ArticleJournal of virology1996
Mutations in the zinc-binding motif of the reovirus capsid protein delta 3 eliminate its ability to associate with capsid protein mu 1.
Article in Journal of virology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- Structure-Based Deep Mining Reveals First-Time Annotations for 46 Percent of the Dark Annotation Space of the 9,671-Member Superproteome of the Nucleocytoplasmic Large DNA Viruses.Journal of virology · 2020Article
- Synthesis and Translation of Viral mRNA in Reovirus-Infected Cells: Progress and Remaining Questions.Viruses · 2018Review
- JAM-A-independent, antibody-mediated uptake of reovirus into cells leads to apoptosis.Journal of virology · 2006Article
- Structural classification of zinc fingers: survey and summary.Nucleic acids research · 2003Article
- Sites and determinants of early cleavages in the proteolytic processing pathway of reovirus surface protein sigma3.Journal of virology · 2002Article
- Structure of the reovirus outer capsid and dsRNA-binding protein sigma3 at 1.8 A resolution.The EMBO journal · 2001Article
- The Cys(3)-His(1) motif of the respiratory syncytial virus M2-1 protein is essential for protein function.Journal of virology · 2000Article
- Article
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Authors and funding
4 authors.
Funding
Abstract
Reovirus capsid protein delta 3 binds both double-stranded RNA (dsRNA) and zinc. Previous studies have revealed that the amino-terminal zinc finger is not required for the ability of delta 3 to bind dsRNA. We expressed wild-type and mutant delta 3 molecules by in vitro transcription/translation to evaluate the importance of the zinc finger for other functions of delta 3. delta 3 molecules with mutations in the zinc finger did not form complexes with capsid protein mu 1 but bound dsRNA more efficiently than wild-type delta 3 did. In contrast, a dsRNA-binding mutant was unimpaired in its ability to associate with mu 1. Studies with delta 3 fragments support these findings and indicate that sequences critical for delta 3's interaction with mu 1 lie in the amino terminus of the molecule. Our finding that mu 1 and dsRNA do not compete for identical binding sites on delta 3 has implications for its function as a translational regulator in infected cells.
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