ArticleJournal of virology1997
Core protein mu2 is a second determinant of nucleoside triphosphatase activities by reovirus cores.
Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
43 citing papers in PubMed, 72 citations in OpenAlex.
- Reovirus recombination is highly selective, and its profiles are primarily dictated by viral gene segment identity.Journal of virology · 2026Article
- Reovirus recombination is highly selective, and its profiles are primarily dictated by viral gene segment identity.bioRxiv : the preprint server for biology · 2025Article
- In situ structures of polymerase complex of mammalian reovirus illuminate RdRp activation and transcription regulation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The reovirus μ2 C-terminal loop inversely regulates NTPase and transcription functions versus binding to factory-forming μNS and promotes replication in tumorigenic cells.Journal of virology · 2021Article
- Captivating Perplexities ofViruses · 2021Review
- Mammalian orthoreovirus core protein μ2 reorganizes host microtubule-organizing center components.Virology · 2020Article
- Polymorphisms in the Most Oncolytic Reovirus Strain Confer Enhanced Cell Attachment, Transcription, and Single-Step Replication Kinetics.Journal of virology · 2020Article
- How Many Mammalian Reovirus Proteins are involved in the Control of the Interferon Response?Pathogens (Basel, Switzerland) · 2019Review
- Synthesis and Translation of Viral mRNA in Reovirus-Infected Cells: Progress and Remaining Questions.Viruses · 2018Review
- Structure of RNA polymerase complex and genome within a dsRNA virus provides insights into the mechanisms of transcription and assembly.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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- Reovirus replication protein μ2 influences cell tropism by promoting particle assembly within viral inclusions.Journal of virology · 2012Article
- Characterization of grass carp reovirus minor core protein VP4.Virology journal · 2012Article
- A single-amino-acid polymorphism in reovirus protein μ2 determines repression of interferon signaling and modulates myocarditis.Journal of virology · 2012Article
- Functional investigation of grass carp reovirus nonstructural protein NS80.Virology journal · 2011Article
- A post-entry step in the mammalian orthoreovirus replication cycle is a determinant of cell tropism.The Journal of biological chemistry · 2010Article
- Conserved structure/function of the orthoreovirus major core proteins.Virus research · 2009Article
- Probing the transcription mechanisms of reovirus cores with molecules that alter RNA duplex stability.Journal of virology · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
NTPase activities in mammalian reovirus cores were examined under various conditions that permitted several new differences to be identified between strains type 1 Lang (T1L) and type 3 Dearing (T3D). One difference concerned the ratio (at pH 8.5) of ATP hydrolysis at 50 degrees C to that at 35 degrees C. A genetic analysis using T1L x T3D reassortant viruses implicated the L3 and M1 gene segments in this difference, with M1 influencing ATPase activity most strongly at high temperatures. L3 and M1 encode the core proteins lambda1 and mu2, respectively. Another difference concerned the absolute levels of GTP hydrolysis by cores at 45 degrees C and pH 6.5. A genetic analysis using T1L x T3D reassortants implicated the M1 gene as the sole determinant of this difference. The results of these experiments, coupled with previous findings (S. Noble and M. L. Nibert, J. Virol. 71:2182-2191, 1997), suggest either that a single type of NTPase in cores is strongly influenced by two different core proteins--lambda1 and mu2--or that cores contain two different types of NTPase influenced by the two proteins. The findings appear relevant for understanding the complex functions of reovirus cores in RNA synthesis and capping.
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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.