ArticleJournal of virology2013
Structure of the NS1 protein N-terminal origin recognition/nickase domain from the emerging human bocavirus.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 29 citations in OpenAlex.
- Twenty years of human bocavirus research: from an unculturable virus of unclear pathogenicity to a culturable human pathogen and gene therapy vector candidate.Clinical microbiology reviews · 2025Review
- NS1-mediated DNMT1 degradation regulates human bocavirus 1 replication and RNA processing.PLoS pathogens · 2024Article
- Antiviral alternatives against important members of the subfamily Parvovirinae: a review.Archives of virology · 2024Review
- The Structures and Functions of Parvovirus Capsids and Missing Pieces: the Viral DNA and Its Packaging, Asymmetrical Features, Nonprotein Components, and Receptor or Antibody Binding and Interactions.Journal of virology · 2023Review
- Characterization of Natural Compounds as Inhibitors of NS1 Endonuclease from Canine Parvovirus Type 2.Journal of microbiology and biotechnology · 2023Article
- High-Resolution Structure of the Nuclease Domain of the Human Parvovirus B19 Main Replication Protein NS1.Journal of virology · 2022Article
- Recent Advances in Molecular Biology of Human Bocavirus 1 and Its Applications.Frontiers in microbiology · 2021Review
- Canine Parvovirus and Its Non-Structural Gene 1 as Oncolytic Agents: Mechanism of Action and Induction of Anti-Tumor Immune Response.Frontiers in oncology · 2021Review
- Whole-genome sequencing analysis of human bocavirus detected in South Korea.Epidemiology and infection · 2018Article
- Mutations in the C-terminus of HBoV NS1 affect the function of NP1.Scientific reports · 2017Article
- Minute Virus of Canines NP1 Protein Governs the Expression of a Subset of Essential Nonstructural Proteins via Its Role in RNA Processing.Journal of virology · 2017Article
- Phosphorylated STAT5 directly facilitates parvovirus B19 DNA replication in human erythroid progenitors through interaction with the MCM complex.PLoS pathogens · 2017Article
- Alternative Polyadenylation of Human Bocavirus at Its 3' End Is Regulated by Multiple Elements and Affects Capsid Expression.Journal of virology · 2017Article
- DNA Damage Signaling Is Required for Replication of Human Bocavirus 1 DNA in Dividing HEK293 Cells.Journal of virology · 2017Article
- Human Parvoviruses.Clinical microbiology reviews · 2017Review
- Human bocavirus: Current knowledge and future challenges.World journal of gastroenterology · 2016Review
- Analysis of cis and trans Requirements for DNA Replication at the Right-End Hairpin of the Human Bocavirus 1 Genome.Journal of virology · 2016Article
- Identification and Functional Analysis of Novel Nonstructural Proteins of Human Bocavirus 1.Journal of virology · 2015Article
- Structures of minute virus of mice replication initiator protein N-terminal domain: Insights into DNA nicking and origin binding.Virology · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Human bocavirus is a newly identified, globally prevalent, parvovirus that is associated with respiratory infection in infants and young children. Parvoviruses encode a large nonstructural protein 1 (NS1) that is essential for replication of the viral single-stranded DNA genome and DNA packaging and may play versatile roles in virus-host interactions. Here, we report the structure of the human bocavirus NS1 N-terminal domain, the first for any autonomous parvovirus. The structure shows an overall fold that is canonical to the histidine-hydrophobic-histidine superfamily of nucleases, which integrates two distinct DNA-binding sites: (i) a positively charged region mediated by a surface hairpin (residues 190 to 198) that is responsible for recognition of the viral origin of replication of the double-stranded DNA nature and (ii) the nickase active site that binds to the single-stranded DNA substrate for site-specific cleavage. The structure reveals an acidic-residue-rich subdomain that is present in bocavirus NS1 proteins but not in the NS1 orthologs in erythrovirus or dependovirus, which may mediate bocavirus-specific interaction with DNA or potential host factors. These results provide insights into recognition of the origin of replication and nicking of DNA during bocavirus genome replication. Mapping of variable amino acid residues of NS1s from four human bocavirus species onto the structure shows a scattered pattern, but the origin recognition site and the nuclease active site are invariable, suggesting potential targets for antivirals against this clade of highly diverse human viruses.
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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 Socratic graph.