The DOI matches its Crossref record; 123 of the 131 references it cites were found in a registry or an index.
HDAC family: What are the cancer relevant targets?
Abstract
Histone deacetylases comprise a family of 18 genes, which are grouped into classes I-IV based on their homology to their respective yeast orthologues. Classes I, II, and IV consist of 11 family members, which are referred to as "classical" HDACs, whereas the 7 class III members are called sirtuins. Classical HDACs are a promising novel class of anti-cancer drug targets. First HDAC inhibitors have been evaluated in clinical trials and show activity against several cancer diseases. However, these compounds act unselectively against several or all 11 HDAC family members. As a consequence, clinical phase I trials document a wide range of side effects. Therefore, the current challenge in the field is to define the cancer relevant HDAC family member(s) in a given tumor type and to design selective inhibitors, which target cancer cells but leave out normal cells. Knockout of single HDAC family members in mice produces a variety of phenotypes ranging from early embryonic death to viable animals with only discrete alterations, indicating that potential side effects of HDAC inhibitors depend on the selectivity of the compounds. Recently, several studies have shown that certain HDAC family members are aberrantly expressed in several tumors and have non-redundant function in controlling hallmarks of cancer cells. The aim of this review is to discuss individual HDAC family members as drug targets in cancer taking into consideration their function under physiological conditions and their oncogenic potential in malignant disease.
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“Unlike other histone deacetylases, inhibition of HDAC6 does not appear to be associated with any toxicity, making it an excellent drug target.7”
From Rational Design and Simple Chemistry Yield a Superior, Neuroprotective HDAC6 Inhibitor, Tubastatin A (2010) · cites this paper as [7]
Citations
Cites
1 retracted
Pulukuri, S. M. K., Gorantla, B., & Rao, J. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705867200 · Cited by 51
RetractedThe Consensus Coding Sequences of Human Breast and Colorectal Cancers
Sjöblom, T., Jones, S., Wood, L. D., Parsons, D. W., Lin, J., Barber, T. D., Mandelker, D. L., Leary, R. J., Ptak, J., Silliman, N., et al. (2006) · Science · doi:10.1126/science.1133427 · Cited by 3,161
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
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
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
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
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714
Kawaguchi, Y., Kovacs, J. J., McLaurin, A. C., Vance, J. M., Ito, A., & Yao, T. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,529
Flagged first, then by citations
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Research works printed but not linked: 1
- Li, 2008, HDAC6 is required for EGF-induced β-catenin nuclear localization, J. Biol. Chem.
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Items 901–1,000 of 1,000
Nde, J., Kempf, C. G., Zimmermann, R. C., Cesare, J., Zhang, Y., Workman, J. L., Florens, L. A., & Washburn, M. P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.08.669391 · Cited by 2
Spirin, P., Vedernikova, V., Volkava, T., Morozov, A. V., Kleymenova, A. A., Zemskaya, A. S., Shyrokova, L., Porozov, Y. B., Glumakova, K. A., Lebedev, T. D., et al. (2025) · Pharmaceutics · doi:10.3390/pharmaceutics17040416 · Cited by 1
Vajen, B., Schäffer, V., Eilers, M., Schlegelberger, B., & Skawran, B. (2025) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-025-04896-w · Cited by 1
Preclinical Characterization of SDFZ‐8, a Highly Potent HDAC1 Inhibitor, for Cancer Immunotherapy
Zhou, Y., Du, J., Li, X., Zhao, H., Xue, J., Liu, Y., Yang, X., Yu, J., Hou, X., & Fang, H. (2025) · MedComm · doi:10.1002/mco2.70500 · Cited by 1
Ramírez, J. E. G., & Mancilla, T. (2023) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14323 · Cited by 1
MYC plus class IIa HDAC inhibition drives mitochondrial dysfunction in non-small cell lung cancer
Park, J., Chen, Y.-Y., Cao, J. J., An, J., Yen, R.-W. C., Outen, J. D., Baylin, S. B., & Topper, M. J. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115722 · Cited by 1
Role of Histone Modifications in Oral Squamous Cell Carcinoma
Tomar, P., Singh, D., Anand, A., Verma, S., Agarwal, N., Mathur, R., PRIYANKA, P., Pamei, S., Gupta, V. K., & Jha, A. K. (2025) · NIPES Journal of Science and Technology Research · doi:10.37933/nipes/7.2.2025.26 · Cited by 1
Zhao, Y., Zhang, M.-Y., Liang, Z., Liu, X., Kong, W., Hu, L., Zhou, Y.-C., Lv, K., Zhao, M., Chen, D., et al. (2025) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2025.143787 · Cited by 1
Wang, X., Du, L., Xue, Y., Su, Y., Yuan, X., Yang, S., Su, W., Gou, W., Chen, X., & Zong, L. (2025) · RSC Advances · doi:10.1039/d5ra06970j · Cited by 1
Arya, D., Khan, G. A., Singh, S., Upadhyay, A., Sharma, B. P., Maharjan, R., Sharma, M. L., Gupt, M. P., Dubey, S. S., Pathak, P., et al. (2025) · Archiv der Pharmazie · doi:10.1002/ardp.70172 · Cited by 1
Targeted HDAC8 inhibition with non-hydroxamate [1,2,4]triazolo[4,3-a] quinoline compounds
Bandaru, N. V. M. R., Fathima, A., Sengar, S., Schweipert, M., Chaitanya, K. S., Mohammed, M.-U.-R., Gore, S. T., Trinath, J., Sharma, V., Abbineni, C., et al. (2026) · Scientific Reports · doi:10.1038/s41598-026-38490-y · Cited by 1
PROTACs in cancer therapy: targeted degradation of GPX4, PARP and epigenetic regulators
Periyasamy, S., Jarrett, T., Truong, J., & Skouta, R. (2026) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2026.2636394 · Cited by 2
Chen, C., Havlínová, B., Vošahlíková, M., Tuckova, R., Stjärnhage, J., Lin, Z., Rayner, C., Bařinka, C., Söhnel, T., Jamieson, S. M. F., et al. (2026) · Inorganic Chemistry Frontiers · doi:10.1039/d6qi00422a · Cited by 1
Dash, S., Shehensha, S., & Dhar, A. K. (2026) · ChemistrySelect · doi:10.1002/slct.73651 · Cited by 1
Therapeutic potential of histone deacetylase inhibitors for breast cancer
Viswanathan, S., Carothers, S., & Ramaswamy, B. (2011) · Clinical Investigation · doi:10.4155/cli.11.29 · Cited by 1
A Sensitive and Flexible Assay for Determining Histone Deacetylase 1 (HDAC1) Activity
Wu, M.-Y., & Wu, R. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3667-0_1 · Cited by 1
Chromatin Signaling in Aging and Cellular Senescence
Couteau, F., & Mallette, F. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802389-1.00016-2 · Cited by 1
Assessment of HDACi-Induced Protein Cleavage by Caspases
Treude, F., Gladbach, T., Plaster, J., & Hartkamp, J. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6527-4_2 · Cited by 1
Pinz, S., & Rascle, A. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6527-4_19 · Cited by 1
Rapid Detection of p53 Acetylation Status in Response to Cellular Stress Signaling
Farkaš, M., & McMahon, S. B. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9434-2_15 · Cited by 1
Epigenetic regulation and microRNA expression
Jurj, A. M., Zănoagă, O., Braicu, C., & Berindan‐Neagoe, I. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-89774-7.00003-0 · Cited by 1
Synthetic Study on Bicyclic Depsipeptides Containing an Intramolecular Disulfide Bond
Narita, K. (2022) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.22-00091 · 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
Niu, K., Yang, L., Song, W., Liu, Z., Yuan, J., Zhang, H., Zhang, W., Wang, J., & Tao, K. (2023) · Shock · doi:10.1097/shk.0000000000002136 · Cited by 1
Epigenetic therapies: histone deacetylases
Blanquart, C. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-91367-6.00022-2 · Cited by 1
Dağsuyu, E., & Yanardağ, R. (2023) · Çukurova medical journal (Online)/Çukurova medical journal · doi:10.17826/cumj.1316664 · Cited by 1
Perez‐Stable, C., Pozas, A. D. L., Reiner, T., Gomez, J., Nagarajan, M. K., Foster, R. T., Ure, D., & Wangpaichitr, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146699 · Cited by 1
Cardiac Plasticity in Health and Disease
Gondalia, R., Rothermel, B. A., Lavandero, S., Gillette, T. G., & Hill, J. A. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-891-7_7 · Cited by 1
Royce, S. G., Ververis, K., & Karagiannis, T. C. (2012) · ISRN Pulmonology · doi:10.5402/2012/452307 · Cited by 1
Cho, K., Choi, W., Crane, C. L., & Park, C. S. (2013) · European Journal of Nutrition · doi:10.1007/s00394-013-0626-3 · Cited by 1
Epigenetik des Urothelkarzinoms
Niegisch, G., Hoffmann, M. J., Koutsogiannouli, E. A., & Schulz, W. A. (2015) · Der Urologe · doi:10.1007/s00120-014-3756-1 · Cited by 1
Hydroxamic Acids as Potent Antioxidants and Their Methods of Evaluation
Mehndiratta, S., Nepali, K., & Satapathy, M. K. (2017) · Springer eBooks · doi:10.1007/978-981-10-4711-4_5 · Cited by 1
Clauß, O., Schäker‐Hübner, L., Wenzel, B., Toussaint, M., Deuther‐Conrad, W., Gündel, D., Teodoro, R., Dukić-Stefanović, S., Ludwig, F., Kopka, K., et al. (2022) · Pharmaceuticals · doi:10.3390/ph15030324 · Cited by 1
Epigenetic Biomarkers in Toxicology
Chintalapati, A. J., & Barile, F. A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814655-2.00045-1 · Cited by 1
Polypharmacology in Clinical Applications—Anticancer Polypharmacology
Wang, Z., & Yang, B. (2022) · Springer eBooks · doi:10.1007/978-3-031-04998-9_3 · Cited by 1
Modeling anticancer pharmacophore based on inhibition of HDAC7
Laboratoire de Thermodynamique et de Physico-Chimie du Milieu, U. D. F. E. D. R. S. F. E. A., Affi, S. T., Doh, S., Coulibaly, S., Konaté, B., & Ziao, N. (2021) · SDRP Journal of Computational Chemistry & Molecular Modelling · doi:10.25177/jccmm.5.3.ra.10776 · Cited by 1
Sang, D. M., Na, I. H., Anh, D. T., Dung, D. T. M., Hang, N. T. T., Phuong‐Anh, N. T., Pham‐The, H., Oanh, D. T. K., Tùng, T. T., Lee, S. J., et al. (2023) · Chemistry & Biodiversity · doi:10.1002/cbdv.202201030 · Cited by 1
Epigenomic and Transcriptional Regulation of Hepatic Metabolism by REV-ERB and Hdac3
Feng, D. (2013) · ScholarlyCommons (University of Pennsylvania) · Cited by 1
Rao‐Bindal, K. (2012) · Digital Commons-TMC (Texas Medical Center) · Cited by 1
Shen, Y., Pei, W., Sun, C., Hu, Y., Li, P., Shen, Y., Zhang, Y., Miao, F., & Zhang, J. (2022) · Research Square · doi:10.21203/rs.3.rs-1863747/v1 · Cited by 1
Helou, M. E. (2017) · theses.fr (ABES) · doi:10.70675/0c7d676dz64a3z4641zb8cbzd99a75ef2126 · Cited by 1
The Discovery of Anticancer Drugs Targeting Epigenetic Enzymes
Ganesan, A. (2012) · Wiley eBooks · doi:10.1002/9783527651085.ch5
Epigenetic Control of Tumor Suppressor Genes in Lung Cancer
Qiu, X., Perez-Soler, R., & Zou, Y. (2012) · InTech eBooks · doi:10.5772/26592
3D MODELING AND CHARACTERIZATION OF HDAC9
Samant, L. R., Sangar, V. C., Khanzode, M., & Chowdhary, A. S. (2014) · International Journal of Pharmacy and Pharmaceutical Sciences
Ito, K., & Mercado, N. (2012) · Wiley eBooks · doi:10.1002/9781119967309.ch5
A Synthetic Biology Approach to Engineering New Anticancer Agents
Wesener, S. R. (2013) · UWM Digital Commons (University of Wisconsin–Milwaukee)
Regulació de l'heterocromatina constitutiva en condicions normals i d'estrès: Paper de SirT1 i d'HP1
Raurell‐Vila, H. (2014) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)
Clinical takeoff for new epigenetic targets
Lou, K.-J. (2013) · Science-Business eXchange · doi:10.1038/scibx.2013.1118
The role of epigenetics in breast cancer progression
Yıldırım, A. (2013) · Utrecht University Repository (Utrecht University)
Development of Fluorogenic Probes for the Detection of Histone Deacetylase Activity
Hori, Y., Baba, R., & Kikuchi, K. (2015) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.14-00202-3
[Diagnosis and treatment of nephroptosis in flying personnel].
Гарилевич, Б. А., & Avdeĭchuk, I. I. (1997) · PubMed
An Overview of Epigenetic Mechanisms in Health and Disease
Westerland, C., & Karagiannis, T. C. (2014) · Springer eBooks · doi:10.1007/978-1-4939-0706-9_3
Isoform-Selective HDAC Inhibition for the Treatment of Lupus Nephritis
Regna, N. L. (2014) · VTechWorks (Virginia Tech)
Lozada, E., & Santiago, L. (2011) · UKnowledge (University of Kentucky)
Elucidation of the Histone Deacetylase 6 Pharmacophore
Kalin, J. H. (2012) · Figshare
Effect of DNA methylation and histone modification during the de-velopment of cloned animals
Guo, L., Li, H., & Han, Z. (2010) · Hereditas (Beijing) · doi:10.3724/sp.j.1005.2010.00762
Researchattenuates TRAIL-induced apoptosis of pancreatic cancer cells
Schüler, S., Fritsche, P., Diersch, S., Arlt, A., Schmid, R. M., Saur, D., & Schneider, G. (2010)
The Role of Histone Deacetylases in Glucose Metabolism: a Mini- Review
Liu, F. (2015) · International Journal of Endocrinology and Metabolic Disorders · doi:10.16966/2380-548x.113
Evaluation of Photoreactive and Phenothiazine-based HDAC Inhibitors
Madriaga, A. (2014) · Figshare
Epigenetics of Dental Stem Cells
Duncan, H. F., & Cooper, P. R. (2016) · Stem cell biology and regenerative medicine · doi:10.1007/978-3-319-33299-4_4
Cho, K. B. (2015) · NDSU Repository (North Dakota State University)
Chapter 11 Zyfl amend and Prostate Cancer Therapy
Whelan, J. N., Zhao, Y., Huang, E., MacDonald, A., & Donohoe, D. R. (2016) · Traditional herbal medicines for modern times · doi:10.1201/9781315370156-12
NUCLEOCYTOSKELETAL CONNECTIONS IN MECHANOTRANSDUCTION
Chambliss, A. B. (2014)
Role of endogenous retrovirus promoter activity in tumor suppression
Krönung, S. K. (2015) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-5097
Investigating the role of epigenetics in scar maintenance
Stevenson, A. W. (2016) · UWA Profiles and Research Repository (UWA)
Venkataramani, V. (2012) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-1184
Las HDAC en la regulación de la expresión génica y el cáncer
Fernández, A. B. (2014) · MoleQla: revista de Ciencias de la Universidad Pablo de Olavide
Functional Characterization and Structure Prediction of HDAC-10: A Bioinformatics Approach
Sabeena, M., Jamil, K., & Nehru, J. (2014)
Sumpf, K. (2017) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-6571
Identification and characterisation of novel cancer testis antigens in human cancer cells
Alsiwiehri, N. O. (2017) · Bangor University Research Portal (Bangor University)
Askarian-Amiri, M., Rodger, E. J., Chatterjee, A., Finlay, G. J., & Baguley, B. C. (2018) · Springer eBooks · doi:10.1007/978-3-319-78310-9_7
Sun, X., Chen, Z. H., & Wang, X. (2018) · Translational bioinformatics · doi:10.1007/978-981-10-8764-6_12
The mutations identified in human HDAC-10 gene and their prognosis in cancer cases
Sabeena, M., Jamil, K., & Swamy, A. V. N. (2018) · INTERNATIONAL JOURNAL OF PHARMACEUTICAL SCIENCE AND HEALTH CARE · doi:10.26808/rs.ph.i8v3.04
Bali, D., Kürekçi, A. E., & Akar, M. N. (2018) · SDÜ Tıp Fakültesi Dergisi · doi:10.17343/sdutfd.373907
Leki wpływające na mechanizmy epigenetyczne w ostrej białaczce szpikowej
Wiśniewski, K., & Góra‐Tybor, J. (2018) · Hematologia · doi:10.5603/hem.2018.0014
Target Identification of HDAC8 Isoform for the Treatment of Cancer
Umamaheswari, A., Puratchikody, A., & Balasubramaniyan, S. (2018) · Advances in medical technologies and clinical practice book series · doi:10.4018/978-1-5225-7326-5.ch007
Classical And Ab Initio Qm/mm Simulations Of Bacterial Enzymes
Dewage, S. W. (2015)
Yufeng, C., Nesa, E. U., Chen, X., Wang, C., Chen, X., Wang, Y., Qu, Y., Mi, S., Guan, S., Zahur, T., et al. (2019) · International Journal of Cancer and Oncology · doi:10.15436/2377-0902.19.2465
The efficacy of HDAC inhibitors in neoplasm treatment
Psiuk, D., Rocka, A. A., Żak, K., Tomczyk, Z., & Filip, A. A. (2020) · Journal of Education Health and Sport · doi:10.12775/jehs.2020.10.08.028
Target Proteins Involved in Aging Mechanism as an Aging Molecular Marker
Kim, M. (2016) · Journal of Life Science · doi:10.5352/jls.2016.26.8.983
MAGNETIC DEVICES IN GLASS APPARATUS. PART II
Gamisch, G., & Ruettiger, W. (1958) · OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information)
Epigenetic Signatures of Breast Cancer Genes
Anant, S., Dhar, A., & Ramalingam, S. (2013) · Springer eBooks · doi:10.1007/978-94-007-6612-9_10
Impacto de los inhibidores de Deacetilasas de Histonas (iHDAC) sobre la funcionalidad de células NK
Rossi, L. E. (2012) · Repositorio Digital Institucional de la Universidad de Buenos Aires (Universidad de Buenos Aires)
Sweatt, J. D., & Day, J. J. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.718018322.793478215
Epigenomic Imaging of Neuropsychiatric Diseases
Bahari‐Javan, S. (2013) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4280
Full PDF of Hematology Reviews 2009, volume 1, issue 1.
Editors, T. L. O. (2011) · Hematology Reports · doi:10.4081/1716
Ning, J. (2022) · Biomedical Journal of Scientific & Technical Research · doi:10.26717/bjstr.2022.43.006887
(2017) · Cancer Studies and Therapeutics · doi:10.31038/cst.2017223
Is the effect of Decitabine limited to hypomethylation and DNMTs?Preprint
Dalvand, S., Namdari, A., Alemi, A., Meshkibaf, M. H., Setayesh, S., Karamallah, M. H., & Farrokhifar, M. (2019) · Research Square · doi:10.21203/rs.2.13184/v1
Effect of 2,6-diketopiperazines derived from α-amino acids over MDA-MB-231 breast cancer cell linePreprint
González, F. P. G., Jiménez, E. M., & Mancilla, T. (2022) · Research Square · doi:10.21203/rs.3.rs-2354174/v1
Ghorbian, M. (2023) · Research Square · doi:10.21203/rs.3.rs-2664627/v1
Novotny‐Diermayr, V., Sangthongpitag, K., Hu, C. Y., Wu, X., Sausgruber, N., Yeo, P., Greicius, G., Pettersson, S., Liang, A. L., Loh, Y. K., et al. (2023) · doi:10.1158/1535-7163.c.6531900.v1
Metadata
- Authors
- Witt, O., Deubzer, H. E., Milde, T., & Oehme, I.
- Affiliations
- German Cancer Research Center (DE)
- Corresponding author
- Witt, Olaf
- Venue
- Cancer Letters
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 277
- Issue
- 1
- Pages
- 8-21
- ISSN
- 0304-3835 (ISSN-L)
- OpenAlex
- W2029148944
- Cited by
- 1,069
- References
- 131
- Citations by year
- 2026: 25 · 2025: 55 · 2024: 56 · 2023: 67 · 2022: 52 · 2021: 54 · 2020: 65 · 2019: 53 · 2018: 64 · 2017: 61 · 2016: 86 · 2015: 75 · 2014: 79 · 2013: 94 · 2012: 73
- FWCI
- 2.83
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cancer Letters (publishedVersion)
- PubMed (publishedVersion)
- MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (submittedVersion)
- Funders
- Bundesministerium für Bildung und Forschung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- histone deacetylase, histone deacetylase inhibitors, sirtuins, class I HDACs, class II HDACs, cancer drug targets, selective inhibitors, oncogenicity
- MeSH terms
- Animals, Antineoplastic Agents, Enzyme Inhibitors, Histone Deacetylases, Humans, Neoplasms, Polymorphism, Genetic, Histone Deacetylase Inhibitors
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