ArticleBiomolecular NMR assignments2021
Article in Biomolecular NMR assignments, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- At the core of the interaction: Probing charged side chains in flexible protein regions with simultaneous nuclear magnetic resonance experiments.Protein science : a publication of the Protein Society · 2026Article
- Article
- Evolution of a fuzzy ribonucleoprotein complex in viral assembly.bioRxiv : the preprint server for biology · 2025Article
- Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation.Nucleic acids research · 2025Article
- A specific phosphorylation-dependent conformational switch in SARS-CoV-2 nucleocapsid protein inhibits RNA binding.Science advances · 2024Article
- Phosphorylation in the Ser/Arg-rich region of the nucleocapsid of SARS-CoV-2 regulates phase separation by inhibiting self-association of a distant helix.The Journal of biological chemistry · 2024Article
- Critical Assessment of Self-Consistency Checks in the All-Atom Molecular Dynamics Simulation of Intrinsically Disordered Proteins.Journal of chemical theory and computation · 2023Article
- A conserved oligomerization domain in the disordered linker of coronavirus nucleocapsid proteins.Science advances · 2023Article
- Accessing isotopically labeled proteins containing genetically encoded phosphoserine for NMR with optimized expression conditions.The Journal of biological chemistry · 2022Article
- Neuropeptides, New Ligands of SARS-CoV-2 Nucleoprotein, a Potential Link between Replication, Inflammation and Neurotransmission.Molecules (Basel, Switzerland) · 2022Article
- The Role of Disordered Regions in Orchestrating the Properties of Multidomain Proteins: The SARS-CoV-2 Nucleocapsid Protein and Its Interaction with Enoxaparin.Biomolecules · 2022Article
- Contributions of the N-terminal intrinsically disordered region of the severe acute respiratory syndrome coronavirus 2 nucleocapsid protein to RNA-induced phase separation.Protein science : a publication of the Protein Society · 2022Article
- NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering.Biomolecules · 2022Article
- SARS-CoV-2 variants preferentially emerge at intrinsically disordered protein sites helping immune evasion.The FEBS journal · 2022Review
- NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.Chemical reviews · 2022Review
- Article
- The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a.Science advances · 2022Article
- Large-Scale Recombinant Production of the SARS-CoV-2 Proteome for High-Throughput and Structural Biology Applications.Frontiers in molecular biosciences · 2021Article
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Authors and funding
8 authors.
Funding
Abstract
The nucleoprotein (N) from SARS-CoV-2 is an essential cofactor of the viral replication transcription complex and as such represents an important target for viral inhibition. It has also been shown to colocalize to the transcriptase-replicase complex, where many copies of N decorate the viral genome, thereby protecting it from the host immune system. N has also been shown to phase separate upon interaction with viral RNA. N is a 419 amino acid multidomain protein, comprising two folded, RNA-binding and dimerization domains spanning residues 45-175 and 264-365 respectively. The remaining 164 amino acids are predicted to be intrinsically disordered, but there is currently no atomic resolution information describing their behaviour. Here we assign the backbone resonances of the first two intrinsically disordered domains (N1, spanning residues 1-44 and N3, spanning residues 176-263). Our assignment provides the basis for the identification of inhibitors and functional and interaction studies of this essential protein.
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