The antiviral sirtuin 3 bridges protein acetylation to mitochondrial integrity and metabolism during human cytomegalovirus infection
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Title
The antiviral sirtuin 3 bridges protein acetylation to mitochondrial integrity and metabolism during human cytomegalovirus infection
Authors
Keywords
Mitochondria, Acetylation, Fatty acids, Enzyme regulation, Proteomes, Viral replication, Mitochondrial membrane, Protein metabolism
Journal
PLoS Pathogens
Volume 17, Issue 4, Pages e1009506
Publisher
Public Library of Science (PLoS)
Online
2021-04-16
DOI
10.1371/journal.ppat.1009506
References
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Note: Only part of the references are listed.- Orchestration of protein acetylation as a toggle for cellular defense and virus replication
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- Sirt3 Mediates Reduction of Oxidative Damage and Prevention of Age-Related Hearing Loss under Caloric Restriction
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- Human Cytomegalovirus Activates Glucose Transporter 4 Expression To Increase Glucose Uptake during Infection
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- Sirt3-Mediated Deacetylation of Evolutionarily Conserved Lysine 122 Regulates MnSOD Activity in Response to Stress
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- SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
- (2010) Matthew D. Hirschey et al. NATURE
- Human cytomegalovirus US9 protein contains an N-terminal signal sequence and a C-terminal mitochondrial localization domain, and does not alter cellular sensitivity to apoptosis
- (2009) L. Mandic et al. JOURNAL OF GENERAL VIROLOGY
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