Chemical phylogenetics of histone deacetylases

MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform

Katoh, K. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf436 · Cited by 17,027

A Rapid Bootstrap Algorithm for the RAxML Web Servers

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MAFFT version 5: improvement in accuracy of multiple sequence alignment

Katoh, K., Kuma, K., Toh, H., & Miyata, T. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki198 · Cited by 5,063

Lysine acetylation targets protein complexes and co-regulates major cellular functions

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Recent developments in the MAFFT multiple sequence alignment program

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Anticancer activities of histone deacetylase inhibitors

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Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer

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Sustained hippocampal chromatin regulation in a mouse model of depression and antidepressant action

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Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis

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Histone acetyltransferase complexes: one size doesn't fit all

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Hydrazide-Based Class I Selective HDAC Inhibitors Completely Reverse Chemoresistance Synergistically in Platinum-Resistant Solid Cancer Cells

Kraft, F. B., Biermann, L., Schäker‐Hübner, L., Hanl, M., Hamacher, A., Kassack, M. U., & Hansen, F. K. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01817 · Cited by 28

Cancer epigenetic therapy: recent advances, challenges, and emerging opportunities

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Design, Synthesis, and Structure-Activity relationships of Evodiamine-Based topoisomerase (Top)/Histone deacetylase (HDAC) dual inhibitors

Zhu, F., Meng, X., Liang, H., Sheng, C., Dong, G., Liu, D., & Wu, S. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.105702 · Cited by 24

Comparative pharmacokinetic properties and antitumor activity of the marine HDACi Largazole and Largazole peptide isostere

Pilon, J. L., Clausen, D. J., Hansen, R. J., Lunghofer, P. J., Charles, B., Rose, B. J., Thamm, D. H., Gustafson, D. L., Bradner, J. E., & Williams, R. M. (2015) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-015-2675-1 · Cited by 24

Histone Deacetylase 8: Characterization of Physiological Divalent Metal Catalysis

Nechay, M. R., Gallup, N. M., Morgenstern, A., Smith, Q. A., Eberhart, M. E., & Alexandrova, A. N. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b00997 · Cited by 25

Selective Inhibitors of Histone Deacetylases 1 and 2 Synergize with Azacitidine in Acute Myeloid Leukemia

Min, C., Moore, N., Shearstone, J. R., Quayle, S. N., Huang, P., van Duzer, J. H., Jarpe, M. B., Jones, S. S., & Yang, M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169128 · Cited by 24

Highly fluorescent and HDAC6 selective scriptaid analogues

Fleming, C. L., Natoli, A. L., Schreuders, J., Devlin, M. G., Yoganantharajah, P., Gibert, Y., Leslie, K. G., New, E. J., Ashton, T. D., & Pfeffer, F. M. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.11.020 · Cited by 24

Current discovery strategies for hepatocellular carcinoma therapeutics

Dai, Q., Zhang, C., Yuan, Z., Sun, Q., & Jiang, Y. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1696769 · Cited by 24

Automated Structure–Activity Relationship Mining: Connecting Chemical Structure to Biological Profiles

Wawer, M. J., Jaramillo, D. E., Dančík, V., Fass, D. M., Haggarty, S. J., Shamji, A. F., Wagner, B. K., Schreiber, S. L., & Clemons, P. A. (2014) · SLAS DISCOVERY · doi:10.1177/1087057114530783 · Cited by 24

Density functional theory (DFT) studies in HDAC-based chemotherapeutics: Current findings, case studies and future perspectives

Khatun, S., Bhagat, R. P., Amin, S. A., Jha, T., & Gayen, S. (2024) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2024.108468 · Cited by 27

Romidepsin for Cutaneous T-Cell Lymphoma

Prince, H. M., Dickinson, M. J., & Khot, A. S. (2013) · Future Oncology · doi:10.2217/fon.13.220 · Cited by 23

A Review on Molecular Docking on HDAC Isoforms: Novel Tool for Designing Selective Inhibitors

Drakontaeidi, A., & Pontiki, E. A. (2023) · Pharmaceuticals · doi:10.3390/ph16121639 · Cited by 24

Romidepsin is effective and well tolerated in older patients with peripheral T-cell lymphoma: analysis of two phase II trials

Shustov, A. R., Coiffier, B., Horwitz, S. M., Sokol, L., Pro, B., Wolfson, J., Balser, B., Eisch, R. A., Popplewell, L. L., Prince, H. M., et al. (2017) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2017.1295143 · Cited by 23

A phase 1 study to assess the safety, tolerability, and pharmacokinetics of CXD101 in patients with advanced cancer

Eyre, T. A., Collins, G. P., Gupta, A., Coupe, N. A., Sheikh, S., Whittaker, J. A., Wang, L. M., Campo, L., Soilleux, E. J., Tysoe, F., et al. (2018) · Cancer · doi:10.1002/cncr.31791 · Cited by 23

Examining the stability of binding modes of the co-crystallized inhibitors of human HDAC8 by molecular dynamics simulation

Uba, A. İ., Weako, J., Keskin, Ö., Gürsoy, A., & Yelekçi, K. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1615989 · Cited by 23

A Substrate-Independent TR-FRET Histone Deacetylase Inhibitor Assay

Marks, B. D., Fakhoury, S. A., Frazee, W. J., Eliason, H. C., & Riddle, S. M. (2011) · SLAS DISCOVERY · doi:10.1177/1087057111422102 · Cited by 23

Histone Acetylation and Deacetylation

Fass, D. M., Kemp, M. M., Schroeder, F. A., Wagner, F. F., Wang, Q., & Holson, E. B. (2012) · Wiley-VCH eBooks · doi:10.1002/3527600906.mcb.201100036 · Cited by 23

Synthesis of 2-(1 H -Indol-2-yl)acetamides via Brønsted Acid-Assisted Cyclization Cascade

Aksenov, N. A., Аксенов, Д. А., Skomorokhov, A. A., Prityko, L. A., Aksenov, A. V., Грязнов, Г. Д., & Rubin, M. (2020) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.0c01344 · Cited by 22

Evidence that HDAC7 acts as an epigenetic “reader” of AR acetylation through NCoR-HDAC3 dissociation

Zhang, Y., Andrade, R. E., Hanna, A. A., & Pflum, M. K. H. (2022) · Cell chemical biology · doi:10.1016/j.chembiol.2022.05.008 · Cited by 22

5-(Trifluoromethyl)-1,2,4-oxadiazole (TFMO)-based highly selective class IIa HDAC inhibitors exhibit synergistic anticancer activity in combination with bortezomib

Asfaha, Y., Bollmann, L. M., Skerhut, A. J., Fischer, F., Horstick‐Muche, N., Roth, D., Wecker, M., Mammen, C., Smits, S. H. J., Fluegen, G., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115907 · Cited by 22

Structure-Guided DOT1L Probe Optimization by Label-Free Ligand Displacement

Yi, J. S., Alexander Joel Federation, Qi, J., Dhe‐Paganon, S., Hadler, M., Xu, X., Pierre, R. S., Varca, A. C., Wu, L., Marineau, J., et al. (2014) · ACS Chemical Biology · doi:10.1021/cb500796d · Cited by 22

Histone deacetylase inhibitors containing a benzamide functional group and a pyridyl cap are preferentially effective human immunodeficiency virus-1 latency-reversing agents in primary resting CD4+ T cells

Kobayashi, Y., Gélinas, C., & Dougherty, J. P. (2017) · Journal of General Virology · doi:10.1099/jgv.0.000716 · Cited by 22

Exploring Derivatives of Quinazoline Alkaloid l -Vasicine as Cap Groups in the Design and Biological Mechanistic Evaluation of Novel Antitumor Histone Deacetylase Inhibitors

Ahmad, M., Aga, M. A., Bhat, J. A., Kumar, B. N., Rouf, A., Capalash, N., Mintoo, M. J., Kumar, A., Mahajan, P., Mondhe, D. M., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00322 · Cited by 23

Development of Substrate‐Derived Sirtuin Inhibitors with Potential Anticancer Activity

Kuhlmann, N., Chollet, C., Baldus, L., Neundorf, I., & Lammers, M. (2017) · ChemMedChem · doi:10.1002/cmdc.201700414 · Cited by 22

A novel HDAC inhibitor with a hydroxy-pyrimidine scaffold

Kemp, M. M., Wang, Q., Fuller, J. H., West, N. H., Martínez, N. M., Morse, E. M., Weïwer, M., Schreiber, S. L., Bradner, J. E., & Koehler, A. N. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.05.098 · Cited by 23

Novel N-hydroxyfurylacrylamide-based histone deacetylase (HDAC) inhibitors with branched CAP group (Part 2)

Feng, T., Wang, H., Su, H. L., Lu, H., Yu, L., Zhang, X., Sun, H., & You, Q. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.06.009 · Cited by 22

Reprogramming of regulatory T cells in inflammatory tumor microenvironment: can it become immunotherapy turning point?

Liu, J., Zhang, B., Zhang, G., & Shang, D. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1345838 · Cited by 21

Discovery of Novel HDAC3 Inhibitors with PD-L1 Downregulating/Degrading and Antitumor Immune Effects

Sun, Z., Xu, C., Cheng, J., Yang, Z., Liu, T., Deng, B., Zhang, X., Peng, X., & Chen, J. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01062 · Cited by 21

Current Trends in the Development of Histone Deacetylase Inhibitors: A Review of Recent Patent Applications

Thaler, F. (2012) · Pharmaceutical Patent Analyst · doi:10.4155/ppa.11.3 · Cited by 21

Chemotherapy in pediatric brain tumor and the challenge of the blood–brain barrier

Reza, M. J., Podany, A. T., Κhan, P., Shaffer, C. L., Siddiqui, J. A., Baranowska‐Kortylewicz, J., Lê, J., Fletcher, C. V., Ether, S. A., & Avedissian, S. N. (2023) · Cancer Medicine · doi:10.1002/cam4.6647 · Cited by 22

Class I Histone Deacetylase-mediated Repression of the Proximal Promoter of the Activity-regulated Cytoskeleton-associated Protein Gene Regulates Its Response to Brain-derived Neurotrophic Factor

Fukuchi, M., Nakashima, F., Tabuchi, A., Shimotori, M., Tatsumi, S., Okuno, H., Bito, H., & Tsuda, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.617258 · Cited by 21

Chemogenomic analysis reveals key role for lysine acetylation in regulating Arc stability

Lalonde, J., Reis, S. A., Sivakumaran, S., Holland, C. S., Wesseling, H., Sauld, J. F. K., Alural, B., Zhao, W., Steen, J. A. J., & Haggarty, S. J. (2017) · Nature Communications · doi:10.1038/s41467-017-01750-7 · Cited by 23

Beyond Histones: New Substrate Proteins of Lysine Deacetylases in Arabidopsis Nuclei

Füßl, M., Lassowskat, I., Née, G., Koskela, M. M., Brünje, A., Tilak, P., Giese, J., Leister, D., Mulo, P., Schwarzer, D., et al. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.00461 · Cited by 21

Pharmacophore-based virtual screening for identification of potential selective inhibitors of human histone deacetylase 6

Uba, A. İ., & Yelekçi, K. (2018) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2018.10.016 · Cited by 22

Combined Ligand and Fragment‐based Drug Design of Selective Histone Deacetylase – 6 Inhibitors

Ružić, D., Petković, M., Agbaba, D. D., Ganesan, A., & Nikolic, K. M. (2019) · Molecular Informatics · doi:10.1002/minf.201800083 · Cited by 21

Combating the Epigenome: Epigenetic Drugs Against Non-Hodgkin‘S Lymphoma

Hassler, M. R., Schiefer, A., & Egger, G. (2013) · Epigenomics · doi:10.2217/epi.13.39 · Cited by 24

Histone deacetylase knockouts modify transcription, CAG instability and nuclear pathology in Huntington disease mice

Kovalenko, M. V., Erdin, S., Andrew, M. A., Claire, J. S., Shaughnessey, M., Hubert, L., Neto, J. L., Stortchevoi, A., Fass, D. M., Pinto, R. M., et al. (2020) · eLife · doi:10.7554/elife.55911 · Cited by 22

Clinically significant responses achieved with romidepsin across disease compartments in patients with cutaneous T-cell lymphoma

Kim, E. J., Kim, Y. H., Rook, A. H., Lerner, A., Duvic, M. A., Reddy, S. A., Robak, T., Becker, J. C., Samtsov, A. V., McCulloch, W. F., et al. (2015) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2015.1014360 · Cited by 20

In vitro cytotoxicity evaluation of HDAC inhibitor Apicidin in pancreatic carcinoma cells subsequent time and dose dependent treatment

Bauden, M. P., Tassidis, H., & Ansari, D. (2015) · Toxicology Letters · doi:10.1016/j.toxlet.2015.03.017 · Cited by 20

Methyl Effect in Azumamides Provides Insight Into Histone Deacetylase Inhibition by Macrocycles

Maolanon, A. R., Villadsen, J. S., Christensen, N. J., Hoeck, C. R., Friis, T., Harris, P., Gotfredsen, C. H., Fristrup, P., & Olsen, C. A. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501399d · Cited by 20

Clinical Efficacy of Romidepsin in Tumor Stage and Folliculotropic Mycosis Fungoides

Foss, F. M., Duvic, M. A., Lerner, A., Waksman, J. A., & Whittaker, S. J. (2016) · Clinical Lymphoma Myeloma & Leukemia · doi:10.1016/j.clml.2016.08.009 · Cited by 20

Chemical optogenetic modulation of inflammation and immunity

Parasar, B., & Chang, P. V. (2016) · Chemical Science · doi:10.1039/c6sc03702j · Cited by 20

Characterization of Histone Deacetylase Expression Within In Vitro and In Vivo Bladder Cancer Model Systems

Buckwalter, J. M., Chan, W. H.-C., Shuman, L., Wildermuth, T., Ellis-Mohl, J., Walter, V., Warrick, J. I., Wu, X., Kaag, M. G., Raman, J. D., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102599 · Cited by 20

Profiling of Substrates for Zinc‐dependent Lysine Deacylase Enzymes: HDAC3 Exhibits Decrotonylase Activity In Vitro

Madsen, A. S., & Olsen, C. A. (2012) · Angewandte Chemie · doi:10.1002/ange.201203754 · Cited by 20

Synthesis of hybrid anticancer agents based on kinase and histone deacetylase inhibitors

Patel, H. B., Chuckowree, I., Coxhead, P., Guille, M., Wang, M., Zuckermann, A. M. E., Williams, R. S. B., Librizzi, M., Paranal, R. M., Bradner, J. E., et al. (2014) · MedChemComm · doi:10.1039/c4md00211c · Cited by 20

Small-molecule control of cytokine function: new opportunities for treating immune disorders

Sundberg, T. B., Xavier, R. J., Schreiber, S. L., & Shamji, A. F. (2014) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2014.08.013 · Cited by 21

Missense substitutions at a conserved 14-3-3 binding site in HDAC4 cause a novel intellectual disability syndrome

Wakeling, E. L., McEntagart, M., Bruccoleri, M., Shaw-Smith, C. J., Stals, K. L., Wakeling, M. N., Barnicoat, A. J., Beesley, C. E., Hanson‐Kahn, A., Kukolich, M. K., et al. (2020) · Human Genetics and Genomics Advances · doi:10.1016/j.xhgg.2020.100015 · Cited by 19

Epigenetic Regulation of Fibroblasts and Crosstalk between Cardiomyocytes and Non-Myocyte Cells in Cardiac Fibrosis

Chu, L., Xie, D., & Xu, D. (2023) · Biomolecules · doi:10.3390/biom13091382 · Cited by 19

Rationale for Possible Targeting of Histone Deacetylase Signaling in Cancer Diseases with a Special Reference to Pancreatic Cancer

Ouaïssi, M., Giger-Pabst, U., Sielezneff, I., Pirró, N., Sastre, B., & Ouaissi, A. (2010) · BioMed Research International · doi:10.1155/2011/315939 · Cited by 19

An azumamide C analogue without the zinc-binding functionality

Villadsen, J. S., Kitir, B., Wich, K., Friis, T., Madsen, A. S., & Olsen, C. A. (2014) · MedChemComm · doi:10.1039/c4md00252k · Cited by 19

Manipulation of the host protein acetylation network by human immunodeficiency virus type 1.

Jeng, M. Y., Ali, I., & Ott, M. (2015) · PubMed · doi:10.3109/10409238.2015.1061973 · Cited by 19

Subcellular Localization of Class I Histone Deacetylases in the Developing Xenopus tectum

Guo, X., Ruan, H., Li, X., Qin, L., Tao, Y., Qi, X., Gao, J., Gan, L., Duan, S., & Shen, W. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00510 · Cited by 21

Incorporation of histone deacetylase inhibitory activity into the core of tamoxifen – A new hybrid design paradigm

Palermo, A. F., Diennet, M., Ezzy, M. E., Williams, B. M., Cotnoir‐White, D., Mader, S., & Gleason, J. L. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.07.026 · Cited by 19

tert‐Butylcarbamate‐Containing Histone Deacetylase Inhibitors: Apoptosis Induction, Cytodifferentiation, and Antiproliferative Activities in Cancer Cells

Valente, S., Trisciuoglio, D., Tardugno, M., Benedetti, R., Labella, D., Secci, D., Mercurio, C., Boggio, R., Tomassi, S., Maro, S. D., et al. (2013) · ChemMedChem · doi:10.1002/cmdc.201300005 · Cited by 19

Screening of novel histone deacetylase 7 inhibitors through molecular docking followed by a combination of molecular dynamics simulations and ligand-based approach

Yuan, Y., Hu, Z., Bao, M., Sun, R., Long, X., Li, L., Li, J., Wu, C., & Bao, J. (2018) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1541141 · Cited by 18

Histone deacetylase 4 deletion broadly affects cardiac epigenetic repression and regulates transcriptional susceptibility via H3K9 methylation

Finke, D., Schanze, L. M., Schreiter, F. C., Kreußer, M. M., Katus, H. A., Backs, J., & Lehmann, L. (2021) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2021.09.001 · Cited by 18

Binding Free Energy (BFE) Calculations and Quantitative Structure–Activity Relationship (QSAR) Analysis of Schistosoma mansoni Histone Deacetylase 8 (smHDAC8) Inhibitors

Simoben, C. V., Ghazy, E., Zeyen, P., Darwish, S., Schmidt, M., Romier, C., Robaa, D., & Sippl, W. (2021) · Molecules · doi:10.3390/molecules26092584 · Cited by 17

Vorinostat-Like Molecules as Structural, Stereochemical, and Pharmacological Tools

Hanessian, S., Auzzas, L., Larsson, A., Zhang, J., Giannini, G., Gallo, G., Ciacci, A., & Cabri, W. (2010) · ACS Medicinal Chemistry Letters · doi:10.1021/ml100028g · Cited by 18

Ischemic preconditioning, retinal neuroprotection and histone deacetylase activities

Fan, J., Alsarraf, O., Chou, C. J., Yates, P. W., Goodwin, N. C., Rice, D. S., & Crosson, C. E. (2016) · Experimental Eye Research · doi:10.1016/j.exer.2016.03.026 · Cited by 18

Tumor immunotherapy—the potential of epigenetic drugs to overcome resistance

Grunewald, C. M., Schulz, W. A., Skowron, M. A., Hoffmann, M. J., & Niegisch, G. (2018) · Translational Cancer Research · doi:10.21037/tcr.2018.06.24 · Cited by 18

Antitumor activity of novel POLA1-HDAC11 dual inhibitors

Dallavalle, S., Musso, L., Cincinelli, R., Darwiche, N., Gervasoni, S. I., Vistoli, G., Guglielmi, M. B., Porta, I. L., Pizzulo, M., Modica, E., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113971 · Cited by 17

Optimization of Resveratrol Used as a Scaffold to Design Histone Deacetylase (HDAC-1 and HDAC-2) Inhibitors

Urias, B. S., Pavan, A. R., Albuquerque, G. R., Prokopczyk, I. M., Alves, T. M. F., de Melo, T. R. F., Sartori, G., da Silva, J. H. M., Chin, C. M., & dos Santos, J. L. (2022) · Pharmaceuticals · doi:10.3390/ph15101260 · Cited by 18

Substrates and Cyclic Peptide Inhibitors of the Oligonucleotide‐Activated Sirtuin 7**

Bolding, J. E., Nielsen, A. L., Jensen, I., Hansen, T. N., Ryberg, L. A., Jameson, S. T., Harris, P., Peters, G. H. J., Denu, J. M., Rogers, J. M., et al. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202314597 · Cited by 17

Development of second generation epigenetic agents

JONES, P. G. (2011) · MedChemComm · doi:10.1039/c1md00199j · Cited by 17

An NAD + -Dependent Sirtuin Depropionylase and Deacetylase (Sir2La) from the Probiotic Bacterium Lactobacillus acidophilus NCFM

Olesen, S. V., Rajabi, N., Svensson, B., Olsen, C. A., & Madsen, A. S. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00306 · Cited by 16

Beyond regulations at DNA levels: A review of epigenetic therapeutics targeting cancer stem cells

Zhang, S., Gong, Y., Li, C., Yang, W., & Li, L. (2020) · Cell Proliferation · doi:10.1111/cpr.12963 · Cited by 18

Species-selective targeting of pathogens revealed by the atypical structure and active site of Trypanosoma cruzi histone deacetylase DAC2

Marek, M., Ramos‐Morales, E., Picchi, G. F. A., Bayer, T., Norström, C., Herp, D., Sales-Junior, P. A., Guerra-Slompo, E. P., Hausmann, K., Chakrabarti, A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110129 · Cited by 18

Alkylating agents induce histone H3K18 hyperacetylation and potentiate HDAC inhibitor-mediated global histone acetylation and cytotoxicity in mantle cell lymphoma

Hiraoka, N., Kikuchi, J., Koyama, D., Wada, T., Mori, S., Nakamura, Y., & Furukawa, Y. (2013) · Blood Cancer Journal · doi:10.1038/bcj.2013.66 · Cited by 17

Utility of18fluoro-deoxyglucose positron emission tomography for prognosis and response assessments in a phase 2 study of romidepsin in patients with relapsed or refractory peripheral T-cell lymphoma

Horwitz, S. M., Coiffier, B., Foss, F. M., Prince, H. M., Sokol, L., Greenwood, M. J., Caballero, D. M., Morschhauser, F., Pinter‐Brown, L. C., Iyer, S. P., et al. (2015) · Annals of Oncology · doi:10.1093/annonc/mdv010 · Cited by 17

Screening and profiling assays for HDACs and sirtuins

Howitz, K. T. (2015) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2015.10.008 · Cited by 17

HDAC1 Is a Required Cofactor of CBFβ-SMMHC and a Potential Therapeutic Target in Inversion 16 Acute Myeloid Leukemia

Richter, L. E., Wang, Y., Becker, M. E., Coburn, R. A., Williams, J. T., Amador, C. C., & Hyde, R. K. (2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-18-0922 · Cited by 16

Discovery of novel class of histone deacetylase inhibitors as potential anticancer agents

El‐Awady, R., Saleh, E., Hamoudi, R., Ramadan, W. S. H., Mazitschek, R., Nael, M. A., Elokely, K. M., Abou-Gharbia, M. A., Childers, W. E., Srinivasulu, V., et al. (2021) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2021.116251 · Cited by 17

Heterocycles–Containing HDAC Inhibitors Active in Cancer: An Overview of the Last Fifteen Years

Raucci, A., Castiello, C., Mai, A., Zwergel, C., & Valente, S. (2024) · ChemMedChem · doi:10.1002/cmdc.202400194 · Cited by 17

Structure–Function Analysis of the Conserved Tyrosine and Diverse π-Stacking among Class I Histone Deacetylases: A QM (DFT)/MM MD Study

Zhou, J., Xie, H., Liu, Z., Luo, H., & Wu, R. (2014) · Journal of Chemical Information and Modeling · doi:10.1021/ci500513n · Cited by 16

Induction of differential apoptotic pathways in multiple myeloma cells by class-selective histone deacetylase inhibitors

Hideshima, T., Mazitschek, R., Santo, L., Mimura, N., Görgün, G., Richardson, P. G. G., Raje, N. S., & Anderson, K. C. (2013) · Leukemia · doi:10.1038/leu.2013.301 · Cited by 16

In‐Bead Screening of Hydroxamic Acids for the Identification of HDAC Inhibitors

Qvortrup, K. M., & Nielsen, T. E. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201511308 · Cited by 16

The Multiple Myeloma Landscape: Epigenetics and Non-Coding RNAs

Coira, I. F., Rincón, R., & Cuendet, M. (2022) · Cancers · doi:10.3390/cancers14102348 · Cited by 16

Inhibition mechanism of SAHA in HDAC: a revisit

Zhou, J., Wu, R., & Luo, H. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp05633k · Cited by 16

Targeting Epigenetics through Histone Deacetylase Inhibitors in Acute Lymphoblastic Leukemia

Mummery, A., Narendran, A., & Lee, K.-Y. (2011) · Current Cancer Drug Targets · doi:10.2174/156800911796798922 · Cited by 16

Synthesis and biological evaluation of aminobenzamides containing purine moiety as class I histone deacetylases inhibitors

Mao, P., He, W., Mai, X., Feng, L.-H., Li, N., Liao, Y.-J., Zhu, C., Li, J., Chen, T., Liu, S.-H., et al. (2021) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2021.116599 · Cited by 9

Molecular mechanisms of bifunctional vitamin D receptor agonist-histone deacetylase inhibitor hybrid molecules in triple-negative breast cancer

Barbier, C., Mansour, A., Ismailova, A., Sarmadi, F., Scarlata, D. A., Bouttier, M., Zeitouni, C., Wang, C. K., Gleason, J. L., & White, J. H. (2022) · Scientific Reports · doi:10.1038/s41598-022-10740-9 · Cited by 15

Rationale for HDAC Inhibitor Therapy in Autoimmunity and Transplantation

Hancock, W. W. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_6 · Cited by 15

FDG-PET imaging reveals local brain glucose utilization is altered by class I histone deacetylase inhibitors

Schroeder, F. A., Chonde, D. B., Riley, M. M., Moseley, C. K., Granda, M. L., Wilson, C. M., Wagner, F. F., Zhang, Y., Gale, J. P., Holson, E. B., et al. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.06.016 · Cited by 14

HR23b expression is a potential predictive biomarker for HDAC inhibitor treatment in mesenchymal tumours and is associated with response to vorinostat

Ihle, M. A., Merkelbach‐Bruse, S., Hartmann, W., Bauer, S., Ratner, N., Sonobe, H., Nishio, J., Larsson, O., Åman, P., Pédeutour, F., et al. (2015) · The Journal of Pathology Clinical Research · doi:10.1002/cjp2.35 · Cited by 15

Thermodynamics of Binding of Structurally Similar Ligands to Histone Deacetylase 8 Sheds Light on Challenges in the Rational Design of Potent and Isozyme-Selective Inhibitors of the Enzyme

Singh, P., Suzuki, T., Mandal, T., Balsubramanian, N., Haldar, M., Mueller, D. J., Strode, J. A., Cook, G. R., Mallik, S., & Srivastava, D. K. (2014) · Biochemistry · doi:10.1021/bi500711x · Cited by 16

PI3K/ NF-κB-dependent TNF-α and HDAC activities facilitate LPS-induced RGS10 suppression in pulmonary macrophages

Almutairi, F., Tucker, S. L., Sarr, D., & Rada, B. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110099 · Cited by 15

High-throughput screening of histone deacetylases and determination of kinetic parameters using fluorogenic assays

Moreno–Yruela, C., & Olsen, C. A. (2021) · STAR Protocols · doi:10.1016/j.xpro.2021.100313 · Cited by 15

Continuous Fluorescent Sirtuin Activity Assay Based on Fatty Acylated Lysines

Zessin, M., Meleshin, M., Hilscher, S., Schiene‐Fischer, C., Bařinka, C., Jung, M., & Schutkowski, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087416 · Cited by 14

Characterizing binding intensity and energetic features of histone deacetylase inhibitor pracinostat towards class I HDAC isozymes through futuristic drug designing strategy

Ganai, S. A. (2021) · In Silico Pharmacology · doi:10.1007/s40203-021-00077-y · Cited by 14

Effects of histone deacetylase inhibitor Scriptaid and parathyroid hormone on osteocyte functions and metabolism

Sun, N., Uda, Y., Azab, E., Kochen, A., Santos, R. N. C. E., Shi, C., Kobayashi, T., Wein, M. N., & Pajevic, P. D. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007312 · Cited by 14

Targeting epigenetic mediators of gene expression in thoracic malignancies

Schrump, D. S. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.03.009 · Cited by 14

Proteolysis-Targeting Chimeras (PROTACs) Based on Macrocyclic Tetrapeptides Selectively Degrade Class I Histone Deacetylases 1–3Preprint

Roatsch, M., Vogelmann, A., Herp, D., Jung, M., & Olsen, C. A. (2020) · ChemRxiv · doi:10.26434/chemrxiv.12416303.v1 · Cited by 14

HDAC in obesity: A critical insight

Nijhawan, P., Behl, T., Khullar, G., Pal, G., Kandhwal, M., & Goyal, A. (2020) · Obesity Medicine · doi:10.1016/j.obmed.2020.100212 · Cited by 13

Lactylation in Cardiovascular Diseases: Current Progress and Perspectives

Wang, Z., Yu, Q., Wang, C., Wang, S., Wang, P., Zhang, L., & Han, S. (2025) · Journal of the American Heart Association · doi:10.1161/jaha.125.043801 · Cited by 13

Targeting histone deacetylases for heart diseases

Jin, G. Y., Wang, K., Zhao, Y., Yuan, S., He, Z., & Zhang, J. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.106601 · Cited by 16

HDAC10 inhibition represses melanoma cell growth and BRAF inhibitor resistance via upregulating SPARC expression

Ling, H., Li, Y., Peng, C., Yang, S., & Seto, E. (2024) · NAR Cancer · doi:10.1093/narcan/zcae018 · Cited by 13

Topical histone deacetylase inhibitor remetinostat improves IMQ-induced psoriatic dermatitis via suppressing dendritic cell maturation and keratinocyte differentiation and inflammation

Jin, L., Jiang, Q., Huang, H., & Zhou, X. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.177011 · Cited by 13

The Biological Significance of Targeting Acetylation-Mediated Gene Regulation for Designing New Mechanistic Tools and Potential Therapeutics

O’Garro, C., Igbineweka, L., Ali, Z., Mezei, M., & Mujtaba, S. (2021) · Biomolecules · doi:10.3390/biom11030455 · Cited by 13

Peptide Microarray-Based Protein Interaction Studies Across Affinity Ranges: Enzyme Stalling, Cross-Linking, Depletion, and Neutralization

Schulte, C., Khayenko, V., & Maric, H. M. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2732-7_10 · Cited by 13

Novel Class IIa-Selective Histone Deacetylase Inhibitors Discovered Using an in Silico Virtual Screening Approach

Hsu, K., Liu, C., Lin, T. E., Hsieh, J.-H., Sung, T.-Y., Tseng, H.-J., Yang, J., & Huang, W. (2017) · Scientific Reports · doi:10.1038/s41598-017-03417-1 · Cited by 54

Isoform-selective histone deacetylase inhibitors

Bieliauskas, A. V., & Pflum, M. K. H. (2008) · Chemical Society Reviews · doi:10.1039/b703830p · Cited by 350

Structure-Based Inhibitor Discovery of Class I Histone Deacetylases (HDACs)

Luo, Y., & Li, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228828 · Cited by 62

Exploration of the binding pocket of histone deacetylases: the design of potent and isoform-selective inhibitors

Uba, A. İ., & Yelekçi, K. (2017) · TURKISH JOURNAL OF BIOLOGY · doi:10.3906/biy-1701-26 · Cited by 20

Explorative Study on Isoform-Selective Histone Deacetylase Inhibitors

Suzuki, T. (2009) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.57.897 · Cited by 57