Phenotypic switching in Candida albicans is controlled by a SIR2 gene

Pérez‐Martín, J., Urı́a, J. A., & Johnson, A. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.9.2580 · Cited by 137 · see citing works

Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2

Afshar, G., & Murnane, J. P. (1999) · Gene · doi:10.1016/s0378-1119(99)00162-6 · Cited by 130 · see citing works

Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily

Angus-Hill, M. L., Dutnall, R. N., Tafrov, S. T., et al. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3338 · Cited by 105 · see citing works

The Conserved Core of a HumanSIR2Homologue Functions in Yeast Silencing

Sherman, J. M., Stone, E. M., Freeman-Cook, L. L., Brachmann, C. B., Boeke, J. D., & Pillus, L. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.9.3045 · Cited by 94 · see citing works

TheSchizosaccharomyces pombe hst4+Gene Is aSIR2Homologue with Silencing and Centromeric Functions

Freeman-Cook, L. L., Sherman, J. M., Brachmann, C. B., et al. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.10.3171 · Cited by 70 · see citing works

An uncertain silence

Sherman, J. M., & Pillus, L. (1997) · Trends in Genetics · doi:10.1016/s0168-9525(97)01198-0 · Cited by 66 · see citing works

Leishmania major: Cell type dependent distribution of a 43 kDa antigen related to silent information regulatory‐2 protein family

Zemzoumi, K., Séréno, D., François, C., Guilvard, E., Lemesre, J.-L., & Oualssi, A. (1998) · Biology of the Cell · doi:10.1016/s0248-4900(98)80020-8 · Cited by 45 · see citing works

Reconstitution of chromatin higher-order structure from histone H5 and depleted chromatin

Graziano, V., Gerchman, S. E., & Ramakrishnan, V. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90124-6 · Cited by 40 · see citing works

Pillars Article: A Role for Histone Acetylation in the Developmental Regulation of V(D)J Recombination. Science. 2000. 287: 495-498

McMurry, M. T., & Krangel, M. S. (2017) · The Journal of Immunology · doi:10.1093/jimmunol/199.1.5 · Cited by 16 · see citing works

Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan

Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796 · 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

Sirtuin activators mimic caloric restriction and delay ageing in metazoans

Wood, J. G., Rogina, B., Lavu, S., Howitz, K., Helfand, S. L., Tatar, M., & Sinclair, D. (2004) · Nature · doi:10.1038/nature02789 · Cited by 1,868 · see citing works

Histone deacetylases and cancer: causes and therapies

Marks, P. A., Rifkind, R. A., Richon, V. M., Breslow, R., Miller, T., & Kelly, W. K. (2001) · Nature reviews. Cancer · doi:10.1038/35106079 · Cited by 1,866 · see citing works

Requirement of NAD and <i>SIR2</i> for Life-Span Extension by Calorie Restriction in <i>Saccharomyces cerevisiae</i>

Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775 · see citing works

NAD+ metabolism and its roles in cellular processes during ageing

Covarrubias, A. J., Perrone, R., Grozio, A., & Verdin, E. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00313-x · Cited by 1,617 · see citing works

The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control

Nakahata, Y., Kaluzova, M., Grimaldi, B., Sahar, S., Hirayama, J., Chen, D., Guarente, L. P., & Sassone-Corsi, P. (2008) · Cell · doi:10.1016/j.cell.2008.07.002 · Cited by 1,427 · 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

Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction

Haigis, M. C., & Guarente, L. P. (2006) · Genes &amp; Development · doi:10.1101/gad.1467506 · Cited by 1,295 · see citing works

Circadian Control of the NAD ⁺ Salvage Pathway by CLOCK-SIRT1

Nakahata, Y., Sahar, S., Astarita, G., Kaluzova, M., & Sassone-Corsi, P. (2009) · Science · doi:10.1126/science.1170803 · Cited by 1,198 · see citing works

SIRT4 Inhibits Glutamate Dehydrogenase and Opposes the Effects of Calorie Restriction in Pancreatic β Cells

Haigis, M. C., Mostoslavsky, R., Haigis, K. M., Fahie, K., Christodoulou, D. C., Murphy, A. J., Valenzuela, D. M., Yancopoulos, G. D., Karow, M., Blander, G., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.057 · Cited by 1,162 · 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

Mechanism of Human SIRT1 Activation by Resveratrol

Borra, M. T., Smith, B. C., & Denu, J. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501250200 · Cited by 1,065 · see citing works

Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration

Lin, S.-J., Kaeberlein, M., Andalis, A. A., Sturtz, L. A., Defossez, P.-A., Culotta, V. C., Fink, G. R., & Guarente, L. (2002) · Nature · doi:10.1038/nature00829 · Cited by 1,057 · see citing works

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 · see citing works

Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux

Wang, Q., Zhang, Y., Yang, C., Xiong, H., Lin, Y., Yao, J., Li, H., Xie, L., Zhao, W., Yao, Y., et al. (2010) · Science · doi:10.1126/science.1179687 · Cited by 1,008 · 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

Mitochondrial Signaling

Butow, R. A., & Avadhani, N. G. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00179-0 · Cited by 882 · see citing works

Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence

Rajman, L., Chwalek, K., & Sinclair, D. A. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.011 · Cited by 865 · see citing works

Slowing ageing by design: the rise of NAD+ and sirtuin-activating compounds

Bonkowski, M. S., & Sinclair, D. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.93 · Cited by 834 · see citing works

Calorie restriction–the SIR2 connection

Guarente, L., & Picard, F. (2005) · Cell · doi:10.1016/j.cell.2005.01.029 · Cited by 793 · see citing works

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 · see citing works

Substrate-specific activation of sirtuins by resveratrol

Kaeberlein, M., McDonagh, T., Heltweg, B., Hixon, J., Westman, E. A., Caldwell, S. D., Napper, A., Curtis, R., DiStefano, P. S., Fields, S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500655200 · Cited by 745 · see citing works

Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae

Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., & Sinclair, D. A. (2003) · Nature · doi:10.1038/nature01578 · Cited by 736 · 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

SIRT3, a Mitochondrial Sirtuin Deacetylase, Regulates Mitochondrial Function and Thermogenesis in Brown Adipocytes

Shi, T., Wang, F., Stieren, E., & Tong, Q. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414670200 · Cited by 712 · see citing works

NAD+ homeostasis in health and disease

Katsyuba, E., Romani, M., Hofer, D., & Auwerx, J. (2020) · Nature Metabolism · doi:10.1038/s42255-019-0161-5 · Cited by 627 · see citing works

Calorie restriction extends yeast life span by lowering the level of NADH

Lin, S.-J., Ford, E., Haigis, M., Liszt, G., & Guarente, L. (2004) · Genes &amp; Development · doi:10.1101/gad.1164804 · Cited by 632 · 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

The SMRT and N-CoR Corepressors Are Activating Cofactors for Histone Deacetylase 3

Guenther, M. G., Barak, O., & Lazar, M. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.18.6091-6101.2001 · Cited by 611 · see citing works

Histone deacetylase inhibitors as new cancer drugs

Marks, P. A., Richon, V. M., Breslow, R., & Rifkind, R. A. (2001) · Current Opinion in Oncology · doi:10.1097/00001622-200111000-00010 · Cited by 531 · see citing works

Mitochondria—A Nexus for Aging, Calorie Restriction, and Sirtuins?

Guarente, L. (2008) · Cell · doi:10.1016/j.cell.2008.01.007 · Cited by 513 · see citing works

Sirtuin Functions in Health and Disease

Yamamoto, H., Schoonjans, K., & Auwerx, J. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0079 · Cited by 480 · see citing works

Sirtuins as potential targets for metabolic syndrome

Guarente, L. (2006) · Nature · doi:10.1038/nature05486 · Cited by 468 · see citing works

Sir2-Independent Life Span Extension by Calorie Restriction in Yeast

Kaeberlein, M., Kirkland, K. T., Fields, S., & Kennedy, B. K. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020296 · Cited by 441 · 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

Genetics and the Specificity of the Aging Process

Hekimi, S., & Guarente, L. (2003) · Science · doi:10.1126/science.1082358 · Cited by 434 · see citing works

Double Strand Breaks Can Initiate Gene Silencing and SIRT1-Dependent Onset of DNA Methylation in an Exogenous Promoter CpG Island

O'Hagan, H. M., Mohammad, H. P., & Baylin, S. B. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000155 · Cited by 386 · see citing works

Chemical mechanisms of histone lysine and arginine modifications

Smith, B. C., & Denu, J. M. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.06.005 · Cited by 390 · see citing works

SIRT1 and energy metabolism

Li, X. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gms108 · Cited by 360 · see citing works

Functional significance of histone deacetylase diversity

Khochbin, S., Verdel, A., Lemercier, C., & Seigneurin-Berny, D. (2001) · Current Opinion in Genetics &amp; Development · doi:10.1016/s0959-437x(00)00174-x · Cited by 366 · see citing works

The Sir2 family of protein deacetylases

Denu, J. M. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.08.010 · Cited by 325 · see citing works

Identification of ‘erasers’ for lysine crotonylated histone marks using a chemical proteomics approach

Bao, X., Wang, Y., Li, X., Li, X.-M., Liu, Z., Yang, T., Wong, C. F., Zhang, J., Hao, Q., & Li, X. D. (2014) · eLife · doi:10.7554/elife.02999 · Cited by 324 · see citing works

A yeast by any other name: Candida glabrata and its interaction with the host

Kaur, R., Domergue, R., Zupancic, M. L., & Cormack, B. P. (2005) · Current Opinion in Microbiology · doi:10.1016/j.mib.2005.06.012 · Cited by 271 · see citing works

The <i>S. cerevisiae</i> SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program

Pijnappel, W. W. M. P., Schaft, D., Roguev, A., Shevchenko, A., Tekotte, H., Wilm, M., Rigaut, G., Séraphin, B., Aasland, R., & Stewart, A. F. (2001) · Genes &amp; Development · doi:10.1101/gad.207401 · Cited by 265 · see citing works

Hippocampal Sirtuin 1 signaling mediates depression-like behavior

Abe-Higuchi, N., Uchida, S., Yamagata, H., Higuchi, F., Hobara, T., Hara, K., Kobayashi, A., & Watanabe, Y. (2016) · Biological Psychiatry · doi:10.1016/j.biopsych.2016.01.009 · Cited by 247 · see citing works

Sirtuin regulation in aging and injury

Poulose, N., & Raju, R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.017 · Cited by 236 · see citing works

Protective effects and mechanisms of sirtuins in the nervous system

Zhang, F., Wang, S., Gan, L., Vosler, P. S., Gao, Y., Zigmond, M. J., & Chen, J. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.09.001 · Cited by 211 · see citing works

Regulation of MnSOD Enzymatic Activity by Sirt3 Connects the Mitochondrial Acetylome Signaling Networks to Aging and Carcinogenesis

Tao, R., Vassilopoulos, A., Parisiadou, L., Yan, Y., & Gius, D. (2014) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2013.5482 · Cited by 194 · see citing works

Nicotinamide Clearance by Pnc1 Directly Regulates Sir2-Mediated Silencing and Longevity

Gallo, C. M., Smith, D. L., & Smith, J. S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.1301-1312.2004 · Cited by 193 · see citing works

TEL contacts multiple co-repressors and specifically associates with histone deacetylase-3

Wang, L., & Hiebert, S. W. (2001) · Oncogene · doi:10.1038/sj.onc.1204479 · Cited by 101 · see citing works

Structure of Histone Deacetylases

Marmorstein, R. (2001) · Structure · doi:10.1016/s0969-2126(01)00690-6 · Cited by 97 · see citing works

Histone deacetylases in fungi: novel members, new facts

Trojer, P. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg473 · Cited by 86 · see citing works

Rapamycin increases rDNA stability by enhancing association of Sir2 with rDNA in Saccharomyces cerevisiae

Ha, C. W., & Huh, W.-K. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq895 · Cited by 77 · see citing works

Between Scylla and Charybdis: p53 links tumor suppression and aging

Campisi, J. (2002) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(02)00006-4 · Cited by 33 · see citing works

Histone deacetylase dHDAC4 is involved in segmentation of the <i>Drosophila</i> embryo and is regulated by gap and pair‐rule genes

Zeremski, M., Stricker, J. R., Fischer, D., Zusman, S. B., & Cohen, D. (2003) · genesis · doi:10.1002/gene.10159 · Cited by 17 · see citing works

Regulation of SIRT2-dependent α-tubulin deacetylation by cellular NAD levels

Skoge, R. H., Dölle, C., & Ziegler, M. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.04.011 · Cited by 65 · see citing works

Antiproliferative and proapoptotic activities of 4-hydroxybenzoic acid-based inhibitors of histone deacetylases

Seidel, C., Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.09.026 · Cited by 60 · see citing works

Global and Specific Responses of the Histone Acetylome to Systematic Perturbation

Feller, C., Forné, I., Imhof, A., & Becker, P. B. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.008 · Cited by 156 · see citing works

Transcriptional Regulation by the Acetylation of Nonhistone Proteins in Humans – A New Target for Therapeutics

Das, C., & Kundu, T. K. (2005) · IUBMB Life · doi:10.1080/15216540500090629 · Cited by 72 · see citing works

In Vitro Histone Acetylation Assay

Brown, J. A. L. (2017) · Current Protocols in Pharmacology · doi:10.1002/cpph.31 · Cited by 2 · see citing works