HDAC8 inhibition blocks SMC3 deacetylation and delays cell cycle progression without affecting cohesin-dependent transcription in MCF7 cancer cells

Mediator and cohesin connect gene expression and chromatin architecture

Kagey, M. H., Newman, J. J., Bilodeau, S., Zhan, Y., Orlando, D. A., van Berkum, N. L., Ebmeier, C. C., Goossens, J., Rahl, P. B., Levine, S. S., et al. (2010) · Nature · doi:10.1038/nature09380 · Cited by 1,939 · see citing works

An oestrogen-receptor-α-bound human chromatin interactome

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Cohesin: Its Roles and Mechanisms

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Pan-cancer network analysis identifies combinations of rare somatic mutations across pathways and protein complexes

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HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle

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The cohesin complex and its roles in chromosome biologyPreprint

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Eco1-Dependent Cohesin Acetylation During Establishment of Sister Chromatid Cohesion

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A Molecular Determinant for the Establishment of Sister Chromatid Cohesion

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

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Acetylation of Smc3 by Eco1 Is Required for S Phase Sister Chromatid Cohesion in Both Human and Yeast

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Cohesin-mediated interactions organize chromosomal domain architecture

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Recurrent mutations in multiple components of the cohesin complex in myeloid neoplasms

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A CTCF-independent role for cohesin in tissue-specific transcriptionPreprint

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CTCF and Cohesin: Linking Gene Regulatory Elements with Their Targets

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Cohesin-based chromatin interactions enable regulated gene expression within preexisting architectural compartments

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Acetylation site specificities of lysine deacetylase inhibitors in human cells

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Genetic alterations of the cohesin complex genes in myeloid malignancies

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Cohesin in cancer: chromosome segregation and beyond

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Leukemia-Associated Cohesin Mutants Dominantly Enforce Stem Cell Programs and Impair Human Hematopoietic Progenitor Differentiation

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Mutations in the cohesin complex in acute myeloid leukemia: clinical and prognostic implications

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Mutation Spectrum and Genotype-Phenotype Correlation in Cornelia de Lange Syndrome

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An Smc3 Acetylation Cycle Is Essential for Establishment of Sister Chromatid Cohesion

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Cohesin loss alters adult hematopoietic stem cell homeostasis, leading to myeloproliferative neoplasms

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Loss-of-function HDAC8 mutations cause a phenotypic spectrum of Cornelia de Lange syndrome-like features, ocular hypertelorism, large fontanelle and X-linked inheritance

Kaiser, F. J., Ansari, M., Braunholz, D., Gil‐Rodríguez, M. C., Decroos, C., Wilde, J. J., Fincher, C. T., Kaur, M., Bando, M., Amor, D. J., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu002 · Cited by 158 · see citing works

Global transcriptional disturbances underlie Cornelia de Lange syndrome and related phenotypes

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Dose-dependent role of the cohesin complex in normal and malignant hematopoiesis

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Hos1 Deacetylates Smc3 to Close the Cohesin Acetylation Cycle

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HDAC8 Inhibition Specifically Targets Inv(16) Acute Myeloid Leukemic Stem Cells by Restoring p53 Acetylation

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Enhanced RAD21 cohesin expression confers poor prognosis and resistance to chemotherapy in high grade luminal, basal and HER2 breast cancers

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Positive regulation of c-Myc by cohesin is direct, and evolutionarily conserved

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Cohesin, a chromatin engagement ring

Remeseiro, S., & Losada, A. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.10.013 · Cited by 97 · see citing works

Suppression of RAD21 gene expression decreases cell growth and enhances cytotoxicity of etoposide and bleomycin in human breast cancer cells

Atienza, J. M., Roth, R. B., Rosette, C., Smylie, K. J., Kammerer, S., Rehbock, J., Ekblom, J., & Denissenko, M. F. (2005) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-04-0241 · Cited by 96 · see citing works

Diverse Developmental Disorders from The One Ring: Distinct Molecular Pathways Underlie the Cohesinopathies

Horsfield, J. A., Print, C. G., & Mönnich, M. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00171 · Cited by 94 · see citing works

Cohesin in development and disease

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An Unbiased Approach To Identify Endogenous Substrates of “Histone” Deacetylase 8

Olson, D. E., Udeshi, N. D., Wolfson, N. A., Pitcairn, C. A., Sullivan, E. D., Jaffe, J. D., Svinkina, T., Natoli, T. E., Lü, X., Paulk, J., et al. (2014) · ACS Chemical Biology · doi:10.1021/cb500492r · Cited by 85 · see citing works

Hos1 Is a Lysine Deacetylase for the Smc3 Subunit of Cohesin

Xiong, B., Lu, S., & Gerton, J. L. (2010) · Current Biology · doi:10.1016/j.cub.2010.08.019 · Cited by 73 · see citing works

Cohesin gene mutations in tumorigenesis: from discovery to clinical significance

Solomon, D. A., Kim, J.-S., & Waldman, T. A. (2014) · BMB Reports · doi:10.5483/bmbrep.2014.47.6.092 · Cited by 63 · see citing works

HDAC8, A Potential Therapeutic Target for the Treatment of Malignant Peripheral Nerve Sheath Tumors (MPNST)

Lopez, G., Bill, K. L. J., Bid, H. K., Braggio, D., Constantino, D., Prudner, B., Zewdu, A., Batte, K., Lev, D., & Pollock, R. E. (2015) · PLOS ONE · doi:10.1371/journal.pone.0133302 · Cited by 60 · see citing works

Cohesin mutations in myeloid malignancies: underlying mechanisms

Leeke, B. J., Marsman, J., O'Sullivan, J. M., & Horsfield, J. A. (2014) · Experimental Hematology and Oncology · doi:10.1186/2162-3619-3-13 · Cited by 50 · see citing works

Gene Regulation by Cohesin in Cancer: Is the Ring an Unexpected Party to Proliferation?

Rhodes, J. M., McEwan, M. V., & Horsfield, J. A. (2011) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-11-0382 · Cited by 41 · see citing works

Cohesin and CTCF differentially regulate spatiotemporal runx1 expression during zebrafish development

Marsman, J., O’Neill, A. C., Kao, B., Rhodes, J. M., Meier, M., Antony, J., Mönnich, M., & Horsfield, J. A. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.11.007 · Cited by 38 · see citing works

Design, synthesis, and evaluation of hydroxamic acid-based molecular probes for in vivo imaging of histone deacetylase (HDAC) in brain.

Wang, C., Eessalu, T. E., Barth, V., Mitch, C. H., Wagner, F. F., Hong, Y., Neelamegam, R., Schroeder, F. A., Holson, E. B., Haggarty, S. J., et al. (2013) · Europe PMC (PubMed Central) · Cited by 34 · see citing works

A neural crest origin for cohesinopathy heart defects

Schuster, K., Leeke, B. J., Meier, M., Wang, Y., Newman, T. A. C., Burgess, S. M., & Horsfield, J. A. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv402 · Cited by 33 · see citing works

HDAC8-Mediated Epigenetic Reprogramming Plays a Key Role in Resistance to Anthrax Lethal Toxin–Induced Pyroptosis in Macrophages

Ha, S.-D., Han, C. Y., Reid, C., & Kim, S. O. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400420 · Cited by 32 · see citing works

Cohesin Is Required for Activation of MYC by Estradiol

McEwan, M. V., Eccles, M. R., & Horsfield, J. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049160 · Cited by 28 · see citing works

Hydroxamic Acid-Based Histone Deacetylase (HDAC) Inhibitors Can Mediate Neuroprotection Independent of HDAC Inhibition

Sleiman, S. F., Olson, D. E., Bourassa, M., Karuppagounder, S. S., Zhang, Y.-L., Gale, J., Wagner, F., Basso, M., Coppola, G., Pinto, J., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1010-14.2014 · Cited by 28 · see citing works

Cohesin modulates transcription of estrogen-responsive genes

Antony, J., Dasgupta, T., Rhodes, J. M., McEwan, M. V., Print, C. G., O'Sullivan, J. M., & Horsfield, J. A. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.12.011 · Cited by 21 · see citing works

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

Marek, M., Shaik, T. B., Heimburg, T., Chakrabarti, A., Lancelot, J., Ramos-Morales, E., Da Veiga, C., Kalinin, D., Melesina, J., Robaa, D., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01087 · Cited by 123 · see citing works

HDAC11 is a regulator of diverse immune functions

Yanginlar, C., & Logie, C. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2017.12.002 · Cited by 106 · see citing works

Hydrogen gas inhibits lung cancer progression through targeting SMC3

Wang, D., Wang, L., Zhang, Y., Zhao, Y., & Chen, G. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.05.055 · Cited by 101 · see citing works

Pathological Role of HDAC8: Cancer and Beyond

Kim, J. Y., Cho, H., Yoo, J. H., Kim, G. W., Jeon, Y. H., Lee, S. W., & Kwon, S. H. (2022) · Cells · doi:10.3390/cells11193161 · Cited by 79 · see citing works

HDAC8-dependent deacetylation of PKM2 directs nuclear localization and glycolysis to promote proliferation in hepatocellular carcinoma

Zhang, R., Shen, M., Wu, C., Chen, Y., Lu, J., Li, J., Zhao, L., Meng, H., Zhou, X., Huang, G., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03212-3 · Cited by 64 · see citing works

Unveiling the role of histone deacetylases in neurological diseases: focus on epilepsy

Cao, D., Zhou, X., Guo, Q., Xiang, M.-Y., Bao, M., He, B., & Mao, X. (2024) · Biomarker Research · doi:10.1186/s40364-024-00687-6 · Cited by 59 · see citing works

Non-Hydroxamate Zinc-Binding Groups as Warheads for Histone Deacetylases

Frühauf, A., & Meyer‐Almes, F. (2021) · Molecules · doi:10.3390/molecules26175151 · Cited by 58 · see citing works

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

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

Selective inhibition of histone deacetylase 3 by novel hydrazide based small molecules as therapeutic intervention for the treatment of cancer

Pulya, S., Patel, T. K., Paul, M., Adhikari, N., Banerjee, S., Routholla, G., Biswas, S., Jha, T., & Ghosh, B. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114470 · Cited by 55 · see citing works

Super-Enhancers, Phase-Separated Condensates, and 3D Genome Organization in Cancer

Tang, S., Vijayakumar, U., Zhang, Y., & Fullwood, M. (2022) · Cancers · doi:10.3390/cancers14122866 · Cited by 46 · see citing works

Characterization of Conformationally Constrained Benzanilide Scaffolds for Potent and Selective HDAC8 Targeting

Hassan, M. M., Israelian, J., Nawar, N., Ganda, G., Manaswiyoungkul, P., Raouf, Y. S., Armstrong, D. R., Sedighi, A., Olaoye, O. O., Erdogan, F., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01025 · Cited by 50 · see citing works

Cohesin mutations in myeloid malignancies

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Inhibition of histone deacetylase 11 promotes human liver cancer cell apoptosis.

Gong, D., Zeng, Z., Yi, F., & Wu, J. (2019) · Europe PMC (PubMed Central) · Cited by 47 · see citing works

miR‐483‐3p suppresses the proliferation and progression of human triple negative breast cancer cells by targeting the HDAC8>oncogene

Menbari, M., Rahimi, K., Ahmadi, A., Mohammadi‐Yeganeh, S., Elyasi, A., Darvishi, N., Hosseini, V., & Abdi, M. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29167 · Cited by 46 · see citing works

A Therapeutic Perspective of HDAC8 in Different Diseases: An Overview of Selective Inhibitors

Fontana, A., Cursaro, I., Carullo, G., Gemma, S., Butini, S., & Campiani, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231710014 · Cited by 47 · see citing works

Cohesin Mutations in Cancer: Emerging Therapeutic Targets

Antony, J., Chin, C. V., & Horsfield, J. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136788 · Cited by 43 · see citing works

Potent and Selective Non‐hydroxamate Histone Deacetylase 8 Inhibitors

Kleinschek, A., Meyners, C., Giorgio, E. D., Brancolini, C., & Meyer‐Almes, F. (2016) · ChemMedChem · doi:10.1002/cmdc.201600528 · Cited by 41 · see citing works

Cooperativity of HOXA5 and STAT3 Is Critical for HDAC8 Inhibition-Mediated Transcriptional Activation of PD-L1 in Human Melanoma Cells

Wang, Y. F., Liu, F., Sherwin, S. K., Farrelly, M. L., Yan, X. G., Croft, A. J., Liu, T., Jin, L., Zhang, X. D., & Jiang, C. C. (2017) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.11.009 · Cited by 41 · see citing works

HDAC8 affects MGMT levels in glioblastoma cell lines via interaction with the proteasome receptor ADRM1

Santos‐Barriopedro, I., Li, Y., Bahl, S., & Seto, E. (2019) · Genes & Cancer · doi:10.18632/genesandcancer.197 · Cited by 41 · see citing works

Azetidin-2-one-based small molecules as dual hHDAC6/HDAC8 inhibitors: Investigation of their mechanism of action and impact of dual inhibition profile on cell viability

Federico, S., Khan, T., Fontana, A., Brogi, S., Benedetti, R., Sarno, F., Carullo, G., Pezzotta, A., Saraswati, A. P., Passaro, E., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114409 · Cited by 37 · see citing works

HDAC8-mediated inhibition of EP300 drives a transcriptional state that increases melanoma brain metastasis

Emmons, M. F., Bennett, R. L., Riva, A., Gupta, K., Carvalho, L. A. D. C., Zhang, C., Macaulay, R. J. B., Dupéré-Richer, D., Fang, B., Seto, E., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43519-1 · Cited by 36 · see citing works

HDAC8 suppresses the epithelial phenotype and promotes EMT in chemotherapy-treated basal-like breast cancer

Pantelaiou‐Prokaki, G., Mieczkowska, I. K., Schmídt, G., Fritzsche, S., Prokakis, E., Gallwas, J. K. S., & Wegwitz, F. (2022) · Clinical Epigenetics · doi:10.1186/s13148-022-01228-4 · Cited by 35 · see citing works

HDAC8 Deacetylates HIF-1α and Enhances Its Protein Stability to Promote Tumor Growth and Migration in Melanoma

Kim, J. Y., Cho, H., Yoo, J. H., Kim, G. W., Jeon, Y. H., Lee, S. W., & Kwon, S. H. (2023) · Cancers · doi:10.3390/cancers15041123 · Cited by 30 · see citing works

Cohesin mutations are synthetic lethal with stimulation of WNT signaling

Chin, C. V., Antony, J., Ketharnathan, S., Labudina, A. A., Gimenez, G., Parsons, K. M., He, J.-S., George, A. J., Pallotta, M. M., Musio, A., et al. (2020) · eLife · doi:10.7554/elife.61405 · Cited by 30 · see citing works

Modeling Cornelia de Lange syndrome in vitro and in vivo reveals a role for cohesin complex in neuronal survival and differentiation

Bottai, D., Spreafico, M., Pistocchi, A., Fazio, G., Adami, R., Grazioli, P., Canu, A., Bragato, C., Rigamonti, S., Parodi, C., et al. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy329 · Cited by 29 · see citing works

Inhibitors of class I HDACs and of FLT3 combine synergistically against leukemia cells with mutant FLT3

Wachholz, V., Mustafa, A. M., Zeyn, Y., Henninger, S. J., Beyer, M., Dzulko, M., Piée‐Staffa, A., Brachetti, C., Haehnel, P. S., Sellmer, A., et al. (2021) · Archives of Toxicology · doi:10.1007/s00204-021-03174-1 · Cited by 28 · see citing works

Targeting Histone Deacetylases 6 in Dual-Target Therapy of Cancer

Beljkaš, M., Ilić, A., Čebzan, A., Radović, B., Djoković, N., Ružić, D., Nikolic, K. M., & Oljačić, S. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15112581 · Cited by 28 · see citing works

HDAC8 regulates neural differentiation through embryoid body formation in P19 cells

Katayama, S., Morii, A., Makanga, J. O., Suzuki, T., Miyata, N., & Inazu, T. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.02.195 · Cited by 27 · see citing works

Matairesinol, an active constituent of HC9 polyherbal formulation, exhibits HDAC8 inhibitory and anticancer activity

Mahajan, M., Suryavanshi, S., Bhowmick, S., Alasmary, F. A., Almutairi, T. M., Islam, M. A., & Kaul-Ghanekar, R. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106588 · Cited by 26 · see citing works

A cohesive look at leukemogenesis: The cohesin complex and other driving mutations in AML

Heimbruch, K. E., Meyer, A. E., Agrawal, P., Viny, A. D., & Rao, S. (2021) · Neoplasia · doi:10.1016/j.neo.2021.01.003 · Cited by 23 · see citing works

The clinical significance of histone deacetylase-8 in human breast cancer

Rahmani, G., Sameri, S., Abbasi, N., Abdi, M., & Najafi, R. (2021) · Pathology - Research and Practice · doi:10.1016/j.prp.2021.153396 · Cited by 22 · see citing works

Validation of HDAC8 Inhibitors as Drug Discovery Starting Points to Treat Acute Kidney Injury

Long, K. E., Vaughn, Z., McDaniels, M. D., Joyasawal, S., Przepiorski, A. J., Parasky, E., Sander, V., Close, D. A., Johnston, P. A., Davidson, A. J., et al. (2022) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.1c00243 · Cited by 20 · see citing works

Time-dependent effects of histone deacetylase inhibition in sepsis-associated acute kidney injury

Wen, X., Li, S., Frank, A., Chen, X., Emlet, D. R., Hukriede, N. A., & Kellum, J. A. (2020) · Intensive Care Medicine Experimental · doi:10.1186/s40635-020-0297-3 · Cited by 18 · see citing works

Mechanistic Insights into the Anti-Proliferative Action of Gut Microbial Metabolites against Breast Adenocarcinoma Cells

Jaye, K. M., Alsherbiny, M. A., Chang, D., Li, C. G., & Bhuyan, D. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015053 · Cited by 15 · see citing works

HDAC8 Prevents Anthrax Lethal Toxin-induced Cell Cycle Arrest through Silencing PTEN in Human Monocytic THP-1 Cells

Ha, S.-D., Cho, W., & Kim, S. O. (2017) · Toxins · doi:10.3390/toxins9050162 · Cited by 15 · see citing works

Reversible acetylation of HDAC8 regulates cell cycle

Sang, C.-W., Li, X., Liu, J., Chen, Z., Xia, M., Yu, M., & Yu, W. (2024) · EMBO Reports · doi:10.1038/s44319-024-00210-w · Cited by 14 · see citing works

One ring to bind them – Cohesin’s interaction with chromatin fibers

Gines, M. M., van Staveren, T., & Wendt, K. S. (2019) · Essays in Biochemistry · doi:10.1042/ebc20180064 · Cited by 12 · see citing works

Ssu72 Dual-Specific Protein Phosphatase: From Gene to Diseases

Hwang, S.-H., Kim, M.-H., & Lee, C.-W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073791 · Cited by 12 · see citing works

MicroRNA-mediated epigenetic regulation of HDAC8 and HDAC6: Functional significance in cervical cancer

Naik, D., & Kalle, A. M. (2024) · Non-coding RNA Research · doi:10.1016/j.ncrna.2024.02.009 · Cited by 11 · see citing works

Combined HDAC8 and checkpoint kinase inhibition induces tumor-selective synthetic lethality in preclinical models

Chang, T.-Y., Yan, Y., Yu, Z.-Y., Rathore, M. G., Lee, N.-Z., Tseng, H.-J., Cheng, L.-H., Huang, W., Zhang, W., Chan, E. R., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci165448 · Cited by 11 · see citing works

Regulation of the mitotic chromosome folding machines

Dekker, B., & Dekker, J. (2022) · Biochemical Journal · doi:10.1042/bcj20210140 · Cited by 11 · see citing works

Structural isomers of cinnamic hydroxamic acids block HCV replication via different mechanisms

Kozlov, M. V., Konduktorov, K. A., Malikova, A. Z., Kamarova, K. A., Shcherbakova, A. S., Solyev, P. N., & Kochetkov, S. N. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111723 · Cited by 11 · see citing works

Identification of drug targets and potential molecular mechanisms for Wantong Jingu Tablet extract in treatment of rheumatoid arthritis: bioinformatics analysis of fibroblast-like synoviocytes

Li, Z., Qi, F., & Li, F. (2020) · Chinese Medicine · doi:10.1186/s13020-020-00339-5 · Cited by 10 · see citing works

Methionine 274 Is Not the Determining Factor for Selective Inhibition of Histone Deacetylase 8 (HDAC8) by L-Shaped Inhibitors

Jänsch, N., Lang, K. L., & Meyer‐Almes, F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911775 · Cited by 8 · see citing works

Securin acetylation prevents precocious separase activation and premature sister chromatid separation

Wang, T., Zou, Y., Meng, H., Zheng, P., Teng, J., Huang, N., & Chen, J. (2024) · Current Biology · doi:10.1016/j.cub.2024.02.038 · Cited by 7 · see citing works

Improved Pharmacokinetic Profiles of HDAC6 Inhibitors via Cap Group Modifications

Olaoye, O. O., Erdogan, F., Gracia-Hernandez, M., Garcha, H. K., Sedighi, A., Ashraf, Q. F., Nawar, N., Geletu, M., Seo, H., Abdallah, D. I., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00479 · Cited by 7 · see citing works

Design, synthesis, and biological evaluation of substituted benzyl-triazolopyridine derivatives as non-hydroxamate based HDAC8 inhibitors

Bandaru, N. V. M. R., Fathima, A., Joshi, V., Schweipert, M., Pathur, O., Chaitanya, K. S., Trinath, J., Sharma, V., Abbineni, C., Meyer‐Almes, F., et al. (2025) · European Journal of Medicinal Chemistry Reports · doi:10.1016/j.ejmcr.2025.100255 · Cited by 3 · see citing works

ZNF521 promotes acute myeloid leukemogenesis by suppressing the expression and acetylation of SMC3

Qin, R., Yang, T., Jiang, H., & Yu, M. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e37528 · Cited by 3 · see citing works

Differential effects of HDAC8 targeting on Foxp3+ Tregs and effector T cells promote antitumor immunity

Kong, F., Xiong, Y., Wang, L., Han, R., Fazelinia, H., Roof, J., Spruce, L. A., Beeler, A. B., & Hancock, W. W. (2025) · JCI Insight · doi:10.1172/jci.insight.186461 · Cited by 1 · see citing works

Targeted HDAC8 inhibition with non-hydroxamate [1,2,4]triazolo[4,3-a] quinoline compounds

Bandaru, N. V. M. R., Fathima, A., Sengar, S., Schweipert, M., Chaitanya, K. S., Mohammed, M.-U.-R., Gore, S. T., Trinath, J., Sharma, V., Abbineni, C., et al. (2026) · Scientific Reports · doi:10.1038/s41598-026-38490-y · Cited by 1 · see citing works

The histone deacetylase family in health and disease

Wen, R., Yang, Y., Zhang, T., Zhang, S.-Y., Yang, X.-R., Zhang, L.-Y., Hao, P.-H., Zheng, Y., Ni, Y., & Zhang, T. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02764-8 · Cited by 1 · see citing works

Comparative analysis of differentially acetylated proteins between Antarctic white‐blooded Chionodraco hamatus and red‐blooded Trematomus bernacchii

Jia, R., Zhai, W., Huang, S., Chen, B., Hu, R., Jiang, S., & Xu, Q. (2025) · Journal of Fish Biology · doi:10.1111/jfb.70203 · Cited by 1 · see citing works

HDAC8-mediated inhibition of EP300 drives a neural crest-like transcriptional state that increases melanoma brain metastasisPreprint

Emmons, M. F., Bennett, R. L., Riva, A., Zhang, C., Macaulay, R. J. B., Dupéré-Richer, D., Fang, B., Seto, E., Koomen, J. M., Li, J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.12.511971 · Cited by 1 · see citing works

Silencing NDC80, RAD21 and BUB1B ameliorates intervertebral disc degeneration by promoting proliferation and inhibiting apoptosis of nucleus pulposus cellsPreprint

Zhang, B., Guan, Y., Liu, W., Guo, W. M., Peng, P., Xing, C., Huang, J., Sun, C., Ruan, W., Ning, G., et al. (2020) · doi:10.21203/rs.3.rs-31592/v1

Knockout of histone deacetylase 8 gene in breast cancer cells may alter the expression pattern of the signaling molecules

Bahrami, N., & Abdi, M. (2024) · Advances in Medical Sciences · doi:10.1016/j.advms.2024.10.003

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

Shared transcriptional signatures between rheumatoid arthritis and lung cancer: a multi-cohort machine learning study identifies CKS2 as a candidate cell cycle marker associated with poor prognosis in lung cancer

Yang, M., Zhang, N., Zha, P., Liu, T., Yang, X., Wu, Y., Zhao, W., Luo, T., Huang, X., Li, W., et al. (2026) · Journal Of Big Data · doi:10.1186/s40537-026-01405-9

Biochemical, biophysical and structural study of proteins associated to human diseases : tcDAC2 and ADAT complex

Ramos‐Morales, E. (2021) · theses.fr (ABES) · doi:10.70675/c6b28473zf6b6z4024z99bfz05629f0484d7

Étude de la restauration de la réponse immunitaire antitumorale dans un modèle murin de cancer pulmonaire induit par une molécule multicible inhibitrice de HDAC et du splicéosome

Ducellier, S. (2023) · doi:10.70675/cb4b0dd4z634bz4299z96a9z469b89375839

A new class of indole-based HDAC8 inhibitors as potential anti-lung cancer agents: in silico design, synthesis, biological assessment and binding interaction analysis

Khatun, S., Muthukumar, V., Himaja, A., Dasgupta, I., Das, K., Ghosh, B., & Gayen, S. (2026) · RSC Medicinal Chemistry · doi:10.1039/d6md00194g

Glucose-6-phosphate dehydrogenase variants modify 3D genomic organization to suppress maladaptive gene expression and vascular disease

Signoretti, C., Matsumura, S., D’silva, M., Williams, C., Marshall, B., Fatehi, S., Drewes, R., Grier, A., Dzieciątkowska, M., D'Alessandro, A., et al. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113204

Evaluation of HDAC8 as a Druggable Target in STAG2 -Mutant Ewing Sarcoma

Olaoye, O. O., Xiong, Y., Rillahan, C. D., Adane, B., DiGiovanni, G., Ross, K. N., Alexe, G., Howard, B., Kirmani, N., Nowak, R. P., et al. (2026) · ACS Chemical Biology · doi:10.1021/acschembio.6c00345

BindingDB Entry 50001930: Characterization of Histone Deacetylase 8 (HDAC8) Selective Inhibition Reveals Specific Active Site Structural and Functional Determinants.

BindingDB (2020) · UC San Diego · doi:10.7270/q2vm4ft7

BindingDB Entry 50016065: Azetidin-2-one-based small molecules as dual hHDAC6/HDAC8 inhibitors: Investigation of their mechanism of action and impact of dual inhibition profile on cell viability.

BindingDB (2023) · UC San Diego · doi:10.7270/q2nc655w

BindingDB Entry 50010799: Characterization of Conformationally Constrained Benzanilide Scaffolds for Potent and Selective HDAC8 Targeting.

BindingDB (2021) · UC San Diego · doi:10.7270/q2cc1470

BindingDB Entry 50016088: Selective inhibition of histone deacetylase 3 by novel hydrazide based small molecules as therapeutic intervention for the treatment of cancer.

BindingDB (2023) · UC San Diego · doi:10.7270/q2fn1b6d

The tumor suppressive role of TFF (trefoil factor family) in pancreatic carcinogenesis

Yamaguchi, J., Yokoyama, Y., Kokuryo, T., & Nagino, M. (2016) · Pancreatology · doi:10.1016/j.pan.2016.06.230

Hos1 Deacetylates Smc3 to Close the Cohesin Acetylation Cycle

Borges, V., Lehane, C., Lopez‐Serra, L., Flynn, H. R., Skehel, M. J., Ben-Shahar, T. R., & Uhlmann, F. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.009 · Cited by 119 · see citing works

Hos1 Is a Lysine Deacetylase for the Smc3 Subunit of Cohesin

Xiong, B., Lu, S., & Gerton, J. L. (2010) · Current Biology · doi:10.1016/j.cub.2010.08.019 · Cited by 73 · see citing works

HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle

Deardorff, M. A., Bando, M., Nakato, R., Watrin, E., Itoh, T., Minamino, M., Saitoh, K., Komata, M., Katou, Y., Clark, D., et al. (2012) · Nature · doi:10.1038/nature11316 · Cited by 577 · see citing works

Oestrogen-dependent regulation of gene expression by cohesin in breast cancer

Dasgupta, T. (2015) · Otago University Research Archive (University of Otago)