ArticleJournal of virology2009
Nucleoside monophosphate complex structures of the endonuclease domain from the influenza virus polymerase PA subunit reveal the substrate binding site inside the catalytic center.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 58 citations in OpenAlex.
- Pharmacophores of Influenza Virus PA Endonuclease Inhibitors.Advances in experimental medicine and biology · 2026Review
- Review
- Structural Studies of Inhibitors with Clinically Relevant Influenza Endonuclease Variants.Biochemistry · 2024Article
- Article
- Identification of Influenza PAMolecules (Basel, Switzerland) · 2021Article
- Structural insights into the substrate specificity of the endonuclease activity of the influenza virus cap-snatching mechanism.Nucleic acids research · 2021Article
- Bibenzyls and bisbybenzyls of bryophytic origin as promising source of novel therapeutics: pharmacology, synthesis and structure-activity.Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences · 2020Review
- Corona virus versus existence of human on the earth: A computational and biophysical approach.International journal of biological macromolecules · 2020Review
- Molecular features of influenza A (H1N1)pdm09 prevalent in Mexico during winter seasons 2012-2014.PloS one · 2017Article
- The Influenza Virus Polymerase Complex: An Update on Its Structure, Functions, and Significance for Antiviral Drug Design.Medicinal research reviews · 2016Review
- N-acylhydrazone inhibitors of influenza virus PA endonuclease with versatile metal binding modes.Scientific reports · 2016Article
- Article
- Investigation of the salicylaldehyde thiosemicarbazone scaffold for inhibition of influenza virus PA endonuclease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Crucial role of PA in virus life cycle and host adaptation of influenza A virus.Medical microbiology and immunology · 2015Review
- An integrated biological approach to guide the development of metal-chelating inhibitors of influenza virus PA endonuclease.Molecular pharmacology · 2015Article
- Emerging antiviral resistant strains of influenza A and the potential therapeutic targets within the viral ribonucleoprotein (vRNP) complex.Virology journal · 2014Review
- Structural analysis of H1N1 and H7N9 influenza A virus PA in the absence of PB1.Scientific reports · 2014Article
- Structural basis for the identification of the N-terminal domain of coronavirus nucleocapsid protein as an antiviral target.Journal of medicinal chemistry · 2014Article
- The N-terminal domain of PA from bat-derived influenza-like virus H17N10 has endonuclease activity.Journal of virology · 2014Article
- High-resolution structure of the N-terminal endonuclease domain of the Lassa virus L polymerase in complex with magnesium ions.PloS one · 2014Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
Highly pathogenic influenza virus strains currently in circulation pose a significant risk of a global pandemic. Following the reported crystal structure of the endonuclease domain from the avian influenza virus polymerase PA subunit, here we report the results of a systematic X-ray crystallographic analysis of its complex with adenosine, uridine, and thymidine nucleoside monophosphates (NMPs). Electron density corresponding to the monophosphate moiety of each nucleotide was apparent in each NMP complex and bound to the catalytic metal. A hydrophobic site was found to contribute to nucleoside binding. The NMP complex structures should represent the conformation of the bound product after nuclease cleavage. Moreover, one solvent molecule was found to occupy an equivalent position to the second reported Mn(2+) ion, where it mediates the interaction between bound NMPs and the N-terminal PA domain in the presence of the Mg(2+) ion. The results presented here indicate a possible cleavage mechanism and identify a distinct nucleotide binding pocket. The identification of this binding pocket opens a new avenue for anti-influenza drug discovery, targeting the cap-dependent endonuclease, in response to the worldwide threat of influenza.
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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.