ArticleInternational journal of molecular sciences2021
Adenovirus Terminal Protein Contains a Bipartite Nuclear Localisation Signal Essential for Its Import into the Nucleus.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Genome-replicating HC-AdV: A novel high-capacity adenoviral vector class featuring enhancedMolecular therapy. Methods & clinical development · 2025Article
- A Review over Mitochondrial Diseases Due to mtDNA Mutations: Recent Advances and Remedial Aspects.Infectious disorders drug targets · 2025Review
- FastAd: A versatile toolkit for rapid generation of single adenoviruses or diverse adenoviral vector libraries.Molecular therapy. Methods & clinical development · 2024Article
- RETRACTED: Regions of Bovine Adenovirus-3 Protein VII Involved in Interactions with Viral and Cellular Proteins.Viruses · 2024Article
- Recent advances in mitochondrial diseases: From molecular insights to therapeutic perspectives.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2022Review
- Importin-Mediated Pathological Tau Nuclear Translocation Causes Disruption of the Nuclear Lamina, TDP-43 Mislocalization and Cell Death.Frontiers in molecular neuroscience · 2022Article
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Authors and funding
7 authors.
Funding
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Abstract
Adenoviruses contain dsDNA covalently linked to a terminal protein (TP) at the 5'end. TP plays a pivotal role in replication and long-lasting infectivity. TP has been reported to contain a nuclear localisation signal (NLS) that facilitates its import into the nucleus. We studied the potential NLS motifs within TP using molecular and cellular biology techniques to identify the motifs needed for optimum nuclear import. We used confocal imaging microscopy to monitor the localisation and nuclear association of GFP fusion proteins. We identified two nuclear localisation signals, PV(R)6VP and MRRRR, that are essential for fully efficient TP nuclear entry in transfected cells. To study TP-host interactions further, we expressed TP in
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