ArticleNature structural & molecular biology2012
Structure of N-terminal domain of ZAP indicates how a zinc-finger protein recognizes complex RNA.
Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 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.
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Who cites it
75 citing papers in PubMed, 113 citations in OpenAlex.
- Lycorine Derivative Inhibits SARS-CoV-2 Replication by Reducing -1 Programmed Ribosomal Frameshifting via Targeting ZAP.MedComm · 2026Article
- Host ZAP activity correlates with the levels of CpG suppression in primate lentiviruses.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Regulation of stress granule maturation and dynamics by poly(ADP-ribose) interaction with PARP13.Nature communications · 2025Article
- ZC3HAV1 facilitates STING activation and enhances inflammation.Communications biology · 2024Article
- Antiviral Effects of Avian Interferon-Stimulated Genes.Animals : an open access journal from MDPI · 2024Review
- Foot-and-mouth disease virus (FMDV) negatively regulates ZFP36 protein expression to alleviate its antiviral activity.Journal of virology · 2024Article
- Positive selection analyses identify a single WWE domain residue that shapes ZAP into a more potent restriction factor against alphaviruses.PLoS pathogens · 2024Article
- Translation Inhibition Mediated by Interferon-Stimulated Genes during Viral Infections.Viruses · 2024Review
- Article
- ZNF283, a Krüppel-associated box zinc finger protein, inhibits RNA synthesis of porcine reproductive and respiratory syndrome virus by interacting with Nsp9 and Nsp10.Veterinary research · 2024Article
- Versatility of the Zinc-Finger Antiviral Protein (ZAP) As a Modulator of Viral Infections.International journal of biological sciences · 2024Review
- Antiviral Activity of Zinc Finger Antiviral Protein (ZAP) in Different Virus Families.Pathogens (Basel, Switzerland) · 2023Review
- The DNA glycosylase NEIL2 is protective during SARS-CoV-2 infection.Nature communications · 2023Article
- Updated protein domain annotation of the PARP protein family sheds new light on biological function.Nucleic acids research · 2023Article
- CpG dinucleotide enrichment in the influenza A virus genome as a live attenuated vaccine development strategy.PLoS pathogens · 2023Article
- Strain-Dependent Restriction of Human Cytomegalovirus by Zinc Finger Antiviral Proteins.Journal of virology · 2023Article
- Role of Dynamics and Mutations in Interactions of a Zinc Finger Antiviral Protein with CG-rich Viral RNA.Journal of chemical information and modeling · 2023Article
- Antiviral activity of zinc against hepatitis viruses: current status and future prospects.Frontiers in microbiology · 2023Review
- Riplet Binds the Zinc Finger Antiviral Protein (ZAP) and Augments ZAP-Mediated Restriction of HIV-1.Journal of virology · 2022Article
- ZAP isoforms regulate unfolded protein response and epithelial- mesenchymal transition.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
15 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
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. How ZAP recognizes its target RNA has been unclear. Here we report the crystal structure of the N-terminal domain of rat ZAP (NZAP225), the major functional domain. The overall structure of NZAP225 resembles a tractor, with four zinc-finger motifs located at the bottom. Structural and functional analyses identified multiple positively charged residues and two putative RNA-binding cavities forming a large putative RNA-binding cleft. ZAP molecules interact to form a dimer that binds to a ZAP-responsive RNA molecule containing two ZAP-binding modules. These results provide insights into how ZAP binds specifically to complex target RNA.
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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.