Cargando…
Thermodynamics of Binding of Structurally Similar Ligands to Histone Deacetylase 8 Sheds Light on Challenges in the Rational Design of Potent and Isozyme-Selective Inhibitors of the Enzyme
[Image: see text] Among the different histone deacetylase (HDAC) isozymes, HDAC8 is the most highly malleable enzyme, and it exhibits the potential to accommodate structurally diverse ligands (albeit with moderate binding affinities) in its active site pocket. To probe the molecular basis of this fe...
Autores principales: | Singh, Raushan K., Suzuki, Takayoshi, Mandal, Tanmay, Balsubramanian, Narayanaganesh, Haldar, Manas, Mueller, Dustin J., Strode, Jerrod A., Cook, Gregory, Mallik, Sanku, Srivastava, D. K. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4263425/ https://www.ncbi.nlm.nih.gov/pubmed/25407689 http://dx.doi.org/10.1021/bi500711x |
Ejemplares similares
-
Role of the Substrate Specificity-Defining Residues of Human SIRT5 in Modulating the Structural Stability and Inhibitory Features of the Enzyme
por: Yu, Junru, et al.
Publicado: (2016) -
Rational thermodynamics
por: Truesdell, C
Publicado: (1984) -
Hydroxamic acid-modified peptide microarrays for profiling isozyme-selective interactions and inhibition of histone deacetylases
por: Moreno-Yruela, Carlos, et al.
Publicado: (2021) -
Rational extended thermodynamics
por: Müller, Ingo, et al.
Publicado: (1998) -
Prostate-Specific Membrane Antigen Targeted Polymersomes
for Delivering Mocetinostat and Docetaxel to Prostate Cancer Cell
Spheroids
por: Karandish, Fataneh, et al.
Publicado: (2016)