Profiling of Substrates for Zinc‐dependent Lysine Deacylase Enzymes: HDAC3 Exhibits Decrotonylase Activity In Vitro
Abstract
Systematic screening of the activities of the eleven human zinc-dependent lysine deacylases against a series of fluorogenic substrates as well as kinetic evaluation revealed substrates for screenings of histone deacetylases HDAC10 and HDAC11 at reasonably low enzyme concentrations. Furthermore, HDAC3 in complex with nuclear receptor corepressor 1 (HDAC3-NCoR1) was shown to harbor decrotonylase activity in vitro.
Integrity signals
Registry
Cites
Statistics
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?
The HDAC3/SMRT/GPS2/TBL1 complex displays significant decrotonylase activity against H3K18cr peptide, with an initial rate 2.4-fold lower than for H3K18ac.
“Consistent with previously published data18 HDAC3 also displayed significant activity against the H3K18cr peptide (Supplementary Fig. 1B), although similar to HDAC1, with an initial rate which was 2.4-fold lower than the H3K18ac substrate.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [18]
A study profiling substrate preferences of HDAC1-11 identified HDAC3 as a potential decrotonylase.
“A study profiling substrate preferences of HDAC1–11 identified HDAC3 as a potential decrotonylase18.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [18]
The HDAC3/NCoR complex hydrolyses Lys-cr at a lower rate than Lys-ac, though still comparable to the deacetylase activities of HDAC8 and HDAC11.
“This is consistent with data from Madsen and Olson18, who showed that the HDAC3/NCoR complex also hydrolysed Lys-cr at a lower rate than Lys-ac, although still comparable to the deacetylase activities of HDAC8 and HDAC11.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [18]
Decrotonylase activity has been described for HDAC1-3 and Sirtuins 1-3.
“To date, decrotonylase activity has been described for HDAC1-3 and Sirtuins 1-316–18,21,22.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [18]
Previous studies failed to detect significant decrotonylase activity for HDAC1/2.
“Previous studies failed to detect significant decrotonylase activity for HDAC1/23,18 and this may be because they were using recombinant enzymes generated in isolation.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [18]
Cites
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883 · see citing works
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040 · see citing works
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 · see citing works
Haberland, M., Montgomery, R. L., & Olson, E. N. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,541 · see citing works
Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902 · see citing works
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 · 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
Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429 · see citing works
Marks, P. A., & Breslow, R. (2007) · Nature Biotechnology · doi:10.1038/nbt1272 · Cited by 1,198 · see citing works
SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin
Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111 · see citing works
Identification of lysine succinylation as a new post-translational modification
Zhang, Z., Tan, M., Xie, Z., Dai, L., Chen, Y., & Zhao, Y. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.495 · Cited by 1,027 · see citing works
An epigenetic blockade of cognitive functions in the neurodegenerating brain
Gräff, J., Rei, D., Guan, J.-S., Wang, W.-Y., Seo, J., Hennig, K. M., Nieland, T. J. F., Fass, D. M., Kao, P. F., Kahn, M., et al. (2012) · Nature · doi:10.1038/nature10849 · Cited by 853 · see citing works
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 · 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
Gao, L., Cueto, M. A., Asselbergs, F., & Atadja, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111871200 · Cited by 744 · see citing works
(2002) · PubMed · Cited by 732 · see citing works
Chemical phylogenetics of histone deacetylases
Bradner, J. E., West, N., Grachan, M. L., Greenberg, E. F., Haggarty, S. J., Warnow, T., & Mazitschek, R. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.313 · Cited by 720 · see citing works
Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
Kazantsev, A. G., & Thompson, L. M. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2681 · Cited by 715 · 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
Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases
Lahm, A., Paolini, C., Pallaoro, M., Nardi, M. C., Jones, P., Neddermann, P., Sambucini, S., Bottomley, M. J., Lo Surdo, P., Carfı́, A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706487104 · Cited by 566 · see citing works
Histone Deacetylase Inhibitors: From Bench to Clinic
Paris, M., Porcelloni, M., Binaschi, M., & Fattori, D. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm7011408 · Cited by 373 · see citing works
Epigenetics—An Epicenter of Gene Regulation: Histones and Histone‐Modifying Enzymes
Biel, M., Wascholowski, V., & Giannis, A. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200461346 · Cited by 321 · see citing works
Epigenetic suppression of GAD65 expression mediates persistent pain
Zhang, Z., Cai, Y.-Q., Zou, F., Bie, B., & Pan, Z. Z. (2011) · Nature Medicine · doi:10.1038/nm.2442 · Cited by 278 · see citing works
Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis
Hutt, D. M., Herman, D., Rodrigues, A. P. C., Noël, S., Pilewski, J. M., Matteson, J., Hoch, B., Kellner, W. A., Kelly, J. W., Schmidt, A., et al. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.275 · Cited by 253 · see citing works
Human HDAC7 Histone Deacetylase Activity Is Associated with HDAC3in Vivo
Fischle, W., Dequiedt, F., Fillion, M., Hendzel, M. J., Voelter, W., & Verdin, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104935200 · Cited by 232 · see citing works
Pimelic Diphenylamide 106 Is a Slow, Tight-binding Inhibitor of Class I Histone Deacetylases
Chou, C. J., Herman, D., & Gottesfeld, J. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807045200 · Cited by 223 · see citing works
Isolation and Characterization of Mammalian HDAC10, a Novel Histone Deacetylase
Kao, H.-Y., Lee, C.-H., Komarov, A., Han, C. C., & Evans, R. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108931200 · Cited by 193 · see citing works
Horne, W. S., Olsen, C. A., Beierle, J. M., Montero, A., & Ghadiri, M. R. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200805900 · Cited by 152 · see citing works
Self-citationIsolation and Characterization of a Novel Class II Histone Deacetylase, HDAC10
Fischer, D. D., Cai, R. L., Bhatia, U., Asselbergs, F. A. M., Song, C., Terry, R., Trogani, N., Widmer, R., Atadja, P. W., & Cohen, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108055200 · Cited by 133 · see citing works
Site‐Specific Incorporation of ε‐N‐Crotonyllysine into Histones
Kim, C. H., Kang, M., Kim, H. J., Chatterjee, A., & Schultz, P. G. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201203349 · Cited by 125 · see citing works
Subtype Selective Substrates for Histone Deacetylases
Heltweg, B., Dequiedt, F., Marshall, B. L., Brauch, C., Yoshida, M., Nishino, N., Verdin, E. M., & Jung, M. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0497592 · Cited by 124 · see citing works
Chemical Probes Identify a Role for Histone Deacetylase 3 in Friedreich's Ataxia Gene Silencing
Xu, C., Soragni, E., Chou, C. J., Herman, D., Plasterer, H. L., Rusche, J. R., & Gottesfeld, J. M. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.07.010 · Cited by 118 · see citing works
Combinatorial profiling of chromatin binding modules reveals multisite discrimination
Garske, A. L., Oliver, S. S., Wagner, E. K., Musselman, C. A., LeRoy, G., Garcia, B. A., Kutateladze, T. G., & Denu, J. M. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.319 · Cited by 117 · see citing works
Improved fluorogenic histone deacetylase assay for high-throughput-screening applications
Wegener, D., Hildmann, C., Riester, D., & Schwienhorst, A. (2003) · Analytical Biochemistry · doi:10.1016/s0003-2697(03)00426-3 · Cited by 112 · see citing works
A Novel Class of Small Molecule Inhibitors of HDAC6
Inks, E. S., Josey, B. J., Jesinkey, S. R., & Chou, C. J. (2011) · ACS Chemical Biology · doi:10.1021/cb200134p · Cited by 103 · see citing works
Old Enzymes, New Tricks: Sirtuins Are NAD+-Dependent De-acylases
Hirschey, M. D. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.10.006 · Cited by 99 · see citing works
Gurard‐Levin, Z. A., Kilian, K. A., Kim, J., Bähr, K., & Mrksich, M. (2010) · ACS Chemical Biology · doi:10.1021/cb100088g · Cited by 89 · see citing works
Short-Chain HDAC Inhibitors Differentially Affect Vertebrate Development and Neuronal Chromatin
Fass, D. M., Shah, R. R., Ghosh, B., Hennig, K. M., Norton, S., Zhao, W., Reis, S. A., Klein, P. S., Mazitschek, R., Maglathlin, R. L., et al. (2010) · ACS Medicinal Chemistry Letters · doi:10.1021/ml1001954 · Cited by 89 · see citing works
Olsen, C. A., & Ghadiri, M. R. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900850t · Cited by 85 · see citing works
Self-citationMontero, A., Beierle, J. M., Olsen, C. A., & Ghadiri, M. R. (2009) · Journal of the American Chemical Society · doi:10.1021/ja809508f · Cited by 83 · see citing works
Self-citationExpansion of the Lysine Acylation Landscape
Olsen, C. A. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201200316 · Cited by 83 · see citing works
Self-citationSIRT3 substrate specificity determined by peptide arrays and machine learning
Smith, B. C., Settles, B., Hallows, W. C., Craven, M. W., & Denu, J. M. (2011) · ACS Chemical Biology · doi:10.1021/cb100218d · Cited by 80 · see citing works
Madsen, A. S., & Olsen, C. A. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300526r · Cited by 73 · see citing works
Self-citationRiester, D., Wegener, D., Hildmann, C., & Schwienhorst, A. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.09.155 · Cited by 68 · see citing works
Non-Natural Macrocyclic Inhibitors of Histone Deacetylases: Design, Synthesis, and Activity
Auzzas, L., Larsson, A., Matera, R., Baraldi, A., Deschênes-Simard, B., Giannini, G., Cabri, W., Battistuzzi, G., Gallo, G., Ciacci, A., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm101092u · Cited by 65 · see citing works
Discovery of HDAC Inhibitors That Lack an Active Site Zn2+-Binding Functional Group
Vickers, C. J., Olsen, C. A., Leman, L. J., & Ghadiri, M. R. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300081u · Cited by 57 · see citing works
Self-citationThe Activity of HDAC8 Depends on Local and Distal Sequences of Its Peptide Substrates
Gurard‐Levin, Z. A., & Mrksich, M. (2008) · Biochemistry · doi:10.1021/bi800053v · Cited by 55 · see citing works
Epigenetik – ein Epizentrum der Genregulation: Histone und histonmodifizierende Enzyme
Biel, M., Wascholowski, V., & Giannis, A. (2005) · Angewandte Chemie · doi:10.1002/ange.200461346 · Cited by 41 · see citing works
Horne, W. S., Olsen, C. A., Beierle, J. M., Montero, A., & Ghadiri, M. R. (2009) · Angewandte Chemie · doi:10.1002/ange.200805900 · Cited by 39 · see citing works
Self-citationHutt, D. M., Olsen, C. A., Vickers, C. J., Herman, D., Chalfant, M. A., Montero, A., Leman, L. J., Burkle, R., Maryanoff, B. E., Balch, W. E., et al. (2011) · ACS Medicinal Chemistry Letters · doi:10.1021/ml200136e · Cited by 28 · see citing works
Self-citationSite‐Specific Incorporation of ε‐N‐Crotonyllysine into Histones
Kim, C. H., Kang, M., Kim, H. J., Chatterjee, A., & Schultz, P. G. (2012) · Angewandte Chemie · doi:10.1002/ange.201203349 · Cited by 24 · see citing works
Vorinostat-Like Molecules as Structural, Stereochemical, and Pharmacological Tools
Hanessian, S., Auzzas, L., Larsson, A., Zhang, J., Giannini, G., Gallo, G., Ciacci, A., & Cabri, W. (2010) · ACS Medicinal Chemistry Letters · doi:10.1021/ml100028g · Cited by 18 · see citing works
Acylierung von Lysinen: Erweiterung des Repertoires
Olsen, C. A. (2012) · Angewandte Chemie · doi:10.1002/ange.201200316 · Cited by 17 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Metabolic regulation of gene expression through histone acylations
Sabari, B. R., Zhang, D., Allis, C. D., & Zhao, Y. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.140 · Cited by 1,134 · see citing works
Class I histone deacetylases (HDAC1–3) are histone lysine delactylases
Moreno-Yruela, C., Zhang, D., Wei, W., Bæk, M., Liu, W., Gao, J., Danková, D., Nielsen, A. L., Bolding, J. E., Yang, L., et al. (2022) · Science Advances · doi:10.1126/sciadv.abi6696 · Cited by 841 · see citing works
Self-citationThirty Years of HDAC Inhibitors: 2020 Insight and Hindsight
Ho, T. C. S., Chan, A. H. Y., & Ganesan, A. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00830 · Cited by 795 · see citing works
Fellows, R., Denizot, J., Stellato, C., Cuomo, A., Jain, P., Stoyanova, E., Balázsi, S., Hajnády, Z., Liebert, A., Kazakevych, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02651-5 · Cited by 568 · see citing works
Advances and Challenges of HDAC Inhibitors in Cancer Therapeutics
McClure, J. J., Li, X., & Chou, C. J. (2018) · Advances in cancer research · doi:10.1016/bs.acr.2018.02.006 · Cited by 356 · see citing works
Bao, X., Wang, Y., Li, X., Li, X.-M., Liu, Z., Yang, T., Wong, C. F., Zhang, J., Hao, Q., & Li, X. D. (2014) · eLife · doi:10.7554/elife.02999 · Cited by 324 · see citing works
Nonenzymatic Protein Acylation as a Carbon Stress Regulated by Sirtuin Deacylases
Wagner, G. R., & Hirschey, M. D. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.027 · Cited by 319 · see citing works
Wei, W., Liu, X., Chen, J., Gao, S., Lu, L., Zhang, H., Ding, G., Wang, Z., Chen, Z., Shi, T., et al. (2017) · Cell Research · doi:10.1038/cr.2017.68 · Cited by 304 · see citing works
Liu, S., Yu, H., Liu, Y., Liu, X., Zhang, Y., Bu, C., Yuan, S., Chen, Z., Xie, G., Li, W., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.07.011 · Cited by 258 · see citing works
Histones: At the Crossroads of Peptide and Protein Chemistry
Müller, M. M., & Muir, T. W. (2015) · Chemical Reviews · doi:10.1021/cr5003529 · Cited by 247 · see citing works
Barnes, C. E., English, D. M., & Cowley, S. M. (2019) · Essays in Biochemistry · doi:10.1042/ebc20180061 · Cited by 225 · see citing works
Global profiling of crotonylation on non-histone proteins
Xu, W., Wan, J., Zhan, J., Li, X., He, H., Shi, Z., & Zhang, H. (2017) · Cell Research · doi:10.1038/cr.2017.60 · Cited by 213 · see citing works
Beyond histone acetylation—writing and erasing histone acylations
Zhao, S., Zhang, X., & Li, H. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.10.001 · Cited by 207 · see citing works
HDAC11 regulates type I interferon signaling through defatty-acylation of SHMT2
Cao, J., Sun, L., Aramsangtienchai, P., Spiegelman, N. A., Zhang, X., Huang, W., Seto, E., & Lin, H. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1815365116 · Cited by 189 · see citing works
Histone deacetylase 11 is a fatty-acid deacylase
Kutil, Z., Novakova, Z., Meleshin, M., Mikesova, J., Schutkowski, M., & Barinka, C. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b00942 · Cited by 174 · see citing works
Histone crotonylation promotes mesoendodermal commitment of human embryonic stem cells
Fang, Y., Xu, X., Ding, J., Yang, L., Doan, M. T., Karmaus, P. W. F., Snyder, N. W., Zhao, Y., Li, J., & Li, X. (2021) · Cell stem cell · doi:10.1016/j.stem.2020.12.009 · Cited by 158 · see citing works
Histone deacetylase 11 is an ε-N-Myristoyllysine hydrolase
Moreno-Yruela, C., Galleano, I., Madsen, A. S., & Olsen, C. A. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.04.007 · Cited by 149 · see citing works
Self-citationKelly, R. D. W., Chandru, A., Watson, P. J., Song, Y., Blades, M., Robertson, N. S., Jamieson, A. G., Schwabe, J. W. R., & Cowley, S. M. (2018) · Scientific Reports · doi:10.1038/s41598-018-32927-9 · Cited by 138 · see citing works
Functions and mechanisms of lysine crotonylation
Wan, J., Liu, H., Chu, J., & Zhang, H. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14650 · Cited by 138 · see citing works
Protein lysine crotonylation: past, present, perspective
Jiang, G., Li, C., Lü, M. K., Lu, K., & Li, H. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03987-z · Cited by 138 · see citing works
The emerging role of protein l-lactylation in metabolic regulation and cell signalling
Ren, H., Tang, Y., & Zhang, D. (2025) · Nature Metabolism · doi:10.1038/s42255-025-01259-0 · Cited by 142 · see citing works
Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADH
Madsen, A. S., Andersen, C. D., Daoud, M., Anderson, K. A., Laursen, J. S., Chakladar, S., Huynh, F. K., Colaço, A. R., Backos, D. S., Fristrup, P., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.668699 · Cited by 110 · see citing works
Self-citationThe Regulation and Function of Histone Crotonylation
Ntorla, A., & Burgoyne, J. R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.624914 · Cited by 107 · see citing works
Lysine crotonylation is involved in hepatocellular carcinoma progression
Wan, J., Liu, H., & Ming, L. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.12.148 · Cited by 106 · see citing works
Yang, Y., Wen, R., Yang, N., Zhang, T., & Liu, C. (2023) · Molecular Medicine · doi:10.1186/s10020-023-00684-9 · Cited by 102 · see citing works
Thaler, F., & Mercurio, C. (2013) · ChemMedChem · doi:10.1002/cmdc.201300413 · Cited by 95 · see citing works
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 95 · see citing works
Fu, Y., Yu, J., Li, F., & Ge, S. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02338-w · Cited by 96 · see citing works
Epigenetic regulators in cancer therapy and progression
Marei, H. E. S. (2025) · npj Precision Oncology · doi:10.1038/s41698-025-01003-7 · Cited by 101 · see citing works
Gattner, M. J., Vrábel, M., & Carell, T. (2012) · Chemical Communications · doi:10.1039/c2cc37836a · Cited by 89 · see citing works
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
The therapeutic hope for HDAC6 inhibitors in malignancy and chronic disease
Batchu, S. N., Brijmohan, A. S., & Advani, A. (2016) · Clinical Science · doi:10.1042/cs20160084 · Cited by 84 · see citing works
Role of histone deacetylases and their inhibitors in neurological diseases
Zhang, L.-Y., Zhang, S.-Y., Wen, R., Zhang, T.-N., & Yang, N. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107410 · Cited by 84 · see citing works
Diverse Activities of Histone Acylations Connect Metabolism to Chromatin Function
Dutta, A., Abmayr, S. M., & Workman, J. L. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.06.038 · Cited by 85 · see citing works
Epigenetic effects of short-chain fatty acids from the large intestine on host cells
Stein, R. A., & Riber, L. (2023) · microLife · doi:10.1093/femsml/uqad032 · Cited by 81 · see citing works
An Expanding Repertoire of Protein Acylations
Xu, Y., Shi, Z., & Bao, L. (2022) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100193 · Cited by 78 · see citing works
Histone Deacetylase Inhibitors and Diabetic Kidney Disease
Hadden, M. J., & Advani, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092630 · Cited by 76 · see citing works
Mechanism of Action for HDAC Inhibitors—Insights from Omics Approaches
Li, W., & Sun, Z. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20071616 · Cited by 77 · see citing works
Histone Acylation beyond Acetylation: Terra Incognita in Chromatin Biology.
Rousseaux, S., & Khochbin, S. (2015) · PubMed Central · doi:10.22074/cellj.2015.506 · Cited by 73 · see citing works
Fluorescent Probes for Single-Step Detection and Proteomic Profiling of Histone Deacetylases
Xie, Y., Ge, J., Lei, J. H., Peng, B., Zhang, H., Wang, D., Pan, S., Chen, G., Chen, L., Wang, Y., et al. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b07334 · Cited by 73 · see citing works
Chromatin dynamics and histone modifications in intestinal microbiota-host crosstalk
Fellows, R., & Varga‐Weisz, P. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.12.005 · Cited by 72 · see citing works
The Effect of Various Zinc Binding Groups on Inhibition of Histone Deacetylases 1–11
Madsen, A. S., Kristensen, H. M. E., Lanz, G., & Olsen, C. A. (2013) · ChemMedChem · doi:10.1002/cmdc.201300433 · Cited by 67 · see citing works
Self-citationUncovering Robust Delactoylase and Depyruvoylase Activities of HDAC Isoforms
Zessin, M., Meleshin, M., Praetorius, L., Sippl, W., Bařinka, C., & Schutkowski, M. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.1c00863 · Cited by 64 · see citing works
SIRT4 is the last puzzle of mitochondrial sirtuins
Li, Y., Zhou, Y., Wang, F., Chen, X., Wang, C., Wang, J., Liu, T., Li, Y., & He, B. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.07.031 · Cited by 63 · see citing works
Tanabe, K., Liu, J., Kato, D., Kurumizaka, H., Yamatsugu, K., Kanai, M., & Kawashima, S. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-21060-2 · Cited by 53 · see citing works
Nielsen, A. L., Rajabi, N., Kudo, N., Lundø, K., Moreno–Yruela, C., Bæk, M., Fontenas, M., Lucidi, A., Madsen, A. S., Yoshida, M., et al. (2021) · RSC Chemical Biology · doi:10.1039/d0cb00036a · Cited by 54 · see citing works
Self-citationThe Function and related Diseases of Protein Crotonylation
Wang, S., Mu, G., Qiu, B., Wang, M., Yu, Z., Wang, W., Wang, J., & Yang, Y. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.58872 · Cited by 54 · see citing works
Targeting Sirtuins: Substrate Specificity and Inhibitor Design
Rajabi, N., Galleano, I., Madsen, A. S., & Olsen, C. A. (2018) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.11.003 · Cited by 52 · see citing works
Self-citationEffects of Histone Modification in Major Depressive Disorder
Wu, M.-S., Li, X., Liu, C., Xu, Q., Huang, J., Gu, S., & Chen, J. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210922150043 · Cited by 53 · see citing works
The mechanisms, regulations, and functions of histone lysine crotonylation
Xie, J., Ju, J., Zhou, P., Chen, H., Wang, S., Wang, K., Wang, T., Chen, Y.-C., Chen, Y.-C., & Wang, K. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01830-w · Cited by 51 · see citing works
Comparison of the Deacylase and Deacetylase Activity of Zinc-Dependent HDACs
McClure, J. J., Inks, E. S., Zhang, C., Peterson, Y. K., Li, J., Chundru, K. J., Lee, B., Buchanan, A., Miao, S., & Chou, C. J. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00321 · Cited by 51 · see citing works
Darwish, S., Ghazy, E., Heimburg, T., Herp, D., Zeyen, P., Salem-Altintas, R., Ridinger, J., Schmidtkunz, K., Robaa, D., Erdmann, F., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147535 · Cited by 45 · see citing works
Role of Sirtuins in Tumor Angiogenesis
Edatt, L., Poyyakkara, A., Raji, G. R., Ramachandran, V., Shankar, S. S., & Kumar, V. B. S. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2019.01516 · Cited by 43 · see citing works
The Contribution of Histone Crotonylation to Tissue Health and Disease: Focus on Kidney Health
Martinez-Moreno, J. M., Fontecha‐Barriuso, M., Martín‐Sánchez, D., Sánchez-Niño, M. D., Ruiz‐Ortega, M., Sanz, A. B., & Ortíz, A. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00393 · Cited by 41 · see citing works
Determination of Slow-Binding HDAC Inhibitor Potency and Subclass Selectivity
Moreno–Yruela, C., & Olsen, C. A. (2022) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.1c00702 · Cited by 41 · see citing works
Self-citationVilladsen, J. S., Stephansen, H. M., Maolanon, A. R., Harris, P., & Olsen, C. A. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4008449 · Cited by 40 · see citing works
Self-citationGober, I. N., & Waters, M. L. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b02836 · Cited by 40 · see citing works
Novel thiourea-based sirtuin inhibitory warheads
Zang, W., Hao, Y., Wang, Z., & Zheng, W. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.05.058 · Cited by 40 · see citing works
One-Atom Substitution Enables Direct and Continuous Monitoring of Histone Deacylase Activity
Zessin, M., Kutil, Z., Meleshin, M., Nováková, Z., Ghazy, E., Kalbas, D., Marek, M., Romier, C., Sippl, W., Bařinka, C., et al. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00786 · Cited by 38 · see citing works
Crotonylation and disease: Current progress and future perspectives
Yang, P., Qin, Y., Zeng, L., He, Y., Xie, Y., Cheng, X., Huang, W. G., & Cao, L. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115108 · Cited by 38 · see citing works
Novel histone modifications and liver cancer: emerging frontiers in epigenetic regulation
Wang, Z., Liu, Z., Lv, M., Luan, Z., Li, T., & Hu, J. (2025) · Clinical Epigenetics · doi:10.1186/s13148-025-01838-8 · Cited by 39 · see citing works
Lin, P., Bai, H., He, L., Huang, Q., Zeng, Q.-H., Pan, Y., Jiang, B., Zhang, F., Zhang, L., & Liu, Q. (2021) · BMC Genomics · doi:10.1186/s12864-020-07365-5 · Cited by 37 · see citing works
Kitir, B., Maolanon, A. R., Ohm, R. G., Colaço, A. R., Fristrup, P., Madsen, A. S., & Olsen, C. A. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00725 · Cited by 38 · see citing works
Self-citationMoreno–Yruela, C., Bæk, M., Vrsanova, A.-E., Schulte, C., Maric, H. M., & Olsen, C. A. (2021) · Nature Communications · doi:10.1038/s41467-020-20250-9 · Cited by 37 · see citing works
Self-citationSwyter, S., Schiedel, M., Monaldi, D., Szunyogh, S., Lehotzky, A., Rumpf, T., Ovádi, J., Sippl, W., & Jung, M. (2018) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2017.0083 · Cited by 34 · see citing works
Distinct biochemical properties of the class I histone deacetylase complexes
Lee, K., Whedon, S. D., Wang, Z. A., & Cole, P. A. (2022) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2022.102179 · Cited by 33 · see citing works
Madsen, A. S., & Olsen, C. A. (2015) · MedChemComm · doi:10.1039/c5md00451a · Cited by 30 · see citing works
Self-citationMostofa, A., Distler, A., Meads, M. B., Sahakian, E., Powers, J. J., Achille, A., Noyes, D., Wright, G., Fang, B., Izumi, V., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.151713 · Cited by 27 · see citing works
Regulatory Mechanism of Protein Crotonylation and Its Relationship with Cancer
Yang, S., Fan, X., & Yu, W. (2024) · Cells · doi:10.3390/cells13211812 · Cited by 27 · see citing works
Characterizing crosstalk in epigenetic signaling to understand disease physiology
Lempiäinen, J. K., & Garcia, B. A. (2023) · Biochemical Journal · doi:10.1042/bcj20220550 · Cited by 26 · see citing works
Human SIRT3 tripeptidic inhibitors containing Nε-thioacetyl-lysine
Chen, B., Wang, J., Huang, Y., & Zheng, W. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.07.008 · Cited by 23 · see citing works
Cao, S., Chen, Z., Yue, L., Jiang, H., Ma, R.-Y., & Dong, L. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.783739 · Cited by 21 · see citing works
Methyl Effect in Azumamides Provides Insight Into Histone Deacetylase Inhibition by Macrocycles
Maolanon, A. R., Villadsen, J. S., Christensen, N. J., Hoeck, C. R., Friis, T., Harris, P., Gotfredsen, C. H., Fristrup, P., & Olsen, C. A. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501399d · Cited by 20 · see citing works
Self-citationAn Update on Lysine Deacylases Targeting the Expanding “Acylome”
Olsen, C. A. (2013) · ChemMedChem · doi:10.1002/cmdc.201300421 · Cited by 19 · see citing works
Self-citationAn azumamide C analogue without the zinc-binding functionality
Villadsen, J. S., Kitir, B., Wich, K., Friis, T., Madsen, A. S., & Olsen, C. A. (2014) · MedChemComm · doi:10.1039/c4md00252k · Cited by 19 · see citing works
Self-citationSlow-Binding and Covalent HDAC Inhibition: A New Paradigm?
Raouf, Y. S., & Moreno–Yruela, C. (2024) · JACS Au · doi:10.1021/jacsau.4c00828 · Cited by 18 · see citing works
Lysine crotonylation in disease: mechanisms, biological functions and therapeutic targets
Ji, Y., Liu, S., Zhang, Y., Min, Y., Wei, L., Guan, C., Yu, H., & Zhang, Z. (2025) · Epigenetics & Chromatin · doi:10.1186/s13072-025-00577-7 · Cited by 18 · see citing works
Protein lysine crotonylation in cellular processions and disease associations
Zhao, H., Han, Y., Zhou, P., Guan, H., & Gao, S. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.06.029 · Cited by 17 · see citing works
Bæk, M., Martín‐Gago, P., Laursen, J. S., Madsen, J. L. H., Chakladar, S., & Olsen, C. A. (2020) · Chemistry – A European Journal · doi:10.1002/chem.201905338 · Cited by 16 · see citing works
Self-citationMetabolic and epigenetic regulation of endoderm differentiation
Fang, Y., & Li, X. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.09.002 · Cited by 17 · see citing works
Stopper, D., Biermann, L., Watson, P. R., Li, J., König, B., Gaynes, M. N., de Carvalho, L. P., Klose, J., Hanl, M., Hamacher, A., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02373 · Cited by 16 · see citing works
Fan, S., Kong, C., Zhou, R., Zheng, X., Ren, D., & Yin, Z. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c08332 · Cited by 15 · see citing works
Crotonylation modification and its role in diseases
Guo, Y., Li, J., & Zhang, K. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1492212 · Cited by 14 · see citing works
Role of Histone Lactylation in Neurological Disorders
Zhang, Y., Yang, F., Li, Q., & Zhang, J.-N. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26167949 · Cited by 14 · see citing works
Xie, Y., Yang, L., Chen, Q., Zhang, J., Feng, L., Chen, J. L., Hao, Q., Zhang, L. N., & Sun, H. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.113120 · Cited by 14 · see citing works
Moreno–Yruela, C., & Olsen, C. A. (2021) · STAR Protocols · doi:10.1016/j.xpro.2021.100313 · Cited by 14 · see citing works
Self-citationHe, Y., Yan, L., Zang, W., & Zheng, W. (2015) · Organic & Biomolecular Chemistry · doi:10.1039/c5ob01721a · Cited by 14 · see citing works
Function and mechanism of lysine crotonylation in health and disease
Hou, L., Chen, Y. J., Zhong, Q., Pei, J., Liu, L., Pi, H., Xie, M., & Zhao, G. (2024) · QJM · doi:10.1093/qjmed/hcae034 · Cited by 11 · see citing works
Protein crotonylation: An emerging regulator in DNA damage response
Ji, P., Zhang, G., Guo, Y., Song, H., Yuan, X., Hu, X., Guo, Z., Xia, P., Shen, R., & Wang, D. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.122059 · Cited by 11 · see citing works
Rooker, D. R., Klyubka, Y., Gautam, R., Tomat, E., & Buccella, D. (2017) · ChemBioChem · doi:10.1002/cbic.201700582 · Cited by 11 · see citing works
Application of crotonylation modification in pan-vascular diseases
Yan, W., Zhang, Y., Dai, Y., & Ge, J. (2024) · Journal of drug targeting · doi:10.1080/1061186x.2024.2372316 · Cited by 10 · see citing works
Protein lysine four‐carbon acylations in health and disease
Fang, Y., & Li, X. (2023) · Journal of Cellular Physiology · doi:10.1002/jcp.30981 · Cited by 10 · see citing works
Histone crotonylation in tumors (Review)
Wang, X., Qu, Y., Li, Z., & Xia, Q. (2025) · Molecular and Clinical Oncology · doi:10.3892/mco.2025.2834 · Cited by 9 · see citing works
Protein crotonylation: Basic research and clinical diseases
Li, D., Lin, L., Xu, F., Feng, T., Tao, Y., Miao, H., & Yang, F. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101694 · Cited by 8 · see citing works
Emerging posttranslational modifications and their roles in DNA damage response
Wu, Z., Liu, Y., Zhang, M., & Wang, D. (2023) · Genome Instability & Disease · doi:10.1007/s42764-023-00115-3 · Cited by 8 · see citing works
Distribution and diversity of classical deacylases in bacteria
Graf, L. G., Moreno–Yruela, C., Qin, C., Schulze, S., Palm, G. J., Schmöker, O., Wang, N., Hocking, D. M., Jebeli, L., Girbardt, B., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-53903-0 · Cited by 7 · see citing works
Self-citationCracking Lysine Crotonylation (Kcr): Enlightening a Promising Post‐Translational Modification
Westerveld, M., Besermenji, K., Aidukas, D., Ostrovitsa, N., & Petracca, R. (2024) · ChemBioChem · doi:10.1002/cbic.202400639 · Cited by 6 · see citing works
The role of CddA and cGNAT2 in crotonylation of proteins in cyanobacteria
Lin, J., Li, Q., Liu, X., Zhan, J., Yuan, L., Yang, M., & Ge, F. (2025) · New Phytologist · doi:10.1111/nph.70310 · Cited by 5 · see citing works
Histone Acyl Code in Precision Oncology: Mechanistic Insights from Dietary and Metabolic Factors
Neja, S. A., Dashwood, W. M., Dashwood, R. H., & Rajendran, P. (2024) · Nutrients · doi:10.3390/nu16030396 · Cited by 5 · see citing works
Mo, W., Wei, S., Xie, X., Liu, T., & Deng, J. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1688548 · Cited by 4 · see citing works
- Authors
- Madsen, A. S., & Olsen, C. A.
- Affiliations
- Technical University of Denmark (DK)
- Corresponding author
- Olsen, Christian A.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2012-08-13
- Volume
- 51
- Issue
- 36
- Pages
- 9083-9087
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W2162595337
- Cited by
- 122
- References
- 53
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 18 · 2023: 9 · 2022: 8 · 2021: 12 · 2020: 7 · 2019: 8 · 2018: 11 · 2017: 7 · 2016: 7 · 2015: 5 · 2014: 6 · 2013: 5 · 2012: 2
- FWCI
- 2.44
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Angewandte Chemie International Edition (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Funders
- Lundbeckfonden (R52-2010-5054)
- 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 › Genomics and Chromatin Dynamics
- Keywords
- histone deacetylase, HDAC3, HDAC10, HDAC11, substrate profiling, fluorogenic substrates, enzyme kinetics, NCOR1, nuclear receptor corepressor, histone deacetylation
- MeSH terms
- Histone Deacetylase 3, HeLa Cells, Histone Deacetylases, Humans, Kinetics, Substrate Specificity, Zinc, Protein Isoforms, Histone Deacetylase Inhibitors, Nuclear Receptor Co-Repressor 1
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