Cited by 262Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.

Molecular Cloning and Characterization of a Novel Histone Deacetylase HDAC10

Open access

Guardiola, Amaris R., Yao, Tso-Pang·2002·Journal of Biological Chemistry

Open this paper in CoChat — free account Open PDF

Abstract

The growing number of proteins controlled by reversible acetylation suggests the existence of a large number of acetyltransferases and deacetylases. Here, we report the identification of a novel class II histone deacetylase, HDAC10. Homology comparison indicates that HDAC10 is most similar to HDAC6. Both contain a unique, putative second catalytic domain not found in other HDACs. In HDAC10, however, this domain is not functional. This tandem organization of two catalytic domains confers resistance to the inhibitors trapoxin B and sodium butyrate, which potently inhibit the deacetylase activity of all other HDAC members. Thus, HDAC10 and HDAC6 share unusual structural and pharmacological characteristics. However, unlike HDAC6, which is normally a cytoplasmic deacetylase, HDAC10 resides in both the nucleus and cytoplasm. In the nucleus, when tethered to a promoter, HDAC10 represses transcription independent of its deacetylase activity, indicating that HDAC10 contains a distinct transcriptional repressor domain. These observations suggest that HDAC10 might uniquely play roles both in the nucleus, as a transcriptional modulator, and in the cytoplasm in an unidentified role. Together, our results identify HDAC10 as a novel deacetylase with distinct structure, pharmacology and localization and further expand the complexity of the HDAC family.

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

Crossref · 10.1074/jbc.m109861200

Cites

30 of 30 references verified0 citation errors · 0 not checkable

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation
McKinsey, T. A., Zhang, C., Lu, J., & Olson, E. N. (2000) · Nature · doi:10.1038/35040593 · Cited by 1,051
A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases
Richon, V. M., Emiliani, S., Verdin, E., Webb, Y., Breslow, R., Rifkind, R. A., & Marks, P. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.3003 · Cited by 914
Microtubules containing acetylated alpha-tubulin in mammalian cells in culture.
Piperno, G., LeDizet, M., & Chang, X. J. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.2.289 · Cited by 873
Three proteins define a class of human histone deacetylases related to yeast Hda1p
Grozinger, C. M., Hassig, C. A., & Schreiber, S. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4868 · Cited by 770
Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation
Yao, T., Segraves, W. A., Oro, A. E., McKeown, M., & Evans, R. M. (1992) · Cell · doi:10.1016/0092-8674(92)90266-f · Cited by 720
Self-citation
Trichostatin A and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function
Yoshida, M., Horinouchi, S., & Beppu, T. (1995) · BioEssays · doi:10.1002/bies.950170510 · Cited by 715
A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors
Saito, A., Yamashita, T., Mariko, Y., Nosaka, Y., Tsuchiya, K., Ando, T., Suzuki, T., Tsuruo, T., & Nakanishi, O. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4592 · Cited by 696
Regulation of activity of the transcription factor GATA-1 by acetylation
Boyes, J., Byfield, P., Nakatani, Y., & Ogryzko, V. (1998) · Nature · doi:10.1038/25166 · Cited by 694

Show all 30 references

Research works printed but not linked: 2

Allfrey, 1964, Proc. Natl, Acad. Sci. U. S. A., 61, 768
Cohen, 1999, Anticancer Res., 19, 4999

Sorted by citations

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
The many roles of histone deacetylases in development and physiology: implications for disease and therapy
Haberland, M., Montgomery, R. L., & Olson, E. N. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,600
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
Self-citation
HDAC2 negatively regulates memory formation and synaptic plasticity
Guan, J.-S., Haggarty, S. J., Giacometti, E., Dannenberg, J.-H., Joseph, N., Gao, J., Nieland, T. J. F., Zhou, Y., Wang, X., Mazitschek, R., et al. (2009) · Nature · doi:10.1038/nature07925 · Cited by 1,644
The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress
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
Self-citation
Inhibition of Histone Deacetylase Activity by Butyrate
Davie, J. R. (2003) · The Journal of Nutrition · doi:10.1093/jn/133.7.2485s · Cited by 1,515
Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis
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
50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond
Verdin, E. M., & Ott, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3931 · Cited by 905
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
Signal transduction mediated by the Ras/Raf/MEK/ERK pathway from cytokine receptors to transcription factors: potential targeting for therapeutic intervention
Chang, F., Steelman, L. S., Lee, J. T., Shelton, J. G., Navolanic, P. M., Blalock, W. L., Franklin, R. A., & McCubrey, J. A. (2003) · Leukemia · doi:10.1038/sj.leu.2402945 · Cited by 738
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
Histone Deacetylases: Unique Players in Shaping the Epigenetic Histone Code
Thiagalingam, S., Cheng, K., Lee, H. J., Mineva, N. D., Thiagalingam, A., & Ponte, J. F. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb05964.x · Cited by 700
Class II histone deacetylases: versatile regulators
Verdin, E., Dequiedt, F., & Kasler, H. G. (2003) · Trends in Genetics · doi:10.1016/s0168-9525(03)00073-8 · Cited by 664
CLINICAL DEVELOPMENT OF HISTONE DEACETYLASE INHIBITORS AS ANTICANCER AGENTS
Drummond, D. C., Noble, C. O., Kirpotin, D. B., Guo, Z., Scott, G. K., & Benz, C. C. (2005) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.095825 · Cited by 494
Histone deacetylases as regulators of inflammation and immunity
Shakespear, M. R., Halili, M. A., Irvine, K. M., Fairlie, D. P., & Sweet, M. J. (2011) · Trends in Immunology · doi:10.1016/j.it.2011.04.001 · Cited by 546
The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin
Butler, L. M., Zhou, X., Xu, W., Scher, H. I., Rifkind, R. A., Marks, P. A., & Richon, V. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.182372299 · Cited by 511
Histone Deacetylase Is a Target of Valproic Acid-Mediated Cellular Differentiation
Gurvich, N., Tsygankova, O. M., Meinkoth, J. L., & Klein, P. S. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-0799 · Cited by 470
Recent developments of HDAC inhibitors: Emerging indications and novel molecules
Bondarev, A. D., Attwood, M. M., Jonsson, J., Chubarev, V. N., Tarasov, V. V., & Schiöth, H. B. (2021) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.14889 · Cited by 451
Class II Histone Deacetylases: from Sequence to Function, Regulation, and Clinical Implication
Yang, X., & Grégoire, S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.2873-2884.2005 · Cited by 428
The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress responsePreprint
Kwon, S., Zhang, Y., & Matthias, P. (2007) · Genes & Development · doi:10.1101/gad.461107 · Cited by 402
Histone deacetylase (HDAC) inhibitors attenuate cardiac hypertrophy by suppressing autophagy
Cao, D. J., Wang, Z. V., Battiprolu, P. K., Jiang, N., Morales, C. R., Kong, Y., Rothermel, B. A., Gillette, T. G., & Hill, J. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015081108 · Cited by 409
HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination
Boyault, C., Sadoul, K., Pabion, M., & Khochbin, S. (2007) · Oncogene · doi:10.1038/sj.onc.1210614 · Cited by 397
Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics
Ali, I., Conrad, R. J., Verdin, E. M., & Ott, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00181 · Cited by 375
The Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy
Guo, L., Tian, Y., & Zhu, W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576946 · Cited by 364
Isoform-selective histone deacetylase inhibitors
Bieliauskas, A. V., & Pflum, M. K. H. (2008) · Chemical Society Reviews · doi:10.1039/b703830p · Cited by 350
Regulation of histone deacetylase activities
Sengupta, N., & Seto, E. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20179 · Cited by 357
Aggresome induction by proteasome inhibitor bortezomib and α-tubulin hyperacetylation by tubulin deacetylase (TDAC) inhibitor LBH589 are synergistic in myeloma cells
Catley, L. P., Weisberg, E., Kiziltepe, T., Tai, Y., Hideshima, T., Neri, P., Tassone, P., Atadja, P. W., Chauhan, D., Munshi, N. C., et al. (2006) · Blood · doi:10.1182/blood-2006-04-016055 · Cited by 336
Runx2 (Cbfa1, AML-3) Interacts with Histone Deacetylase 6 and Represses the p21 CIP1/WAF1 Promoter
Westendorf, J. J., Zaidi, S. K., Cascino, J. E., Kahler, R. A., van Wijnen, A. J., Lian, J. B., Yoshida, M., Stein, G. S., & Li, X. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.22.7982-7992.2002 · Cited by 319
Histone deacetylase inhibitors: from target to clinical trials
Kelly, W. K., O’Connor, O. A., & Marks, P. A. (2002) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.11.12.1695 · Cited by 256
Histone Deacetylase Inhibitors Promote Osteoblast Maturation
Schroeder, T. M., & Westendorf, J. J. (2005) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.050813 · Cited by 244
Class IIa histone deacetylases: regulating the regulators
Martin, M., Kettmann, R., & Dequiedt, F. (2007) · Oncogene · doi:10.1038/sj.onc.1210613 · Cited by 253
Histone Deacetylase 3 Interacts with Runx2 to Repress the Osteocalcin Promoter and Regulate Osteoblast Differentiation
Schroeder, T. M., Kahler, R. A., Li, X., & Westendorf, J. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403702200 · Cited by 244
Targeting histone deacetylase in cancer therapy
Lin, S.-P., Chen, C., Lin, S.-P., Weng, J., & Chen, C. (2006) · Medicinal Research Reviews · doi:10.1002/med.20056 · Cited by 242
Regulation of microtubule dynamics by inhibition of the tubulin deacetylase HDAC6
Zilberman, Y., Ballestrem, C., Carramusa, L., Mazitschek, R., Khochbin, S., & Bershadsky, A. D. (2009) · Journal of Cell Science · doi:10.1242/jcs.046813 · Cited by 250
Histone deacetylase inhibitors: new drugs for the treatment of inflammatory diseases?
Blanchard, F., & Chipoy, C. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(04)03309-4 · Cited by 241
Rational Development of Histone Deacetylase Inhibitors as Anticancer Agents: A Review
Acharya, M. R., Sparreboom, A., Venitz, J., & Figg, W. D. (2005) · Molecular Pharmacology · doi:10.1124/mol.105.014167 · Cited by 231
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
From 1957 to Nowadays: A Brief History of Epigenetics
Peixoto, P., Cartron, P., Sérandour, A. A., & Hervouet, É. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207571 · Cited by 245
Histone deacetylase inhibitors as therapeutics for polyglutamine disorders
Butler, R. K., & Bates, G. P. (2006) · Nature reviews. Neuroscience · doi:10.1038/nrn1989 · Cited by 215
Understanding the role of histone deacetylase and their inhibitors in neurodegenerative disorders: current targets and future perspective
Kumar, V., Kundu, S., Singh, A., & Singh, S. (2022) · Current Neuropharmacology · doi:10.2174/1570159x19666210609160017 · Cited by 210
A Limited Group of Class I Histone Deacetylases Acts To Repress Human Immunodeficiency Virus Type 1 Expression
Keedy, K. S., Archin, N. M., Gates, A. T., Espeseth, A. S., Hazuda, D. J., & Margolis, D. M. (2009) · Journal of Virology · doi:10.1128/jvi.02585-08 · Cited by 199
Histone deacetylase 10 structure and molecular function as a polyamine deacetylase
Hai, Y., Shinsky, S. A., Porter, N. J., & Christianson, D. W. (2017) · Nature Communications · doi:10.1038/ncomms15368 · Cited by 200
Histone deacetylase HDAC8 associates with smooth muscle α‐actin and is essential for smooth muscle cell contractility
Waltregny, D., Glénisson, W., Tran, S. L., North, B. J., Verdin, E. M., Colige, A., & Castronovo, V. (2005) · The FASEB Journal · doi:10.1096/fj.04-2303fje · Cited by 197
Class II (IIa)-Selective Histone Deacetylase Inhibitors. 1. Synthesis and Biological Evaluation of Novel (Aryloxopropenyl)pyrrolyl Hydroxyamides
Mai, A., Massa, S., Pezzi, R., Simeoni, S., Rotili, D., Nebbioso, A., Scognamiglio, A., Altucci, L., Loidl, P., & Brosch, G. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049002a · Cited by 185
Down-regulation of Histone Deacetylases Stimulates Adipocyte Differentiation
Yoo, E. J., Chung, J.-J., Choe, S. S., Kim, K. H., & Kim, J. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508982200 · Cited by 184
Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain
Tong, J. J. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.5.1114 · Cited by 181
Class II Histone Deacetylases Are Directly Recruited by BCL6 Transcriptional Repressor
Lemercier, C., Brocard, M.-P., Puvion-dutilleul, F., Kao, H., Albagli, O., & Khochbin, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201736200 · Cited by 172
Targeting Histone Deacetylases for Cancer Therapy: From Molecular Mechanisms to Clinical Implications
Li, Z., & Zhu, W. (2014) · International Journal of Biological Sciences · doi:10.7150/ijbs.9067 · Cited by 164
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
The Histone Deacetylase 9 Gene Encodes Multiple Protein Isoforms
Petrie, K. R., Guidez, F., Howell, L., Healy, L. E., Waxman, S., Greaves, M. F., & Zelent, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212935200 · Cited by 147
Characterization of the two catalytic domains in histone deacetylase 6
Zou, H., Wu, Y., Navre, M., & Sang, B. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.12.144 · Cited by 144
Mechanisms Regulating Adipocyte Expression of Resistin
Hartman, H. B., Hu, X., Tyler, K. X., Dalal, C. K., & Lazar, M. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201451200 · Cited by 145
Histone deacetylase inhibitors: potential targets responsible for their anti-cancer effect
Dickinson, M. J., Johnstone, R. W., & Prince, H. M. (2010) · Investigational New Drugs · doi:10.1007/s10637-010-9596-y · Cited by 147
Regulation of the HIF-1α stability by histone deacetylases
Kim, S. H., Jeong, J.-W., Park, J. Y., Lee, J., Seo, J., Jung, B., Bae, M., & Kim, K. (2007) · Oncology Reports · doi:10.3892/or.17.3.647 · Cited by 144
The Tale of Protein Lysine Acetylation in the Cytoplasm
Sadoul, K., Wang, J., Diagouraga, B., & Khochbin, S. (2010) · BioMed Research International · doi:10.1155/2011/970382 · Cited by 148
Valproate and Amitriptyline Exert Common and Divergent Influences on Global and Gene Promoter-Specific Chromatin Modifications in Rat Primary Astrocytes
Perišić, T., Zimmermann, N., Kirmeier, T., Asmus, M., Tuorto, F., Uhr, M., Holsboer, F., Rein, T., & Zschocke, J. (2009) · Neuropsychopharmacology · doi:10.1038/npp.2009.188 · Cited by 135
Expression of Histone Deacetylase 8, a Class I Histone Deacetylase, Is Restricted to Cells Showing Smooth Muscle Differentiation in Normal Human Tissues
Waltregny, D., de Leval, L., Glénisson, W., Tran, S. L., North, B. J., Bellahcène, A., Weidle, U. H., Verdin, E. M., & Castronovo, V. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63320-2 · Cited by 131
Deactylase Inhibitors Disrupt Cellular Complexes Containing Protein Phosphatases and Deacetylases
Brush, M., Guardiola, A. R., Connor, J. H., Yao, T., & Shenolikar, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310997200 · Cited by 128
Self-citation
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
HDAC6 regulates androgen receptor hypersensitivity and nuclear localization via modulating Hsp90 acetylation in castration-resistant prostate cancer.
Ai, J., Wang, Y., Dar, J. A., Liu, J., Liu, L., Nelson, J. B., & Wang, Z. (2009) · Molecular Endocrinology · doi:10.1210/me.2009-0188 · Cited by 126
Recent progress on HDAC inhibitors with dual targeting capabilities for cancer treatment
Peng, X., Sun, Z., Kuang, P., & Chen, J. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112831 · Cited by 120
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
A novel domain in histone deacetylase 1 and 2 mediates repression of cartilage‐specific genes in human chondrocytes
Hong, S., Derfoul, A., Mouriès, L. P., & Hall, D. J. (2009) · The FASEB Journal · doi:10.1096/fj.09-133215 · Cited by 117
Inhibition of Class IIb Histone Deacetylase Significantly Improves Cloning Efficiency in Mice1
Ono, T., Li, C., Mizutani, E., Terashita, Y., Yamagata, K., & Wakayama, T. (2010) · Biology of Reproduction · doi:10.1095/biolreprod.110.085282 · Cited by 112
Competitive inhibition of histone deacetylase activity by trichostatin A and butyrate
Sekhavat, A., Sun, J., & Davie, J. (2007) · Biochemistry and Cell Biology · doi:10.1139/o07-145 · Cited by 110
Fasting and High-Fat Diet Alter Histone Deacetylase Expression in the Medial Hypothalamus
Funato, H., Oda, S., Yokofujita, J., Igarashi, H., & Kuroda, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018950 · Cited by 110
Phylogenetic analysis, subcellular localization, and expression patterns of RPD3/HDA1 family histone deacetylases in plants
Alinsug, M. V., Yu, C. W., & Wu, K. (2009) · BMC Plant Biology · doi:10.1186/1471-2229-9-37 · Cited by 102
Regulation of lifespan by histone deacetylase
Chang, K. T., & Min, K. (2002) · Ageing Research Reviews · doi:10.1016/s1568-1637(02)00003-x · Cited by 99
Histone deacetylases function as novel potential therapeutic targets for cancer
Zhang, H., Shang, Y., Chen, H., & Li, J. (2016) · Hepatology Research · doi:10.1111/hepr.12757 · Cited by 100
Selective Inhibition of Histone Deacetylase 10: Hydrogen Bonding to the Gatekeeper Residue is Implicated
Géraldy, M. N. E., Morgen, M., Sehr, P. A., Steimbach, R. R., Moi, D., Ridinger, J., Oehme, I., Witt, O., Malz, M., Nogueira, M. S., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01936 · Cited by 96
Histone Deacetylase 7 Promotes Toll-like Receptor 4-dependent Proinflammatory Gene Expression in Macrophages
Shakespear, M. R., Hohenhaus, D. M., Kelly, G., Kamal, N. A., Gupta, P. K., Labzin, L. I., Schroder, K., Garceau, V., Barbero, S., Iyer, A., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.496281 · Cited by 98
Towards Selective Inhibition of Histone Deacetylase Isoforms: What Has Been Achieved, Where We Are and What Will Be Next
Thaler, F., & Mercurio, C. (2013) · ChemMedChem · doi:10.1002/cmdc.201300413 · Cited by 99
Chemical ablation of androgen receptor in prostate cancer cells by the histone deacetylase inhibitor LAQ824
Chen, L., Meng, S., Wang, H., Bali, P., Bai, W., Li, B., Atadja, P. W., Bhalla, K. N., & Wu, J. (2005) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-04-0287 · Cited by 96
Metabolic reprogramming by class I and II histone deacetylases
Mihaylova, M. M., & Shaw, R. J. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.09.003 · Cited by 100
Activation of the Growth-Differentiation Factor 11 Gene by the Histone Deacetylase (HDAC) Inhibitor Trichostatin A and Repression by HDAC3
Zhang, X. M., Wharton, W., Yuan, Z., Tsai, S., Olashaw, N., & Seto, E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.12.5106-5118.2004 · Cited by 95
Will broad-spectrum histone deacetylase inhibitors be superseded by more specific compounds?
Karagiannis, T. C., & El‐Osta, A. (2006) · Leukemia · doi:10.1038/sj.leu.2404464 · Cited by 95
Histone Deacetylase Inhibitors for Cancer Therapy
Kim, T., Bang, Y., & Robertson, K. D. (2006) · Epigenetics · doi:10.4161/epi.1.1.2644 · Cited by 91
Chemical Genetic Modifier Screens
Koeller, K. M., Haggarty, S. J., Perkins, B. D., Leykin, I., Wong, J. C., Kao, M.-C. J., & Schreiber, S. L. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00093-0 · Cited by 89
Developmental expression of histone deacetylase 11 in the murine brain
Liu, H., Hu, Q., Kaufman, A. R., D’Ercole, A. J., & Ye, P. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21521 · Cited by 88
Histone Deacetylase 7 Promotes PML Sumoylation and Is Essential for PML Nuclear Body Formation
Gao, C., Ho, C.-C., Reineke, E. L., Lam, M. C., Cheng, X., Stanya, K. J., Liu, Y., Chakraborty, S., Shih, H.-M., & Kao, H. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00874-08 · Cited by 87
Induction and superinduction of growth arrest and DNA damage gene 45 (GADD45) α and β messenger RNAs by histone deacetylase inhibitors trichostatin A (TSA) and butyrate in SW620 human colon carcinoma cells
Chen, Z., Clark, S., Birkeland, M., Sung, C.-M., Lago, A., Liu, R., Kirkpatrick, R., Johanson, K., Winkler, J. D., & Hu, E. (2002) · Cancer Letters · doi:10.1016/s0304-3835(02)00322-1 · Cited by 87
Kinetics and Comparative Reactivity of Human Class I and Class IIb Histone Deacetylases
Schultz, B. E., Misialek, S., Wu, J., Tang, J., Conn, M. T., Tahilramani, R., & Wong, L. (2004) · Biochemistry · doi:10.1021/bi0494471 · Cited by 88
Multiple domains of the Receptor-Interacting Protein 140 contribute to transcription inhibition
Castet‐Nicolas, A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh524 · Cited by 83
Medicinal chemistry updates of novel HDACs inhibitors (2020 to present)
He, X., Hui, Z., Xu, L., Bai, R., Gao, Y., Wang, Z., Xie, T., & Ye, X.-Y. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113946 · Cited by 89
Microtubule-associated deacetylase HDAC6 promotes angiogenesis by regulating cell migration in an EB1-dependent manner
Li, D., Xie, S., Ren, Y., Huo, L., Gao, J., Cui, D., Liu, M., & Zhou, J. (2011) · Protein & Cell · doi:10.1007/s13238-011-1015-4 · Cited by 79
Histone deacetylases: Focus on the nervous system
Morrison, B. E., Majdzadeh, N., & D’Mello, S. R. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7035-9 · Cited by 84
Inhibition of Histone Deacetylase 10 Induces Thioredoxin-Interacting Protein and Causes Accumulation of Reactive Oxygen Species in SNU-620 Human Gastric Cancer Cells
Lee, J., Jeong, E.-G., Choi, M.-C., Kim, S.-H., Park, J., Song, S., Park, J., Bang, Y., & Kim, T.-Y. (2010) · Molecules and Cells · doi:10.1007/s10059-010-0094-z · Cited by 78
The use of diversity profiling to characterize chemical modulators of the histone deacetylases
Blackwell, L. J., Norris, J. L., Suto, C. M., & Janzen, W. P. (2008) · Life Sciences · doi:10.1016/j.lfs.2008.03.004 · Cited by 79
Corepressor Recruitment by Agonist-Bound Nuclear Receptors
White, J. H., Fernandes, I., Mader, S., & Yang, X. (2004) · Vitamins and hormones · doi:10.1016/s0083-6729(04)68004-6 · Cited by 85
HDAC Family Members Intertwined in the Regulation of Autophagy: A Druggable Vulnerability in Aggressive Tumor Entities
Koeneke, E., Witt, O., & Oehme, I. (2015) · Cells · doi:10.3390/cells4020135 · Cited by 76
Rice histone deacetylase 10 and Arabidopsis histone deacetylase 14 genes encode N ‐acetylserotonin deacetylase, which catalyzes conversion of N ‐acetylserotonin into serotonin, a reverse reaction for melatonin biosynthesis in plants
Lee, K., Lee, H. Y., & Back, K. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12460 · Cited by 77
Human MI-ER1 Alpha and Beta Function as Transcriptional Repressors by Recruitment of Histone Deacetylase 1 to Their Conserved ELM2 Domain
Ding, Z., Gillespie, L. L., & Paterno, G. D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.250-258.2003 · Cited by 78
Evolution of the arginase fold and functional diversity
Dowling, D., Costanzo, L. D., Gennadios, H. A., & Christianson, D. W. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7554-z · Cited by 75
Histone Deacetylase Inhibitors: The Epigenetic Therapeutics That Repress Hypoxia‐Inducible Factors
Chen, S., & Sang, N. (2010) · BioMed Research International · doi:10.1155/2011/197946 · Cited by 73
Screening of histone deacetylases (HDAC) expression in human prostate cancer reveals distinct class I HDAC profiles between epithelial and stromal cells.
Waltregny, D., North, B. J., Mellaert, F. V., de Leval, J., Verdin, E. M., & CASTRONOVO, V. (2004) · PubMed · doi:10.4081/897 · Cited by 71
Histone Deacetylase 10 Regulates the Cell Cycle G2/M Phase Transition via a Novel Let-7–HMGA2–Cyclin A2 Pathway
Li, Y., Peng, L., & Seto, E. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00400-15 · Cited by 71
The Role of Histone Acetylation-/Methylation-Mediated Apoptotic Gene Regulation in Hepatocellular Carcinoma
Rajan, P. K., Udoh, U. S., Sanabria, J. D., Banerjee, M., Smith, G., Schade, M. S., Sanabria, J. A., Sodhi, K., Pierre, S. V., Xie, Z., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238894 · Cited by 72
Modulation of antigen‐presenting cells by HDAC inhibitors: implications in autoimmunity and cancer
Woan, K. V., Sahakian, E., Sotomayor, E. M., Seto, E., & Villagra, A. (2011) · Immunology and Cell Biology · doi:10.1038/icb.2011.96 · Cited by 71
Targeting Histone Deacetylases: A Novel Approach in Parkinson’s Disease
Sharma, S., & Taliyan, R. (2015) · Parkinson s Disease · doi:10.1155/2015/303294 · Cited by 71
Valproic acid: how it works. Or not
Lagace, D. C., O'Brien, W. T., Gurvich, N., Nachtigal, M. W., & Klein, P. S. (2004) · Clinical Neuroscience Research · doi:10.1016/j.cnr.2004.09.013 · Cited by 72

Authors: Guardiola, A. R., & Yao, T.-P.
Affiliations: Duke Medical Center (US)
Corresponding author: Yao, Tso-Pang
ORCID: Yao, Tso-Pang
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2002-02
Volume: 277
Issue: 5
Pages: 3350-3356
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m109861200
OpenAlex: W1987366741
Cited by: 253
References: 30
Citations by year: 2026: 4 · 2025: 8 · 2024: 7 · 2023: 10 · 2022: 10 · 2021: 16 · 2020: 10 · 2019: 5 · 2018: 9 · 2017: 9 · 2016: 3 · 2015: 11 · 2014: 11 · 2013: 8 · 2012: 13
FWCI: 5.56
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6818 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: Damon Runyon Cancer Research Foundation
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
Keywords: HDAC10, histone deacetylase, class II HDACs, HDAC6, transcriptional repression, nuclear localization, cytoplasmic localization, histone acetylation, deacetylase inhibitors
MeSH terms: Histone Deacetylase 6, Amino Acid Sequence, Cell Line, Chromosome Mapping, Chromosomes, Human, Pair 22, Cloning, Molecular, Gene Expression Regulation, Histone Deacetylases, Humans, Molecular Sequence Data, Phylogeny, Recombinant Proteins, Repressor Proteins, Transcription, Genetic, Transfection, Polymerase Chain Reaction, Sequence Alignment, Sequence Homology, Amino Acid, DNA Primers, Catalytic Domain

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

Molecular Cloning and Characterization of a Novel Histone Deacetylase HDAC10

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks