ArticleJournal of virology1997
Inhibition of parvovirus minute virus of mice replication by a peptide involved in the oligomerization of nonstructural protein NS1.
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 23 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
23 citing papers in PubMed, 41 citations in OpenAlex.
- Cancer Treatment Goes Viral: Using Viral Proteins to Induce Tumour-Specific Cell Death.Cancers · 2019Review
- The 5' Untranslated Region of the Capsid Protein 2 Gene of Mink Enteritis Virus Is Essential for Its Expression.Journal of virology · 2018Article
- DNA Binding and Cleavage by the Human Parvovirus B19 NS1 Nuclease Domain.Biochemistry · 2016Article
- Recent insights into the development of therapeutics against coronavirus diseases by targeting N protein.Drug discovery today · 2016Review
- Structures of minute virus of mice replication initiator protein N-terminal domain: Insights into DNA nicking and origin binding.Virology · 2015Article
- Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein.FEBS letters · 2013Article
- The putative metal coordination motif in the endonuclease domain of human Parvovirus B19 NS1 is critical for NS1 induced S phase arrest and DNA damage.International journal of biological sciences · 2012Article
- Effect of ATP binding and hydrolysis on dynamics of canine parvovirus NS1.Journal of virology · 2010Article
- Replication initiator protein NS1 of the parvovirus minute virus of mice binds to modular divergent sites distributed throughout duplex viral DNA.Journal of virology · 2007Article
- A viral adaptor protein modulating casein kinase II activity induces cytopathic effects in permissive cells.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Targeting of autonomous parvoviruses to colon cancer by insertion of Tcf sites in the P4 promoter.Cancer gene therapy · 2006Article
- Modulation of minute virus of mice cytotoxic activities through site-directed mutagenesis within the NS coding region.Journal of virology · 2003Article
- Novel PKCeta is required to activate replicative functions of the major nonstructural protein NS1 of minute virus of mice.Journal of virology · 2003Article
- Replicating parvoviruses that target colon cancer cells.Journal of virology · 2003Article
- Caspase cleavage of the nonstructural protein NS1 mediates replication of Aleutian mink disease parvovirus.Journal of virology · 2003Article
- Regulation of minute virus of mice NS1 replicative functions by atypical PKClambda in vivo.Journal of virology · 2003Article
- Initiation of minute virus of mice DNA replication is regulated at the level of origin unwinding by atypical protein kinase C phosphorylation of NS1.Journal of virology · 2001Article
- DNA unwinding functions of minute virus of mice NS1 protein are modulated specifically by the lambda isoform of protein kinase C.Journal of virology · 1999Article
- Activation of promoter P4 of the autonomous parvovirus minute virus of mice at early S phase is required for productive infection.Journal of virology · 1999Article
- A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice.Journal of virology · 1999Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The large nonstructural protein NS1 of the minute virus of mice and other parvoviruses is involved in essential steps of the viral life cycle, such as DNA replication and transcriptional regulation, and is a major contributor to the toxic effect on host cells. Various biochemical functions, such as ATP binding, ATPase, site-specific DNA binding and nicking, and helicase activities, have been assigned to NS1. Homo-oligomerization is a prerequisite for a number of proteins to be fully functional. In particular, helicases generally act as homo-oligomers. Indirect evidence of NS1 self-association has been recently obtained by a nuclear cotransport assay (J. P. Nüesch and P. Tattersall, Virology 196:637-651, 1993). In order to demonstrate the oligomerizing property of NS1 in a direct way and localize the protein region(s) involved, the yeast two-hybrid system was used in combination with deletion mutagenesis across the whole NS1 molecule, followed by high-resolution mapping of the homo-oligomerization domain by a peptide enzyme-linked immunosorbent assay method. This study led to the identification of a distinct NS1 peptide that contains a bipartite domain involved in NS1 oligomerization. Furthermore, this isolated peptide was found to act as a specific competitive inhibitor and suppress NS1 helicase activity in vitro and parvovirus DNA replication in vivo, arguing for the involvement of NS1 oligomerization in these processes. Our results point to drug targeting of oligomerization motifs of viral regulatory proteins as a potentially useful antiviral strategy.
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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.