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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: | , , , , , , , , , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
2007
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| Soggetti: | |
| 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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