ArticleJournal of virology1997
Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells.
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 99 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
99 citing papers in PubMed, 160 citations in OpenAlex.
- Targeting Picornavirus Nonstructural 2C Protein: Structure, Function, and Antiviral Discovery.ACS infectious diseases · 2026Review
- BEV 2C protein inhibits the NF-κB signalling pathway to promote viral replication by targeting IKBKB and p65.Veterinary research · 2025Article
- A cardioviral 2C-ATP complex structure reveals the essential role of a conserved arginine in regulation of cardioviral 2C activity.Journal of virology · 2024Article
- In vitro reconstitution reveals membrane clustering and RNA recruitment by the enteroviral AAA+ ATPase 2C.PLoS pathogens · 2024Article
- Picornavirus 2C proteins: structure-function relationships and interactions with host factors.Frontiers in cellular and infection microbiology · 2024Review
- Coxsackievirus A6 2C protein antagonizes IFN-β production through MDA5 and RIG-I depletion.Journal of virology · 2023Article
- A comparative analysis of parechovirus protein structures with other picornaviruses.Open biology · 2021Article
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- Rational design of highly potent broad-spectrum enterovirus inhibitors targeting the nonstructural protein 2C.PLoS biology · 2020Article
- Development of broad-spectrum enterovirus antivirals based on quinoline scaffold.Bioorganic chemistry · 2020Article
- The Structure, Function, and Mechanisms of Action of Enterovirus Non-structural Protein 2C.Frontiers in microbiology · 2020Review
- Fluoxetine Inhibits Enterovirus Replication by Targeting the Viral 2C Protein in a Stereospecific Manner.ACS infectious diseases · 2019Article
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- Article
- Crystal structure of a soluble fragment of poliovirus 2CATPase.PLoS pathogens · 2018Article
- Viral Discovery in the Invasive Australian Cane Toad (Rhinella marina) Using Metatranscriptomic and Genomic Approaches.Journal of virology · 2018Article
- Model of OSBP-Mediated Cholesterol Supply to Aichi Virus RNA Replication Sites Involving Protein-Protein Interactions among Viral Proteins, ACBD3, OSBP, VAP-A/B, and SAC1.Journal of virology · 2018Article
- Multiple poliovirus-induced organelles suggested by comparison of spatiotemporal dynamics of membranous structures and phosphoinositides.PLoS pathogens · 2018Article
- T135I substitution in the nonstructural protein 2C enhances foot-and-mouth disease virus replication.Virus genes · 2017Article
39 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Poliovirus protein 2C is a 329-amino acid-protein that is essential for viral RNA synthesis and may perform multiple functions. In infected cells, it is associated with virus-specific membrane vesicles. Recombinant 2C protein expressed in transfected cells has been shown to associate with and induce rearrangement of the intracellular membrane network. This study was designed to map the determinants of membrane binding and rearrangement in the 2C protein. Computer-assisted analysis of the protein sequence led to a prediction that the protein folds into a structure composed of three domains. Expression plasmids that encode each or combinations of these predicted domains were used to examine the abilities of the partial protein sequences to associate with intracellular membranes and to induce rearrangement of these membranes in HeLa cells. Biochemical fractionation procedures suggested that the N-terminal region of the protein was required for membrane association. Electron microscopic and immunoelectron microscopic observation showed that both the N- and C-terminal regions, but not the central portion, of 2C protein interact with intracellular membranes and induce major changes in their morphology. The central portion, when fused to the N-terminal region, altered the specific membrane architecture induced by the N-terminal region, giving rise to vesicles resembling those observed during poliovirus infection.
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What OpenQuestion holds
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.