Hdac3 is essential for the maintenance of chromatin structure and genome stability
Open accessAbstract
Hdac3 is essential for efficient DNA replication and DNA damage control. Deletion of Hdac3 impaired DNA repair and greatly reduced chromatin compaction and heterochromatin content. These defects corresponded to increases in histone H3K9,K14ac; H4K5ac; and H4K12ac in late S phase of the cell cycle, and histone deposition marks were retained in quiescent Hdac3-null cells. Liver-specific deletion of Hdac3 culminated in hepatocellular carcinoma. Whereas HDAC3 expression was downregulated in only a small number of human liver cancers, the mRNA levels of the HDAC3 cofactor NCOR1 were reduced in one-third of these cases. siRNA targeting of NCOR1 and SMRT (NCOR2) increased H4K5ac and caused DNA damage, indicating that the HDAC3/NCOR/SMRT axis is critical for maintaining chromatin structure and genomic stability.
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
HDAC3 is required for genome maintenance and DNA replication in hematopoietic cells.
“HDAC3 was found to be required for genome maintenance and DNA replication in hematopoietic cells (27, 28); therefore, HDAC3 inhibition is suspected to be responsible for bone marrow toxicity seen with nonselective HDAC inhibitors (29).”
From TNG260 Is a Small-Molecule CoREST Inhibitor That Sensitizes <i>STK11</i> -Mutant Tumors to Anti–PD-1 Immunotherapy (2025) · cites this paper as [28]
The Results (‘Hdac3 is required for genomic stability’; page not provided) report increased chromosome breaks and gaps after Hdac3 deletion in mouse embryonic fibroblasts, and the paper states that Hdac3 is essential for efficient DNA replication. The cited copy does not establish those requirements in hematopoietic cells; its Discussion mentions bone-marrow cells only when considering possible effects of HDAC inhibitors. (LLM, conf=0.88)
Experimental — accuracy not yet measuredHDAC3 affects genome instability.
“Preliminary studies have shown that HDAC3 affects genome instability.”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Bhaskara et al., 2010
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
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466 · see citing works
Cisplatin: mode of cytotoxic action and molecular basis of resistance
Siddik, Z. H. (2003) · Oncogene · doi:10.1038/sj.onc.1206933 · Cited by 3,335 · see citing works
Anticancer activities of histone deacetylase inhibitors
Bolden, J. E., Peart, M. J., & Johnstone, R. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2133 · Cited by 2,919 · see citing works
Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868 · see citing works
Hörlein, A., Näär, A. M., Heinzel, T., Torchia, J., Gloss, B. R., Kurokawa, R., Ryan, A. K., Kamei, Y., Söderström, M., Glass, C. K., et al. (1995) · Nature · doi:10.1038/377397a0 · Cited by 2,035 · see citing works
A transcriptional co-repressor that interacts with nuclear hormone receptors
Chen, J. D., & Evans, R. M. (1995) · Nature · doi:10.1038/377454a0 · Cited by 1,794 · 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
NCBI GEO: archive for high-throughput functional genomic data
Barrett, T., Troup, D. B., Wilhite, S. E., Ledoux, P., Rudnev, D., Evangelista, C., Kim, I. F., Soboleva, A., Tomashevsky, M., Marshall, K. A., et al. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn764 · Cited by 1,043 · see citing works
X-ray structure of a tetranucleosome and its implications for the chromatin fibre
Schalch, T., Duda, S., Sargent, D. F., & Richmond, T. J. (2005) · Nature · doi:10.1038/nature03686 · Cited by 839 · see citing works
Genome‐wide molecular profiles of HCV‐induced dysplasia and hepatocellular carcinoma†
Wurmbach, E., Chen, Y., Khitrov, G., Zhang, W., Roayaie, S., Schwartz, M., Fiel, M. I., Thung, S. N., Mazzaferro, V., Bruix, J., et al. (2007) · Hepatology · doi:10.1002/hep.21622 · Cited by 721 · see citing works
HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics
Gallinari, P., Marco, S. D., Jones, P., Pallaoro, M., & Steinkühler, C. (2007) · Cell Research · doi:10.1038/sj.cr.7310149 · Cited by 678 · see citing works
Celis, J. E., & Celis, A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.10.3262 · Cited by 636 · see citing works
Nucleosome Assembly by a Complex of CAF-1 and Acetylated Histones H3/H4
Verreault, A., Kaufman, P. D., Kobayashi, R., & Stillman, B. (1996) · Cell · doi:10.1016/s0092-8674(00)81326-4 · Cited by 634 · see citing works
Butler, L. M., Agus, D. B., Scher, H. I., Higgins, B., Rose, A., Cordon‐Cardo, C., Thaler, H. T., Rifkind, R. A., Marks, P. A., & Richon, V. M. (2000) · PubMed · Cited by 613 · 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
Wilson, A. J., Byun, D.-S., Popova, N., Murray, L. B., L'Italien, K., Sowa, Y., Arango, D., Velcich, A., Augenlicht, L. H., & Mariadason, J. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510023200 · Cited by 575 · see citing works
Self-citationPerissi, V., Aggarwal, A. K., Glass, C. K., Rose, D. W., & Rosenfeld, M. G. (2004) · Cell · doi:10.1016/s0092-8674(04)00133-3 · Cited by 566 · see citing works
The histone tails of the nucleosome
Luger, K., & Richmond, T. J. (1998) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(98)80134-2 · Cited by 525 · see citing works
Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4.
Sobel, R. E., Cook, R. G., Perry, C. A., Annunziato, A. T., & Allis, C. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.4.1237 · Cited by 513 · see citing works
Neumann, H., Hancock, S. M., Buning, R., Routh, A. L., Chapman, L., Somers, J., Owen‐Hughes, T., van Noort, J., Rhodes, D., & Chin, J. W. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.027 · Cited by 498 · 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
HP1-β mobilization promotes chromatin changes that initiate the DNA damage response
Ayoub, N., Jeyasekharan, A. D. D., Bernal, J. A., & Venkitaraman, A. R. (2008) · Nature · doi:10.1038/nature06875 · Cited by 403 · see citing works
Bhaskara, S., Chyla, B., Amann, J. M., Knutson, S. K., Cortez, D., Sun, Z., & Hiebert, S. W. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.030 · Cited by 369 · see citing works
Self-citationXu, X. Z. S., Huang, J., Xu, Z., Qian, B., Zhu, Z., Yan, Q., Cai, T., Zhang, X., Xiao, H., Qu, J., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241522398 · Cited by 363 · 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
Silencing factors participate in DNA repair and recombination in Saccharomyces cerevisiae
Tsukamoto, Y., Kato, J.-I., & Ikeda, H. (1997) · Nature · doi:10.1038/42288 · Cited by 332 · see citing works
Gunjan, A., & Verreault, A. (2003) · Cell · doi:10.1016/s0092-8674(03)00896-1 · Cited by 325 · 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
Doxorubicin-DNA Adducts Induce a Non-Topoisomerase II–Mediated Form of Cell Death
Swift, L. P., Rephaeli, A., Nudelman, A., Phillips, D. R., & Cutts, S. M. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3410 · Cited by 314 · see citing works
Liver-specific deletion of histone deacetylase 3 disrupts metabolic transcriptional networks
Knutson, S. K., Chyla, B. J., Amann, J. M., Bhaskara, S., Huppert, S. S., & Hiebert, S. W. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.51 · Cited by 271 · see citing works
Self-citationPijnappel, 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 & Development · doi:10.1101/gad.207401 · Cited by 265 · see citing works
Heterochromatin protein 1 is recruited to various types of DNA damage
Luijsterburg, M. S., Dinant, C., Lans, H., Stap, J., Wiernasz, E., Lagerwerf, S., Warmerdam, D. O., Lindh, M., Brink, M. C., Dobrucki, J. W., et al. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200810035 · Cited by 264 · 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
Self-citationKondo, Y., Shen, L., Ahmed, S., Boumber, Y., Sekido, Y., Haddad, B. R., & Issa, J. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002037 · Cited by 235 · see citing works
HDAC3: taking the SMRT-N-CoRrect road to repression
Karagianni, P., & Wong, J. (2007) · Oncogene · doi:10.1038/sj.onc.1210612 · Cited by 221 · see citing works
Liao, Y.-L., Sun, Y.-M., Chau, G.-Y., et al. (2008) · Oncogene · doi:10.1038/onc.2008.168 · Cited by 205 · see citing works
Duplication and Maintenance of Heterochromatin Domains
Taddei, A., Roche, D. M. J., Sibarita, J., Turner, B. M., & Almouzni, G. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.6.1153 · Cited by 202 · see citing works
Marchion, D. C., Biçaku, E., DAUD, A. I., Richon, V. M., Sullivan, D. M., & Münster, P. N. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20045 · Cited by 185 · see citing works
Han, J., Zhou, H., Li, Z., Xu, R.-M., & Zhang, Z. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702496200 · Cited by 179 · see citing works
Ashwell, S., & Zabludoff, S. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-5138 · Cited by 162 · see citing works
MicroRNA-34 mediates AR-dependent p53-induced apoptosis in prostate cancer
Rokhlin, O. W., Scheinker, V., Taghiyev, A. F., Bumcrot, D. A., Glover, R. A., & Cohen, M. B. (2008) · Cancer Biology & Therapy · doi:10.4161/cbt.7.8.6284 · Cited by 159 · see citing works
Potential Role for 53BP1 in DNA End-joining Repair through Direct Interaction with DNA
Iwabuchi, K., Basu, B. P., Kysela, B. P., Kurihara, T., Shibata, M. S., Guan, D., Cao, Y., Hamada, T., Imamura, K., Jeggo, P. A., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304066200 · Cited by 150 · see citing works
The impact of heterochromatin on DSB repair
Goodarzi, A. A., Noon, A. T., & Jeggo, P. A. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370569 · Cited by 149 · see citing works
N-CoR-HDAC Corepressor Complexes: Roles in Transcriptional Regulation by Nuclear Hormone Receptors
Jones, P. L., & Shi, Y. (2003) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-55747-7_9 · Cited by 137 · see citing works
HDAC3 overexpression and colon cancer cell proliferation and differentiation
Spurling, C. C., Godman, C. A., Noonan, E. J., Rasmussen, T. P., Rosenberg, D. W., & Giardina, C. A. (2007) · Molecular Carcinogenesis · doi:10.1002/mc.20373 · Cited by 126 · see citing works
Effects of histone acetylation, ubiquitination and variants on nucleosome stability
Li, W., Nagaraja, S., Delcuve, G. P., Hendzel, M. J., & Davie, J. (1993) · Biochemical Journal · doi:10.1042/bj2960737 · Cited by 121 · see citing works
Johnson, C. A., White, D. A., Lavender, J. S., O'Neill, L. P., & Turner, B. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107942200 · Cited by 119 · see citing works
HP1-β is required for development of the cerebral neocortex and neuromuscular junctions
Aucott, R. L., Bullwinkel, J., Yu, Y., Shi, W., Billur, M., Brown, J. P., Menzel, U., Kioussis, D., Wang, G., Reisert, I., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200804041 · Cited by 117 · see citing works
S‐phase patterns of cyclin (PCNA) antigen staining resemble topographical patterns of DNA synthesis
Madsen, P., & Celis, J. E. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)80068-5 · Cited by 109 · see citing works
Deletion 5q in myelodysplastic syndrome: a paradigm for the study of hemizygous deletions in cancer
Ebert, B. L. (2009) · Leukemia · doi:10.1038/leu.2009.53 · Cited by 101 · see citing works
Distinctive higher-order chromatin structure at mammalian centromeres
Gilbert, N., & Allan, J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211322798 · Cited by 97 · see citing works
Codina, A., Love, J. D., Li, Y., Lazar, M. A., Neuhaus, D., & Schwabe, J. W. R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500299102 · Cited by 95 · see citing works
DNA Damage Repair and Response Proteins as Targets for Cancer Therapy
Lieberman, H. B. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708783497328 · Cited by 88 · see citing works
Baschnagel, A., Russo, A. L., Burgan, W. E., Carter, D., Beam, K., Palmieri, D., Steeg, P. S., Tofilon, P. J., & Camphausen, K. A. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0038 · Cited by 86 · see citing works
Exonuclease Function of Human Mre11 Promotes Deletional Nonhomologous End Joining
Zhuang, J., Jiang, G., Willers, H., & Xia, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.059444 · Cited by 68 · see citing works
Self-citationJohannsdottir, H., Jönsson, G. B., Jóhannesdóttir, G., Agnarsson, B. A., Eerola, H., Arason, A., Heikkilä, P., Egilsson, V., Olsson, H. L., Johannsson, O. T., et al. (2006) · International Journal of Cancer · doi:10.1002/ijc.21934 · Cited by 65 · see citing works
Suzuki, M., Endo, M., Shinohara, F., et al. (2009) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-009-0969-x · Cited by 61 · see citing works
Histone deacetylase Rpd3 antagonizes Sir2-dependent silent chromatin propagation
Zhou, J., Zhou, B. O., Lenzmeier, B. A., & Zhou, J. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp233 · Cited by 60 · see citing works
Olive, P. L., Banáth, J. P., & Banáth, J. P. (1995) · Radiation Research · doi:10.2307/3579022 · Cited by 45 · see citing works
Genomic Organization and Chromosomal Localization of the Human Histone Deacetylase 3 Gene
Mahlknecht, U., Emiliani, S., Najfeld, V., Young, S., & Verdin, E. M. (1999) · Genomics · doi:10.1006/geno.1998.5645 · Cited by 29 · see citing works
Yu, J., Palmer, C. M., Alenghat, T., Li, Y., Kao, G. D., & Lazar, M. A. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1902 · Cited by 24 · see citing works
Sugimura, K., Fukushima, Y., Ishida, M., et al. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.06.016 · Cited by 20 · see citing works
Qiu, L., Yao, D., Zong, L., Lu, Y., Huang, H., Wu, W., & Wu, X. (2008) · PubMed · Cited by 19 · see citing works
p53 Chromatin Epigenetic Domain Organization and p53 Transcription
Su, C.-H., Shann, Y.-J., & Hsu, M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00704-08 · Cited by 17 · see citing works
Efficiency of Composite Laboratory Tests in the Diagnosis of Liver Malignancies
Pavesi, F., Lotzniker, M., Scarabelli, M., et al. (1989) · The International Journal of Biological Markers · doi:10.1177/172460088900400306 · Cited by 8 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The COSMIC Cancer Gene Census: describing genetic dysfunction across all human cancers
Sondka, Z., Bamford, S., Cole, C. G., Ward, S. A., Dunham, I., & Forbes, S. A. (2018) · Nature Reviews Cancer · doi:10.1038/s41568-018-0060-1 · Cited by 1,597 · see citing works
Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
Falkenberg, K. J., & Johnstone, R. W. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4360 · Cited by 1,564 · see citing works
New and emerging HDAC inhibitors for cancer treatment
West, A. C., & Johnstone, R. W. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69738 · Cited by 1,404 · see citing works
Ketone bodies as signaling metabolites
Newman, J. C., & Verdin, E. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.09.002 · Cited by 966 · see citing works
β-Hydroxybutyrate: A Signaling Metabolite
Newman, J. C., & Verdin, E. (2017) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071816-064916 · Cited by 872 · see citing works
“HDAC3 regulates expression of gluconeogenic genes (86), and HDAC3 knockout mice have reduced fasting glucose and insulin levels (8, 26, 63).”
Solovei, I., Wang, A. S., Thanisch, K., Schmidt, C. S., Krebs, S., Zwerger, M., Cohen, T. V., Devys, D., Foisner, R., Peichl, L., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.009 · Cited by 809 · see citing works
The effects of deregulated DNA damage signalling on cancer chemotherapy response and resistance
Bouwman, P., & Jonkers, J. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3342 · Cited by 615 · see citing works
Fellows, R., Denizot, J., Stellato, C., Cuomo, A., Jain, P., Stoyanova, E., Balázsi, S., Hajnády, Z., Liebert, A., Kazakevych, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02651-5 · Cited by 568 · see citing works
Delcuve, G. P., Khan, D. H., & Davie, J. R. (2012) · Clinical Epigenetics · doi:10.1186/1868-7083-4-5 · Cited by 505 · see citing works
Emerging roles of the corepressors NCoR1 and SMRT in homeostasis
Mottis, A., Mouchiroud, L., & Auwerx, J. (2013) · Genes & Development · doi:10.1101/gad.214023.113 · Cited by 297 · see citing works
Insights into the activation mechanism of class I HDAC complexes by inositol phosphates
Watson, P. J., Millard, C. J., Riley, A. M., Robertson, N. S., Wright, L. C., Godage, H. Y., Cowley, S. M., Jamieson, A. G., Potter, B. V. L., & Schwabe, J. W. R. (2016) · Nature Communications · doi:10.1038/ncomms11262 · Cited by 244 · see citing works
Integrative regulation of physiology by histone deacetylase 3
Emmett, M. J., & Lazar, M. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0076-0 · Cited by 202 · see citing works
Janczura, K. J., Volmar, C.-H., Sartor, G. C., Rao, S. J., Ricciardi, N. R., Lambert, G., Brothers, S. P., & Wahlestedt, C. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1805436115 · Cited by 183 · see citing works
RetractedHistone deacetylase 3 (HDAC3) inhibitors as anticancer agents: A review
Sarkar, R., Banerjee, S., Amin, S. A., Adhikari, N., & Jha, T. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112171 · Cited by 121 · see citing works
HDAC3 is essential for DNA replication in hematopoietic progenitor cells
Summers, A. R., Fischer, M. A., Stengel, K. R., Zhao, Y., Kaiser, J. F., Wells, C. E., Hunt, A., Bhaskara, S., Luzwick, J. W., Sampathi, S., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci60806 · Cited by 87 · see citing works
Self-citationSIRT7 mediates L1 elements transcriptional repression and their association with the nuclear lamina
Vazquez, B. N., Thackray, J. K., Simonet, N. G., Chahar, S., Kane-Goldsmith, N., Newkirk, S. J., Lee, S., Xing, J., Verzi, M. P., An, W., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz519 · Cited by 79 · see citing works
Behravan, H., Hartikainen, J. M., Tengström, M., Pylkäs, K., Winqvist, R., Kosma, V., & Mannermaa, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-31573-5 · Cited by 75 · see citing works
Changes in nucleosome occupancy associated with metabolic alterations in aged mammalian liver
Bochkis, I. M., Przybylski, D., Chen, J., & Regev, A. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.048 · Cited by 78 · see citing works
Long, J., Jia, M.-Y., Fang, W.-Y., Chen, X.-J., Mu, L.-L., Wang, Z.-Y., Shen, Y., Xiang, R.-F., Wang, L.-N., Wang, L., et al. (2020) · Blood · doi:10.1182/blood.2019003538 · Cited by 84 · see citing works
Long, J., Fang, W. Y., Chang, L., Gao, W. H., Shen, Y., Jia, M. Y., Zhang, Y. X., Wang, Y., Dou, H. B., Zhang, W. J., et al. (2017) · Leukemia · doi:10.1038/leu.2017.130 · Cited by 78 · see citing works
Phelps, M. P., Bailey, J. N., Vleeshouwer-Neumann, T., & Chen, E. Y. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610270114 · Cited by 62 · see citing works
Adhikari, N., Jha, T., & Ghosh, B. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01676 · Cited by 74 · see citing works
HDACs and the epigenetic plasticity of cancer cells: target the complexity
Brancolini, C., Gagliano, T., & Minisini, M. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108190 · Cited by 55 · see citing works
Yan, Y., An, J., Yang, Y., Wu, D., Bai, Y., Cao, W., Ma, L., Chen, J., Yu, Z., He, Y., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708478 · Cited by 53 · see citing works
Mani, C., Tripathi, K., Luan, S., Clark, D. W., Andrews, J. F., Vindigni, A., Thomas, G., & Palle, K. (2020) · Oncogene · doi:10.1038/s41388-020-1167-x · Cited by 27 · see citing works
Nishimoto, K., Niida, H., Uchida, C., Ohhata, T., Kitagawa, K., Motegi, A., Suda, T., & Kitagawa, M. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-20-0214 · Cited by 21 · see citing works
Ahronian, L. G., Sahu, S., Zhang, M., Patel, A. S., Geng, K., Bhattacharya, R., Falchook, G. S., Goldman, J. W., Spira, A. I., Punekar, S. R., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-25-0998 · Cited by 9 · see citing works
“HDAC3 was found to be required for genome maintenance and DNA replication in hematopoietic cells (27, 28); therefore, HDAC3 inhibition is suspected to be responsible for bone marrow toxicity seen with nonselective HDAC inhibitors (29).”
- Authors
- Bhaskara, S., Knutson, S. K., Jiang, G., Chandrasekharan, M. B., Wilson, A. J., Zheng, S., Yenamandra, A., Locke, K., Yuan, J.-L., Bonine-Summers, A. R., Wells, C. E., Kaiser, J. F., Washington, M. K., Zhao, Z., Wagner, F. F., Sun, Z.-W., Xia, F., Holson, E. B., Khabele, D., & Hiebert, S. W.
- Affiliations
- Vanderbilt University (US)
- Vanderbilt University Medical Center (US)
- Broad Institute (US)
- Corresponding author
- Hiebert, Scott W.
- ORCID
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2010-11
- Volume
- 18
- Issue
- 5
- Pages
- 436-447
- ISSN
- 1535-6108 (ISSN-L)
- PMC
- PMC3004468
- OpenAlex
- W2059002036
- Cited by
- 353
- References
- 65
- Citations by year
- 2026: 6 · 2025: 15 · 2024: 23 · 2023: 23 · 2022: 17 · 2021: 21 · 2020: 28 · 2019: 23 · 2018: 28 · 2017: 28 · 2016: 26 · 2015: 19 · 2014: 27 · 2013: 28 · 2012: 31
- FWCI
- 9.00
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cancer Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (P30 CA 68485, R01CA141071, R01CA109355, F32CA138091, R01CA077274, R01CA064140, T32CA009582, P30CA068485, R01 CA64140, R01-CA77274)
- National Institute of Diabetes and Digestive and Kidney Diseases (P30 DK58404, P30DK058404)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- HDAC3, chromatin structure, genome stability, DNA replication, DNA damage response, DNA repair, heterochromatin, histone acetylation, histone H3K9 acetylation, histone deposition, hepatocellular carcinoma, NCOR1, SMRT, histone deacetylase
- MeSH terms
- Histone Deacetylase 3, Acetylation, Animals, Chromatin, DNA Damage, DNA Repair, DNA Replication, Carcinoma, Hepatocellular, Histone Deacetylases, Histones, Humans, Liver Neoplasms, Experimental, RNA, Messenger, Down-Regulation, Gene Expression Regulation, Neoplastic, S Phase, RNA Interference, Chromatin Assembly and Disassembly, Genomic Instability, Cell Line, Tumor, Mice, Nuclear Receptor Co-Repressor 1, Nuclear Receptor Co-Repressor 2
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