The DOI matches its Crossref record; 123 of the 131 references it cites were found in a registry or an index.
HDAC family: What are the cancer relevant targets?
Abstract
Histone deacetylases comprise a family of 18 genes, which are grouped into classes I-IV based on their homology to their respective yeast orthologues. Classes I, II, and IV consist of 11 family members, which are referred to as "classical" HDACs, whereas the 7 class III members are called sirtuins. Classical HDACs are a promising novel class of anti-cancer drug targets. First HDAC inhibitors have been evaluated in clinical trials and show activity against several cancer diseases. However, these compounds act unselectively against several or all 11 HDAC family members. As a consequence, clinical phase I trials document a wide range of side effects. Therefore, the current challenge in the field is to define the cancer relevant HDAC family member(s) in a given tumor type and to design selective inhibitors, which target cancer cells but leave out normal cells. Knockout of single HDAC family members in mice produces a variety of phenotypes ranging from early embryonic death to viable animals with only discrete alterations, indicating that potential side effects of HDAC inhibitors depend on the selectivity of the compounds. Recently, several studies have shown that certain HDAC family members are aberrantly expressed in several tumors and have non-redundant function in controlling hallmarks of cancer cells. The aim of this review is to discuss individual HDAC family members as drug targets in cancer taking into consideration their function under physiological conditions and their oncogenic potential in malignant disease.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Unlike other histone deacetylases, inhibition of HDAC6 does not appear to be associated with any toxicity, making it an excellent drug target.7”
From Rational Design and Simple Chemistry Yield a Superior, Neuroprotective HDAC6 Inhibitor, Tubastatin A (2010) · cites this paper as [7]
Citations
Cites
1 retracted
Pulukuri, S. M. K., Gorantla, B., & Rao, J. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705867200 · Cited by 51
RetractedThe Consensus Coding Sequences of Human Breast and Colorectal Cancers
Sjöblom, T., Jones, S., Wood, L. D., Parsons, D. W., Lin, J., Barber, T. D., Mandelker, D. L., Leary, R. J., Ptak, J., Silliman, N., et al. (2006) · Science · doi:10.1126/science.1133427 · Cited by 3,161
Histone deacetylases (HDACs): characterization of the classical HDAC family
RUIJTER, A. J. M. D., GENNIP, A. H. V., CARON, H. N., KEMP, S., & KUILENBURG, A. B. P. V. (2003) · Biochemical Journal · doi:10.1042/bj20021321 · Cited by 3,114
Anticancer activities of histone deacetylase inhibitors
Bolden, J. E., Peart, M. J., & Johnstone, R. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2133 · Cited by 2,919
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,234
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714
Kawaguchi, Y., Kovacs, J. J., McLaurin, A. C., Vance, J. M., Ito, A., & Yao, T. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,529
Flagged first, then by citations
8 of the 131 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Li, 2008, HDAC6 is required for EGF-induced β-catenin nuclear localization, J. Biol. Chem.
Cited by
Sorted by citations
Godoy, P., Hewitt, N. J., Albrecht, U., Andersen, M. E., Ansari, N., Bhattacharya, S., Bode, J. G., Bolleyn, J., Borner, C., Böttger, J., et al. (2013) · Archives of Toxicology · doi:10.1007/s00204-013-1078-5 · Cited by 1,280
Oral squamous cell carcinomas: state of the field and emerging directions
Tan, Y., Wang, Z., Xu, M., Li, B., Huang, Z., Qin, S., Nice, E. C., Tang, J., & Huang, C. (2023) · International Journal of Oral Science · doi:10.1038/s41368-023-00249-w · Cited by 965
Rational Design and Simple Chemistry Yield a Superior, Neuroprotective HDAC6 Inhibitor, Tubastatin A
Butler, K. V., Kalin, J., Brochier, C., Vistoli, G., Langley, B., & Kozikowski, A. P. (2010) · Journal of the American Chemical Society · doi:10.1021/ja102758v · Cited by 801
The world of protein acetylation
Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 847
Pan, S.-Y., Zhou, S.-F., Gao, S.-H., Yu, Z., Zhang, S.-F., Tang, M.-K., Sun, J.-N., Ma, D., Han, Y., Fong, W. F., et al. (2013) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2013/627375 · Cited by 750
Sato, F., Tsuchiya, S., Meltzer, S. J., & Shimizu, K. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08089.x · Cited by 604
Mihaylova, M. M., Vasquez, D. S., Ravnskjaer, K., Denechaud, P.-D., Yu, R. T., Alvarez, J. G., Downes, M., Evans, R. M., Montminy, M., & Shaw, R. J. (2011) · Cell · doi:10.1016/j.cell.2011.03.043 · Cited by 533
Delcuve, G. P., Khan, D. H., & Davie, J. R. (2012) · Clinical Epigenetics · doi:10.1186/1868-7083-4-5 · Cited by 505
Epigenetics in cancer: Targeting chromatin modifications
Ellis, L., Atadja, P. W., & Johnstone, R. W. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0860 · Cited by 488
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
Nepali, K., Sharma, S., Sharma, M., Bedi, P. M. S., & Dhar, K. L. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.03.018 · Cited by 445
Role of Zinc in Immune System and Anti-Cancer Defense Mechanisms
Skrajnowska, D., & Bobrowska‐Korczak, B. (2019) · Nutrients · doi:10.3390/nu11102273 · Cited by 441
Targeted Cancer Therapy: Giving Histone Deacetylase Inhibitors All They Need To Succeed
Gryder, B. E., Sodji, Q. H., & Oyelere, A. K. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.3 · Cited by 404
Selective in vivo metabolic cell-labeling-mediated cancer targeting
Wang, H., Wang, R., Cai, K., He, H., Liu, Y., Yen, J. S., Wang, Z., Xu, M., Sun, Y., Zhou, X., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2297 · Cited by 392
Post-translational modifications of tubulin: pathways to functional diversity of microtubules
Song, Y., & Brady, S. T. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.10.004 · Cited by 377
Indole in the target-based design of anticancer agents: A versatile scaffold with diverse mechanisms
Dadashpour, S., & Emami, S. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.02.065 · Cited by 353
Histone deacetylase 6 plays a role as a distinct regulator of diverse cellular processes
Li, Y., Shin, D., & Kwon, S. H. (2012) · FEBS Journal · doi:10.1111/febs.12079 · Cited by 351
HDAC6 as a target for neurodegenerative diseases: what makes it different from the other HDACs?
Simões-Pires, C., Zwick, V., Nurisso, A., Schenker, E., Carrupt, P.-A., & Cuendet, M. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-7 · Cited by 341
Histone deacetylase 6 in cancer
Li, T., Zhang, C., Hassan, S., Liu, X., Song, F., Chen, K., Zhang, W., & Yang, J. (2018) · Journal of Hematology & Oncology · doi:10.1186/s13045-018-0654-9 · Cited by 337
Inside HDACs with more selective HDAC inhibitors
Roche, J., & Bertrand, P. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.05.047 · Cited by 327
HDAC inhibitor‐based therapies: Can we interpret the code?
New, M. I., Olzscha, H., & Thangue, N. B. L. (2012) · Molecular Oncology · doi:10.1016/j.molonc.2012.09.003 · Cited by 315
MicroRNA epigenetic signatures in human disease
Piletič, K., & Kunej, T. (2016) · Archives of Toxicology · doi:10.1007/s00204-016-1815-7 · Cited by 304
The Redox Basis of Epigenetic Modifications: From Mechanisms to Functional Consequences
Cyr, A. R., & Domann, F. E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3492 · Cited by 301
HDAC8: a multifaceted target for therapeutic interventions
Chakrabarti, A., Oehme, I., Witt, O., Oliveira, G., Sippl, W., Romier, C., Pierce, R. J., & Jung, M. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.04.013 · Cited by 284
Self-citationTarget engagement and drug residence time can be observed in living cells with BRET
Robers, M. B., Dart, M. L., Woodroofe, C. C., Zimprich, C., Kirkland, T. A., Machleidt, T., Kupcho, K. R., Levin, S., Hartnett, J. R., Zimmerman, K., et al. (2015) · Nature Communications · doi:10.1038/ncomms10091 · Cited by 281
Ocio, E. M., Richardson, P. G. G., Rajkumar, S. V., Palumbo, A. P., Mateos, M., Orlowski, R. Z., Kumar, S. K., Usmani, S. Z., Roodman, D., Niesvizky, R., et al. (2013) · Leukemia · doi:10.1038/leu.2013.350 · Cited by 239
Safa, A. R., Saadatzadeh, M. R., Cohen‐Gadol, A., Pollok, K. E., & Bijangi‐Vishehsaraei, K. (2015) · Genes & Diseases · doi:10.1016/j.gendis.2015.02.001 · Cited by 230
Inhibitors of histone deacetylase as antitumor agents: A critical review
Mohammed, M., Chandrasekar, M., Jeyapal, G. P., & Nanjan, M. J. (2016) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2016.05.005 · Cited by 231
Isoform-specific histone deacetylase inhibitors: The next step?
Balasubramanian, S., Verner, E. J., & Buggy, J. J. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.02.013 · Cited by 228
Targeting Histone Deacetylases with Natural and Synthetic Agents: An Emerging Anticancer Strategy
Singh, A. K., Bishayee, A., & Pandey, A. K. (2018) · Nutrients · doi:10.3390/nu10060731 · Cited by 229
Molecular hybridization: a powerful tool for multitarget drug discovery
Pinheiro, P. D. S. M., Franco, L. S., Montagnoli, T. L., & Fraga, C. A. M. (2024) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2024.2322990 · Cited by 230
Histone deacetylase 10 promotes autophagy-mediated cell survival
Oehme, I., Linke, J.-P., Böck, B. C., Milde, T., Lodrini, M., Hartenstein, B., Wiegand, I., Eckert, C., Roth, W., Kool, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300113110 · Cited by 221
Self-citationHistone Deacetylase 6 in Health and Disease
Seidel, C., Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2015) · Epigenomics · doi:10.2217/epi.14.69 · Cited by 219
Buurman, R., Gürlevik, E., Schäffer, V., Eilers, M., Sandbothe, M., Kreipe, H. H., Wilkens, L., Schlegelberger, B., Kühnel, F., & Skawran, B. (2012) · Gastroenterology · doi:10.1053/j.gastro.2012.05.033 · Cited by 211
Moreno, D. A., Scrideli, C. A., Cortez, M. A. A., De Paula Queiroz, R., Valera, E. T., Da Silva Silveira, V., Yunes, J. A., Brandalise, S. R., & Tone, L. G. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08301.x · Cited by 208
Milde, T., Oehme, I., Korshunov, A., Kopp‐Schneider, A., Remke, M., Northcott, P. A., Deubzer, H. E., Lodrini, M., Taylor, M. D., von Deimling, A., et al. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-0395 · Cited by 192
Self-citationThree-Dimensional Cell Growth Confers Radioresistance by Chromatin Density Modification
Storch, K., Eke, I., Borgmann, K., Krause, M., Richter, C., Becker, K., Schröck, E., & Cordes, N. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3848 · Cited by 197
Pipalia, N. H., Cosner, C. C., Huang, A., Chatterjee, A., Bourbon, P., Farley, N., Helquist, P., Wiest, O., & Maxfield, F. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014890108 · Cited by 180
Marek, L., Hamacher, A., Hansen, F. K., Kuna, K., Gohlke, H., Kassack, M. U., & Kurz, T. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301254q · Cited by 185
CASTILHO, R. M., SQUARIZE, C. H., & Almeida, L. O. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071506 · Cited by 187
Rettig, I., Koeneke, E., Trippel, F., Mueller, W. C., Burhenne, J., Kopp‐Schneider, A., Fabian, J., Schober, A., Fernekorn, U., von Deimling, A., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.24 · Cited by 184
Self-citationDriver mutations of cancer epigenomes
Roy, D. M., Walsh, L. A., & Chan, T. A.-T. (2014) · Protein & Cell · doi:10.1007/s13238-014-0031-6 · Cited by 188
Yuan, J., Yang, F., Chen, B.-F., Lu, Z. J., Huo, X., Zhou, W., Wang, F., & Sun, S. (2010) · Hepatology · doi:10.1002/hep.24606 · Cited by 182
Histone Deacetylase Inhibitors In The Treatment Of Cancer: Overview And Perspectives
Giannini, G., Cabri, W., Fattorusso, C., & Rodriquez, M. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.80 · Cited by 182
Dysregulated Class I histone deacetylases are indicators of poor prognosis in multiple myeloma
Mithraprabhu, S., Kalff, A., Chow, A. L., Khong, T. T., & Spencer, A. G. (2014) · Epigenetics · doi:10.4161/15592294.2014.983367 · Cited by 180
Histone deacetylase inhibitors facilitate partner preference formation in female prairie voles
Wang, H., Duclot, F., Liu, Y., Wang, Z., & Kabbaj, M. (2013) · Nature Neuroscience · doi:10.1038/nn.3420 · Cited by 173
Parbin, S., Kar, S., Shilpi, A., Sengupta, D., Deb, M., Rath, S. K., & Patra, S. K. (2013) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155413506582 · Cited by 174
Development of chidamide for peripheral T-cell lymphoma, the first orphan drug approved in China
Lu, X., Ning, Z., Li, Z., Cao, H., & Wang, X. (2016) · Intractable & Rare Diseases Research · doi:10.5582/irdr.2016.01024 · Cited by 172
Zhang, D., Wu, C.-T., Qi, X., Meijering, R. A. M., Hoogstra‐Berends, F., Tadevosyan, A., Deniz, G. Ç., Durdu, S., Akar, A. R., Sibon, O. C. M., et al. (2013) · Circulation · doi:10.1161/circulationaha.113.005300 · Cited by 177
HDAC inhibitors and immunotherapy; a double edged sword?
Kroesen, M., Gielen, P. R., Brok, I. C., Armandari, I., Hoogerbrugge, P. M., & Adema, G. J. (2014) · Oncotarget · doi:10.18632/oncotarget.2289 · Cited by 168
Epigenetic regulation in mammalian preimplantation embryo development
Shi, L., & Wu, J. (2009) · Reproductive Biology and Endocrinology · doi:10.1186/1477-7827-7-59 · Cited by 166
Regulating the Regulators: The Post‐Translational Code of Class I HDAC1 and HDAC2
Segré, C. V., & Chiocca, S. (2010) · BioMed Research International · doi:10.1155/2011/690848 · Cited by 166
Histone deacetylase inhibitors suppress mutant p53 transcription via histone deacetylase 8
Yan, W., Liu, S., Xu, E., Zhang, J., Zhang, Y., Chen, X., & Chen, X. (2013) · Oncogene · doi:10.1038/onc.2012.81 · Cited by 153
Schrump, D. S. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2787 · Cited by 153
Hdac7 promotes lung tumorigenesis by inhibiting Stat3 activation
Lei, Y., Liu, L., Zhang, S., Guo, S., Li, X., Wang, J., Su, B., Fang, Y., Chen, X., Ke, H., et al. (2017) · Molecular Cancer · doi:10.1186/s12943-017-0736-2 · Cited by 152
Epigenetics and MicroRNAs in Cancer
Ramassone, A., Pagotto, S., Veronese, A., & Visone, R. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020459 · Cited by 152
Paino, F., Noce, M. L., Tirino, V., Naddeo, P., Desiderio, V., Pirozzi, G., ROSA, A. D., Laino, L., Altucci, L., & Papaccio, G. (2013) · Stem Cells · doi:10.1002/stem.1544 · Cited by 148
Koshikawa, N., Hayashi, J.-I., Nakagawara, A., & Takenaga, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.054221 · Cited by 147
Roles of Histone Deacetylases and Inhibitors in Anticancer Therapy
Verza, F. A., Das, U., Fachin, A. L., Dimmock, J. R., & Marins, M. (2020) · Cancers · doi:10.3390/cancers12061664 · Cited by 149
Aberrant expression and activity of histone deacetylases in sporadic idiopathic pulmonary fibrosis
Korfei, M., Skwarna, S., Henneke, I., MacKenzie, B., Klymenko, O., Saito, S., Ruppert, C., von der Beck, D., Mahavadi, P., Klepetko, W., et al. (2015) · Thorax · doi:10.1136/thoraxjnl-2014-206411 · Cited by 144
Histone Modifications in Senescence-Associated Resistance to Apoptosis by Oxidative Stress
Sanders, Y. Y., Liu, H., Zhang, X., Hecker, L., Bernard, K., Desai, L., Liu, G., & Thannickal, V. J. (2013) · Redox Biology · doi:10.1016/j.redox.2012.11.004 · Cited by 138
Histone Deacetylase Inhibition and Dietary Short-Chain Fatty Acids
Licciardi, P. V., Ververis, K., & Karagiannis, T. C. (2011) · ISRN Allergy · doi:10.5402/2011/869647 · Cited by 145
Histone deacetylase (HDAC) inhibitors reduce the glial inflammatory response in vitro and in vivo
Faraco, G., Pittelli, M. G., Cavone, L., Fossati, S., Porcu, M., Mascagni, P., Fossati, G., Moroni, F., & Chiarugi, A. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.07.019 · Cited by 141
Novotny‐Diermayr, V., Sangthongpitag, K., Hu, C. Y., Wu, X., Sausgruber, N., Yeo, P., Greicius, G., Pettersson, S., Liang, A. L., Loh, Y. K., et al. (2010) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0689 · Cited by 138
Development and therapeutic impact of HDAC6-selective inhibitors
Dallavalle, S., Pisano, C., & Zunino, F. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.06.014 · Cited by 137
Fiegler, N., Textor, S., Arnold, A., Rölle, A., Oehme, I., Breuhahn, K., Moldenhauer, G., Witzens‐Harig, M., & Cerwenka, A. (2013) · Blood · doi:10.1182/blood-2013-02-482513 · Cited by 135
Self-citationVenkataramani, V., Rossner, C., Iffland, L., Schweyer, S., Tamboli, I. Y., Walter, J., Wirths, O., & Bayer, T. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.057836 · Cited by 133
Song, C., Zhu, S., Wu, C., & Kang, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.498758 · Cited by 133
Milde, T., Lodrini, M., Savelyeva, L., Korshunov, A., Kool, M., Brueckner, L. M., Antunes, A. S. L. M., Oehme, I., Pekrun, A., Pfister, S. M., et al. (2012) · Journal of Neuro-Oncology · doi:10.1007/s11060-012-0978-1 · Cited by 139
Self-citationJung, K. H., Noh, J. H., Kim, J. K., Eun, J. W., Bae, H. J., Xie, H. J., Chang, Y. G., Kim, M., Park, H., Lee, J. Y., et al. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24090 · Cited by 135
Development and Therapeutic Implications of Selective Histone Deacetylase 6 Inhibitors
Kalin, J. H., & Bergman, J. A. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4001659 · Cited by 131
Targeting Histone Deacetylases in Diseases: Where Are We?
Benedetti, R., Conte, M., & Altucci, L. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5776 · Cited by 129
Revisit dietary fiber on colorectal cancer: butyrate and its role on prevention and treatment
Encarnação, J. C., Abrantes, A. M., Pires, A. S., & Botelho, M. F. (2015) · Cancer and Metastasis Reviews · doi:10.1007/s10555-015-9578-9 · Cited by 126
Regulation of microRNAs by epigenetics and their interplay involved in cancer
Liu, X., Chen, X., Yu, X., Tao, Y., Bode, A. M., Dong, Z., & Cao, Y. (2013) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/1756-9966-32-96 · Cited by 125
Wagner, F. F., Olson, D. E., Gale, J. P., Kaya, T., Weïwer, M., Aidoud, N., Thomas, M., Davoine, E. L., Lemercier, B. C., Zhang, Y., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301355j · Cited by 121
Felice, C., Lewis, A., Armuzzi, A., Lindsay, J., & Silver, A. R. (2014) · Alimentary Pharmacology & Therapeutics · doi:10.1111/apt.13008 · Cited by 120
Matus, D. Q., Lohmer, L. L., Kelley, L. C., Schindler, A. J., Kohrman, A. Q., Barkoulas, M., Zhang, W., Chi, Q., & Sherwood, D. R. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.10.002 · Cited by 119
Jeong, J. B., Choi, J., Lou, Z., Jiang, X., & Lee, S. (2013) · International Immunopharmacology · doi:10.1016/j.intimp.2013.04.006 · Cited by 121
Strategies To Design Selective Histone Deacetylase Inhibitors
Melesina, J., Simoben, C. V., Praetorius, L., Bülbül, E. F., Robaa, D., & Sippl, W. (2021) · ChemMedChem · doi:10.1002/cmdc.202000934 · Cited by 118
MiR-145 functions as a tumor suppressor by directly targeting histone deacetylase 2 in liver cancer
Noh, J. H., Chang, Y. G., Kim, M. G., Jung, K. H., Kim, J. K., Bae, H. J., Eun, J. W., Shen, Q., Kim, S.-J., Kwon, S. H., et al. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.03.003 · Cited by 102
Cancer metabolism: New insights into classic characteristics
Kato, Y., Maeda, T., Suzuki, A., & Baba, Y. (2017) · Japanese Dental Science Review · doi:10.1016/j.jdsr.2017.08.003 · Cited by 121
Histone Acetylation Modifiers in the Pathogenesis of Alzheimer’s Disease
Lu, X., Wang, L., Yu, C., Yu, D., & Yu, G. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00226 · Cited by 124
Targeting histone acetylation in pulmonary hypertension and right ventricular hypertrophy
Chelladurai, P., Boucherat, O., Stenmark, K. R., Kracht, M., Seeger, W., Bauer, U., Bonnet, S., & Pullamsetti, S. S. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14932 · Cited by 117
Commensal microbiota regulates T cell fate decision in the gut
Furusawa, Y., Obata, Y., & Hase, K. (2014) · Seminars in Immunopathology · doi:10.1007/s00281-014-0455-3 · Cited by 121
Xie, H. J., Noh, J. H., Kim, J. K., Jung, K. H., Eun, J. W., Bae, H. J., Kim, M., Chang, Y. G., Lee, J. Y., Park, H., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034265 · Cited by 117
Rodrigues, D. A., Ferreira‐Silva, G. Á., Ferreira, A. C. S., Fernandes, R. A., Kwee, J. K., Sant’Anna, C. M. R., Ionta, M., & Fraga, C. A. M. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01525 · Cited by 116
Histone deacetylase 8 (HDAC8) and its inhibitors with selectivity to other isoforms: An overview
Banerjee, S., Adhikari, N., Amin, S. A., & Jha, T. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.12.039 · Cited by 114
HDAC11 is a novel drug target in carcinomas
Deubzer, H. E., Schier, M. C., Oehme, I., Lodrini, M., Haendler, B., Sommer, A., & Witt, O. (2013) · International Journal of Cancer · doi:10.1002/ijc.27876 · Cited by 112
Self-citationTargeting Histone Deacetylase 8 as a Therapeutic Approach to Cancer and Neurodegenerative Diseases
Chakrabarti, A., Melesina, J., Kolbinger, F. R., Oehme, I., Senger, J., Witt, O., Sippl, W., & Jung, M. (2016) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0117 · Cited by 111
Self-citationCahill, N., Bergh, A.-C., Kanduri, M., Göransson‐Kultima, H., Mansouri, L., Isaksson, A., Ryan, F., Smedby, K. E. E., Juliusson, G., Sundström, C., et al. (2012) · Leukemia · doi:10.1038/leu.2012.245 · Cited by 111
Inhibition of HDAC1 and DNMT1 Modulate RGS10 Expression and Decrease Ovarian Cancer Chemoresistance
Çaçan, E., Ali, M. W., Boyd, N., Hooks, S. B., & Greer, S. F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087455 · Cited by 110
Protomártir, M. C., Garcia-Alberich, C., Blasco-Angulo, N., Vall‐llaura, N., Nàger, M., Herreros, J., Comella, J. X., Sanchı́s, D., & Llovera, M. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.412 · Cited by 108
Leng, Y., Wu, Y., Lei, S., Zhou, B., Qiu, Z., Wang, K., & Xia, Z. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9494052 · Cited by 108
Mechanisms of Resistance to Histone Deacetylase Inhibitors
Lee, J., Choy, M. L., & Marks, P. A. (2012) · Advances in cancer research · doi:10.1016/b978-0-12-394387-3.00002-1 · Cited by 110
Jung, K. H., Noh, J. H., Kim, J. K., Eun, J. W., Bae, H. J., Chang, Y. G., Kim, M., Park, W. S., Lee, J. Y., Lee, S.-Y., et al. (2012) · Hepatology · doi:10.1002/hep.25699 · Cited by 110
Wu, L.-M., Yang, Z., Zhou, L., Zhang, F., Xie, H., Feng, X., Wu, J., & Zheng, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014460 · Cited by 106
RetractedKalin, J. H., Butler, K. V., Akimova, T., Hancock, W. W., & Kozikowski, A. P. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200773h · Cited by 107
Wang, K., Liu, L., Mao, D., Hou, M., Tan, C., Mao, Z., & Liu, B. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202114600 · Cited by 106
Histone deacetylase inhibitors as a new weapon in the arsenal of differentiation therapies of cancer
Botrugno, O. A., Santoro, F., & Minucci, S. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.02.027 · Cited by 105
Targeting histone deacetylases in T-cell lymphoma
Moskowitz, A. J., & Horwitz, S. M. (2016) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2016.1247956 · Cited by 103
Metadata
- Authors
- Witt, O., Deubzer, H. E., Milde, T., & Oehme, I.
- Affiliations
- German Cancer Research Center (DE)
- Corresponding author
- Witt, Olaf
- Venue
- Cancer Letters
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 277
- Issue
- 1
- Pages
- 8-21
- ISSN
- 0304-3835 (ISSN-L)
- OpenAlex
- W2029148944
- Cited by
- 1,069
- References
- 131
- Citations by year
- 2026: 25 · 2025: 55 · 2024: 56 · 2023: 67 · 2022: 52 · 2021: 54 · 2020: 65 · 2019: 53 · 2018: 64 · 2017: 61 · 2016: 86 · 2015: 75 · 2014: 79 · 2013: 94 · 2012: 73
- FWCI
- 2.83
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cancer Letters (publishedVersion)
- PubMed (publishedVersion)
- MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (submittedVersion)
- Funders
- Bundesministerium für Bildung und Forschung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- histone deacetylase, histone deacetylase inhibitors, sirtuins, class I HDACs, class II HDACs, cancer drug targets, selective inhibitors, oncogenicity
- MeSH terms
- Animals, Antineoplastic Agents, Enzyme Inhibitors, Histone Deacetylases, Humans, Neoplasms, Polymorphism, Genetic, Histone Deacetylase Inhibitors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review