HDAC family: What are the cancer relevant targets?

The 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

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The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress

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Design, synthesis and anti-tumor activity study of novel histone deacetylase inhibitors containing isatin-based caps and o-phenylenediamine-based zinc binding groups

Gao, S., Zang, J., Gao, Q., Liang, X., Ding, Q., Li, X., Xu, W., Chou, C. J., & Zhang, Y. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.03.036 · Cited by 42

Design, synthesis and biological evaluation of novel 2-aminobenzamides containing dithiocarbamate moiety as histone deacetylase inhibitors and potent antitumor agents

Xie, R., Li, Y., Tang, P., & Yuan, Q. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.08.041 · Cited by 42

Spirohydantoins and 1,2,4-triazole-3-carboxamide derivatives as inhibitors of histone deacetylase: Design, synthesis, and biological evaluation

Aboeldahab, A. M. A., Beshr, E. A. M., Shoman, M. E., Rabea, S. M., & Aly, O. M. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.01.021 · Cited by 42

Synthesis and biological evaluation of N-aryl salicylamides with a hydroxamic acid moiety at 5-position as novel HDAC–EGFR dual inhibitors

Zuo, M., Zheng, Y., Lu, S., Li, Y., & Zhang, S. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.05.034 · Cited by 42

Differential molecular mechanistic behavior of HDACs in cancer progression

Singh, T., Kaur, P., Singh, P., Singh, S., & Munshi, A. (2022) · Medical Oncology · doi:10.1007/s12032-022-01770-4 · Cited by 42

Pre-mRNA splicing: Role of epigenetics and implications in disease

Khan, D. H., Jahan, S., & Davie, J. (2012) · Advances in Biological Regulation · doi:10.1016/j.jbior.2012.04.003 · Cited by 41

The therapeutic effect of histone deacetylase inhibitor PCI-24781 on gallbladder carcinoma in BK5.erbB2 mice

Kitamura, T., Connolly, K., Ruffino, L., Ajiki, T., Lueckgen, A., DiGiovanni, J., & Kiguchi, K. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.01.018 · Cited by 41

Sp1-dependent Activation of HDAC7 Is Required for Platelet-derived Growth Factor-BB-induced Smooth Muscle Cell Differentiation from Stem Cells

Zhang, L., Jin, M., Margariti, A., Wang, G., Luo, Z., Zampetaki, A., Zeng, L., Ye, S., Zhu, J., & Xiao, Q. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.153999 · Cited by 41

VPA inhibits breast cancer cell migration by specifically targeting HDAC2 and down-regulating Survivin

Zhang, L., Wang, G., Wang, L., Song, C., Leng, Y., Wang, X., & Kang, J. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-1085-x · Cited by 42

Stabilized Peptide HDAC Inhibitors Derived from HDAC1 Substrate H3K56 for the Treatment of Cancer Stem–Like Cells In Vivo

Wang, D., Li, W., Zhao, R., Chen, L., Liu, N., Tian, Y., Zhao, H., Xie, M., Lu, F., Fang, Q., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-1421 · Cited by 41

Silencing Sirtuin 6 induces cell cycle arrest and apoptosis in non-small cell lung cancer cell lines

Krishnamoorthy, V., & Ravikumar, V. (2020) · Genomics · doi:10.1016/j.ygeno.2020.04.027 · Cited by 42

Loop Interactions and Dynamics Tune the Enzymatic Activity of the Human Histone Deacetylase 8

Kunze, M. B. A., Wright, D. W., Werbeck, N. D., Kirkpatrick, J., Coveney, P. V., & Hansen, D. F. (2013) · Journal of the American Chemical Society · doi:10.1021/ja408184x · Cited by 41

Lysine Deacetylase (KDAC) Regulatory Pathways: an Alternative Approach to Selective Modulation

Dyke, M. W. V. (2014) · ChemMedChem · doi:10.1002/cmdc.201300444 · Cited by 42

Two‐stage additional evidence support association of common variants in the HDAC3 with the increasing risk of schizophrenia susceptibility

Jia, X., Zhang, T., Li, L., Fu, D., Lin, H., Chen, G., Liu, X., & Guan, F. (2016) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.32491 · Cited by 40

Crucial function of histone deacetylase 1 for differentiation of teratomas in mice and humans

Lagger, S., Meunier, D., Mikula, M., Brunmeir, R., Schlederer, M., Artaker, M., Pusch, O., Egger, G., Hagelkrüys, A., Mikulits, W., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.264 · Cited by 40

Histone deacetylase inhibitor sulforaphane: The phytochemical with vibrant activity against prostate cancer

Ganai, S. A. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.04.022 · Cited by 40

Epigenetic treatment combinations to effectively target cisplatin‐resistant germ cell tumors: past, present, and future considerations

Oing, C., Skowron, M. A., Bokemeyer, C., & Nettersheim, D. (2019) · Andrology · doi:10.1111/andr.12611 · Cited by 40

Design and synthesis of novel Flavone-based histone deacetylase inhibitors antagonizing activation of STAT3 in breast cancer

Wei, M., Xie, M., Zhang, Z., Wei, Y., Zhang, J., Pan, H., Li, B., Wang, J., Song, Y., Chong, C., et al. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112677 · Cited by 40

Synthesis, biological evaluation, and molecular docking analysis of novel linker-less benzamide based potent and selective HDAC3 inhibitors

Routholla, G., Pulya, S., Patel, T., Abdul Amin, S., Adhikari, N., Biswas, S., Jha, T., & Ghosh, B. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105050 · Cited by 39

Discussion on structure classification and regulation function of histone deacetylase and their inhibitor

Han, H., Feng, X., He, T., Wu, Y., He, T., Yue, Z., & Zhou, W. (2023) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14366 · Cited by 39

Synthesis, bioevaluation and docking study of 5-substitutedphenyl-1,3,4-thiadiazole-based hydroxamic acids as histone deacetylase inhibitors and antitumor agents

Nam, N., Huong, T. L., Dung, D. T. M., Dung, P. T. P., Oanh, D. T. K., Park, S. H., Kim, K., Han, B. W., Yun, J., Kang, J. S., et al. (2013) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2013.832238 · Cited by 39

Activation of mPTP-dependent mitochondrial apoptosis pathway by a novel pan HDAC inhibitor resminostat in hepatocellular carcinoma cells

Fu, M., Shi, W., Li, Z., & Liu, H. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.04.147 · Cited by 39

LTR12 promoter activation in a broad range of human tumor cells by HDAC inhibition

Krönung, S. K., Beyer, U., Chiaramonte, M. L., Dolfini, D., Mantovani, R., & Dobbelstein, M. (2016) · Oncotarget · doi:10.18632/oncotarget.9255 · Cited by 41

PEGylated Cationic Vectors Containing a Protease-Sensitive Peptide as a miRNA Delivery System for Treating Breast Cancer

Zeng, Y., Zhou, Z., Fan, M., Gong, T., Zhang, Z., & Sun, X. (2016) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b00726 · Cited by 40

Histone deacetylase 3 overexpression in human cholangiocarcinoma and promotion of cell growth via apoptosis inhibition

Yin, Y., Zhang, M., Dorfman, R. G., Li, Y., Zhao, Z., Pan, Y., Zhou, Q., Huang, S. H., Zhao, S., Yao, Y., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2016.457 · Cited by 39

The B7 Family Member B7-H6: a New Bane of Tumor

Chen, Y., Mo, J., Jia, X., & He, Y. (2017) · Pathology & Oncology Research · doi:10.1007/s12253-017-0357-5 · Cited by 39

Cell‑specific histone modifications in atherosclerosis (Review)

Jiang, W., Agrawal, D. K., & Boosani, C. S. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9142 · Cited by 40

CAP rigidification of MS-275 and chidamide leads to enhanced antiproliferative effects mediated through HDAC1, 2 and tubulin polymerization inhibition

Singh, A., Chang, T.-Y., Kaur, N., Hsu, K., Yen, Y., Lin, T. E., Lai, M.-J., Lee, S., & Liou, J. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113169 · Cited by 39

Design, synthesis and biological evaluation of brain penetrant benzazepine-based histone deacetylase 6 inhibitors for alleviating stroke-induced brain infarction

Guo, Z., Zhang, Z., Zhang, Y., Wang, G., Huang, Z., Zhang, Q., & Li, J. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113383 · Cited by 39

Distinct Defects in Synaptic Differentiation of Neocortical Neurons in Response to Prenatal Valproate Exposure

Iijima, Y., Behr, K., Iijima, T., Biemans, B., Bischofberger, J., & Scheiffele, P. (2016) · Scientific Reports · doi:10.1038/srep27400 · Cited by 39

Epigenetic regulation and therapeutic targets in the tumor microenvironment

Xie, Z., Zhou, Z., Yang, S., Zhang, S., & Shao, B. (2023) · Molecular Biomedicine · doi:10.1186/s43556-023-00126-2 · Cited by 38

Negative Regulation of the Acetyltransferase TIP60-p53 Interplay by UHRF1 (Ubiquitin-like with PHD and RING Finger Domains 1)

Dai, C., Shi, D., & Gu, W. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.476606 · Cited by 38

Deacetylase inhibitors repress STAT5-mediated transcription by interfering with bromodomain and extra-terminal (BET) protein function

Pinz, S., Unser, S., Buob, D., Fischer, P., Jobst, B., & Rascle, A. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv188 · Cited by 38

Design and synthesis of novel and highly-active pan-histone deacetylase (pan-HDAC) inhibitors

Tashima, T., Murata, H., & Kodama, H. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.05.001 · Cited by 38

Regulation of intestinal serotonin transporter expression via epigenetic mechanisms: role of HDAC2

Gill, R. K., Kumar, A., Malhotra, P., Maher, D., Singh, V., Dudeja, P. K., Alrefai, W. A., & Saksena, S. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00361.2012 · Cited by 41

Synergy between histone deacetylase inhibitors and DNA-damaging agents is mediated by histone deacetylase 2 in colorectal cancer

Alzoubi, S., Brody, L., Rahman, S., Mahul-Mellier, A.-L., Mercado, N., Ito, K., El-Bahrawy, M., Silver, A., Boobis, A., Bell, J. D., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9887 · Cited by 37

Epigenetics as a Therapeutic Target in Osteoarthritis

Núñez-Carro, C., Blanco-Blanco, M., Villagrán-Andrade, K. M., Blanco, F., & de Andrés, M. D. (2023) · Pharmaceuticals · doi:10.3390/ph16020156 · Cited by 38

MiR-376a and Histone Deacetylation 9 Form A Regulatory Circuitry in Hepatocellular Carcinoma

Zheng, Y., Chen, H., Yin, M., Ye, X., Chen, G., Zhou, X., Yin, L., Zhang, C., & Ding, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000369733 · Cited by 37

Sensitization of tumor cells by targeting histone deacetylases

Perego, P., Zuco, V., Gatti, L., & Zunino, F. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.11.010 · Cited by 37

Histone acetyltransferases and deacetylases: molecular and clinical implications to gastrointestinal carcinogenesis

Sun, W., Zhou, X., Zheng, J., Lu, M., Nie, J.-Y., Yang, X., & Zheng, Z. (2011) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmr113 · Cited by 40

Histone deacetylase inhibition enhances in-vivo bone regeneration induced by human periodontal ligament cells

Huynh, N. C., Everts, V. E., Nifuji, A., Pavasant, P., & Ampornaramveth, R. S. (2016) · Bone · doi:10.1016/j.bone.2016.11.017 · Cited by 37

Canonical and Non-Canonical Autophagy in HIV-1 Replication Cycle

Leymarie, O., Lepont, L., & Berlioz‐Torrent, C. (2017) · Viruses · doi:10.3390/v9100270 · Cited by 37

Structure–Activity and Structure–Toxicity Relationships of Peptoid‐Based Histone Deacetylase Inhibitors with Dual‐Stage Antiplasmodial Activity

Mackwitz, M. K. W., Hesping, E., Antonova‐Koch, Y., Diedrich, D., Woldearegai, T. G., Skinner‐Adams, T. S., Clarke, M., Schöler, A., Limbach, L., Kurz, T., et al. (2019) · ChemMedChem · doi:10.1002/cmdc.201800808 · Cited by 37

Discovery of 1,2,4-oxadiazole-Containing hydroxamic acid derivatives as histone deacetylase inhibitors potential application in cancer therapy

Yang, Z., Shen, M., Tang, M., Zhang, W., Cui, X. J., Zhang, Z., Pei, H., Li, Y., Hu, M., Bai, P., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.05.089 · Cited by 37

Exploration of certain 1,3-oxazole- and 1,3-thiazole-based hydroxamic acids as histone deacetylase inhibitors and antitumor agents

Anh, D. T., Pham‐The, H., Le‐Thi‐Thu, H., Park, E. J., Jun, H. W., Kang, J. S., Kwon, J., Dung, D. T. M., Anh, V. T., Huệ, V. T. M., et al. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.103988 · Cited by 37

Histone deacetylase 1 and 2 in mesenchymal tumors

Pacheco, M., & Nielsen, T. O. (2011) · Modern Pathology · doi:10.1038/modpathol.2011.157 · Cited by 37

Oncogenic potential of CK 2α and its regulatory role in EGF ‐induced HDAC 2 expression in human liver cancer

Kim, H. S., Chang, Y. G., Bae, H. J., Eun, J. W., Shen, Q., Park, S. J., Shin, W. C., Lee, E. K., Park, S., Ahn, Y. M., et al. (2013) · FEBS Journal · doi:10.1111/febs.12652 · Cited by 37

The Landscape of Signaling Pathways and Proteasome Inhibitors Combinations in Multiple Myeloma

Paradžik, T., Bandini, C., Mereu, E., Labrador, M., Taìana, E., Amodio, N., Neri, A., & Piva, R. (2021) · Cancers · doi:10.3390/cancers13061235 · Cited by 36

Screening of selective histone deacetylase inhibitors by proteochemometric modeling

Wu, D., Huang, Q., Zhang, Y., Zhang, Q., Liu, Q., Gao, J. A., Cao, Z., & Zhu, R. (2012) · BMC Bioinformatics · doi:10.1186/1471-2105-13-212 · Cited by 38

A toolbox for class I HDACs reveals isoform specific roles in gene regulation and protein acetylation

Hess, L., Moos, V., Lauber, A. A., Reiter, W., Schuster, M. K., Hartl, N., Lackner, D. H., Boenke, T., Koren, A., Guzzardo, P. M., et al. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010376 · Cited by 38

Histone deacetylase inhibition results in a common metabolic profile associated with HT29 differentiation

Alcarraz‐Vizán, G., Boren, J., Lee, W. P., & Cascante, M. (2010) · Metabolomics · doi:10.1007/s11306-009-0192-0 · Cited by 36

The role of HDAC2 in chromatin remodelling and response to chemotherapy in ovarian cancer

Huang, R., Langdon, S. P., Tse, M., Mullen, P., Um, I. H., Faratian, D., & Harrison, D. J. (2015) · Oncotarget · doi:10.18632/oncotarget.6618 · Cited by 36

Romidepsin for the treatment of T-cell lymphomas

McGraw, A. (2013) · American Journal of Health-System Pharmacy · doi:10.2146/ajhp120163 · Cited by 35

Aggresome formation is regulated by RanBPM through an interaction with HDAC6

Salemi, L. M., Almawi, A. W., Lefebvre, K. J., & Schild‐Poulter, C. (2014) · Biology Open · doi:10.1242/bio.20147021 · Cited by 35

Epigenetic‐mediated immune suppression of positive co‐stimulatory molecules in chemoresistant ovarian cancer cells

Çaçan, E. (2017) · Cell Biology International · doi:10.1002/cbin.10729 · Cited by 35

Combinatorial In Silico Strategy towards Identifying Potential Hotspots during Inhibition of Structurally Identical HDAC1 and HDAC2 Enzymes for Effective Chemotherapy against Neurological Disorders

Ganai, S. A., Abdullah, E., Rashid, R., & Altaf, M. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00357 · Cited by 36

Design and Synthesis of Dihydroxamic Acids as HDAC6/8/10 Inhibitors

Morgen, M., Steimbach, R. R., Géraldy, M. N. E., Hellweg, L., Sehr, P. A., Ridinger, J., Witt, O., Oehme, I., Herbst‐Gervasoni, C. J., Osko, J. D., et al. (2020) · ChemMedChem · doi:10.1002/cmdc.202000149 · Cited by 35

Broad-Spectrum HDAC Inhibitors Promote Autophagy through FOXO Transcription Factors in Neuroblastoma

Körholz, K. F., Ridinger, J., Krunic, D., Najafi, S., Gerloff, X. F., Frese, K., Meder, B., Peterziel, H., Vega-Rubín-de-Celis, S., Witt, O., et al. (2021) · Cells · doi:10.3390/cells10051001 · Cited by 35

Development of Fluorinated Peptoid-Based Histone Deacetylase (HDAC) Inhibitors for Therapy-Resistant Acute Leukemia

Reßing, N., Schliehe‐Diecks, J., Watson, P. R., Sönnichsen, M., Cragin, A. D., Schöler, A., Yang, J. C., Schäker‐Hübner, L., Borkhardt, A., Christianson, D. W., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01418 · Cited by 35

Identification of Novel Natural Dual HDAC and Hsp90 Inhibitors for Metastatic TNBC Using e-Pharmacophore Modeling, Molecular Docking, and Molecular Dynamics Studies

Abdelmoniem, N., Abdallah, M. H., Mukhtar, R. M., Moutasim, F., Ahmed, A. R., Edris, A., Ibraheem, W., Makki, A. A., Elshamly, E. M., Elhag, R. I., et al. (2023) · Molecules · doi:10.3390/molecules28041771 · Cited by 35

Chemical regulation of mid- and late-life longevities in Drosophila

McDonald, P. J., Maizi, B. M., & Arking, R. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.09.006 · Cited by 35

Manipulating Protein Acetylation in Breast Cancer: A Promising Approach in Combination with Hormonal Therapies?

Linarès, A., Dalenc, F., Balaguer, P., Boulle, N., & Cavaillès, V. (2010) · BioMed Research International · doi:10.1155/2011/856985 · Cited by 36

Histone deacetylase 5 promotes the proliferation of glioma cells by upregulation of Notch 1

Liu, Q., Zheng, J., CHEN, J.-K., Yan, X., Chen, H., Nong, W., & Huang, H. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.2395 · Cited by 35

Design and Optimization of Novel Hydroxamate-Based Histone Deacetylase Inhibitors of Bis-Substituted Aromatic Amides Bearing Potent Activities against Tumor Growth and Metastasis

Yang, F., Zhang, T., Wu, H., Yang, Y., Liu, N., Chen, A., Li, Q., Li, J., Qin, L., Jiang, B., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5012148 · Cited by 35

Synthesis and Preclinical Evaluation of a Highly Improved Anticancer Prodrug Activated by Histone Deacetylases and Cathepsin L

Ueki, N., Wang, W., Swenson, C., McNaughton, C., Sampson, N. S., & Hayman, M. J. (2016) · Theranostics · doi:10.7150/thno.13826 · Cited by 35

Histone deacetylase 8 is deregulated in urothelial cancer but not a target for efficient treatment

Lehmann, M., Hoffmann, M. J., Koch, A., Ulrich, S. M., Schulz, W. A., & Niegisch, G. (2014) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-014-0059-8 · Cited by 34

Simultaneously defining cell phenotypes, cell cycle, and chromatin modifications at single‐cell resolution

Chambliss, A. B., Wu, P., Chen, W., Sun, S. X., & Wirtz, D. (2013) · The FASEB Journal · doi:10.1096/fj.12-227108 · Cited by 34

Histone Deacetylase Inhibitors Inhibit the Proliferation of Gallbladder Carcinoma Cells by Suppressing AKT/mTOR Signaling

Zhang, P., Guo, Z., Wu, Y., Hu, R., Du, J., He, X., Jiao, X., & Zhu, X. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136193 · Cited by 35

Mechanism and stereoselectivity of HDAC I inhibition by (R)-9-hydroxystearic acid in colon cancer

Parolin, C., Calonghi, N., Presta, E., Boga, C., Caruana, P., Naldi, M., Andrisano, V., Masotti, L., & Sartor, G. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.07.007 · Cited by 34

Inhibition of the NAD-Dependent Protein Deacetylase SIRT2 Induces Granulocytic Differentiation in Human Leukemia Cells

Sunami, Y., Araki, M., Hironaka, Y., Morishita, S., Kobayashi, M., Liew, E. L., Edahiro, Y., Tsutsui, M., Ohsaka, A., & Komatsu, N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057633 · Cited by 35

The mechanism of stem cell differentiation into smooth muscle cells

Wang, G., Luo, Z., Xu, Q., & Xiao, Q. (2010) · Thrombosis and Haemostasis · doi:10.1160/th09-11-0794 · Cited by 35

Role for Class I histone deacetylases in multidrug resistance

Xu, Y., Jiang, Z., Yin, P., Li, Q., & Liu, J. (2011) · Experimental Cell Research · doi:10.1016/j.yexcr.2011.11.010 · Cited by 34

Metabolism, longevity and epigenetics

Cosentino, C., & Mostoslavsky, R. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1295-3 · Cited by 35

Inhibition of Zinc-Dependent Histone Deacetylases with a Chemically Triggered Electrophile

Bošković, Ž., Kemp, M. M., Freedy, A. M., Viswanathan, V. S., Pop, M. S., Fuller, J. H., Martínez, N. M., Figueroa-Lazú, S., Hong, J. A., Lewis, T. A., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00012 · Cited by 34

The HDAC6/8/10 inhibitor TH34 induces DNA damage-mediated cell death in human high-grade neuroblastoma cell lines

Kolbinger, F. R., Koeneke, E., Ridinger, J., Heimburg, T., Müller, M., Bayer, T., Sippl, W., Jung, M., Gunkel, N., Miller, A. K., et al. (2018) · Archives of Toxicology · doi:10.1007/s00204-018-2234-8 · Cited by 34

Targeting epigenetic modifications as a potential therapeutic option for diabetic retinopathy

Kumari, N., Karmakar, A., & Ganesan, S. K. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29180 · Cited by 34

Molecular mechanisms underlying eicosapentaenoic acid inhibition of HDAC1 and DNMT expression and activity in carcinoma cells

Ceccarelli, V., Ronchetti, S., Marchetti, M. C., Calvitti, M., Riccardi, C., Grignani, F., & Vecchini, A. (2020) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2020.194481 · Cited by 34

Multitarget Anticancer Agents Based on Histone Deacetylase and Protein Kinase CK2 Inhibitors

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LukS-PV Inhibits Hepatocellular Carcinoma Progression by Downregulating HDAC2 Expression

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