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Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases

Previous findings have suggested that class IIa histone deacetylases (HDACs) (HDAC4, -5, -7, and -9) are inactive on acetylated substrates, thus differing from class I and IIb enzymes. Here, we present evidence supporting this view and demonstrate that class IIa HDACs are very inefficient enzymes on...

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Autori principali: Lahm, A., Paolini, C., Pallaoro, M., Nardi, M. C., Jones, P., Neddermann, P., Sambucini, S., Bottomley, M. J., Lo Surdo, P., Carfí, A., Koch, U., De Francesco, R., Steinkühler, C., Gallinari, P.
Natura: Artigo
Lingua:Inglês
Pubblicazione: National Academy of Sciences 2007
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC2077257/
https://ncbi.nlm.nih.gov/pubmed/17956988
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0706487104
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