Curcumin and hydroxamate-derivative (PCI-34058) interfere with histone deacetylase I catalytic core Asp-His charge relay system: atomistic simulation studies. (Q39019571)

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scientific article published on 10 April 2015

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English	Curcumin and hydroxamate-derivative (PCI-34058) interfere with histone deacetylase I catalytic core Asp-His charge relay system: atomistic simulation studies.	scientific article published on 10 April 2015

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5 March 2020

Curcumin and hydroxamate-derivative (PCI-34058) interfere with histone deacetylase I catalytic core Asp-His charge relay system: atomistic simulation studies (English)

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Oluwamodupe Ejelonu

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I O Omotuyi

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M O Abiodun

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K Komolafe

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O Olusanya

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10 April 2015

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Journal of Molecular Modeling

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https://scigraph.springernature.com/pub.10.1007/s00894-015-2655-8

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Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily

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

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GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation

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Comparison of multiple Amber force fields and development of improved protein backbone parameters

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Development and testing of a general amber force field

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Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation

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Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion.

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Activation and inhibition of histone deacetylase 8 by monovalent cations

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Structures of Metal-Substituted Human Histone Deacetylase 8 Provide Mechanistic Inferences on Biological Function,

1 reference

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