ArticlePLoS pathogens2017
Crystal structure of Middle East respiratory syndrome coronavirus helicase.
Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed, 152 citations in OpenAlex.
- Recent advances in functional studies of coronavirus NSP13 helicase and challenges in inhibitor development.Virulence · 2026Review
- Motif V is an allosteric couple between the SARS-CoV-2 nsp13 nucleotide triphosphatase and helicase active sites.The Journal of biological chemistry · 2026Article
- The dynamic interactions between virus infections and nonsense-mediated decay.Human molecular genetics · 2025Review
- Human Schlafen 14 Cleavage of Short Double-Stranded RNAs Underpins its Antiviral Activity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Repurposing Vancomycin as a Potential Antiviral Agent Against PEDV via nsp13 Helicase Inhibition.Animals : an open access journal from MDPI · 2025Article
- Duplex Unwinding Mechanism of Coronavirus MERS-CoV nsp13 Helicase.Chemical & biomedical imaging · 2025Article
- Analogs of NIH Molecular Probe ML283 Are Potent SARS-CoV-2 Helicase Inhibitors.ACS chemical biology · 2025Article
- Activity and inhibition of the SARS-CoV-2 Omicron nsp13 R392C variant using RNA duplex unwinding assays.SLAS discovery : advancing life sciences R & D · 2024Article
- Generalized open-source workflows for atomistic molecular dynamics simulations of viral helicases.GigaScience · 2024Article
- SARS-CoV-2 helicase might interfere with cellular nonsense-mediated RNA decay: insights from a bioinformatics study.BMC genomic data · 2023Article
- Article
- An iron-sulfur cluster in the zinc-binding domain of the SARS-CoV-2 helicase modulates its RNA-binding and -unwinding activities.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Coronaviruses SARS-CoV, MERS-CoV, and SARS-CoV-2 helicase inhibitors: a systematic review ofJournal of virus eradication · 2023Review
- Ultrasound assisted Cu-catalyzed Ullmann-Goldberg type coupling-cyclization in a single pot: Synthesis andJournal of molecular structure · 2023Article
- Vaccine development for zoonotic viral diseases caused by positive‑sense single‑stranded RNA viruses belonging to theExperimental and therapeutic medicine · 2023Review
- Two Years into the COVID-19 Pandemic: Lessons Learned.ACS infectious diseases · 2022Review
- Proteolytic Processing of the Coronavirus Replicase Nonstructural Protein 14 Exonuclease Is Not Required for Virus Replication but Alters RNA Synthesis and Viral Fitness.Journal of virology · 2022Article
- The SARS-CoV-2 helicase as a target for antiviral therapy: Identification of potential small molecule inhibitors by in silico modelling.Journal of molecular graphics & modelling · 2022Article
- Evolution of SARS-CoV-2 in Spain during the First Two Years of the Pandemic: Circulating Variants, Amino Acid Conservation, and Genetic Variability in Structural, Non-Structural, and Accessory Proteins.International journal of molecular sciences · 2022Article
- Replication of the coronavirus genome: A paradox among positive-strand RNA viruses.The Journal of biological chemistry · 2022Review
9 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
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Middle East respiratory syndrome coronavirus (MERS-CoV) remains a threat to public health worldwide; however, effective vaccine or drug against CoVs remains unavailable. CoV helicase is one of the three evolutionary most conserved proteins in nidoviruses, thus making it an important target for drug development. We report here the first structure of full-length coronavirus helicase, MERS-CoV nsp13. MERS-CoV helicase has multiple domains, including an N-terminal Cys/His rich domain (CH) with three zinc atoms, a beta-barrel domain and a C-terminal SF1 helicase core with two RecA-like subdomains. Our structural analyses show that while the domain organization of nsp13 is conserved throughout nidoviruses, the individual domains of nsp13 are closely related to the equivalent eukaryotic domains of Upf1 helicases. The most distinctive feature differentiating CoV helicases from eukaryotic Upf1 helicases is the interaction between CH domain and helicase core.
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Registered trials
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.