Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor.

By A. Vannini, C. Volpari, G. Filocamo, E. C. Casavola, M. Brunetti, D. Renzoni, P. Chakravarty, C. Paolini, R. de Francesco, P. Gallinari and 2 more. Proceedings of the National Academy of Sciences of the United States of America, 2004

623 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/03c10a313fe9a3fe15c2052dfba5f2319155ebba

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In Molecular Biology

1. W-S Xu
2. PA Marks
3. Xiang-Jiao Yang
4. E. Seto
5. Weisheng Xu
6. R. Parmigiani
7. Guangdi Wang
8. Tien L. Huang

In Oncology

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2. PA Marks
3. Xiang-Jiao Yang

Citations in the corpus

• The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men (2008, background): “html">Supplementary information S2a (figure) ) for protein kinase A phosphorylation and negative regulation of deacetylase activit”
• New and emerging HDAC inhibitors for cancer treatment. (2014, neutral): “org Volume 124 Number 1 January 2014 35 in normal but not tumor cells (50).”
• 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).”
• Therapeutic application of histone deacetylase inhibitors for central nervous system disorders (2008, background): “Several highly potent in vitro and in vivo HDAC inhibitors have been designed and developed, and some lead compounds have demonstrated activity in the impressively low nanomolar rang”
• Histone Deacetylase Inhibitors: Potential in Cancer Therapy (2009, positive): “Based on the co-crystal structures of hydroxamate inhibitors with HDAC4, HDAC 8 and an anaerobic bacterial HDAC like protein (HDLP) [Finnin et al., 1999; Somoza et al., 2004; Vannini et al., 2004], it is clear that these functional groups interact with three conserved regions of the active site.”
• 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].”