| Literature DB >> 28261707 |
Seungyong You1, James Froberg1, Junru Yu2, Manas Haldar3, Abbas Sedigh2, Sanku Mallik3, D K Srivastava2, Yongki Choi1.
Abstract
Using single-molecule approaches, we directly observed the dynamic interaction between HDAC8 and various ligands as well as conformational interconversions during the catalytic reaction. Statistical analysis identified key kinetic parameters, demonstrating that the enzymatic activity is highly sensitive to both minor variations in the ligand structures and small synthetic molecules.Entities:
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Year: 2017 PMID: 28261707 PMCID: PMC5510773 DOI: 10.1039/c6cc09949a
Source DB: PubMed Journal: Chem Commun (Camb) ISSN: 1359-7345 Impact factor: 6.222