ArticleJournal of virology1997
Processing of a cellular polypeptide by 3CD proteinase is required for poliovirus ribonucleoprotein complex formation.
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 24 papers.
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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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Who cites it
24 citing papers in PubMed.
- Article
- Picornavirus 3C Proteins Intervene in Host Cell Processes through Proteolysis and Interactions with RNA.Viruses · 2023Review
- Attenuating RNA Viruses with Expanded Genetic Codes to Evoke Adjustable Immune Response in PylRS-tRNACUAPyl Transgenic Mice.Vaccines · 2023Article
- Review
- Innate immune evasion mediated by picornaviral 3C protease: Possible lessons for coronaviral 3C-like protease?Reviews in medical virology · 2021Review
- Structures and Functions of Viral 5' Non-Coding Genomic RNA Domain-I in Group-B Enterovirus Infections.Viruses · 2020Review
- Picornaviruses and RNA Metabolism: Local and Global Effects of Infection.Journal of virology · 2019Review
- Poliovirus replication requires the N-terminus but not the catalytic Sec7 domain of ArfGEF GBF1.Cellular microbiology · 2010Article
- Mechanistic consequences of hnRNP C binding to both RNA termini of poliovirus negative-strand RNA intermediates.Journal of virology · 2010Article
- Rupintrivir is a promising candidate for treating severe cases of Enterovirus-71 infection.World journal of gastroenterology · 2010Article
- Activation of cellular Arf GTPases by poliovirus protein 3CD correlates with virus replication.Journal of virology · 2007Article
- Stimulation of poliovirus synthesis in a HeLa cell-free in vitro translation-RNA replication system by viral protein 3CDpro.Journal of virology · 2005Article
- 3'-Terminal sequence in poliovirus negative-strand templates is the primary cis-acting element required for VPgpUpU-primed positive-strand initiation.Journal of virology · 2005Article
- Functional interaction of heterogeneous nuclear ribonucleoprotein C with poliovirus RNA synthesis initiation complexes.Journal of virology · 2005Article
- Regulation of poliovirus 3C protease by the 2C polypeptide.Journal of virology · 2004Article
- Cell-dependent role for the poliovirus 3' noncoding region in positive-strand RNA synthesis.Journal of virology · 2004Article
- Functional dissection of a poliovirus cis-acting replication element [PV-cre(2C)]: analysis of single- and dual-cre viral genomes and proteins that bind specifically to PV-cre RNA.Journal of virology · 2003Article
- Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Cleavage of RasGAP and phosphorylation of mitogen-activated protein kinase in the course of coxsackievirus B3 replication.Journal of virology · 1999Article
- Switch from translation to RNA replication in a positive-stranded RNA virus.Genes & development · 1998Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Poliovirus interactions with host cells were investigated by studying the formation of ribonucleoprotein complexes at the 3' end of poliovirus negative-strand RNA which are presumed to be involved in viral RNA synthesis. It was previously shown that two host cell proteins with molecular masses of 36 and 38 kDa bind to the 3' end of viral negative-strand RNA at approximately 3 to 4 h after infection. We tested the hypothesis that preexisting cellular proteins are modified during the course of infection and are subsequently recruited to play a role in viral replication. It was demonstrated that the 38-kDa protein, either directly or indirectly, is the product of processing by poliovirus 3CD/3C proteinase. Only the modified 38-kDa protein, not its precursor protein, has a high affinity for binding to the 3' end of viral negative-strand RNA. This modification depends on proteolytically active proteinase, and a direct correlation between the levels of 3CD proteinase and the 38-kDa protein was demonstrated in infected tissue culture cells. The nucleotide (nt) 5-10 region (positive-strand numbers) of poliovirus negative-strand RNA is important for binding of the 38-kDa protein. Deletion of the nt 5-10 region in full-length, positive-strand RNA renders the RNA noninfectious in transfection experiments. These results suggest that poliovirus 3CD/3C proteinase processes a cellular protein which then plays an essential role during the viral life cycle.
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