Probing the structure-activity relationship of endogenous histone deacetylase complexes with immobilized peptide-inhibitors

Histone deacetylases (HDACs) are key regulators of numerous cellular proteins by removing acetylation marks from modified lysine residues. Peptide‐based HDAC probes containing α‐aminosuberic acid ω‐hydroxamate have been established as useful tools for investigating substrate selectivity and composit...

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Veröffentlicht in:	Journal of peptide science 2016-05, Vol.22 (5), p.352-359
Hauptverfasser:	Sindlinger, Julia, Bierlmeier, Jan, Geiger, Lydia-Christina, Kramer, Katharina, Finkemeier, Iris, Schwarzer, Dirk
Format:	Artikel
Sprache:	eng
Schlagworte:	activity-based probes HDAC inhibitors HDACs HeLa Cells Histone Deacetylase Inhibitors - chemical synthesis Histone Deacetylase Inhibitors - chemistry Histone Deacetylase Inhibitors - pharmacology Histone Deacetylases - metabolism Humans Hydroxamic Acids - chemistry lysine acetylation Molecular Structure Peptides Peptides - chemical synthesis Peptides - chemistry Peptides - pharmacology Structure-Activity Relationship
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