ArticleProtein & cell2015
Insight into the Ebola virus nucleocapsid assembly mechanism: crystal structure of Ebola virus nucleoprotein core domain at 1.8 Å resolution.
Article in Protein & cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
41 citing papers in PubMed, 69 citations in OpenAlex.
- In Silico Identification of Antiviral Peptides as Potential Leads Against Sudan Ebolavirus VP-40.BioMed research international · 2026Article
- Discovery of three small-molecule inhibitors targetingThe Journal of general virology · 2025Article
- Structural basis for Ebola virus nucleocapsid assembly and function regulated by VP24.Nature communications · 2025Article
- A comprehensive overview on the crosstalk between microRNAs and viral pathogenesis and infection.Medicinal research reviews · 2025Review
- Impact of Ebola virus nucleoprotein on VP40 virus-like particle production: a computational approach.Communications biology · 2024Article
- Novel Antiviral Molecules against Ebola Virus Infection.International journal of molecular sciences · 2023Article
- Assembly and transport of filovirus nucleocapsids.PLoS pathogens · 2022Review
- The Role of Nucleoprotein in Immunity to Human Negative-Stranded RNA Viruses-Not Just Another Brick in the Viral Nucleocapsid.Viruses · 2022Review
- The two-stage interaction of Ebola virus VP40 with nucleoprotein results in a switch from viral RNA synthesis to virion assembly/budding.Protein & cell · 2022Article
- The Nucleocapsid of Paramyxoviruses: Structure and Function of an Encapsidated Template.Viruses · 2021Review
- Structural and Functional Aspects of Ebola Virus Proteins.Pathogens (Basel, Switzerland) · 2021Review
- Article
- Ebola Virus Inclusion Body Formation and RNA Synthesis Are Controlled by a Novel Domain of Nucleoprotein Interacting with VP35.Journal of virology · 2020Article
- Nucleocapsid Structure of Negative Strand RNA Virus.Viruses · 2020Review
- Global phosphoproteomic analysis of Ebola virions reveals a novel role for VP35 phosphorylation-dependent regulation of genome transcription.Cellular and molecular life sciences : CMLS · 2020Article
- Identification of interferon-stimulated genes that attenuate Ebola virus infection.Nature communications · 2020Article
- Article
- Crystal Structure of African Swine Fever Virus pS273R Protease and Implications for Inhibitor Design.Journal of virology · 2020Article
- Article
- Distinct Genome Replication and Transcription Strategies within the Growing Filovirus Family.Journal of molecular biology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ebola virus (EBOV) is a key member of Filoviridae family and causes severe human infectious diseases with high morbidity and mortality. As a typical negative-sense single-stranded RNA (-ssRNA) viruses, EBOV possess a nucleocapsid protein (NP) to facilitate genomic RNA encapsidation to form viral ribonucleoprotein complex (RNP) together with genome RNA and polymerase, which plays the most essential role in virus proliferation cycle. However, the mechanism of EBOV RNP formation remains unclear. In this work, we solved the high resolution structure of core domain of EBOV NP. The polypeptide of EBOV NP core domain (NP(core)) possesses an N-lobe and C-lobe to clamp a RNA binding groove, presenting similarities with the structures of the other reported viral NPs encoded by the members from Mononegavirales order. Most strikingly, a hydrophobic pocket at the surface of the C-lobe is occupied by an α-helix of EBOV NP(core) itself, which is highly conserved among filoviridae family. Combined with other biochemical and biophysical evidences, our results provides great potential for understanding the mechanism underlying EBOV RNP formation via the mobility of EBOV NP element and enables the development of antiviral therapies targeting EBOV RNP formation.
Indexed as
Identifiers
What OpenQuestion holds
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.