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The E3 ligase malin plays a pivotal role in promoting nuclear glycogenolysis and histone acetylation
Author(s) -
Katherine J. Donohue,
Matthew S. Gentry,
Ramon C. Sun
Publication year - 2020
Publication title -
annals of translational medicine
Language(s) - English
Resource type - Journals
eISSN - 2305-5847
pISSN - 2305-5839
DOI - 10.21037/atm.2020.01.130
Subject(s) - acetylation , ubiquitin ligase , histone , glycogenolysis , microbiology and biotechnology , chemistry , ubiquitin , biology , biochemistry , metabolism , dna , gene
Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY, USA; Markey Cancer Center University of Kentucky, Lexington, KY, USA; Department of Neuroscience, University of Kentucky, Lexington, KY, USA Correspondence to: Matthew S. Gentry; Ramon C. Sun. University of Kentucky, 741 South Limestone Street, B179, Lexington, KY 40536-0509, USA. Email: matthew.gentry@uky.edu; ramon.sun@uky.edu. Provenance and Peer Review: This article was commissioned and reviewed by the Section Editor Dr. Ran Mo (Department of Burn and Plastic Surgery, Nanjing Drum Tower Hospital, Nanjing, China). Response to: Feron O. The many metabolic sources of acetyl-CoA to support histone acetylation and influence cancer progression. Ann Transl Med 2019;7:S277.

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