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Chemical phylogenetics of histone deacetylases
Open accessAbstract
The broad study of histone deacetylases in chemistry, biology and medicine relies on tool compounds to derive mechanistic insights. A phylogenetic analysis of Class I and II HDACs as targets of a comprehensive, structurally diverse panel of inhibitors revealed unexpected isoform selectivity even among compounds widely perceived as non-selective. The synthesis and study of a focused library of cinnamic hydroxamates allowed the identification of a first non-selective HDAC inhibitor. These data will guide a more informed use of HDAC inhibitors as chemical probes and therapeutic agents.
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“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 [26]
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“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 [26]
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“This is consistent with previous reports postulating that an intramolecular hydrogen bond between the amine and carbonyl must be broken to permit successful zinc chelation, and a desolvation penalty is paid for this rearrangement to occur (1, 25-28, 34).”
From Histone Deacetylase (HDAC) Inhibitor Kinetic Rate Constants Correlate with Cellular Histone Acetylation but Not Transcription and Cell Viability (2013) · cites this paper as [26]
Experimental — accuracy not yet measuredIn the citing paper
“Class IIa enzymes (Lahm et al., 2007) as well as HDAC3 (Madsen and Olsen, 2012a), HDAC8 (Bradner et al., 2010), and HDAC11 (Inks et al., 2012) removed the physiologically non-relevant trifluoroacetamide (Ktfa).”
From Histone deacetylase 11 is an ε-N-Myristoyllysine hydrolase (2018) · cites this paper as Bradner et al., 2010
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MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform
Katoh, K. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf436 · Cited by 17,027
A Rapid Bootstrap Algorithm for the RAxML Web Servers
Stamatakis, A., Hoover, P., & Rougemont, J. (2008) · Systematic Biology · doi:10.1080/10635150802429642 · Cited by 7,028
MAFFT version 5: improvement in accuracy of multiple sequence alignment
Katoh, K., Kuma, K., Toh, H., & Miyata, T. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki198 · Cited by 5,063
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
Recent developments in the MAFFT multiple sequence alignment program
Katoh, K., & Toh, H. (2008) · Briefings in Bioinformatics · doi:10.1093/bib/bbn013 · Cited by 3,629
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
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,234
Sustained hippocampal chromatin regulation in a mouse model of depression and antidepressant action
Tsankova, N. M., Berton, O., Renthal, W., Kumar, A., Neve, R. L., & Nestler, E. J. (2006) · Nature Neuroscience · doi:10.1038/nn1659 · Cited by 1,780
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
Histone acetyltransferase complexes: one size doesn't fit all
Lee, K. K. W., & Workman, J. L. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2145 · Cited by 1,091
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Werner, M. S., Loschko, T., King, T. D., Theska, T., Franz‐Wachtel, M., Maček, B., & Sommer, R. J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.21.500386 · Cited by 1
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Booth, S. W., Eyre, T. A., Whittaker, J. A., Campo, L., Wang, L. M., Soilleux, E. J., Royston, D. J., Rees, G., Kesavan, M., Hildyard, C., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15047655
Licandro, S. A., Crippa, L., Pomarico, R., Perego, R., Fossati, G., Leoni, F., & Steinkühler, C. (2021) · Figshare · doi:10.6084/m9.figshare.15041206
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Chapman, S. (2013) · University Library - University of Saskatchewan (University of Saskatchewan)
Licandro, S. A., Crippa, L., Pomarico, R., Perego, R., Fossati, G., Leoni, F., & Steinkühler, C. (2021) · Figshare · doi:10.6084/m9.figshare.15041200
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Licandro, S. A., Crippa, L., Pomarico, R., Perego, R., Fossati, G., Leoni, F., & Steinkühler, C. (2021) · Figshare · doi:10.6084/m9.figshare.15041203
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Metadata
- Authors
- Bradner, J. E., West, N., Grachan, M. L., Greenberg, E. F., Haggarty, S. J., Warnow, T., & Mazitschek, R.
- Affiliations
- Broad Institute (US)
- Harvard University (US)
- The University of Texas at Austin (US)
- Corresponding author
- Bradner, James E
- Mazitschek, Ralph
- Venue
- Nature Chemical Biology
- Published
- 2010-02-07
- Volume
- 6
- Issue
- 3
- Pages
- 238-243
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- PMC
- PMC2822059
- OpenAlex
- W2083784041
- Semantic Scholar
- 68c4985bcae290a761e64065e7e4cfe062700c7f
- Cited by
- 720
- References
- 31
- Citations by year
- 2026: 18 · 2025: 25 · 2024: 27 · 2023: 28 · 2022: 37 · 2021: 50 · 2020: 41 · 2019: 34 · 2018: 39 · 2017: 42 · 2016: 61 · 2015: 64 · 2014: 53 · 2013: 67 · 2012: 62
- FWCI
- 27.21
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Wellcome Trust
- National Institutes of Health (n01co12400-79-0-22)
- Centers for Disease Control and Prevention (N01-C0-012400)
- National Institute on Drug Abuse (R01DA028301)
- National Cancer Institute (N01-CO-012400, K08CA128972, P01CA078048, T32CA079443)
- 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
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Keywords
- histone deacetylase, histone deacetylase inhibitors, isoform selectivity, class I HDACs, class II HDACs, class IIa HDACs, focused libraries, chemical probes, enzyme inhibition mechanism
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 ›
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