ArticleJournal of virology2011
Mobility and interactions of coronavirus nonstructural protein 4.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
46 citing papers in PubMed.
- Genome-scale CRISPR screen identifies TMEM198 driving double membrane vesicle formation in swine alphacoronavirus and murine betacoronavirus infected cells.PLoS pathogens · 2025Article
- The SARS-CoV-2 NSP4 T492I mutation promotes double-membrane vesicle formation to facilitate transmission.Virologica Sinica · 2025Article
- A coronaviral pore-replicase complex links RNA synthesis and export from double-membrane vesicles.Science advances · 2024Article
- Oligomeric assembly of the C-terminal and transmembrane region of SARS-CoV-2 nsp3.Journal of virology · 2024Article
- Multiple Lines of Evidence Support 199 SARS-CoV-2 Positively Selected Amino Acid Sites.International journal of molecular sciences · 2024Article
- Mechanism, structural and functional insights into nidovirus-induced double-membrane vesicles.Frontiers in immunology · 2024Review
- An ncRNA transcriptomics-based approach to design siRNA molecules against SARS-CoV-2 double membrane vesicle formation and accessory genes.BMC infectious diseases · 2023Article
- Crystal structure of the CoV-Y domain of SARS-CoV-2 nonstructural protein 3.Scientific reports · 2023Article
- Scalable Inhibitors of the Nsp3-Nsp4 Coupling in SARS-CoV-2.ACS omega · 2023Article
- A review on structural, non-structural, and accessory proteins of SARS-CoV-2: Highlighting drug target sites.Immunobiology · 2023Review
- Article
- Unique mutations in SARS-CoV-2 Omicron subvariants' non-spike proteins: Potential impacts on viral pathogenesis and host immune evasion.Microbial pathogenesis · 2022Review
- Endomembrane remodeling in SARS-CoV-2 infection.Cell insight · 2022Review
- Lipid and Nucleocapsid N-Protein Accumulation in COVID-19 Patient Lung and Infected Cells.Microbiology spectrum · 2022Article
- Why do SARS-CoV-2 NSPs rush to the ER?Journal of neurology · 2021Review
- Understanding COVID-19 via comparative analysis of dark proteomes of SARS-CoV-2, human SARS and bat SARS-like coronaviruses.Cellular and molecular life sciences : CMLS · 2021Article
- Unpacking Pandora From Its Box: Deciphering the Molecular Basis of the SARS-CoV-2 Coronavirus.International journal of molecular sciences · 2020Review
- Review
- Various Facets of Pathogenic Lipids in Infectious Diseases: Exploring Virulent Lipid-Host Interactome and Their Druggability.The Journal of membrane biology · 2020Review
- The molecular virology of coronaviruses.The Journal of biological chemistry · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Green fluorescent protein (GFP)-tagged mouse hepatitis coronavirus nonstructural protein 4 (nsp4) was shown to localize to the endoplasmic reticulum (ER) and to be recruited to the coronavirus replicative structures. Fluorescence loss in photobleaching and fluorescence recovery after photobleaching experiments demonstrated that while the membranes of the ER are continuous with those harboring the replicative structures, the mobility of nsp4 at the latter structures is relatively restricted. In agreement with that observation, nsp4 was shown to be engaged in homotypic and heterotypic interactions, the latter with nsp3 and nsp6. In addition, the coexpression of nsp4 with nsp3 affected the subcellular localization of the two proteins.
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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.