ReviewCell cycle (Georgetown, Tex.)2019
Lysine-specific post-translational modifications of proteins in the life cycle of viruses.
Review in Cell cycle (Georgetown, Tex.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Phage tail protein methylation enabling the virus to bind to the surface of bacterial cells is vital for progeny infectivity.Cell insight · 2026Article
- The vesicular stomatitis virus matrix protein promotes FACT subunit depletion to suppress the FEAR pathway.PLoS pathogens · 2026Article
- Acetylation-mediated regulation of ALV viral proteins: Implications for retroviral inhibition.PLoS pathogens · 2026Article
- Activation and Evasion of the FEAR Pathway by RNA Viruses.bioRxiv : the preprint server for biology · 2025Article
- Increased preference for lysine over arginine in spike proteins of SARS-CoV-2 BA.2.86 variant and its daughter lineages.PloS one · 2025Article
- Epigenetic and epitranscriptomic regulation during oncogenicFrontiers in microbiology · 2024Review
- Functional diversity: update of the posttranslational modification of Epstein-Barr virus coding proteins.Cellular and molecular life sciences : CMLS · 2022Review
- Protein Acetylation Going Viral: Implications in Antiviral Immunity and Viral Infection.International journal of molecular sciences · 2022Review
- Sources, fates and treatment strategies of typical viruses in urban sewage collection/treatment systems: A review.Desalination · 2022Article
- Interferon‑stimulated gene 15 promotes progression of endometrial carcinoma and weakens antitumor immune response.Oncology reports · 2022Article
- Article
- SUMOylation Is Essential for Dengue Virus Replication and Transmission in the MosquitoFrontiers in microbiology · 2022Article
- In silico investigation of the viroporin E as a vaccine target against SARS-CoV-2.American journal of physiology. Lung cellular and molecular physiology · 2021Article
- Catalytic activity regulation through post-translational modification: the expanding universe of protein diversity.Advances in protein chemistry and structural biology · 2020Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The process of protein post-translational modifications (PTM) is one of the critical mechanisms of regulation of many cellular processes, which makes it an attractive target for various viruses. Since viruses cannot replicate on their own, they have developed unique abilities to alter metabolic and signaling cell pathways, including protein PTMs, to ensure faithful replication of their genomes. This review describes several ways of how lysine-specific PTMs are used by various viruses to ensure its successful invasion and replication. Covalent modifications like acetylation, ubiquitination, and methylation form a complex system of reversible and often competing modifications, which adds an additional level of complexity to the system of regulation of the activity of host proteins involved in viral replication and propagation. In furthering these, we also describe the manner in which PTM pathways can also be accosted by various types of viruses to neutralize the host's cellular mechanisms for anti-viral protection and highlight key areas for future therapeutic targeting and design.
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