Determination of the class and isoform selectivity of small-molecule histone deacetylase inhibitors
Open accessAbstract
The human HDAC (histone deacetylase) family, a well-validated anticancer target, plays a key role in the control of gene expression through regulation of transcription. While HDACs can be subdivided into three main classes, the class I, class II and class III HDACs (sirtuins), it is presently unclear whether inhibiting multiple HDACs using pan-HDAC inhibitors, or targeting specific isoforms that show aberrant levels in tumours, will prove more effective as an anticancer strategy in the clinic. To address the above issues, we have tested a number of clinically relevant HDACis (HDAC inhibitors) against a panel of rhHDAC (recombinant human HDAC) isoforms. Eight rhHDACs were expressed using a baculoviral system, and a Fluor de Lys™ (Biomol International) HDAC assay was optimized for each purified isoform. The potency and selectivity of ten HDACs on class I isoforms (rhHDAC1, rhHDAC2, rhHDAC3 and rhHDAC8) and class II HDAC isoforms (rhHDAC4, rhHDAC6, rhHDAC7 and rhHDAC9) was determined. MS-275 was HDAC1-selective, MGCD0103 was HDAC1- and HDAC2-selective, apicidin was HDAC2- and HDAC3-selective and valproic acid was a specific inhibitor of class I HDACs. The hydroxamic acid-derived compounds (trichostatin A, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat) were potent pan-HDAC inhibitors. The growth-inhibitory effect of the HDACis on HeLa cells showed that both pan-HDAC and class-I-specific inhibitors inhibited cell growth. The results also showed that both pan-HDAC and class-I-specific inhibitor treatment resulted in increased acetylation of histones, but only pan-HDAC inhibitor treatment resulted in increased tubulin acetylation, which is in agreement with their activity towards the HDAC6 isoform.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
Benzamide-containing HDACi possess greater isoform selectivity profiles, targeting specifically only the class I subgroup of HDACs.
“They have also been demonstrated to possess greater isoform selectivity profiles, targeting specifically only the class I subgroup of HDACs (6-10, 26, 38, 39).”
From Histone Deacetylase (HDAC) Inhibitor Kinetic Rate Constants Correlate with Cellular Histone Acetylation but Not Transcription and Cell Viability (2013) · cites this paper as [38]
SAHA and TSA selectivity profiles extended well beyond HDAC1 and HDAC2.
“but their selectivity profiles extended well beyond these isoforms as reported previously (12, 13, 26, 29, 30, 38).”
From Histone Deacetylase (HDAC) Inhibitor Kinetic Rate Constants Correlate with Cellular Histone Acetylation but Not Transcription and Cell Viability (2013) · cites this paper as [38]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679 · see citing works
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 · see citing works
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 · see citing works
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,211 · see citing works
Histone deacetylases and cancer: causes and therapies
Marks, P. A., Rifkind, R. A., Richon, V. M., Breslow, R., Miller, T., & Kelly, W. K. (2001) · Nature reviews. Cancer · doi:10.1038/35106079 · Cited by 1,866 · see citing works
Acetylation and deacetylation of non-histone proteins
Glozak, M. A., Sengupta, N., Zhang, X., & Seto, E. (2005) · Gene · doi:10.1016/j.gene.2005.09.010 · Cited by 1,584 · see citing works
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 · see citing works
Histone-deacetylase inhibitors: novel drugs for the treatment of cancer
Johnstone, R. W. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd772 · Cited by 1,515 · see citing works
Gregoretti, I., Lee, Y.-M., & Goodson, H. V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.006 · Cited by 1,456 · see citing works
Epigenetic therapy of cancer: past, present and future
Yoo, C. B., & Jones, P. A. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd1930 · Cited by 1,291 · see citing works
Olsen, E. A., Kim, Y. H., Kuzel, T. M., Pacheco, T. R., Foss, F. M., Parker, S. R. S., Frankel, S. R., Chen, C., Ricker, J. L., Arduino, J. M., et al. (2007) · Journal of Clinical Oncology · doi:10.1200/jco.2006.10.2434 · Cited by 1,057 · see citing works
Bali, P., Pranpat, M., Bradner, J., Balasis, M., Fiskus, W., Guo, F., Rocha, K., Kumaraswamy, S., Boyapalle, S., Atadja, P., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500186200 · Cited by 755 · see citing works
Fischle, W., Dequiedt, F., Hendzel, M. J., Guenther, M. G., Lazar, M. A., Voelter, W., & Verdin, E. (2002) · Molecular Cell · doi:10.1016/s1097-2765(01)00429-4 · Cited by 754 · see citing works
HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S., & Matthias, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg115 · Cited by 740 · see citing works
In vivo destabilization of dynamic microtubules by HDAC6‐mediated deacetylation
Matsuyama, A., Shimazu, T., Sumida, Y., Saito, A., Yoshimatsu, Y., Seigneurin‐Berny, D., Osada, H., Komatsu, Y., Nishino, N., Khochbin, S., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf682 · Cited by 720 · see citing works
Histone deacetylases, transcriptional control, and cancer
Cress, W. D., & Seto, E. (2000) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(200007)184:1 · Cited by 619 · see citing works
The SMRT and N-CoR Corepressors Are Activating Cofactors for Histone Deacetylase 3
Guenther, M. G., Barak, O., & Lazar, M. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.18.6091-6101.2001 · Cited by 611 · see citing works
The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2
Krämer, O. H., Zhu, P., Ostendorff, H. P., Golebiewski, M., Tiefenbach, J., Peters, M. A., Brill, B., Groner, B., Bach, I., Heinzel, T., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg315 · Cited by 523 · see citing works
Upregulation and Nuclear Recruitment of HDAC1 in Hormone Refractory Prostate Cancer
Halkidou, K., Gaughan, L., Cook, S., Leung, H. Y., Neal, D. E., & Robson, C. N. (2004) · The Prostate · doi:10.1002/pros.20022 · Cited by 515 · see citing works
Identification of Novel Isoform-Selective Inhibitors within Class I Histone Deacetylases
Hu, E., Dul, E., Sung, C.-M., Chen, Z., Kirkpatrick, R. B., Zhang, G., Johanson, K., Liu, R., Lago, A. M., Hofmann, G. A., et al. (2003) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.103.055541 · Cited by 350 · see citing works
Expression Profile of Histone Deacetylase 1 in Gastric Cancer Tissues
Choi, J., Kwon, H. J., Yoon, B., Kim, J., Han, S., Joo, H. J., & Kim, D.-Y. (2001) · Japanese Journal of Cancer Research · doi:10.1111/j.1349-7006.2001.tb02153.x · Cited by 349 · see citing works
Increased expression of histone deacetylase 2 is found in human gastric cancer
SONG, J., Noh, J. H., LEE, J. H., Eun, J. W., Ahn, Y. M., Kim, S. Y., Lee, S. H., Park, W. S., Yoo, N. J., Lee, J. Y., et al. (2005) · Apmis · doi:10.1111/j.1600-0463.2005.apm_04.x · Cited by 347 · see citing works
Vorinostat: a new oral histone deacetylase inhibitor approved for cutaneous T-cell lymphoma
Duvic, M., & Vu, J. (2007) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.16.7.1111 · Cited by 345 · see citing works
Wade, P. A. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.7.693 · Cited by 319 · see citing works
Inhibitors of the HSP90 Molecular Chaperone: Current Status
Sharp, S. Y., & Workman, P. (2006) · Advances in cancer research · doi:10.1016/s0065-230x(06)95009-x · Cited by 311 · see citing works
Acetylation and chromosomal functions
Cheung, W. L., Briggs, S. D., & Allis, C. D. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00096-x · Cited by 290 · see citing works
Class II histone deacetylases: Structure, function, and regulation
Bertos, N., Wang, A. H., & Yang, X.-J. (2001) · Biochemistry and Cell Biology · doi:10.1139/o01-032 · Cited by 278 · see citing works
Kuendgen, A., Schmid, M., Schlenk, R. F., Knipp, S., Hildebrandt, B., Steidl, C., Germing, U., Haas, R. R., Döhner, H., & Gattermann, N. (2005) · Cancer · doi:10.1002/cncr.21552 · Cited by 224 · see citing works
Histone deacetylase as a new target for cancer chemotherapy
Yoshida, M., Furumai, R., Nishiyama, M., Komatsu, Y., Nishino, N., & Horinouchi, S. (2001) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s002800100300 · Cited by 217 · see citing works
Histone deacetylase inhibitors in cancer therapy
Rasheed, W. K., Johnstone, R. W., & Prince, H. M. (2007) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.16.5.659 · Cited by 211 · see citing works
Association of valproate‐induced teratogenesis with histone deacetylase inhibition in vivo
Gurvich, N., Berman, M. G., Wittner, B. S., Gentleman, R. C., Klein, P. S., & Green, J. B. A. (2005) · The FASEB Journal · doi:10.1096/fj.04-3425fje · Cited by 191 · see citing works
Aberrant expression of histone deacetylase 6 in oral squamous cell carcinoma
Sakuma, T., Uzawa, K., Onda, T., Shiiba, M., Yokoe, H., Shibahara, T., & Tanzawa, H. (2006) · International Journal of Oncology · doi:10.3892/ijo.29.1.117 · Cited by 185 · see citing works
Two Catalytic Domains Are Required for Protein Deacetylation
Zhang, Y., Gilquin, B., Khochbin, S., & Matthias, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500241200 · Cited by 161 · see citing works
Gantt, S. L., Gattis, S. G., & Fierke, C. A. (2006) · Biochemistry · doi:10.1021/bi060212u · Cited by 151 · see citing works
Development of histone deacetylase inhibitors for cancer treatment
Marchion, D. C., & Münster, P. N. (2007) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.7.4.583 · Cited by 149 · see citing works
Histone deacetylase inhibitors open new doors in cancer therapy
McLaughlin, F., & Thangue, N. B. L. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.05.034 · Cited by 147 · see citing works
Bartling, B., Hofmann, H., Boettger, T., Hansen, G., Burdach, S. E. G., Silber, R., & Simm, A. (2005) · Lung Cancer · doi:10.1016/j.lungcan.2005.02.006 · Cited by 123 · see citing works
How mammalian transcriptional repressors work
Thiel, G., Lietz, M., & Hohl, M. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04174.x · Cited by 108 · see citing works
Codina, A., Love, J. D., Li, Y., Lazar, M. A., Neuhaus, D., & Schwabe, J. W. R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500299102 · Cited by 95 · see citing works
Lee, H., Sengupta, N., Villagra, A., Rezai‐Zadeh, N., & Seto, E. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01971-05 · Cited by 86 · see citing works
Kaiser, M., Zavrski, I., Sterz, J., et al. (2006) · PubMed · Cited by 85 · see citing works
Experimental therapy of malignant gliomas using the inhibitor of histone deacetylase MS-275
Eyüpoglu, I. Y., Hahnen, E., Tränkle, C., Savaskan, N. E., Siebzehnrübl, F. A., Buslei, R., Lemke, D., Wick, W., Fahlbusch, R., & Blümcke, I. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0533 · Cited by 71 · see citing works
Differential protein acetylation induced by novel histone deacetylase inhibitors
Glaser, K. B., Li, J., Pease, L. J., Staver, M. J., Marcotte, P. A., Guo, J., Frey, R. R., Garland, R. B., Heyman, H. R., Wada, C. K., et al. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.10.082 · Cited by 66 · see citing works
Piekarz, R., Sackett, D. L., & Bates, S. E. (2007) · The Cancer Journal · doi:10.1097/ppo.0b013e31803c73cc · Cited by 52 · see citing works
Protein deacetylases: enzymes with functional diversity as novel therapeutic targets.
Yoshida, M., Shimazu, T., & Matsuyama, A. (2003) · PubMed · Cited by 43 · see citing works
Novel Sulfonamide Derivatives as Inhibitors of Histone Deacetylase
Finn, P. W., Bandara, M., Butcher, C., Finn, A., Hollinshead, R., Khan, N., Law, N. M., Murthy, S., Romero, R., Watkins, C., et al. (2005) · Helvetica Chimica Acta · doi:10.1002/hlca.200590129 · Cited by 41 · see citing works
Self-citationValproate enhances imatinib‐induced growth arrest and apoptosis in chronic myeloid leukemia cells
Morotti, A., Cilloni, D., Messa, F., Arruga, F., Defilippi, I., Carturan, S., Catalano, R., Rosso, V., Chiarenza, A., Pilatrino, C., et al. (2006) · Cancer · doi:10.1002/cncr.21725 · Cited by 36 · see citing works
Steele, N. L., Vidal, L., Plumb, J., Attard, G., Rasmussen, A., Buhl-Jensen, P., Brown, R. E., Blagden, S. P., Evans, J. A., & Bono, J. S. D. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.23.16_suppl.3035 · Cited by 19 · see citing works
Gelmon, K. A., Tolcher, A., Carducci, M. A., et al. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.23.16_suppl.3147 · Cited by 18 · see citing works
Kalita, A., Maroun, C. R., Bonfils, C., et al. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.23.16_suppl.9631 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Anti-inflammatory Agents: Present and Future
Dinarello, C. A. (2010) · Cell · doi:10.1016/j.cell.2010.02.043 · Cited by 1,095 · see citing works
HDAC family: What are the cancer relevant targets?
Witt, O., Deubzer, H. E., Milde, T., & Oehme, I. (2009) · Cancer Letters · doi:10.1016/j.canlet.2008.08.016 · Cited by 1,069 · see citing works
Multiple roles of HDAC inhibition in neurodegenerative conditions
Chuang, D.-M., Leng, Y., Marinova, Z., Kim, H.-J., & Chiu, C.-T. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2009.06.002 · Cited by 676 · see citing works
Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes
Bantscheff, M., Hopf, C., Savitski, M. M., Dittmann, A., Grandi, P., Michon, A.-M., Schlegl, J., Abraham, Y., Becher, I., Bergamini, G., et al. (2011) · Nature Biotechnology · doi:10.1038/nbt.1759 · Cited by 659 · see citing works
Epigenetic Therapy Ties MYC Depletion to Reversing Immune Evasion and Treating Lung Cancer
Topper, M. J., Vaz, M., Chiappinelli, K. B., DeStefano Shields, C. E., Niknafs, N., Yen, R.-W. C., Wenzel, A., Hicks, J., Ballew, M., Stone, M., et al. (2017) · Cell · doi:10.1016/j.cell.2017.10.022 · Cited by 537 · see citing works
Lauffer, B. E. L., Mintzer, R., Fong, R., Mukund, S., Tam, C., Zilberleyb, I., Flicke, B., Ritscher, A., Fedorowicz, G., Vallero, R., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.490706 · Cited by 429 · see citing works
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 · see citing works
Isoform-selective histone deacetylase inhibitors
Bieliauskas, A. V., & Pflum, M. K. H. (2008) · Chemical Society Reviews · doi:10.1039/b703830p · Cited by 350 · see citing works
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 · see citing works
Shukla, S., & Tekwani, B. L. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00537 · Cited by 314 · see citing works
Ning, Z.-Q., Li, Z.-B., Newman, M. J., Shan, S., Wang, X.-H., Pan, D.-S., Zhang, J., Dong, M., Du, X., & Lu, X.-P. (2012) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-011-1766-x · Cited by 303 · see citing works
Identifying drug targets in tissues and whole blood with thermal-shift profiling
Perrin, J., Werner, T., Kurzawa, N., Rutkowska, A., Childs, D. D., Kalxdorf, M., Poeckel, D., Stonehouse, E., Strohmer, K., Heller, B., et al. (2020) · Nature Biotechnology · doi:10.1038/s41587-019-0388-4 · Cited by 178 · see citing works
Witt, A. E., Lee, C.-W., Lee, T. I., Azzam, D. J., Wang, B., Caslini, C., Petrocca, F., Grosso, J., Jones, M., Cohick, E. B., et al. (2017) · Oncogene · doi:10.1038/onc.2016.337 · Cited by 172 · see citing works
HDAC2: a critical factor in health and disease
Krämer, O. H. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2009.09.007 · Cited by 157 · see citing works
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 · see citing works
Venkataramani, 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 · see citing works
Histone deacetylase 3 (HDAC3) inhibitors as anticancer agents: A review
Sarkar, R., Banerjee, S., Amin, S. A., Adhikari, N., & Jha, T. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112171 · Cited by 121 · see citing works
HDAC inhibitors as cognitive enhancers in fear, anxiety and trauma therapy: Where do we stand?
Whittle, N., & Singewald, N. (2014) · Biochemical Society Transactions · doi:10.1042/bst20130233 · Cited by 117 · see citing works
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 · see citing works
Natural Products as a Potential Modulator of Microglial Polarization in Neurodegenerative Diseases
Jin, X., Liu, M.-Y., Zhang, D.-F., Zhong, X., Du, K., Qian, P., Gao, H., & Wei, M.-J. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104253 · Cited by 109 · see citing works
Epigenetic memory: The Lamarckian brain
Fischer, A. (2014) · The EMBO Journal · doi:10.1002/embj.201387637 · Cited by 107 · see citing works
Antidepressant action of HDAC inhibition in the prefrontal cortex
Covington, H. E., Maze, I., Vialou, V., & Nestler, E. J. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.04.030 · Cited by 97 · see citing works
Histone deacetylase 8 is required for centrosome cohesion and influenza A virus entry
Yamauchi, Y., Boukari, H., Banerjee, I., Sbalzarini, I. F., Horvath, P., & Helenius, A. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002316 · Cited by 84 · see citing works
The Zinc-Binding Group Effect: Lessons from Non-Hydroxamic Acid Vorinostat Analogs
Geurs, S., Clarisse, D., De Bosscher, K., & D’hooghe, M. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00226 · Cited by 58 · see citing works
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
Epigenetic mechanisms within the cingulate cortex regulate innate anxiety-like behavior
Sah, A., Sotnikov, S., Kharitonova, M., Schmuckermair, C., Diepold, R. P., Landgraf, R., Whittle, N., & Singewald, N. (2019) · International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyz004 · Cited by 24 · see citing works
Scott, H., Smith, A. E., Barker, G. R., Uney, J. B., & Warburton, E. C. (2017) · Neuroepigenetics · doi:10.1016/j.nepig.2017.02.001 · Cited by 18 · see citing works
SALL4 is a CRL3REN/KCTD11 substrate that drives Sonic Hedgehog-dependent medulloblastoma
Lospinoso Severini, L., Loricchio, E., Navacci, S., Basili, I., Alfonsi, R., Bernardi, F., Moretti, M., Conenna, M., Cucinotta, A., Coni, S., et al. (2024) · Cell Death & Differentiation · doi:10.1038/s41418-023-01246-6 · Cited by 13 · see citing works
“…100 μ g/ml up to 8 h; Sigma-Aldrich), mocetinostat (MGCD0103, 0.5 μ M up to 72 h; synthetized in house as a dihydrobromide salt as described in [80]), thalidomide (Thal, 10 – 20 μ M up to 72 h; Tocris Bioscience, Bristol, UK), and Smoothened Agonist (SAG, 200 nM, Alexis Biochemicals,…”
Influential
- Authors
- Khan, N., Jeffers, M., Kumar, S., Hackett, C., Boldog, F., Khramtsov, N., Qian, X., Mills, E., Berghs, S. C., Carey, N., Finn, P. W., Collins, L. S., Tumber, A., Ritchie, J. W., Jensen, P. B., Lichenstein, H. S., & Sehested, M.
- Affiliations
- Topotarget UK Ltd, 87a Milton Park, Abingdon, Oxon, OX14 4RY, U.K.
- CuraGen Corporation, 322 East Main Street, Branford, CT 06405, U.S.A.
- Topotarget A/S, Symbion Science Park, Fruebjergvej 3, Copenhagen 2100, Denmark
- Corresponding author
- Khan, Nagma
- Carey, Nessa
- Tumber, Anthony
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2007-12-21
- Volume
- 409
- Issue
- 2
- Pages
- 581-589
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2050931169
- Semantic Scholar
- 6a52875af70d1397078cf79878d215f6cd4080bc
- Cited by
- 713
- References
- 50
- Citations by year
- 2026: 9 · 2025: 16 · 2024: 20 · 2023: 22 · 2022: 24 · 2021: 31 · 2020: 32 · 2019: 34 · 2018: 26 · 2017: 44 · 2016: 37 · 2015: 43 · 2014: 47 · 2013: 66 · 2012: 53
- FWCI
- 21.31
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- histone deacetylase inhibitors, HDAC isoform selectivity, pan-HDAC inhibitors, class I HDACs, class II HDACs, sirtuins, entinostat, MGCD0103, apicidin, valproic acid, hydroxamic acid derivatives, trichostatin A, vorinostat, belinostat, panobinostat, tubulin acetylation, histone acetylation, HeLa cells, anticancer drug targets
- MeSH terms
- Acetylation, Cloning, Molecular, Enzyme Inhibitors, HeLa Cells, Histone Deacetylases, Humans, Recombinant Proteins, Protein Isoforms, Cell Proliferation, 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
