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Updated: Jul 13, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
Ubiquitination, phosphorylation, and acetylation--triple threat in muscle wasting
1Department of Surgery, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215, USA. phasselg@bidmc.harvard.edu
Abstract:
Loss of muscle mass is commonly seen in patients with critical illness and is associated with increased expression of multiple genes controlling protein breakdown. Transcription factors that are activated during muscle wasting include NF-kB and members of the FOXO and C/EBP transcription factor families. The activity of these transcription factors is regulated by multiple posttranslational modifications, including ubiquitination, phosphorylation, and acetylation, providing for a complex and integrated network of regulatory mechanisms in muscle wasting. Targeting posttranslational modifications of transcription factors may prove important in the prevention and treatment of the debilitating consequences of muscle wasting.
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