An Isochemogenic set of inhibitors to define the therapeutic potential of histone deacetylases in β-cell protection

β-Cell Deficit and Increased β-Cell Apoptosis in Humans With Type 2 Diabetes

Butler, A. E., Janson, J., Bonner-Weir, S., Ritzel, R., Rizza, R. A., & Butler, P. C. (2003) · Diabetes · doi:10.2337/diabetes.52.1.102 · Cited by 4,011 · see citing works

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 2,211 · see citing works

Glucose-induced β cell production of IL-1β contributes to glucotoxicity in human pancreatic islets

Maedler, K., Sergeev, P., Ris, F., Oberholzer, J., Joller‐Jemelka, H. I., Spinas, G. A., Kaiser, N., Halban, P. A., & Donath, M. Y. (2002) · Journal of Clinical Investigation · doi:10.1172/jci200215318 · Cited by 1,006 · see citing works

Bayesian statistical analysis of protein side‐chain rotamer preferences

Dunbrack, R. L., & Cohen, F. E. (1997) · Protein Science · doi:10.1002/pro.5560060807 · Cited by 776 · see citing works

Application of multiple sequence alignment profiles to improve protein secondary structure prediction

Cuff, J. A., & Barton, G. J. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20000815)40:3 · Cited by 768 · see citing works

Initiation and execution of lipotoxic ER stress in pancreatic β-cells

Cunha, D. A., Hekerman, P., Ladrière, L., Bazarra-Castro, A., Ortis, F., Wakeham, M. C., Moore, F., Rasschaert, J., Cardozo, A. K., Bellomo, E. A., et al. (2008) · Journal of Cell Science · doi:10.1242/jcs.026062 · Cited by 593 · see citing works

Oxidative stress: the vulnerable β-cell

Lenzen, S. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360343 · Cited by 535 · see citing works

HDAC inhibitors in cancer biology: emerging mechanisms and clinical applications

Khan, O., & La Thangue, N. B. (2012) · Immunology & Cell Biology · doi:10.1038/icb.2011.100 · Cited by 450 · see citing works

Histone Deacetylase (HDAC) Inhibitor Kinetic Rate Constants Correlate with Cellular Histone Acetylation but Not Transcription and Cell Viability

Lauffer, B. E. L., Mintzer, R., Fong, R., Mukund, S., Tam, C., Zilberleyb, I., Flicke, B., Ritscher, A., Fedorowicz, G., Vallero, R., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.490706 · Cited by 429 · see citing works

HDAC3-selective inhibitor enhances extinction of cocaine-seeking behavior in a persistent manner

Malvaez, M., McQuown, S. C., Rogge, G. A., Astarabadi, M., Jacques, V., Carreiro, S. T., Rusche, J. R., & Wood, M. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1213364110 · Cited by 400 · see citing works

Clinical Toxicities of Histone Deacetylase Inhibitors

Subramanian, S., Bates, S. E., Wright, J. J., Espinoza-Delgado, I., & Piekarz, R. L. (2010) · Pharmaceuticals · doi:10.3390/ph3092751 · Cited by 386 · see citing works

Direct detection of CH/π interactions in proteins

Plevin, M. J., Bryce, D. L., & Boisbouvier, J. (2010) · Nature Chemistry · doi:10.1038/nchem.650 · Cited by 288 · see citing works

Exploration of the HDAC2 foot pocket: Synthesis and SAR of substituted N-(2-aminophenyl)benzamides

Bressi, J. C., Jennings, A. J., Skene, R., Wu, Y., Melkus, R., Jong, R. D., O’Connell, S., Grimshaw, C. E., Navre, M., & Gangloff, A. R. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.03.091 · Cited by 261 · see citing works

Targeting the pancreatic β-cell to treat diabetes

Vetere, A., Choudhary, A., Burns, S. M., & Wagner, B. K. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4231 · Cited by 253 · see citing works

Chemical Genetics: Where Genetics and Pharmacology Meet

Knight, Z. A., & Shokat, K. M. (2007) · Cell · doi:10.1016/j.cell.2007.01.021 · Cited by 244 · see citing works

Cancer biology: mechanism of antitumour action of vorinostat (suberoylanilide hydroxamic acid), a novel histone deacetylase inhibitor

Richon, V. M. (2006) · British Journal of Cancer · doi:10.1038/sj.bjc.6603463 · Cited by 240 · see citing works

Overlapping functions of Hdac1 and Hdac2 in cell cycle regulation and haematopoiesis

Wilting, R. H., Yanover, E., Heideman, M. R., Jacobs, H., Horner, J. W., van der Torre, J., DePinho, R. A., & Dannenberg, J. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.136 · Cited by 229 · see citing works

Pimelic Diphenylamide 106 Is a Slow, Tight-binding Inhibitor of Class I Histone Deacetylases

Chou, C. J., Herman, D., & Gottesfeld, J. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807045200 · Cited by 223 · see citing works

Aliphatic C−H/π Interactions: Methane−Benzene, Methane−Phenol, and Methane−Indole Complexes

McDonald, A. R., Figgs, M. S., Sinnokrot, M. O., et al. (2006) · The Journal of Physical Chemistry A · doi:10.1021/jp062740l · Cited by 195 · see citing works

Exploration of the internal cavity of histone deacetylase (HDAC) with selective HDAC1/HDAC2 inhibitors (SHI-1:2)

Methot, J. L., Chakravarty, P. K., Chenard, M., Close, J., Cruz, J. C., Dahlberg, W. K., Fleming, J., Hamblett, C. L., Hamill, J. E., Harrington, P., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.12.031 · Cited by 191 · see citing works

Novel Aminophenyl Benzamide-Type Histone Deacetylase Inhibitors with Enhanced Potency and Selectivity

Moradei, O. M., Mallais, T. C., Frechette, S., Paquin, I., Tessier, P. E., Leit, S. M., Fournel, M., Bonfils, C., Trachy-Bourget, M.-C., Liu, J., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm701079h · Cited by 166 · see citing works

HDAC inhibitors in parasitic diseases

Andrews, K. T., Haque, A., & Jones, M. K. (2011) · Immunology and Cell Biology · doi:10.1038/icb.2011.97 · Cited by 165 · see citing works

Two New Pimelic Diphenylamide HDAC Inhibitors Induce Sustained Frataxin Upregulation in Cells from Friedreich's Ataxia Patients and in a Mouse Model

Rai, M., Soragni, E., Chou, C. J., Barnes, G., Jones, S. E., Rusche, J. R., Gottesfeld, J. M., & Pandolfo, M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008825 · Cited by 148 · see citing works

Translating slow-binding inhibition kinetics into cellular and in vivo effects

Walkup, G. K., You, Z., Ross, P. L., Allen, E. K. H., Daryaee, F., Hale, M. R., O’Donnell, J. C., Ehmann, D. E., Schuck, V., Buurman, E. T., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1796 · Cited by 145 · see citing works

Deciphering the molecular and biologic processes that mediate histone deacetylase inhibitor–induced thrombocytopenia

Bishton, M. J., Harrison, S. J., Martin, B. P., McLaughlin, N. M., James, C., Josefsson, E. C., Henley, K. J., Kile, B. T., Prince, H. M., & Johnstone, R. W. (2011) · Blood · doi:10.1182/blood-2010-11-318055 · Cited by 141 · see citing works

Chronic Oral Administration of CI-994: A Phase I Study

Prakash, S., Foster, B. J., Meyer, M., Wozniak, A., Heilbrun, L. K., Flaherty, L. E., Zalupski, M. M., Radulovic, L. L., Valdivieso, M., & LoRusso, P. M. (2001) · Investigational New Drugs · doi:10.1023/a:1006489328324 · Cited by 136 · see citing works

Death Protein 5 and p53-Upregulated Modulator of Apoptosis Mediate the Endoplasmic Reticulum Stress–Mitochondrial Dialog Triggering Lipotoxic Rodent and Human β-Cell Apoptosis

Cunha, D. A., Igoillo-Esteve, M., Gurzov, E. N., Germano, C. M., Naamane, N., Marhfour, I., Fukaya, M., Vanderwinden, J.-M., Gysemans, C., Mathieu, C., et al. (2012) · Diabetes · doi:10.2337/db12-0123 · Cited by 130 · see citing works

The dynameomics rotamer library: Amino acid side chain conformations and dynamics from comprehensive molecular dynamics simulations in water

Scouras, A. D., & Daggett, V. (2010) · Protein Science · doi:10.1002/pro.565 · Cited by 117 · see citing works

Signal-dependent repression of DUSP5 by class I HDACs controls nuclear ERK activity and cardiomyocyte hypertrophy

Ferguson, B. S., Harrison, B. C., Jeong, M. Y., Reid, B. G., Wempe, M. F., Wagner, F. F., Holson, E. B., & McKinsey, T. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301509110 · Cited by 108 · see citing works

Kinetically selective inhibitors of histone deacetylase 2 (HDAC2) as cognition enhancers

Wagner, F. F., Zhang, Y.-L., Fass, D. M., Joseph, N., Gale, J. P., Weïwer, M., McCarren, P., Fisher, S. L., Kaya, T., Zhao, W.-N., et al. (2015) · Chemical Science · doi:10.1039/c4sc02130d · Cited by 104 · see citing works

Glucose-induced beta cell dysfunction in vivo in rats: link between oxidative stress and endoplasmic reticulum stress

Tang, C., Koulajian, K., Schuiki, I., Zhang, L., Desai, T. S., Ivovic, A., Wang, P. T., Doucette, C. A., Wheeler, M. B., Minassian, B. A., et al. (2012) · Diabetologia · doi:10.1007/s00125-012-2474-8 · Cited by 103 · see citing works

Histone deacetylase 3 inhibition improves glycaemia and insulin secretion in obese diabetic rats

Lundh, M., Galbo, T., Poulsen, S. S., & Mandrup-Poulsen, T. R. (2015) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12470 · Cited by 101 · see citing works

Small Molecule Inhibitors of Zinc-dependent Histone Deacetylases

Wagner, F. F., Weïwer, M., Lewis, M. C., & Holson, E. B. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0226-1 · Cited by 99 · see citing works

Inhibition of Histone Deacetylase 3 Protects Beta Cells from Cytokine-Induced Apoptosis

Chou, D. H., Holson, E. B., Wagner, F. F., Tang, A. J., Maglathlin, R. L., Lewis, T. A., Schreiber, S. L., & Wagner, B. K. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.05.010 · Cited by 95 · see citing works

Histone deacetylases 1 and 3 but not 2 mediate cytokine-induced beta cell apoptosis in INS-1 cells and dispersed primary islets from rats and are differentially regulated in the islets of type 1 diabetic children

Lundh, M., Christensen, D. P., Nielsen, M. D., Richardson, S. J., Dahllöf, M. S., Skovgaard, T., Berthelsen, J., Dinarello, C. A., Stevenazzi, A., Mascagni, P., et al. (2012) · Diabetologia · doi:10.1007/s00125-012-2615-0 · Cited by 90 · see citing works

Epigenetics and Psychiatry

Mahgoub, M., & Monteggia, L. M. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0213-6 · Cited by 84 · see citing works

A novel histone deacetylase inhibitor Chidamide induces apoptosis of human colon cancer cells

Liu, L., Chen, B., Qin, S., Li, S., He, X., Qiu, S., Zhao, W., & Zhao, H. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.01.011 · Cited by 78 · see citing works

Selective HDAC Inhibition for the Disruption of Latent HIV-1 Infection

Barton, K. M., Archin, N. M., Keedy, K. S., Espeseth, A. S., Zhang, Y.-L., Gale, J., Wagner, F. F., Holson, E. B., & Margolis, D. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102684 · Cited by 76 · see citing works

Image-Guided Synthesis Reveals Potent Blood-Brain Barrier Permeable Histone Deacetylase Inhibitors

Seo, Y. J., Kang, Y., Muench, L., Reid, A. E., Caesar, S., Jean, L., Wagner, F. F., Holson, E. B., Haggarty, S. J., Weiss, P., et al. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500021p · Cited by 63 · see citing works

Toxicological and metabolic considerations for histone deacetylase inhibitors

Fraczek, J., Vanhaecke, T., & Rogiers, V. (2013) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.2013.754011 · Cited by 58 · see citing works

Quantitation and characterization of human megakaryocyte colony‐forming cells using a standardized serum‐free agarose assay

Hogge, D. E., Fanning, S. F., Bockhold, K., et al. (1997) · British Journal of Haematology · doi:10.1046/j.1365-2141.1997.d01-2092.x · Cited by 57 · see citing works

Studies of Benzamide‐ and Thiol‐Based Histone Deacetylase Inhibitors in Models of Oxidative‐Stress‐Induced Neuronal Death: Identification of Some HDAC3‐Selective Inhibitors

Chen, Y., He, R., Chen, Y., D'Annibale, M. A., Langley, B., & Kozikowski, A. P. (2009) · ChemMedChem · doi:10.1002/cmdc.200800461 · Cited by 51 · see citing works

Non-Cancer Uses of Histone Deacetylase Inhibitors: Effects on Infectious Diseases and β-Hemoglobinopathies+

Rotili, D., Simonetti, G., Savarino, A., et al. (2009) · Current Topics in Medicinal Chemistry · doi:10.2174/156802609788085296 · Cited by 47 · see citing works

Delayed and Prolonged Histone Hyperacetylation with a Selective HDAC1/HDAC2 Inhibitor

Methot, J. L., Hoffman, D. M., Witter, D. J., Stanton, M. G., Harrington, P., Hamblett, C. L., Siliphaivanh, P., Wilson, K. J., Hubbs, J. L., Heidebrecht, R. W., et al. (2014) · ACS Medicinal Chemistry Letters · doi:10.1021/ml4004233 · Cited by 35 · see citing works

Application of human CFU-Mk assay to predict potential thrombocytotoxicity of drugs

Pessina, A., Parent‐Massin, D., Albella, B., et al. (2008) · Toxicology in Vitro · doi:10.1016/j.tiv.2008.11.006 · Cited by 29 · see citing works

Divergent Kinetics Differentiate the Mechanism of Action of Two HDAC Inhibitors

Kral, A. M., Ozerova, N. D. S., Close, J., Jung, J. O., Chénard, M., Fleming, J. C., Haines, B. B., Harrington, P., Maclean, J. K. F., Miller, T. A., et al. (2014) · Biochemistry · doi:10.1021/bi400936h · Cited by 21 · see citing works

CFU‐MK Assay for Acute Thrombocytopenia

Parent‐Massin, D., & Sibiril, Y. (2008) · Current Protocols in Toxicology · doi:10.1002/0471140856.tx2005s37 · Cited by 4 · see citing works

In vitro and in vivo effects of acetyldinaline on murine megakaryocytopoiesis

Volpe, D. A., LoRusso, P. M., Foster, B. J., et al. (2004) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-004-0783-4 · Cited by 3 · see citing works

Targeting innate immune mediators in type 1 and type 2 diabetes

Donath, M. Y., Dinarello, C. A., & Mandrup-Poulsen, T. (2019) · Nature Reviews Immunology · doi:10.1038/s41577-019-0213-9 · Cited by 416 · see citing works

<i>CREBBP</i> Inactivation Promotes the Development of HDAC3-Dependent Lymphomas

Jiang, Y., Ortega-Molina, A., Geng, H., Ying, H.-Y., Hatzi, K., Parsa, S., McNally, D., Wang, L., Doane, A. S., Agirre, X., et al. (2017) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0975 · Cited by 278 · see citing works

Targeting histone deacetylases for cancer therapy: Trends and challenges

Liang, T., Wang, F., Elhassan, R. M., Cheng, Y., Tang, X., Chen, W., Fang, H., & Hou, X. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.02.007 · Cited by 222 · see citing works

Selective inhibition of HDAC3 targets synthetic vulnerabilities and activates immune surveillance in lymphoma

Mondello, P., Tadros, S., Teater, M., Fontan, L., Chang, A. Y., Jain, N., Yang, H., Singh, S., Ying, H.-Y., Chu, C.-S., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-0116 · Cited by 167 · see citing works

Histone deacetylase 3 (HDAC3) inhibitors as anticancer agents: A review

Sarkar, R., Banerjee, S., Amin, S. A., Adhikari, N., & Jha, T. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112171 · Cited by 121 · see citing works

The Process and Strategy for Developing Selective Histone Deacetylase 3 Inhibitors

Cao, F., Zwinderman, M., & Dekker, F. (2018) · Molecules · doi:10.3390/molecules23030551 · Cited by 66 · see citing works

Dissecting Histone Deacetylase 3 in Multiple Disease Conditions: Selective Inhibition as a Promising Therapeutic Strategy

Adhikari, N., Jha, T., & Ghosh, B. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01676 · Cited by 74 · see citing works

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 · see citing works

HDACs and the epigenetic plasticity of cancer cells: target the complexity

Brancolini, C., Gagliano, T., & Minisini, M. (2022) · Pharmacology &amp; Therapeutics · doi:10.1016/j.pharmthera.2022.108190 · Cited by 55 · see citing works

Synthesis, Molecular Docking and Biological Characterization of Pyrazine Linked 2-Aminobenzamides as New Class I Selective Histone Deacetylase (HDAC) Inhibitors with Anti-Leukemic Activity

Ibrahim, H. S., Abdelsalam, M., Zeyn, Y., Zessin, M., Mustafa, A.-H. M., Fischer, M. A., Zeyen, P., Sun, P., Bülbül, E. F., Vecchio, A., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010369 · Cited by 50 · see citing works

Class I Histone Deacetylase Inhibition by Tianeptinaline Modulates Neuroplasticity and Enhances Memory

Zhao, W.-N., Ghosh, B., Tyler, M., Lalonde, J., Joseph, N. F., Kosaric, N., Fass, D. M., Tsai, L.-H., Mazitschek, R., & Haggarty, S. J. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00116 · Cited by 35 · see citing works

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 · see citing works

The discovery of novel HDAC3 inhibitors via virtual screening and <i>in vitro</i> bioassay

Xia, J., Hu, H., Xue, W., Wang, X. S., & Wu, S. (2018) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2018.1437156 · Cited by 24 · see citing works

Supplementary Figures 1-2 from Statins Increase p21 through Inhibition of Histone Deacetylase Activity and Release of Promoter-Associated HDAC1/2

Lin, Y., Lin, J., Chou, C., et al. (2023) · doi:10.1158/0008-5472.22374644.v1

Defining the Role of HDAC3 Deacetylation and Decrotonylation in T Cells

Martinez, K., Shapiro, M., Rajcula, M. J., et al. (2023) · The Journal of Immunology · doi:10.4049/jimmunol.210.supp.219.10

Discovery of histone deacetylase 3 (HDAC3)-specific PROTACs

Xiao, Y., Wang, J., Zhao, L., Chen, X., Zheng, G., Zhang, X., & Liao, D. (2020) · Chemical Communications · doi:10.1039/d0cc03243c · Cited by 130 · see citing works

VDUP1 inhibits NF-κB activity via association with HDAC1 and HDAC3 (109.14)

Park, Y., Suh, H., Jung, H., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.186.supp.109.14

HDAC3 in action: Expanding roles in inflammation and inflammatory diseases

He, R., He, Z., Zhang, T., Liu, B., Gao, M., Li, N., & Geng, Q. (2024) · Cell Proliferation · doi:10.1111/cpr.13731 · Cited by 23 · see citing works