ArticleJournal of virology2017
Structural Insight into Nucleoprotein Conformation Change Chaperoned by VP35 Peptide in Marburg Virus.
Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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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.
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Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- Structure and assembly of Borna disease virus 1 nucleoprotein-RNA complexes.Science advances · 2026Article
- Assembly of the Linear Viral Nucleocapsid.Microorganisms · 2026Article
- Conserved Filovirus Proteins as Targets of Broad-Spectrum Antivirals.bioRxiv : the preprint server for biology · 2025Article
- Article
- Cryo-EM structure of single-layered nucleoprotein-RNA complex from Marburg virus.Nature communications · 2024Article
- How does the polymerase of non-segmented negative strand RNA viruses commit to transcription or genome replication?Journal of virology · 2024Review
- Design of a novel multi-epitope vaccine against Marburg virus using immunoinformatics studies.BMC biotechnology · 2024Article
- Structural and Dynamical Basis of VP35-RBD Inhibition by Marine Fungi Compounds to Combat Marburg Virus Infection.Marine drugs · 2024Article
- Cryoelectron microscopic structure of the nucleoprotein-RNA complex of the European filovirus, Lloviu virus.PNAS nexus · 2023Article
- Emergence of Marburg virus: a global perspective on fatal outbreaks and clinical challenges.Frontiers in microbiology · 2023Review
- Structure and Dynamics of the Unassembled Nucleoprotein of Rabies Virus in Complex with Its Phosphoprotein Chaperone Module.Viruses · 2022Article
- Pathogenicity and virulence of Marburg virus.Virulence · 2022Review
- Assembly and transport of filovirus nucleocapsids.PLoS pathogens · 2022Review
- Structural insight into Marburg virus nucleoprotein-RNA complex formation.Nature communications · 2022Article
- Mining of Marburg Virus Proteome for Designing an Epitope-Based Vaccine.Frontiers in immunology · 2022Article
- The Nucleocapsid of Paramyxoviruses: Structure and Function of an Encapsidated Template.Viruses · 2021Review
- New Perspectives on the Biogenesis of Viral Inclusion Bodies in Negative-Sense RNA Virus Infections.Cells · 2021Review
- Article
- Nucleocapsid Structure of Negative Strand RNA Virus.Viruses · 2020Review
- Distinct Genome Replication and Transcription Strategies within the Growing Filovirus Family.Journal of molecular biology · 2019Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Marburg virus (MARV) encodes a nucleoprotein (NP) to encapsidate its genome by oligomerization and form a ribonucleoprotein complex (RNP). According to previous investigation on nonsegmented negative-sense RNA viruses (nsNSV), the newly synthesized NPs must be prevented from indiscriminately binding to noncognate RNAs. During the viral RNA synthesis process, the RNPs undergo a transition from an RNA-bound form to a template-free form, to open access for the interaction between the viral polymerase and the RNA template. In filoviruses, this transition is regulated by VP35 peptide and other viral components. To further understand the dynamic process of filovirus RNP formation, we report here the structure of MARV NP
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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.