Cargando…
The Activity of HDAC8 Depends on Local and Distal Sequences of Its Peptide Substrates
[Image: see text] This paper introduces a flexible assay for characterizing the activities of the histone deacetylase enzymes. The approach combines mass spectrometry with self-assembled monolayers that present acetylated peptides and enables a label-free and one-step assay of this biochemical activ...
Autores principales: | Gurard-Levin, Zachary A., Mrksich, Milan |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2008
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2605276/ https://www.ncbi.nlm.nih.gov/pubmed/18470998 http://dx.doi.org/10.1021/bi800053v |
Ejemplares similares
-
Peptide Arrays Identify Isoform-Selective Substrates for Profiling Endogenous Lysine Deacetylase Activity
por: Gurard-Levin, Zachary A., et al.
Publicado: (2010) -
High-Throughput Screening of Small Molecule Libraries using SAMDI Mass Spectrometry
por: Gurard-Levin, Zachary A., et al.
Publicado: (2011) -
Rate Enhancement of an Interfacial Biochemical Reaction through Localization of Substrate and Enzyme by an Adaptor Domain
por: Li, Jing, et al.
Publicado: (2010) -
Acetyltransferase p300/CBP Associated Factor (PCAF)
Regulates Crosstalk-Dependent Acetylation of Histone H3 by Distal
Site Recognition
por: Kornacki, James R., et al.
Publicado: (2014) -
Tyrosine phosphatase activity is restricted by basic charge substituting mutation of substrates
por: Huang, Che-Fan, et al.
Publicado: (2022)