Cited by 769Histone Deacetylase Inhibitors ResearchEnzyme function and inhibitionCholinesterase and Neurodegenerative Diseases

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Chemical phylogenetics of histone deacetylases

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Bradner, James E, West, Nathan, Grachan, Melissa L, Greenberg, Edward F, Haggarty, Stephen J, Warnow, Tandy, Mazitschek, Ralph·2010·Nature Chemical Biology

DOI 10.1038/nchembio.313PMC PMC2822059

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Abstract

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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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
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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
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
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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Self-citation
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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
ORCID: Bradner, James E
Greenberg, Edward F
Haggarty, Stephen J
Warnow, Tandy
Mazitschek, Ralph
Venue: Nature Chemical Biology
Publisher: Springer Science and Business Media LLC
Published: 2010-02-07
Volume: 6
Issue: 3
Pages: 238-243
ISSN: 1552-4450 (ISSN-L)
1552-4469
DOI: 10.1038/nchembio.313
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

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Chemical phylogenetics of histone deacetylases

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