The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Structure, mechanism, and inhibition of histone deacetylases and related metalloenzymes
Open accessAbstract
Metal-dependent histone deacetylases (HDACs) catalyze the hydrolysis of acetyl-L-lysine side chains in histone and non-histone proteins to yield L-lysine and acetate. This chemistry plays a critical role in the regulation of numerous biological processes. Aberrant HDAC activity is implicated in various diseases, and HDACs are validated targets for drug design. Two HDAC inhibitors are currently approved for cancer chemotherapy, and other inhibitors are in clinical trials. To date, X-ray crystal structures are available for four human HDACs (2, 4, 7, 8) and three HDAC-related deacetylases from bacteria (histone deacetylase-like protein, HDLP; histone deacetylase-like amidohydrolase, HDAH; acetylpolyamine amidohydrolase, APAH). Structural comparisons among these enzymes reveal a conserved constellation of active site residues, suggesting a common mechanism for the metal-dependent hydrolysis of acetylated substrates. Structural analyses of HDACs and HDAC-related deacetylases guide the design of tight-binding inhibitors, and future prospects for developing isozyme-specific inhibitors are quite promising.
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Cites
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
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A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
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Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
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Lysine Acetylation: Codified Crosstalk with Other Posttranslational Modifications
Yang, X.-J., & Seto, E. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.002 · Cited by 1,006
Histone Deacetylase Inhibitors in Cancer Therapy
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Histone deacetylase inhibitors: Potential in cancer therapy
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Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases
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“To date, this α/β fold has been observed in structures of the catalytic domains of HDAC2 [18••], HDAC4 [19], and HDAC7 [20], and full-length HDAC8 [21, 22].”
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Cited by
Histone deacetylase 6 structure and molecular basis of catalysis and inhibition
Hai, Y., & Christianson, D. W. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2134 · Cited by 521
Self-citationStructural insights into HDAC6 tubulin deacetylation and its selective inhibition
Miyake, Y., Keusch, J. J., Wang, L., Saito, M., Hess, D., Wang, X., Melancon, B. J., Helquist, P., Gut, H., & Matthias, P. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2140 · Cited by 315
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
Self-citationUnusual zinc-binding mode of HDAC6-selective hydroxamate inhibitors
Porter, N. J., Mahendran, A., Breslow, R., & Christianson, D. W. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718823114 · Cited by 190
Self-citationMarek, M., Kannan, S., Hauser, A.-T., Moraes Mourão, M., Caby, S., Cura, V., Stolfa, D. A., Schmidtkunz, K., Lancelot, J., Andrade, L., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003645 · Cited by 173
Metadata
- Authors
- Lombardi, P. M., Cole, K. E., Dowling, D. P., & Christianson, D. W.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2011-12
- Volume
- 21
- Issue
- 6
- Pages
- 735-743
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2009954700
- Cited by
- 277
- References
- 54
- FWCI
- 0.72
- Type
- journal article
- Language
- en
- Open access
- green
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