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Literature DB >> 16719825

Rational design of non-hydroxamate histone deacetylase inhibitors.

Abstract

While most inhibitors of histone deacetylases (HDACs) are hydroxamic acid derivatives, several non-hydroxamates have recently been developed as inhibitors and attracted quite a deal of attention. In this review, we present the rational design, inhibitory effect and antiproliferative activity of non-hydroxamate HDAC inhibitors.

Entities: Chemical

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Year: 2006 PMID： 16719825 DOI： 10.2174/138955706776876186

Source DB: PubMed Journal: Mini Rev Med Chem ISSN： 1389-5575 Impact factor: 3.862

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Cited

7 in total

1. Identifying chelators for metalloprotein inhibitors using a fragment-based approach.

Authors: Jennifer A Jacobsen; Jessica L Fullagar; Melissa T Miller; Seth M Cohen
Journal: J Med Chem Date: 2010-12-28 Impact factor: 7.446

2. Synthesis of (S)-2-Boc-Amino-8-(R)-(tert-butyldimethylsilanyloxy) decanoic acid, a Precursor to the Unusual Amino Acid Residue of the Anticancer Agent Microsporin B.

Authors: Wenxin Gu; Richard B Silverman
Journal: Tetrahedron Lett Date: 2011-10-19 Impact factor: 2.415

7. Generation of the first structure-based pharmacophore model containing a selective "zinc binding group" feature to identify potential glyoxalase-1 inhibitors.

Authors: Qosay Al-Balas; Mohammad Hassan; Buthina Al-Oudat; Hassan Alzoubi; Nizar Mhaidat; Ammar Almaaytah
Journal: Molecules Date: 2012-11-22 Impact factor: 4.411

7 in total

Rational design of non-hydroxamate histone deacetylase inhibitors.

1. Identifying chelators for metalloprotein inhibitors using a fragment-based approach.

2. Synthesis of (S)-2-Boc-Amino-8-(R)-(tert-butyldimethylsilanyloxy) decanoic acid, a Precursor to the Unusual Amino Acid Residue of the Anticancer Agent Microsporin B.

3. Novel histone deacetylase 8 ligands without a zinc chelating group: exploring an 'upside-down' binding pose.

4. Computational exploration of zinc binding groups for HDAC inhibition.

5. Histone deacetylase inhibitors through click chemistry.

6. Novel glyoxalase-I inhibitors possessing a "zinc-binding feature" as potential anticancer agents.

7. Generation of the first structure-based pharmacophore model containing a selective "zinc binding group" feature to identify potential glyoxalase-1 inhibitors.