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While MITF does not exhibit druggable activity, its expression was shown to be attenuated by multiple histone deacetylase (HDAC -inhibitor drugs [53].
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Using an all-in-one construct carrying PTG, we disrupt the deacetylase domain in multiple histone deacetylases (HDACs) in human cells simultaneously.
Galli, M. et al. A phase II multiple dose clinical trial of histone deacetylase inhibitor ITF2357 in patients with relapsed or progressive multiple myeloma.
Transcriptional signature of histone deacetylase inhibition in multiple myeloma: biological and clinical implications.
Preclinical data and early clinical experience supporting the use of histone deacetylase inhibitors in multiple myeloma.
Repression requires histone deacetylase activity suggesting multiple components are involved in Groucho competition with β-catenin.
Our data also reveals that AES opposes LEF-1 transcription activation and that both Groucho and AES repression require histone deacetylase activity suggesting multiple steps in Groucho competition with β-catenin.
Multiple mechanisms of action were identified, including histone deacetylase inhibition, tubulin modulation and pre-mRNA processing.
Furthermore, multiple studies have observed that inhibition of histone deacetylase (HDAC), trichostatin A (TSA), valproic acid (VPA) and nicotinamide (NAM) enhances HBV replication, suggesting that histone acetylation may promote HBV replication [ 7, 8].
However, we have shown that HDA6 is a broad specificity histone deacetylase capable of removing acetyl groups from multiple lysines of multiple histones [16], suggesting that HDA6 might erase histone acetylation throughout the regions to which it is recruited.
The proteasome inhibitor bortezomib demonstrates marked pre-clinical activity when combined with the histone deacetylase inhibitor vorinostat in leukemia, multiple myeloma, and mantle cell lymphoma (MCL) cells.
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