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HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics
Abstract
Histone deacetylases (HDACs) and histone acetyl transferases (HATs) are two counteracting enzyme families whose enzymatic activity controls the acetylation state of protein lysine residues, notably those contained in the N-terminal extensions of the core histones. Acetylation of histones affects gene expression through its influence on chromatin conformation. In addition, several non-histone proteins are regulated in their stability or biological function by the acetylation state of specific lysine residues. HDACs intervene in a multitude of biological processes and are part of a multiprotein family in which each member has its specialized functions. In addition, HDAC activity is tightly controlled through targeted recruitment, protein-protein interactions and post-translational modifications. Control of cell cycle progression, cell survival and differentiation are among the most important roles of these enzymes. Since these processes are affected by malignant transformation, HDAC inhibitors were developed as antineoplastic drugs and are showing encouraging efficacy in cancer patients.
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“The mammalian HDAC family consists of 18 isoforms categorized into four major classes (Classes I–IV) (Zhang et al., 2024; Glozak et al., 2005; Gallinari et al., 2007; Yang and Grégoire, 2005), as summarized in Table 1 (Vanaja et al., 2018; Johnstone, 2002; Gao et al., 2002; Tong et al., 2002; Hubbert et al., 2002).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Gallinari et al., 2007
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Cites
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
Histone deacetylases (HDACs): characterization of the classical HDAC family
RUIJTER, A. J. M. D., GENNIP, A. H. V., CARON, H. N., KEMP, S., & KUILENBURG, A. B. P. V. (2003) · Biochemical Journal · doi:10.1042/bj20021321 · Cited by 3,114
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903
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
DNA methylation and human disease
Robertson, K. D. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1655 · Cited by 2,864
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 2,788
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,234
The diverse functions of histone lysine methylation
Martin, C., & Zhang, Y. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1761 · Cited by 2,157
Dent, S., Denu, J. M., & Allis, C. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.81 · Cited by 1,906
Research works printed but not linked: 1
- Vaisburg A . Discovery and development of MGCD0103 – an orally active HDAC inhibitor in human clinical trials. XIXth International Symposium on Medical Chemistry, Istanbul, Aug 29-Sep 2, 2006.
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Beilner, D., Kühn, C., Kost, B., Vilsmaier, T., Vattai, A., Kaltofen, T., Mahner, S., Schmoeckel, E., Dannecker, C., Jückstöck, J., et al. (2021) · Archives of Gynecology and Obstetrics · doi:10.1007/s00404-021-06053-3 · Cited by 3
DNA Methylation in Mammalian Cells
Winata, P., William, M., Keena, V. A., Takahashi, K. L., & Cheng, Y. Y. (2018) · InTech eBooks · doi:10.5772/intechopen.72991 · Cited by 4
“The discovery of both HDACi and DNMTi provide options for clinical treatment alone or possible use with other agents in combination therapies for the treatment of various diseases that are related to epigenetic abnormalities [117].”
BackgroundHerp, D., Ridinger, J., Robaa, D., Shinsky, S. A., Schmidtkunz, K., Yesiloglu, T. Z., Bayer, T., Sehr, P. A., Gunkel, N., Miller, A. K., et al. (2020) · ChemRxiv · doi:10.26434/chemrxiv.12440096.v3 · Cited by 2
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Nezhad, A. F. (2022) · Preprints.org · doi:10.20944/preprints202208.0265.v1 · Cited by 2
Hao, L., Lu, W., Wu, J., Chen, Y., Xu, D., & Wang, P. (2024) · Scientific Reports · doi:10.1038/s41598-024-59724-x · Cited by 2
HDAC6 as a therapeutic target for HPV E7-driven cervical cancer
Jiang, W., Liu, S., & Fu, L. (2025) · Genome Instability & Disease · doi:10.1007/s42764-025-00154-y · Cited by 2
“Both classes require zinc for their catalytic activity and share structural similarities with HDA1, a deacetylase originally identified in yeast (Gallinari et al., 2007).”
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Epigenetic programming of macrophages across inflammatory and malignant diseases
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Zambrano, Á., Paiva, L., Nualart, D. P., Jara, M. C., Spichiger, C., Muñoz, J. L. P., Vargas‐Chacoff, L., & Morera, F. J. (2025) · Aquaculture · doi:10.1016/j.aquaculture.2025.743225 · Cited by 2
Zhang, Y., Wen, D., Ho, C., Liu, Y., Wang, X., Zhou, Z., Gao, Y., & Li, Q. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.ads0594 · Cited by 3
Shelke, S., Jawarkar, R. D., Khatale, P. N., Shah, U., Alzahrani, A. Y. A., Samad, A., Al-Hussain, S. A., Al‐Mutairi, A. A., & Zaki, M. E. A. (2026) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2025.109271 · Cited by 2
Cap-Modified Hydroxamate Analogues as Histone Deacetylases Inhibitors and Antitumor Agents
Zhang, Q., Feng, J., & Li, J. (2014) · Bulletin of the Korean Chemical Society · doi:10.5012/bkcs.2014.35.1.129 · Cited by 2
Combination of Salermide and Cholera Toxin B Induce Apoptosis in MCF-7 but Not in MRC-5 Cell Lines.
Salahshoor, M. R., Dastjerdi, M. N., Jalili, C., Mardani, M., Khazaei, M., Shabanizadeh, A., Valiani, A., & Roshankhah, S. (2013) · Europe PMC (PubMed Central) · Cited by 2
Kamalesh, D., & Sudandiradoss, C. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27083 · Cited by 2
(2022) · Biointerface Research in Applied Chemistry · doi:10.33263/briac132.198 · Cited by 2
Gut microbiome-derived metabolites in host health and diseases
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Design and synthesis of peptides as stabilizers of histone deacetylase 4
Lill, A., Schweipert, M., Nehls, T., Wurster, E., Lermyte, F., Meyer‐Almes, F., & Schmitz, K. (2024) · Journal of Peptide Science · doi:10.1002/psc.3603 · Cited by 2
“3,4,6,13 The current model assumes that HDAC4 binds with its extended N-terminal domain to the DNA-binding transcription factor MEF2 and then recruits the SMRT/NCoR-HDAC3 complex.”
Levidou, G., Arsenakis, D., Bolovis, D. I., Meyer, R., Brucker, C. V. M., Papadopoulos, T., & Theocharis, S. E. (2024) · Biomedicines · doi:10.3390/biomedicines12050947 · Cited by 2
“The members of the HDAC protein family are divided into four classes according to the corresponding homology to the yeast S. Cerevisiae [1,2,4].”
BackgroundŞahin, N. M. M., Erdogan, B., & Yelekçi, K. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e35020 · Cited by 3
“Histone deacetylases (HDACs) display a crucial role in various cellular and mechanistic pathways [3], catalyzing the deacetylation processes of the N-terminal lysine residues of the histone and nonhistone proteins regulating the gene expression [4].”
BackgroundSkarzyńska, A., Turek, S., Pisz, M., Aparna, A., Pląder, W., & Pawełkowicz, M. E. (2025) · Genes · doi:10.3390/genes16020127 · Cited by 2
Kim, H. J., An, U. R., Yoon, H. J., Lim, H., Hwang, K., Kim, Y. S., & Kim, H. R. (2025) · Tuberculosis & respiratory diseases · doi:10.4046/trd.2024.0090 · Cited by 2
“HDACs deacetylate histone lysine for condensation and subsequently inhibit chromatin 6 , thereby regulating the expression of oncogenes and exhibiting anticancer effects 1 .”
Signal transduction pathways controlling Ins2 gene activity and beta cell state transitions
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Phenotypic Manifestations of a New Variant in HDAC4 Gene
Ianniello, M., Angelis, V. D., Ottaiano, A., Ruggiero, R., Sirica, R., Petrillo, N., Fico, A., Cerbone, T., Rosania, C., Mormile, R., et al. (2025) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.33029 · Cited by 2
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“Histone Deacetylase (HDAC) inhibitors are a class of drugs that block the activity of HDAC enzymes, which play a key role in regulating gene expression by modifying the structure of chromatin [119].”
Chen, H., Guo, Z., Li, P., Liao, W., Li, Y., Li, B., Li, Y., Zhu, Q., Lu, Y., Huang, L., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-12522-5 · Cited by 2
Hauff, K. D., Mitchell, R. W., Xu, F. Y., Dembinski, T. C., Mymin, D., Zha, X., Choy, P. C., & Hatch, G. M. (2011) · Lipids · doi:10.1007/s11745-011-3582-9 · Cited by 2
Werner, J. (2011) · International Journal of Oncology · doi:10.3892/ijo.2011.1239 · Cited by 2
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BackgroundStanisheva, D. V., Atanasov, G. R., Apostolova, M. D., & Petrov, O. (2020) · Current Bioactive Compounds · doi:10.2174/1573407216666200214093400 · Cited by 2
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Farooqui, A. A. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3804-5_7 · Cited by 2
Campit, S., Bhowmick, R., Lu, T., Saoji, A. V., Jin, R., Shay, M. R., Robida, A. M., & Chandrasekaran, S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.27.530260 · Cited by 2
“Acetyl-CoA is the substrate for histone acetyltransferases (HATs) 5,6 , while sirtuins, a family of histone deacetylases (HDACs), remove acetyl and other acyl moieties from lysine residues using NAD+ 7,8 .”
BackgroundChen, C., Saha, E., Fischer, J., Guebila, M. B., Fanfani, V., Shutta, K. H., Padi, M., Glass, K., DeMeo, D. L., Lopes‐Ramos, C. M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.03.636354 · Cited by 2
“HDACs, known for their role in reducing acetylation levels 47 , also showed sex-biased patterns.”
Ramírez, J. E. G., & Mancilla, T. (2023) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14323 · Cited by 1
“…acetyl groups of the ε - amino groups of the lysine residues of the histones that form the chromatin resulting in packing of the structure and preventing gene transcription and causing gene silencing, reversibly regulated by histone acetyltransferases (HATs) (Gallinari et al., 2007; Struhl, 1998).”
BackgroundTargeting Epigenetic Readers Using Small Molecule Binders and PROTAC Degraders
Boccia, E., Gazzillo, E., Chini, M. G., Bifulco, G., & Lauro, G. (2024) · Interdisciplinary cancer research · doi:10.1007/16833_2024_240 · Cited by 1
Banerjee, S., Baidya, S. K., Jha, T., Ghosh, B., & Adhikari, N. (2024) · Medicinal Chemistry · doi:10.2174/0115734064329669241007060848 · Cited by 1
Jamshidi, Z., Abnous, K., Ghodsi, R., Taghdisi, S. M., & Hadizadeh, F. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108879 · Cited by 1
Aksel, A. B., Gozelle, M., Bakar‐Ates, F., Özkan, Y., Özkan, E., & Eren, G. (2025) · Polycyclic aromatic compounds · doi:10.1080/10406638.2025.2562259 · Cited by 1
Zhang, W., Yan, W., Wei, T., Che, S., Sun, Y., Xiao, A., Wu, J., Zhan, Y., Li, H., Lu, T., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01789 · Cited by 3
Lv, C., Zhao, Y., Luo, L., Ye, C., Rao, C., Feng, B., Yu, W., Xiao, X., Wang, C., & Huang, W. (2025) · Scientific Reports · doi:10.1038/s41598-025-23887-y · Cited by 1
“Epigenetic alterations in cancer development critically regulate gene expression through post-translational modifications, such as acetylation, methylation, and phosphorylation 20 .”
Wu, L., Li, Z., Wang, L., Lu, Y., Lou, G., Zhang, B., & Wang, N. (2025) · Cells · doi:10.3390/cells14221822 · Cited by 1
“Histone deacetylases (HDACs) are important epigenetic regulators, and their abnormalities are closely related to malignant tumor phenotypes [6].”
Shin, Y., Kim, S. M., Rhie, S. K., & An, W. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01622-4 · Cited by 1
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“…[26,346,347] iii) placental HDAC9 is down-regulated in preeclampsia [34,40] and iv) HDAC9 is an expansive modulator of related cellular processes including placentation, immunity, angiogenesis, and GPCR signaling [34,40,42,46,86,131,167,212,348], more comprehensive explorations are warranted.”
Garcia-Franco, P. M., Falcó-Martí, F. J., Jeblaoui, H., del Rio, M. A., Ortega-Alarcón, D., Vega, S., Galano-Frutos, J. J., Abián, O., & Velázquez‐Campoy, A. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149851 · Cited by 1
Bhabha, F., Prince, H. M., Campbell, B. A., van der Weyden, C., Ong, X., Casan, J. M. L., & McCormack, C. J. (2025) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2025.2598662 · Cited by 1
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Oyanagi, M., Konno, T., Nishida, S., Kohno, T., Kimura, I., Nakano, M., Ohwada, K., Kakuki, T., Obata, K., Kakiuchi, A., et al. (2026) · European Archives of Oto-Rhino-Laryngology · doi:10.1007/s00405-025-09959-9 · Cited by 1
Yang, K., Qin, X., Wang, Y., Yan, W., Yao, M., Yu, C., Yu, C., Shi, S., Zhao, Y., Zhou, L., et al. (2026) · Journal of Advanced Research · doi:10.1016/j.jare.2026.02.013 · Cited by 1
Nagel, A., Hass, E. W., Hayes, H., Huelbes, L., Oliveira, S. A., Hardin, H. M., Marasigan, M., Nisenbaum, E. S., Misztal, C. I., Telischi, F. F., et al. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27062636 · Cited by 1
Usmani, K., Chakraborty, K., Rajput, D., Jain, S. K., & Yadav, S. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.153690 · Cited by 1
Rajput, S., Singh, S. K., Yadav, P., Khurana, A., Weiskirchen, R., & Navik, U. (2026) · Military Medical Research · doi:10.1016/j.mmr.2026.100024 · Cited by 2
“…of nucleotide-binding oligomerization domain, leucine-rich repeat, and pyrin domain containing 3 (NLRP3) inflammasome by regulating upstream and downstream signaling factors, such as activation of pro-IL-1 , p65 subunit, and MyD88, leading to further inflammation and ROS generation [22,23].”
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Wang, J.-J., Gao, Y., Ji, X.-Q., Yin, J.-Y., Zhang, M., Wang, B., Liu, H., Feng, S., Wang, N., Lu, G., et al. (2026) · Medicinal Research Reviews · doi:10.1002/med.70052 · Cited by 2
Zhu, W. (2010) · ScholarlyCommons (University of Pennsylvania) · Cited by 1
Zhu, Y., Teng, M., & Li, X. (2011) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309111040589 · Cited by 1
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BackgroundDuan, H., Zhang, Y., Zhou, K., Wang, C., Qiu, D., & Hua, Y. (2017) · PubMed Central · doi:10.7499/j.issn.1008-8830.2017.04.022 · Cited by 1
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BackgroundInfluentialGagare, S. S., Choudhari, V. P., & Jain, A. (2020) · International Journal of ChemTech Research · doi:10.20902/ijctr.2019.130310 · Cited by 1
Liu, F., Ding, X., Xu, X., Wang, F., Chu, X., & Jiang, J. (2022) · Angewandte Chemie · doi:10.1002/ange.202203243 · Cited by 1
Kanmodi, R., Oddiri, R. T., Arowosegbe, M., & Rahmon, S. (2023) · Scientific African · doi:10.1016/j.sciaf.2023.e01940 · Cited by 1
Teixeira, F. C., Roque, É. M. S., de Aguiar, A. M., Silva, S. A., Bezerra, V. B. F., Gomes, O. H. A., Fietto, L. G., & Alves, M. S. (2024) · Plant Gene · doi:10.1016/j.plgene.2024.100459 · Cited by 1
Gismene, C., de Moraes, F. R., Bauermeister, A., da Costa, T. S., Calmon, M. F., Cerbino, L. E. D. A. P., Rahal, P., Góes, R. M., de Moraes, L. A. B., Tasić, L., et al. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c01029 · Cited by 1
Hu, L. I. (2013) · Loyola eCommons (Loyola University of Chicago) · Cited by 1
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Thakur, R. K., & Mishra, D. P. (2012) · Advances in Bioscience and Biotechnology · doi:10.4236/abb.2012.326093 · Cited by 1
“There are various HDAC inhibitors currently under cancer clinical trials [107,108].”
BackgroundHammad, S. (2021) · American Journal of Biomedical Science & Research · doi:10.34297/ajbsr.2021.13.001888 · Cited by 1
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Mahadevan, J. (2015) · IUScholarWorks (Indiana University) · doi:10.7912/c2/1897 · Cited by 1
Schwarzer, D. (2008) · Springer eBooks · doi:10.1007/978-3-540-38918-7_264 · Cited by 1
Agrawal, T., Paul, D., Mishra, A., Arunkumar, G., Pal, S., & Rakshit, T. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.08.588551 · Cited by 1
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Heath, J. N. (2010) · University of Birmingham Institutional Research Archive (University of Birmingham) · Cited by 1
Activation mechanism of AhR pathway in intestinal epithelial cells by commensal bacteria
Marinelli, L. (2018) · theses.fr (ABES) · doi:10.70675/fcff0336z601cz4152z97f7z6e398d94c34b · Cited by 1
Roles of Cytoplasmic Deacetylase Hdac6 in Oncogenic Tumorigenesis
Lee, Y. (2008) · DukeSpace (Duke University)
Stem Cell Differentiation: General Approaches
Domínguez‐Bendala, J. (2009) · Humana Press eBooks · doi:10.1007/978-1-60761-132-5_4
Epigenetic Biomarkers in Melanoma
Liu, S., Ren, S., Howell, P., & Riker, A. I. (2011) · Springer eBooks · doi:10.1007/978-1-60761-433-3_8
Epigenetics and Targeted Therapy in Acute Leukemia
Ma, X., Jiang, S., Huang, Y., Zou, Y., Zheng, R., & Xiao, L. (2011) · InTech eBooks · doi:10.5772/21265
MYC and MNT in transcriptional regulation and chromatin dynamics
Wahlström, T. (2014) · Figshare
Bush, K. A. (2011) · Loyola eCommons (Loyola University of Chicago)
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Wesener, S. R. (2013) · UWM Digital Commons (University of Wisconsin–Milwaukee)
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Gupta, M., Singh, G., & Gupta, S. (2013) · Springer eBooks · doi:10.1007/978-3-642-38111-9_7 · Cited by 1
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Lemper, M., Snykers, S., Vanhaecke, T., Paépe, K. D., & Rogiers, V. (2014) · Kompass Dermatologie · doi:10.1159/000356994
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Wagner, J. M., & Jung, M. (2010) · Pharmazie in unserer Zeit · doi:10.1002/pauz.201000363
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BackgroundSong, W., Huang, Y., Jia, X., Gong, X., Zhen, L., & Fan, Y. (2013) · World Congress on Medical Physics and Biomedical Engineering, September 7 - 12, 2009, Munich, Germany · doi:10.1007/978-3-642-29305-4_53
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SILVEIRA, C., Benetti, F., Seguenka, B., Nicoletti, G., Martins, W. F., Salla, A. C. V., MELO, F. N., & Bertolin, T. E. (2015) · Anais do Congresso Brasileiro de Engenharia Química · doi:10.5151/chemeng-cobeq2014-0098-27053-155444
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Streetly, M. J., Laubach, J. P., Richardson, P. G. G., & Schey, S. (2013) · Cambridge University Press eBooks · doi:10.1017/cbo9780511862465.012
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Dénommé, G. M. (2015) · Lu Zone Ul (Laurentian University)
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Rudnicki, D. L. (2012) · CU Scholar (University of Colorado Boulder)
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Corrêa, C. A. P. (2017) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.17.2017.tde-04012017-111344
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Zeng, Y. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/tvpm-m937
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Metadata
- Authors
- Gallinari, P., Marco, S. D., Jones, P., Pallaoro, M., & Steinkühler, C.
- Affiliations
- Institute of Molecular Biology and Pathology (IT)
- Corresponding author
- Steinkühler, Christian
- Venue
- Cell Research
- Published
- 2007-02-27
- Volume
- 17
- Issue
- 3
- Pages
- 195-211
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- OpenAlex
- W2031954417
- Semantic Scholar
- 755cb3e836171a20f267d47b6677a035efcf7c22
- Cited by
- 678
- References
- 165
- Citations by year
- 2026: 47 · 2025: 87 · 2024: 38 · 2023: 37 · 2022: 52 · 2021: 58 · 2020: 30 · 2019: 29 · 2018: 28 · 2017: 20 · 2016: 29 · 2015: 22 · 2014: 27 · 2013: 38 · 2012: 20
- FWCI
- 2.44
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Research (publishedVersion)
- PubMed (publishedVersion)
- 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
- histone deacetylase, histone acetyltransferase, histone acetylation, gene transcription, chromatin conformation, histone deacetylase inhibitors, cancer therapeutics, non-histone protein acetylation, post-translational modification, cell cycle regulation, cell differentiation, malignant transformation
- MeSH terms
- Acetylation, Animals, Histone Deacetylases, Histones, Humans, Models, Biological, Models, Molecular, Molecular Biology, Neoplasms, Transcription, Genetic, Histone Deacetylase Inhibitors
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