ArticleJournal of molecular biology2008
Variable oligomerization modes in coronavirus non-structural protein 9.
Article in Journal of molecular biology, 2008. 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, 57 citations in OpenAlex.
- Nanobody against SARS-CoV-2 non-structural protein Nsp9 inhibits viral replication in human airway epithelia.Molecular therapy. Nucleic acids · 2024Article
- Assessing nanobody interaction with SARS-CoV-2 Nsp9.PloS one · 2024Article
- Classification, replication, and transcription ofFrontiers in microbiology · 2023Review
- Inside-out: Antibody-binding reveals potential folding hinge-points within the SARS-CoV-2 replication co-factor nsp9.PloS one · 2023Article
- Computational exploration of the dual role of the phytochemical fortunellin: Antiviral activities against SARS-CoV-2 and immunomodulatory abilities against the host.Computers in biology and medicine · 2022Article
- 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
- Identification of intrinsically disorder regions in non-structural proteins of SARS-CoV-2: New insights into drug and vaccine resistance.Molecular and cellular biochemistry · 2022Article
- Exploring the Targets of Novel Corona Virus and Docking-based Screening of Potential Natural Inhibitors to Combat COVID-19.Current topics in medicinal chemistry · 2022Article
- NMR-Based Analysis of Nanobodies to SARS-CoV-2 Nsp9 Reveals a Possible Antiviral Strategy Against COVID-19.Advanced biology · 2021Article
- An atomistic model of the coronavirus replication-transcription complex as a hexamer assembled around nsp15.The Journal of biological chemistry · 2021Article
- Backbone chemical shift assignments for the SARS-CoV-2 non-structural protein Nsp9: intermediate (ms - μs) dynamics in the C-terminal helix at the dimer interface.Biomolecular NMR assignments · 2021Article
- Coronavirus replication-transcription complex: Vital and selective NMPylation of a conserved site in nsp9 by the NiRAN-RdRp subunit.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Understanding COVID-19 via comparative analysis of dark proteomes of SARS-CoV-2, human SARS and bat SARS-like coronaviruses.Cellular and molecular life sciences : CMLS · 2021Article
- Potential Pathogenicity Determinants Identified from Structural Proteomics of SARS-CoV and SARS-CoV-2.Molecular biology and evolution · 2021Article
- Structure and Function of Major SARS-CoV-2 and SARS-CoV Proteins.Bioinformatics and biology insights · 2021Review
- Structural and functional insights into non-structural proteins of coronaviruses.Microbial pathogenesis · 2021Review
- Potentially adaptive SARS-CoV-2 mutations discovered with novel spatiotemporal and explainable AI models.Genome biology · 2020Article
- A pocket guide on how to structure SARS-CoV-2 drugs and therapies.Biochemical Society transactions · 2020Review
- An Overview of the Crystallized Structures of the SARS-CoV-2.The protein journal · 2020Review
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Non-structural protein 9 (Nsp9) of coronaviruses is believed to bind single-stranded RNA in the viral replication complex. The crystal structure of Nsp9 of human coronavirus (HCoV) 229E reveals a novel disulfide-linked homodimer, which is very different from the previously reported Nsp9 dimer of SARS coronavirus. In contrast, the structure of the Cys69Ala mutant of HCoV-229E Nsp9 shows the same dimer organization as the SARS-CoV protein. In the crystal, the wild-type HCoV-229E protein forms a trimer of dimers, whereas the mutant and SARS-CoV Nsp9 are organized in rod-like polymers. Chemical cross-linking suggests similar modes of aggregation in solution. In zone-interference gel electrophoresis assays and surface plasmon resonance experiments, the HCoV-229E wild-type protein is found to bind oligonucleotides with relatively high affinity, whereas binding by the Cys69Ala and Cys69Ser mutants is observed only for the longest oligonucleotides. The corresponding mutations in SARS-CoV Nsp9 do not hamper nucleic acid binding. From the crystal structures, a model for single-stranded RNA binding by Nsp9 is deduced. We propose that both forms of the Nsp9 dimer are biologically relevant; the occurrence of the disulfide-bonded form may be correlated with oxidative stress induced in the host cell by the viral infection.
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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.