ReviewCells2019
Viral Appropriation: Laying Claim to Host Nuclear Transport Machinery.
Review in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed.
- Tripartite motif-containing 34 (TRIM34) protein interacts with the nucleocytoplasmic transport machinery and negatively modulates antiviral responses.PLoS pathogens · 2026Article
- Therapeutic options for the treatment of post-acute sequelae of COVID-19: a scoping review.BMC infectious diseases · 2025Article
- Arabidopsis RNA-binding proteins interact with viral structural proteins and modify turnip yellows virus accumulation.Plant physiology · 2024Article
- CDK7/CDK9 mediates transcriptional activation to prime paraptosis in cancer cells.Cell & bioscience · 2024Article
- Quantitative comparison of nuclear transport inhibition by SARS coronavirus ORF6 reveals the importance of oligomerization.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Prospective mode of action of Ivermectin: SARS-CoV-2.European journal of medicinal chemistry reports · 2022Review
- Nuclear-localized human respiratory syncytial virus NS1 protein modulates host gene transcription.Cell reports · 2021Article
- Article
- Crosstalk between nucleocytoplasmic trafficking and the innate immune response to viral infection.The Journal of biological chemistry · 2021Review
- Application of multiple omics and network projection analyses to drug repositioning for pathogenic mosquito-borne viruses.Scientific reports · 2021Article
- Emerging antiviral therapeutics for human adenovirus infection: Recent developments and novel strategies.Antiviral research · 2021Review
- Transportin-1: A Nuclear Import Receptor with Moonlighting Functions.Frontiers in molecular biosciences · 2021Review
- Strength in Diversity: Nuclear Export of Viral RNAs.Viruses · 2020Review
- Inhibition of Human Adenovirus Replication by the Importin α/β1 Nuclear Import Inhibitor Ivermectin.Journal of virology · 2020Article
- Ivermectin: potential candidate for the treatment of Covid 19.The Brazilian journal of infectious diseases : an official publication of the Brazilian Society of Infectious DiseasesArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein nuclear transport is an integral process to many cellular pathways and often plays a critical role during viral infection. To overcome the barrier presented by the nuclear membrane and gain access to the nucleus, virally encoded proteins have evolved ways to appropriate components of the nuclear transport machinery. By binding karyopherins, or the nuclear pore complex, viral proteins influence their own transport as well as the transport of key cellular regulatory proteins. This review covers how viral proteins can interact with different components of the nuclear import machinery and how this influences viral replicative cycles. We also highlight the effects that viral perturbation of nuclear transport has on the infected host and how we can exploit viruses as tools to study novel mechanisms of protein nuclear import. Finally, we discuss the possibility that drugs targeting these transport pathways could be repurposed for treating viral infections.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.