The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Development of a histone deacetylase 6 inhibitor and its biological effects
Open accessAbstract
Significance: We discovered a hydroxamic acid-based small-molecule N -hydroxy-4-(2-[(2-hydroxyethyl)(phenyl)amino]-2-oxoethyl)benzamide selectively inhibits histone deacetylase 6 catalytic activity in vivo and in vitro.
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“Accordingly, the potency of HPOB against HDAC6 is comparable to SAHA-like inhibitors, but HPOB potency against other isozymes is significantly reduced.43”
From Histone deacetylase 6 structure and molecular basis of catalysis and inhibition (2016) · cites this paper as [43]
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Cites
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
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
Marks, P. A., & Breslow, R. (2007) · Nature Biotechnology · doi:10.1038/nbt1272 · Cited by 1,198
Self-citationHDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153
Sarkar, S., Davies, J. E., Huang, Z., Tunnacliffe, A., & Rubinsztein, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609532200 · Cited by 1,142
Haggarty, S. J., Koeller, K. M., Wong, J. C., Grozinger, C. M., & Schreiber, S. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0430973100 · Cited by 1,066
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
HDAC6 controls autophagosome maturation essential for ubiquitin‐selective quality‐control autophagy
Lee, J., Koga, H., Kawaguchi, Y., Tang, W., Wong, E., Gao, Y., Pandey, U. B., Kaushik, S., Tresse, E., Lu, J., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.405 · Cited by 756
Self-citationHDAC6 Modulates Cell Motility by Altering the Acetylation Level of Cortactin
Zhang, X. M., Yuan, Z., Zhang, Y., Yong, S., Salas-Burgos, A., Koomen, J. M., Olashaw, N., Parsons, J. T., Yang, X., Dent, S., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.033 · Cited by 731
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
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Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
Falkenberg, K. J., & Johnstone, R. W. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4360 · Cited by 1,564
HDACs and HDAC Inhibitors in Cancer Development and TherapyPreprint
Li, Y., & Seto, E. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026831 · Cited by 1,337
Off-target toxicity is a common mechanism of action of cancer drugs undergoing clinical trials
Lin, A., Giuliano, C. J., Palladino, A. C., John, K. M., Abramowicz, C., Yuan, M. L., Sausville, E. L., Lukow, D. A., Liu, L., Chait, A. R., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aaw8412 · Cited by 769
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
“43”
Inside HDACs with more selective HDAC inhibitors
Roche, J., & Bertrand, P. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.05.047 · Cited by 327
Metadata
- Authors
- Lee, J.-H., Mahendran, A., Yao, Y., Ngo, L., Venta-Perez, G., Choy, M. L., Kim, N., Ham, W.-S., Breslow, R., & Marks, P. A.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Columbia University (US)
- Corresponding author
- Marks, Paul A.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2013-09-10
- Volume
- 110
- Issue
- 39
- Pages
- 15704-15709
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3785767
- OpenAlex
- W2148383035
- Cited by
- 141
- References
- 28
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 6 · 2023: 7 · 2022: 7 · 2021: 15 · 2020: 15 · 2019: 17 · 2018: 16 · 2017: 12 · 2016: 14 · 2015: 13 · 2014: 7
- FWCI
- 5.53
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Servier
- National Cancer Institute (P30CA08748-44, P30CA008748)
- 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 › Epigenetics and DNA Methylation
- Keywords
- HDAC6, HDAC6 inhibitors, isoform-selective inhibition, hydroxamic acids, DNA-damaging agents, growth inhibition, small molecule inhibitors
- MeSH terms
- Vorinostat, Acetylation, Animals, Antineoplastic Agents, Autophagy, Cell Line, Transformed, Cell Survival, Doxorubicin, Etoposide, Histone Deacetylases, Histones, Humans, Hydroxamic Acids, Trehalose, Tubulin, Apoptosis, Xenograft Model Antitumor Assays, Cell Line, Tumor, Mice, DNA Breaks, Double-Stranded, Histone Deacetylase Inhibitors
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