Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases.

By J. Somoza, R. Skene, B. Katz, C. Mol, J. Ho, A. Jennings, C. Luong, A. Arvai, J. Buggy, Ellen Chi and 12 more. Structure, 2004

694 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/3f3a8cb723abad6b05b1dbcc91a52823ad6e1447

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In Molecular Biology

1. PA Marks
2. W-S Xu
3. E. Seto
4. Ricky W. Johnstone
5. S. Minucci
6. Pier Giuseppe Pelicci
7. Guangdi Wang
8. Tien L. Huang

In Oncology

1. E. Seto
2. Ricky W. Johnstone
3. S. Minucci
4. PA Marks
5. Pier Giuseppe Pelicci

Citations in the corpus

• Histone deacetylase inhibitors: molecular mechanisms of action (2007, background): “More recently, the crystal structure of HDAC8–hydroxamate interaction has been solved (Somoza et al., 2004; Vannini et al., 2004).”
• Histone Deacetylase Inhibitors: Potential in Cancer Therapy (2009, background): “A number of HDAC isoform selective or specific inhibitors are currently in development [Haggarty et al., 2003; Somoza et al., 2004; Kozikowski et al., 2007; Rasheed et al., 2007; Butler and Kozikowski, 2008; Estiu et al., 2008; Khan et al., 2008; Moradei et al., 2008; Jones et al., 2008a; Schemies e”
• Erasers of histone acetylation: the histone deacetylase enzymes. (2014, background): “Crystal structures of HDAC8 revealed that S39 lies at the surface of HDAC8, roughly 20 Å from the opening to the HDAC8 active site (Somoza et al. 2004).”
• Histone Deacetylase Inhibitors in Clinical Studies as Templates for New Anticancer Agents (2015, background): “of the active site, whereas the metal binding moiety resides in the interior of the protein and form complexes with the metal ion [34,154–156].”
• New and emerging HDAC inhibitors for cancer treatment. (2014, positive): “org Volume 124 Number 1 January 2014 assisted with in silico screening for appropriate chemical inhibitors (50, 72), the most promising of which is PCI-34051.”
• Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer (2006, background): “From the structure of HDAC8 or HDLP (a HDAC-like protein isolated from Aquifex aeolicus ), and the structure of these enzymes in complex with a small number of HDACi, a few key points have emerged about the active site that support a pharmacophore model for HDAC inhibitio”