Strategies To Design Selective Histone Deacetylase Inhibitors

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Determination of the class and isoform selectivity of small-molecule histone deacetylase inhibitors

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Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases

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Histone deacetylase 6 structure and molecular basis of catalysis and inhibition

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Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase.

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FR901228, a Potent Antitumor Antibiotic, Is a Novel Histone Deacetylase Inhibitor

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A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas

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

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Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin

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Class I HDACs Share a Common Mechanism of Regulation by Inositol Phosphates

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Selective class IIa histone deacetylase inhibition via a nonchelating zinc-binding group

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Identification of Novel Isoform-Selective Inhibitors within Class I Histone Deacetylases

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Different accessibilities in chromatin to histone acetylase.

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Inside HDACs with more selective HDAC inhibitors

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Structural and Functional Analysis of the Human HDAC4 Catalytic Domain Reveals a Regulatory Structural Zinc-binding Domain

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Structural insights into HDAC6 tubulin deacetylation and its selective inhibition

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Chidamide (CS055/HBI-8000): a new histone deacetylase inhibitor of the benzamide class with antitumor activity and the ability to enhance immune cell-mediated tumor cell cytotoxicity

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Romidepsin: a new therapy for cutaneous T-cell lymphoma and a potential therapy for solid tumors

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Why Hydroxamates May Not Be the Best Histone Deacetylase Inhibitors—What Some May Have Forgotten or Would Rather Forget?

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Structure, mechanism, and inhibition of histone deacetylases and related metalloenzymes

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

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Human HDAC7 Harbors a Class IIa Histone Deacetylase-specific Zinc Binding Motif and Cryptic Deacetylase Activity

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Molecular Cloning and Characterization of a Novel Histone Deacetylase HDAC10

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Zinc binding groups for histone deacetylase inhibitors

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Inhibition of maize histone deacetylases by HC toxin, the host-selective toxin of Cochliobolus carbonum.

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Selective Histone Deacetylase 6 Inhibitors Bearing Substituted Urea Linkers Inhibit Melanoma Cell Growth

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Structural Studies of Human Histone Deacetylase 8 and Its Site-Specific Variants Complexed with Substrate and Inhibitors^,

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Histone deacetylase 10 structure and molecular function as a polyamine deacetylase

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Histone deacetylases: structural determinants of inhibitor selectivity

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Design and evaluation of ‘Linkerless’ hydroxamic acids as selective HDAC8 inhibitors

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Unusual zinc-binding mode of HDAC6-selective hydroxamate inhibitors

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HDAC6 inhibition effectively reverses chemotherapy-induced peripheral neuropathy

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HDAC11 regulates type I interferon signaling through defatty-acylation of SHMT2

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Histone Deacetylase (HDAC) Inhibitors with a Novel Connecting Unit Linker Region Reveal a Selectivity Profile for HDAC4 and HDAC5 with Improved Activity against Chemoresistant Cancer Cells

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Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation

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Histone deacetylase 11 is a fatty-acid deacylase

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Structural Basis for the Inhibition of Histone Deacetylase 8 (HDAC8), a Key Epigenetic Player in the Blood Fluke Schistosoma mansoni

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Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis

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HDAC inhibitors in parasitic diseases

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Rapid Discovery of Highly Potent and Selective Inhibitors of Histone Deacetylase 8 Using Click Chemistry to Generate Candidate Libraries

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Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors

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Crystal Structure of a Bacterial Class 2 Histone Deacetylase Homologue

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Design, Synthesis, and Biological Evaluation of Potent and Selective Class IIa Histone Deacetylase (HDAC) Inhibitors as a Potential Therapy for Huntington’s Disease

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Structural Basis of the Antiproliferative Activity of Largazole, a Depsipeptide Inhibitor of the Histone Deacetylases

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Catalytic Activity and Inhibition of Human Histone Deacetylase 8 Is Dependent on the Identity of the Active Site Metal Ion

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Trifluoromethyl ketones as inhibitors of histone deacetylase

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Histone deacetylase 11 is an ε-N-Myristoyllysine hydrolase

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Next-generation of selective histone deacetylase inhibitors

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Development of a histone deacetylase 6 inhibitor and its biological effects

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Synthesis of 7200 Small Molecules Based on a Substructural Analysis of the Histone Deacetylase Inhibitors Trichostatin and Trapoxin

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A Series of Potent and Selective, Triazolylphenyl-Based Histone Deacetylases Inhibitors with Activity against Pancreatic Cancer Cells and Plasmodium falciparum

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Developing potent PROTACs tools for selective degradation of HDAC6 protein

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Apicidins: Novel cyclic tetrapeptides as coccidiostats and antimalarial agents from Fusarium pallidoroseum

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Targeting Histone Deacetylases in Diseases: Where Are We?

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Structure-Based Design and Synthesis of Novel Inhibitors Targeting HDAC8 from <i>Schistosoma mansoni</i> for the Treatment of Schistosomiasis

Heimburg, T., Chakrabarti, A., Lancelot, J., Marek, M., Melesina, J., Hauser, A.-T., Shaik, T. B., Duclaud, S., Robaa, D., Erdmann, F., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01478 · Cited by 124 · see citing works

Characterization of Histone Deacetylase 8 (HDAC8) Selective Inhibition Reveals Specific Active Site Structural and Functional Determinants

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Functional Differences in Epigenetic ModulatorsSuperiority of Mercaptoacetamide-Based Histone Deacetylase Inhibitors Relative to Hydroxamates in Cortical Neuron Neuroprotection Studies

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Identification of Histone Deacetylase Inhibitors with Benzoylhydrazide Scaffold that Selectively Inhibit Class I Histone Deacetylases

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Potent and Selective Inhibition of Histone Deacetylase 6 (HDAC6) Does Not Require a Surface-Binding Motif

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Synthesis and Biological Investigation of Oxazole Hydroxamates as Highly Selective Histone Deacetylase 6 (HDAC6) Inhibitors

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Design, Synthesis, and Pharmacological Evaluation of Novel N -Acylhydrazone Derivatives as Potent Histone Deacetylase 6/8 Dual Inhibitors

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Discovery of Selective Histone Deacetylase 6 Inhibitors Using the Quinazoline as the Cap for the Treatment of Cancer

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Targeting Histone Deacetylase 8 as a Therapeutic Approach to Cancer and Neurodegenerative Diseases

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Histone Deacetylase 6-Selective Inhibitors and the Influence of Capping Groups on Hydroxamate-Zinc Denticity

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Development of Allosteric Hydrazide-Containing Class I Histone Deacetylase Inhibitors for Use in Acute Myeloid Leukemia

McClure, J. J., Zhang, C., Inks, E. S., Peterson, Y. K., Li, J., & Chou, C. J. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01385 · Cited by 108 · see citing works

Lysine Deacetylase Inhibitors in Parasites: Past, Present, and Future Perspectives

Hailu, G. S., Robaa, D., Forgione, M., Sippl, W., Rotili, D., & Mai, A. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01595 · Cited by 106 · see citing works

Highly Potent and Selective Histone Deacetylase 6 Inhibitors Designed Based on a Small-Molecular Substrate

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Tropolones As Lead-Like Natural Products: The Development of Potent and Selective Histone Deacetylase Inhibitors

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Synthesis and Biological Investigation of Phenothiazine-Based Benzhydroxamic Acids as Selective Histone Deacetylase 6 Inhibitors

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Selective Inhibition of Histone Deacetylase 10: Hydrogen Bonding to the Gatekeeper Residue is Implicated

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Discovery of histone deacetylase 8 selective inhibitors

Tang, W., Luo, T., Greenberg, E. F., Bradner, J. E., & Schreiber, S. L. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.01.134 · Cited by 95 · see citing works

Discovery of the First Histone Deacetylase 6/8 Dual Inhibitors

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Discovery of (2E)-3-{2-Butyl-1-[2-(diethylamino)ethyl]-1H-benzimidazol-5-yl}-N-hydroxyacrylamide (SB939), an Orally Active Histone Deacetylase Inhibitor with a Superior Preclinical Profile

Wang, H., Yu, N., Chen, D., Lee, K. C. L., Lye, P. L., Chang, J. W. W., Deng, W., Ng, M., Lu, T., Khoo, M. L., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm2003552 · Cited by 93 · see citing works

Structure-Based Design and Biological Characterization of Selective Histone Deacetylase 8 (HDAC8) Inhibitors with Anti-Neuroblastoma Activity

Heimburg, T., Kolbinger, F. R., Zeyen, P., Ghazy, E., Herp, D., Schmidtkunz, K., Melesina, J., Shaik, T. B., Erdmann, F., Schmidt, M., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01447 · Cited by 92 · see citing works

Analogues of trichosтatin a and trapoxin B as histone deacetylase inhibitors

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Short-Chain HDAC Inhibitors Differentially Affect Vertebrate Development and Neuronal Chromatin

Fass, D. M., Shah, R. R., Ghosh, B., Hennig, K. M., Norton, S., Zhao, W., Reis, S. A., Klein, P. S., Mazitschek, R., Maglathlin, R. L., et al. (2010) · ACS Medicinal Chemistry Letters · doi:10.1021/ml1001954 · Cited by 89 · see citing works

HDAC6 Brain Mapping with [18F]Bavarostat Enabled by a Ru-Mediated Deoxyfluorination

Strebl, M. G., Campbell, A. J., Zhao, W., Schroeder, F. A., Riley, M. M., Chindavong, P. S., Morin, T., Haggarty, S. J., Wagner, F. F., Ritter, T., et al. (2017) · ACS Central Science · doi:10.1021/acscentsci.7b00274 · Cited by 87 · see citing works

Activity-Guided Design of HDAC11-Specific Inhibitors

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Histone Deacetylase Inhibitors through Click Chemistry

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Molecular Insights into Azumamide E Histone Deacetylases Inhibitory Activity

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Structures of Metal-Substituted Human Histone Deacetylase 8 Provide Mechanistic Inferences on Biological Function,

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Structural Basis of Catalysis and Inhibition of HDAC6 CD1, the Enigmatic Catalytic Domain of Histone Deacetylase 6

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Substrate and inhibitor specificity of class 1 and class 2 histone deacetylases

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Discovery of the First-in-Class Dual Histone Deacetylase–Proteasome Inhibitor

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Synthesis and Biological Evaluation of ortho‐Aryl N‐Hydroxycinnamides as Potent Histone Deacetylase (HDAC) 8 Isoform‐Selective Inhibitors

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Discovery of the First N -Hydroxycinnamamide-Based Histone Deacetylase 1/3 Dual Inhibitors with Potent Oral Antitumor Activity

Li, X., Inks, E. S., Li, X., Hou, J., Chou, C. J., Zhang, J., Jiang, Y., Zhang, Y., & Xu, W. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401877m · Cited by 76 · see citing works

Molecular Basis for the Antiparasitic Activity of a Mercaptoacetamide Derivative That Inhibits Histone Deacetylase 8 (HDAC8) from the Human Pathogen Schistosoma mansoni

Stolfa, D. A., Marek, M., Lancelot, J., Hauser, A.-T., Walter, A., Leproult, E., Melesina, J., Rumpf, T., Wurtz, J.-M., Cavarelli, J., et al. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.03.007 · Cited by 75 · see citing works

3-Hydroxypyridin-2-thione as Novel Zinc Binding Group for Selective Histone Deacetylase Inhibition

Patil, V., Sodji, Q. H., Kornacki, J. R., Mrksich, M., & Oyelere, A. K. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301769u · Cited by 73 · see citing works

Binding of the Microbial Cyclic Tetrapeptide Trapoxin A to the Class I Histone Deacetylase HDAC8

Porter, N. J., & Christianson, D. W. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00330 · Cited by 73 · see citing works

Innovative Strategies for Selective Inhibition of Histone Deacetylases

Maolanon, A. R., Madsen, A. S., & Olsen, C. A. (2016) · Cell Chemical Biology · doi:10.1016/j.chembiol.2016.06.011 · Cited by 72 · see citing works

Design, Synthesis, and Biological Activity of NCC149 Derivatives as Histone Deacetylase 8‐Selective Inhibitors

Suzuki, T., Muto, N., Bando, M., Itoh, Y., Masaki, A., Ri, M., Ota, Y., Nakagawa, H., Iida, S., Shirahige, K., et al. (2014) · ChemMedChem · doi:10.1002/cmdc.201300414 · Cited by 71 · see citing works

Multicomponent Synthesis and Binding Mode of Imidazo[1,2-a]pyridine-Capped Selective HDAC6 Inhibitors

Mackwitz, M. K. W., Hamacher, A., Osko, J. D., Held, J., Schöler, A., Christianson, D. W., Kassack, M. U., & Hansen, F. K. (2018) · Organic Letters · doi:10.1021/acs.orglett.8b01118 · Cited by 68 · see citing works

The Effect of Various Zinc Binding Groups on Inhibition of Histone Deacetylases 1–11

Madsen, A. S., Kristensen, H. M. E., Lanz, G., & Olsen, C. A. (2013) · ChemMedChem · doi:10.1002/cmdc.201300433 · Cited by 67 · see citing works

A series of novel, potent, and selective histone deacetylase inhibitors

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Targeting breast cancer stem cells by novel HDAC3-selective inhibitors

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Synthesis and Biological Evaluation of Triazol-4-ylphenyl-Bearing Histone Deacetylase Inhibitors as Anticancer Agents

He, R. L., Chen, Y., Chen, Y., Ougolkov, A. V., Zhang, J., Savoy, D. N., Billadeau, D. D., & Kozikowski, A. P. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901667k · Cited by 66 · 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

2-Trifluoroacetylthiophenes, a novel series of potent and selective class II histone deacetylase inhibitors

JONES, P. G., Bottomley, M. J., Carfı́, A., Cecchetti, O., Ferrigno, F., Surdo, P. L., Ontoria, J. M., Rowley, M., Scarpelli, R., Schultz‐Fademrecht, C., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.02.026 · Cited by 64 · see citing works

Entropy as a Driver of Selectivity for Inhibitor Binding to Histone Deacetylase 6

Porter, N. J., Wagner, F. F., & Christianson, D. W. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00367 · Cited by 64 · see citing works

Azetidinones as Zinc‐Binding Groups to Design Selective HDAC8 Inhibitors

Galletti, P., Quintavalla, A., Ventrici, C., Giannini, G., Cabri, W., Penco, S., Gallo, G., Vincenti, S., & Giacomini, D. (2009) · ChemMedChem · doi:10.1002/cmdc.200900309 · Cited by 63 · see citing works

Structure of ‘linkerless’ hydroxamic acid inhibitor-HDAC8 complex confirms the formation of an isoform-specific subpocket

Tabackman, A. A., Frankson, R., Marsan, E. S., Perry, K., & Cole, K. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.06.023 · Cited by 63 · see citing works

Discovery of Inhibitors of Schistosoma mansoni HDAC8 by Combining Homology Modeling, Virtual Screening, and in Vitro Validation

Kannan, S., Melesina, J., Hauser, A., Chakrabarti, A., Heimburg, T., Schmidtkunz, K., Walter, A., Marek, M., Pierce, R. J., Romier, C., et al. (2014) · Journal of Chemical Information and Modeling · doi:10.1021/ci5004653 · Cited by 62 · see citing works

Identification of a Novel Aminotetralin Class of HDAC6 and HDAC8 Selective Inhibitors

Tang, G., Wong, J. C., Zhang, W., Wang, Z., Zhang, N., Peng, Z., Zhang, Z., Rong, Y., Li, S., Zhang, M., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5008962 · Cited by 62 · see citing works

Diphenylmethylene hydroxamic acids as selective class IIa histone deacetylase inhibitors

Tessier, P., Smil, D. V., Wahhab, A., Leit, S. M., Rahil, J. F., Li, Z., Déziel, R., & Besterman, J. M. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.08.010 · Cited by 59 · see citing works

Variable Active Site Loop Conformations Accommodate the Binding of Macrocyclic Largazole Analogues to HDAC8

Decroos, C., Clausen, D. J., Haines, B. E., Wiest, O., Williams, R. M., & Christianson, D. W. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00010 · Cited by 58 · see citing works

Design and synthesis of novel HDAC8 inhibitory 2,5-disubstituted-1,3,4-oxadiazoles containing glycine and alanine hybrids with anti cancer activity

Pidugu, V. R., Yarla, N. S., Pedada, S. R., Kalle, A. M., & Satya, A. K. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.09.022 · Cited by 58 · see citing works

A Novel Series of Potent and Selective Ketone Histone Deacetylase Inhibitors with Antitumor Activity in Vivo

JONES, P. G., Altamura, S., Francesco, R. D., Paz, O. G., Kinzel, O. D., Mesiti, G., Monteagudo, E. S., Pescatore, G., Rowley, M., Verdirame, M., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800079s · Cited by 58 · see citing works

N-alkyl-hydroxybenzoyl anilide hydroxamates as dual inhibitors of HDAC and HSP90, downregulating IFN-γ induced PD-L1 expression

Mehndiratta, S., Lin, M.-H., Wu, Y.-W., Chen, C., Wu, T.-Y., Chuang, K.-H., Chao, M., Chen, Y., Pan, S., Chen, M.-C., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111725 · Cited by 58 · see citing works

Discovery of HDAC Inhibitors That Lack an Active Site Zn2+-Binding Functional Group

Vickers, C. J., Olsen, C. A., Leman, L. J., & Ghadiri, M. R. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300081u · Cited by 57 · see citing works

Potent, Selective, and CNS-Penetrant Tetrasubstituted Cyclopropane Class IIa Histone Deacetylase (HDAC) Inhibitors

Luckhurst, C. A., Breccia, P., Stott, A. J., Aziz, O., Birch, H. L., Bürli, R. W., Hughes, S. J., Jarvis, R. E., Lamers, M. B. A. C., Leonard, P. M., et al. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00302 · Cited by 57 · see citing works

Insights into the Recruitment of Class IIa Histone Deacetylases (HDACs) to the SMRT/NCoR Transcriptional Repression Complex

Hudson, G. M., Watson, P. J., Fairall, L., Jamieson, A. G., & Schwabe, J. W. R. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.661058 · Cited by 56 · see citing works

Design, synthesis, and evaluation of cyclic amide/imide-bearing hydroxamic acid derivatives as class-selective histone deacetylase (HDAC) inhibitors

Shinji, C., Maeda, S., Imai, K., Yoshida, M., Hashimoto, Y., & Miyachi, H. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2006.07.008 · Cited by 56 · see citing works

Novel Benzohydroxamate-Based Potent and Selective Histone Deacetylase 6 (HDAC6) Inhibitors Bearing a Pentaheterocyclic Scaffold: Design, Synthesis, and Biological Evaluation

Vergani, B., Sandrone, G., Marchini, M., Ripamonti, C., Cellupica, E., Galbiati, E., Caprini, G., Pavich, G., Porro, G., Rocchio, I., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01194 · Cited by 56 · see citing works

Exploring Structural Determinants of Inhibitor Affinity and Selectivity in Complexes with Histone Deacetylase 6

Osko, J. D., Porter, N. J., Poli, A. N. R., Xiao, Y., Rokka, J., Jung, M., Hooker, J. M., Salvino, J. M., & Christianson, D. W. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01540 · Cited by 56 · see citing works

Discovery of Potent, Isoform-Selective Inhibitors of Histone Deacetylase Containing Chiral Heterocyclic Capping Groups and aN-(2-Aminophenyl)benzamide Binding Unit

Marson, C. M., Matthews, C. J., Yiannaki, E., Atkinson, S. J., Soden, P. E., Shukla, L., Lamadema, N., & Thomas, N. S. B. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400634n · Cited by 54 · see citing works

Novel 2, 5-diketopiperazine derivatives as potent selective histone deacetylase 6 inhibitors: Rational design, synthesis and antiproliferative activity

Chen, X., Chen, X., Steimbach, R. R., Wu, T., Li, H., Dan, W., Shi, P., Cao, C., Li, D., Miller, A. K., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111950 · Cited by 53 · see citing works

Rational design and diversity-oriented synthesis of peptoid-based selective HDAC6 inhibitors

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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

Development and characterization of a CNS-penetrant benzhydryl hydroxamic acid class IIa histone deacetylase inhibitor

Luckhurst, C. A., Aziz, O., Beaumont, V., Bürli, R. W., Breccia, P., Maillard, M. C., Haughan, A. F., Lamers, M. B. A. C., Leonard, P. M., Matthews, K. L., et al. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.11.009 · Cited by 50 · see citing works

Hydroxamic Acids Block Replication of Hepatitis C Virus

Ai, T., Xü, Y., Qiu, L., Geraghty, R. J., & Chen, L. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501330g · Cited by 50 · see citing works

Structure of Prokaryotic Polyamine Deacetylase Reveals Evolutionary Functional Relationships with Eukaryotic Histone Deacetylases,

Lombardi, P. M., Angell, H. D., Whittington, D. A., Flynn, E. F., Rajashankar, K. R., & Christianson, D. W. (2011) · Biochemistry · doi:10.1021/bi101859k · Cited by 50 · see citing works

Natural and Synthetic Macrocyclic Inhibitors of the Histone Deacetylase Enzymes

Maolanon, A. R., Kristensen, H. M. E., Leman, L. J., Ghadiri, M. R., & Olsen, C. A. (2016) · ChemBioChem · doi:10.1002/cbic.201600519 · Cited by 49 · see citing works

Development of N-Hydroxycinnamamide-Based Histone Deacetylase Inhibitors with an Indole-Containing Cap Group

Zhang, Y., Yang, P., Chou, C. J., Liu, C., Wang, X., & Xu, W. (2013) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300366t · Cited by 48 · see citing works

Discovery of a Potent Class I Selective Ketone Histone Deacetylase Inhibitor with Antitumor Activity in Vivo and Optimized Pharmacokinetic Properties

Kinzel, O. D., Llauger, L., Pescatore, G., Rowley, M., Schultz‐Fademrecht, C., Monteagudo, E. S., Fonsi, M., Paz, O. G., Fiore, F., Steinkühler, C., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9004303 · Cited by 46 · see citing works

Structural insights into bacterial resistance to cerulenin

Trajtenberg, F., Altabe, S., Larrieux, N., Ficarra, F. A., de Mendoza, D., Buschiazzo, A., & Schujman, G. E. (2014) · FEBS Journal · doi:10.1111/febs.12785 · Cited by 46 · see citing works

Homology modeling of parasite histone deacetylases to guide the structure-based design of selective inhibitors

Melesina, J., Robaa, D., Pierce, R. J., Romier, C., & Sippl, W. (2015) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2015.10.006 · Cited by 46 · see citing works

Design and Synthesis of Orally Bioavailable Aminopyrrolidinone Histone Deacetylase 6 Inhibitors

Lin, X., Chen, W.-M., Qiu, Z., Guo, L., Zhu, W., Li, W., Wang, Z., Zhang, W., Zhang, Z., Rong, Y., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm502011f · Cited by 44 · see citing works

A Novel Class of Schistosoma mansoni Histone Deacetylase 8 (HDAC8) Inhibitors Identified by Structure-Based Virtual Screening and In Vitro Testing

Simoben, C., Robaa, D., Chakrabarti, A., Schmidtkunz, K., Marek, M., Lancelot, J., Kannan, S., Melesina, J., Shaik, T., Pierce, R., et al. (2018) · Molecules · doi:10.3390/molecules23030566 · Cited by 44 · see citing works

Potent Histone Deacetylase Inhibitors Derived from 4-(Aminomethyl)-N-hydroxybenzamide with High Selectivity for the HDAC6 Isoform

Blackburn, C., Barrett, C., Chin, J. E., Garcia, K., Gigstad, K. M., Gould, A. E., Gutierrez, J. A., Harrison, S., Hoar, K. M., Lynch, C., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400385r · Cited by 43 · see citing works

Synthesis of N‐Hydroxycinnamides Capped with a Naturally Occurring Moiety as Inhibitors of Histone Deacetylase

Huang, W., Chen, C., Chao, S.-W., Lee, S., Hsu, F., Lu, Y., Hung, M., & Chang, C. (2010) · ChemMedChem · doi:10.1002/cmdc.200900494 · Cited by 42 · see citing works

Isoxazole moiety in the linker region of HDAC inhibitors adjacent to the Zn-chelating group: Effects on HDAC biology and antiproliferative activity

Tapadar, S., He, R. L., Luchini, D. N., Billadeau, D. D., & Kozikowski, A. P. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.04.058 · Cited by 42 · see citing works

N-Hydroxy-(4-oxime)-cinnamide: A versatile scaffold for the synthesis of novel histone deacetilase (HDAC) inhibitors

Giannini, G., Marzi, M., Pezzi, R., Brunetti, T., Battistuzzi, G., Marzo, M. D., Cabri, W., Vesci, L., & Pisano, C. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.02.029 · Cited by 41 · see citing works

Small Molecule Antagonists of the Interaction between the Histone Deacetylase 6 Zinc-Finger Domain and Ubiquitin

Harding, R., de Freitas, R. F., Collins, P. M., Franzoni, I., Ravichandran, M., Ouyang, H., Juárez‐Ornelas, K. A., Lautens, M., Schapira, M., von Delft, F., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00933 · Cited by 41 · see citing works

Continuous Activity Assay for HDAC11 Enabling Reevaluation of HDAC Inhibitors

Kutil, Z., Mikešová, J., Zessin, M., Meleshin, M., Nováková, Z., Alquicer, G., Kozikowski, A. P., Sippl, W., Bařinka, C., & Schutkowski, M. (2019) · ACS Omega · doi:10.1021/acsomega.9b02808 · Cited by 40 · see citing works

Design, Synthesis, and Biological Evaluation of Tetrahydroisoquinoline-Based Histone Deacetylase 8 Selective Inhibitors

Taha, T. Y., Aboukhatwa, S. M., Knopp, R. C., Ikegaki, N., Abdelkarim, H., Jayaprakash, N., Lu, Y., Neelarapu, R., Hanigan, T. W., Thatcher, G. R. J., et al. (2017) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.7b00126 · Cited by 39 · see citing works

Chidamide tablets: HDAC inhibition to treat lymphoma

Xu, Y., Zhang, P., & Liu, Y. (2017) · Drugs of today · doi:10.1358/dot.2017.53.3.2595452 · Cited by 39 · see citing works

Macrocyclic Peptoid–Peptide Hybrids as Inhibitors of Class I Histone Deacetylases

Olsen, C. A., Montero, A., Leman, L. J., & Ghadiri, M. R. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300162r · Cited by 38 · see citing works

Identification of HDAC6‐Selective Inhibitors of Low Cancer Cell Cytotoxicity

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One-Atom Substitution Enables Direct and Continuous Monitoring of Histone Deacylase Activity

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Design, synthesis, and biological evaluation of novel HDAC/CD13 dual inhibitors for the treatment of cancer

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Preferential HDAC6 inhibitors derived from HPOB exhibit synergistic antileukemia activity in combination with decitabine

Tretbar, M., Schliehe‐Diecks, J., von Bredow, L., Tan, K., Roatsch, M., Tu, J., Kemkes, M., Sönnichsen, M., Schöler, A., Borkhardt, A., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116447 · Cited by 11 · see citing works

Hydroxamic acid hybrids as histone deacetylase inhibitors for cancer therapy: an update (2022 to date)

Cheng, Y., Zhuang, Y., Zhu, N., You, Y., & Hu, M. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108700 · Cited by 12 · see citing works

Application of Ligand- and Structure-Based Prediction Models for the Design of Alkylhydrazide-Based HDAC3 Inhibitors as Novel Anti-Cancer Compounds

Bülbül, E. F., Robaa, D., Sun, P., Mahmoudi, F., Melesina, J., Zessin, M., Schutkowski, M., & Sippl, W. (2023) · Pharmaceuticals · doi:10.3390/ph16070968 · Cited by 11 · see citing works

Development and Characterization of the First Selective Class IIb Histone Deacetylase Degraders

Zhai, S., Honin, I., Schäker‐Hübner, L., Hanl, M., Jacobi, L., Dressler, F., Pieńkowska, D. E., König, P., Gerhartz, J., Voget, R., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00674 · Cited by 11 · see citing works

Development of Novel ROCK Inhibitors via 3D-QSAR and Molecular Docking Studies: A Framework for Multi-Target Drug Design

Beljkaš, M., Petković, M., Vuletić, A. M., Djurić, A., Santibanez, J. F., Srdić‐Rajić, T., Nikolic, K. M., & Oljačić, S. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16101250 · Cited by 11 · see citing works

Recent Insights into the Creation of Histone Deacetylase Inhibitors for the Treatment of Human Diseases

Александрович, Ю. П., Aleksandrova, Y. R., & Евгеньевна, Н. М. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178629 · Cited by 10 · see citing works

Histone deacetylase inhibitor panobinostat in combination with rapamycin confers enhanced efficacy against triple-negative breast cancer

Wu, K., Zhang, H., Zhou, L., Chen, L., Mo, C., Xu, S., Lin, J., Kong, L., & Chen, X. (2022) · Experimental Cell Research · doi:10.1016/j.yexcr.2022.113362 · Cited by 10 · see citing works

Spirotetrahydroisoquinoline-Based Histone Deacetylase Inhibitors as New Antifibrotic Agents: Biological Evaluation in Human Fibroblasts from Bronchoalveolar Lavages of Idiopathic Pulmonary Fibrosis Patients

Fontana, A., Bergantini, L., Carullo, G., Scalvini, L., d’Alessandro, M., Papulino, C., Cameli, P., Gangi, S., Vincenzi, F., Varani, K., et al. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00456 · Cited by 9 · see citing works

Changes in chromatin accessibility and transcriptional landscape induced by HDAC inhibitors in TP53 mutated patient-derived colon cancer organoids

Gagliano, T., Kerschbamer, E., Baccarani, U., Minisini, M., Giorgio, E. D., Dalla, E., Weichenberger, C. X., Cherchi, V. A., Terrosu, G., & Brancolini, C. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116374 · Cited by 9 · see citing works

Integrated molecular modeling and dynamics approaches revealed the mechanism of selective inhibition of HDAC6/8

Li, Y., Liu, S., Xu, X., Xu, J., Yang, L., & Hu, L. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2272751 · Cited by 8 · see citing works

Novel HDAC1 and HDAC2 Inhibitors for Treating Diseases

Sabnis, R. W. (2021) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.1c00488 · Cited by 8 · see citing works

Key structural requirements of benzamide derivatives for histone deacetylase inhibition: design, synthesis and biological evaluation

Cheshmazar, N., Hamzeh‐Mivehroud, M., Hemmati, S., Abolhasani, H., Heidari, F., Charoudeh, H. N., Zessin, M., Schutkowski, M., Sippl, W., & Dastmalchi, S. (2024) · Future Medicinal Chemistry · doi:10.4155/fmc-2023-0122 · Cited by 7 · see citing works

Rationally designed febuxostat-based hydroxamic acid and its pH-Responsive nanoformulation elicits anti-tumor activity

Ritika, R., Liao, Z.-Y., Chen, P.-Y., Rao, N. V., Mathew, J., Sharma, R., Grewal, A. S., Singh, G., Mehan, S., Liou, J., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116866 · Cited by 7 · see citing works

The Effect of Vicinal Difluorination on the Conformation and Potency of Histone Deacetylase Inhibitors

Ariawan, D., Mansour, F., Richardson, N., Bhadbhade, M. M., Ho, J., & Hunter, L. (2021) · Molecules · doi:10.3390/molecules26133974 · Cited by 7 · see citing works

Modified Suberoylanilide Hydroxamic Acid Reduced Drug-Associated Immune Cell Death and Organ Damage under Lipopolysaccharide Inflammatory Challenge

Truong, N., Goodis, C. C., Cottingham, A. L., Shaw, J. R., Fletcher, S., & Pearson, R. M. (2022) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.2c00119 · Cited by 8 · see citing works

Novel ( E )-3-(1-substituted-1 H -indazol-5-yl)- N -hydroxypropenamides as histone deacetylase inhibitors: design, synthesis and structure–activity relationships

Doan, M. S., Park, E. J., Anh, D. T., Dung, D. T. M., Quang-Bao, L., Pham‐The, H., Oanh, D. T. K., Tùng, T. T., Na, I. H., Kwon, J. H., et al. (2023) · New Journal of Chemistry · doi:10.1039/d2nj04894a · Cited by 7 · see citing works

Suberoylanilide Hydroxamic Acid Analogs with Heteroaryl Amide Group and Different Chain Length: Synthesis and Effect on Histone Deacetylase

Micheletti, G., Boga, C., Drius, G., Bordoni, S., & Calonghi, N. (2024) · Molecules · doi:10.3390/molecules29010238 · Cited by 8 · see citing works

Histone deacetylase (HDAC) inhibitor specificity determinants are preserved in a class of dual HDAC/non-covalent proteasome inhibitors

Chan, A. M., Mitchell, A., Grogan, L., Shapiro, P. S., & Fletcher, S. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.117680 · Cited by 7 · see citing works

Medicinal Chemistry of Anti-HIV-1 Latency Chemotherapeutics: Biotargets, Binding Modes and Structure-Activity Relationship Investigation

Wang, Y., Wei, L., Hu, W., Yu, P.-X., Li, Z., Yu, H.-P., & Li, X. (2022) · Molecules · doi:10.3390/molecules28010003 · Cited by 7 · see citing works

Proteasomal Degradation of Zn-Dependent Hdacs: The E3-Ligases Implicated and the Designed Protacs That Enable Degradation

Márquez-Cantudo, L., Ramos, A., Coderch, C., & de Pascual‐Teresa, B. (2021) · Molecules · doi:10.3390/molecules26185606 · Cited by 7 · see citing works

Reworked Discocyclina occurring together with Lepidocyclina in the Oligocene of San Vicente de la Barquera (northern Spain)

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Recent progress in synthetic strategies to develop potent, HDAC8-selective, small-molecule inhibitors

Lowe, B. D., & Fletcher, S. (2025) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2025.130312 · Cited by 6 · see citing works

Design and synthesis of bioreductive prodrugs of class I histone deacetylase inhibitors and their biological evaluation in virally transfected acute myeloid leukemia cells

Abdelsalam, M. A. M., Zmyslia, M., Schmidtkunz, K., Vecchio, A., Hilscher, S., Ibrahim, H. S., Schutkowski, M., Jung, M., Jessen‐Trefzer, C., & Sippl, W. (2023) · Archiv der Pharmazie · doi:10.1002/ardp.202300536 · Cited by 6 · see citing works

First-in-Class Potent, Dual HDAC6/Proteasome Inhibitors Lacking a Hydroxamic Acid Motif: Discovery of Novel Anti-Multiple Myeloma Agents

Chan, A. M., Lowe, B. D., Cottingham, A. L., Eker, D. V., Aytenfisu, A. H., Jones, J. W., MacKerell, A. D., Pearson, R. M., & Fletcher, S. (2025) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5c00500 · Cited by 5 · see citing works

Phenylacetyl-/Trolox- Amides: Synthesis, Sigma-1, HDAC-6, and Antioxidant Activities

Flores, R., Iqbal, S., & Sikazwe, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015295 · Cited by 5 · see citing works

Pioneering first-in-class HDAC-ROCK inhibitors as potential multitarget anticancer agents

Beljkaš, M., Ružić, D., Djurić, A., Vuletić, A. M., Nchugoua, G., Jallet, C., Cadet-Daniel, V., Arimondo, P. B., Santibanez, J. F., Srdić‐Rajić, T., et al. (2025) · Future Medicinal Chemistry · doi:10.1080/17568919.2025.2459589 · Cited by 5 · see citing works

Augmenting the Anti‐Leukemic Activity of the BCL‐2 Inhibitor Venetoclax Through Its Transformation Into Polypharmacologic Dual BCL‐2/HDAC1 and Dual BCL‐2/HDAC6 Inhibitors

Chan, A. M., Eberly, C. L., Drennen, B., Goodis, C. C., Wuyts, Z., Civin, C. I., & Fletcher, S. (2025) · Drug Development Research · doi:10.1002/ddr.70084 · Cited by 5 · see citing works

Lysine Deacetylase Substrate Selectivity: A Dynamic Ionic Interaction Specific to KDAC8

Toro, T. B., Swanier, J. S., Bezue, J. A., Broussard, C. G., & Watt, T. J. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00384 · Cited by 5 · see citing works

InhibitWin duo: Rational design and structural insights into dual PARP/HDAC inhibitors for synergistic DNA repair disruption and epigenetic modulation

Elkafoury, E. M., El-Moselhy, T. F., El‐Hamamsy, M. H., El-Bastawissy, E. A., Afarinkia, K., Salih, M. A. M., El‐Damasy, A. K., Ibrahim, M. A. A., ElShewy, A. M., Shawky, A. M., et al. (2026) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2026.118743 · Cited by 4 · see citing works

New potent N‐hydroxycinnamamide‐based histone deacetylase inhibitors suppress proliferation and trigger apoptosis in THP‐1 leukaemia cells

Onuščáková, M., Kauerová, T., Fialova, E., Pížová, H., Garaj, V., Kemka, M., Frecer, V., Kollár, P., & Bobáľ, P. (2025) · Archiv der Pharmazie · doi:10.1002/ardp.202400889 · Cited by 4 · see citing works

Synthesis and structure‐activity relationship of thiol‐based histone deacetylase 6 inhibitors

Guo, Z., Zhang, Y., Bao, Y., Huang, Z., Gu, X. Q., Wang, G., & Li, J. (2022) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14055 · Cited by 4 · see citing works

Dona Flor and her two husbands: Discovery of novel HDAC6/AKT2 inhibitors for myeloid cancer treatment

Waitman, K. B., Martin, H., Carlos, J. A. E. G., Braga, R. C., Souza, V. A. M., Melo-Filho, C. C., Hilscher, S., Toledo, M. F. Z. J., Tavares, M. T., Costa-Lotufo, L. V., et al. (2024) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2025.110990 · Cited by 3 · see citing works

Comprehensive medicinal chemistry survey highlights a portfolio of lead molecules for Alzheimer’s disease therapy

Bhansali, P. R., Sonkusare, S. M., Savale, S. S., Wijayasinghe, Y. S., Liao, Y., Sloan, D. C., Chaturbhuj, G. U., & Muntean, B. S. (2025) · Frontiers in Chemistry · doi:10.3389/fchem.2025.1642190 · Cited by 3 · see citing works

DESIGN AND COMPUTATIONAL ANALYSIS OF NEW ISATIN-IMINE HYBRIDS AS SELECTIVE HDAC6 INHIBITORS

AL-GBURI, K. M. H., Naser, N. H., & Jasamai, M. (2025) · International Journal of Applied Pharmaceutics · doi:10.22159/ijap.2025v17i3.53658 · Cited by 3 · see citing works

Carboxamide-Bearing Panobinostat Analogues Designed To Interact with E103-D104 at the Cavity Opening of Class I HDAC Isoforms

Rosser, C. A., Feeney, S. V., Roth, L., Hibbs, D. E., Gotsbacher, M. P., & Codd, R. (2025) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.4c00494 · Cited by 3 · see citing works

Development of a Cellular Model Mimicking Specific HDAC Inhibitors

Hess, L., Moos, V., & Seiser, C. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2788-4_4 · Cited by 3 · see citing works

New insights into possible HDAC inhibitor resistance in DLBCL - Comment on 'defining cellular responses to HDAC-selective inhibitors reveals that efficient targeting of HDAC3 is required to elicit cytotoxicity and overcome naïve resistance to pan-HDACi in diffuse large B cell lymphoma' by Havas et al.

Kiesslich, T., Mayr, C., Bekric, D., & Neureiter, D. (2023) · Translational Oncology · doi:10.1016/j.tranon.2023.101820 · Cited by 3 · see citing works

Integrated QSAR, molecular docking, and dynamics-based discovery of a potent selective HDAC1 inhibitor with therapeutic potential in aggressive cancers

Shelke, S., Jawarkar, R. D., Khatale, P. N., Shah, U., Alzahrani, A. Y. A., Samad, A., Al-Hussain, S. A., Al‐Mutairi, A. A., & Zaki, M. E. A. (2026) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2025.109271 · Cited by 2 · see citing works

Fragment‐Based Design of Pseudo‐Natural Products, Synthesis, and Evaluation of Their HIV ‐1 Latency‐Reversing Properties

Tanyi, S. A., Eni, D. B., Abdelsalam, M. A. M., Tjegbe, M. J. M., Schmidt, M., Ndip, R. N., Tietjen, I., Sippl, W., & Ntie‐Kang, F. (2026) · Chemical Biology & Drug Design · doi:10.1111/cbdd.70235 · Cited by 2 · see citing works

Structure-Based Design and Free Energy Perturbation-Guided Synthesis of Novel VEGFR2 and HDAC Dual Inhibitors with Potent Antitumor Efficacy

Li, Y., Liu, S., Hu, S., Zhang, R., Wang, X., Xu, J., Yao, K., Lu, C., Li, G., Wu, Z., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01650 · Cited by 2 · see citing works

Recommended Tool Compounds: Isoform- and Class-Specific Histone Deacetylase Inhibitors

Schäker‐Hübner, L., & Hansen, F. K. (2026) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00619 · Cited by 3 · see citing works

Fair and Square: Design, Synthesis and Biological Evaluations of Squaric Acid Derivatives as Novel HDAC8 Inhibitors

Long, N., Meyer‐Almes, F., Kopranovic, A., & Wren, S. P. (2026) · ChemMedChem · doi:10.1002/cmdc.70270 · Cited by 2 · see citing works

Determining Potency of Inhibitors Targeting Histone Deacetylase 6 by Quantification of Acetylated Tubulin in Cells

Mikesova, J., Ondrakova, M., Jelínková, I., Ptáček, J., Nováková, Z., & Bařinka, C. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2788-4_29 · Cited by 2 · see citing works

2-Substituted 1,5-benzothiazepine-based HDAC inhibitors exert anticancer activities on human solid and acute myeloid leukemia cell lines

Vita, S. D., Meninno, S., Capasso, L., Colarusso, E., Chini, M. G., Lauro, G., Rinaldi, R., Cicco, A. D., Sian, V., Terracciano, S., et al. (2023) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2023.117444 · Cited by 2 · see citing works

Modulation of biological activities in adipose derived stem cells by histone deacetylation

Abdallah, S. H., Tabebi, M., Qanadilo, S., Ali, N., Wang, J., D’Arcy, P., Zhong, W., Sjöberg, F., Elmasry, M., & El-Serafi, A. T. (2025) · Scientific Reports · doi:10.1038/s41598-024-84652-1 · Cited by 2 · see citing works

Development of Pyrazine-Anilinobenzamides as Histone Deacetylase HDAC1–3 Selective Inhibitors and Biological Testing Against Pancreas Cancer Cell Lines

Abdelsalam, M. A. M., Ibrahim, H. S., Krauß, L., Zessin, M., Vecchio, A., Hastreiter, S., Schutkowski, M., Schneider, G., & Sippl, W. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2788-4_10 · Cited by 2 · see citing works

New and Effective Inhibitor of Class I HDACs, Eimbinostat, Reduces the Growth of Hematologic Cancer Cells and Triggers Apoptosis

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 · see citing works

The design, synthesis, and evaluation of the biological activity of hydroxamic derivatives of sorafenib

Kleymenova, A. A., Abramov, I. A., Tkachev, Y. V., Galeeva, P. S., Kleymenova, V. A., Zakirova, N. F., Kochetkov, S. N., & Kozlov, M. V. (2025) · Acta Naturae · doi:10.32607/actanaturae.27566 · Cited by 1 · see citing works

Exploration of 2-Mercaptoquinazolin-4(3H)-one Based N-Hydroxyheptanamides as Histone Deacetylase Inhibitors: Design, Synthesis, and Anticancer Bioevaluation

Thảo, L. T. P., Kim, H. K., Ngoc, H. K., Kang, D. H., Kim, H. Y., Kang, J. S., Anh, D. T., Tùng, T. T., Han, S., & Nam, N. (2025) · Pharmaceutical Research · doi:10.1007/s11095-025-03928-x · Cited by 1 · see citing works

Synthesis and biological evaluation of ortho -phenyl phenylhydroxamic acids containing phenothiazine with improved selectivity for class IIa histone deacetylases

Hsu, K., Huang, Y., Chu, J.-C., Huang, Y.-W., Hu, J., Lin, T. E., Yen, S., Weng, J.-R., & Huang, W.-J. (2024) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2024.2406025 · Cited by 1 · see citing works

Novel (E)‐3‐(3‐Oxo‐4‐substituted‐3,4‐dihydro‐2H‐benzo[b][1,4]oxazin‐6‐yl)‐N‐hydroxypropenamides as Histone Deacetylase Inhibitors: Design, Synthesis and Bioevaluation

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 · see citing works

Aza-SAHA Derivatives are Selective Histone Deacetylase 10 Chemical Probes That Inhibit Polyamine DeacetylationPreprint

Steimbach, R. R., Herbst‐Gervasoni, C. J., Klinke, G., Géraldy, M. N. E., Tihanyi, G., Ridinger, J., Poschet, G., Oehme, I., Christianson, D. W., Gunkel, N., et al. (2021) · ChemRxiv · doi:10.33774/chemrxiv-2021-37shs · Cited by 1 · see citing works

Harnessing Deep Belief Networks for Selective HDAC6 Inhibitors Identification

Corbaci, T., Durdağı, S., & Doğan, B. (2025) · Journal of Computational Biophysics and Chemistry · doi:10.1142/s2737416525500978

Decoding HDACs and its inhibitors-artificial intelligence assisted smart software based super computational modelling technology in targeting cancer and neurological disorders of the brain

Rizwan, A., Aqeel, A., & Farooqi, H. (2025) · Network Modeling Analysis in Health Informatics and Bioinformatics · doi:10.1007/s13721-025-00589-z

Zinc-Dependent Histone Deacetylase (HDAC) Inhibitors: Therapeutic Potential, Pharmacophore Structure, and Methods for Testing Deacylase Activity

Zemskaya, A. S., Kochetkov, S. N., & Kozlov, M. V. (2025) · Molecular Biology · doi:10.1134/s002689332570027x

Repositioning HDAC Inhibitors for Glioma Treatment: Synthesis and Biological Evaluation

Furtado, L. C., Waitman, K. B., Silva, N. A. T. F., Gouvea, L. M., Kronenberger, T., Toledo, M. F. Z. J., Ferreira, E. G., Machado‐Neto, J. A., Kruyt, F. A. E., Parise‐Filho, R., et al. (2026) · ACS Omega · doi:10.1021/acsomega.5c11083 · Cited by 1 · see citing works

Tuning HDAC Inhibition, Cell Uptake, and Antiproliferative Activity of Vorinostat-Derived Half-Sandwich Complexes with Phosphine Co-Ligands

Chen, C., Havlínová, B., Vošahlíková, M., Tuckova, R., Lin, Z., Bařinka, C., Jamieson, S. M. F., Ware, D. C., & Hartinger, C. G. (2026) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6c02897

Epigenetic Control of Stress-Induced Depression: Emerging Roles of HDAC3 and HDAC6

Mohan, A. S., Narayanan, J., Kashid, V. A., Patel, R. J., & Prajapati, B. G. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27167313

A 2-in-1 Strategy for the Discovery of Compact HDAC8 Protac Degraders

Liu, Y., Awasthee, N., Xiao, Y., Hale, S. M., Hu, W., He, M. Y., Gour, A., Yang, W., Sharma, A., Kridel, R., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c01636

Innovative Strategies for Selective Inhibition of Histone Deacetylases

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Structural determinants of affinity and selectivity in the binding of inhibitors to histone deacetylase 6

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Drug Discovery for Histone Deacetylase Inhibition: Past, Present and Future of Zinc-Binding Groups

Pires, G. S., Tolomeu, H. V., Rodrigues, D. A., Lima, L. M., Fraga, C. A. M., & Pinheiro, P. D. S. M. (2025) · Pharmaceuticals · doi:10.3390/ph18040577 · Cited by 25 · see citing works

Histone deacetylases: structural determinants of inhibitor selectivity

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Design of Selective Histone Deacetylase Inhibitors: Rethinking Classical Pharmacophore

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