Evidence map›Paper›PMID 26119732›Full record

ArticleCell reports2015

Assembly of the Ebola Virus Nucleoprotein from a Chaperoned VP35 Complex.

Robert N Kirchdoerfer, Dafna M Abelson, Sheng Li, Malcolm R Wood, Erica Ollmann Saphire

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
9.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

89 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Discovery of three small-molecule inhibitors targetingThe Journal of general virology · 2025
    Article
  6. 25 Years of Ebola Virus VP35 Research.Journal of molecular biology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Negative and ambisense RNA virus ribonucleocapsids: more than protective armor.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  15. Article
  16. Novel Antiviral Molecules against Ebola Virus Infection.International journal of molecular sciences · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Article

29 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Robert N KirchdoerferDepartment of Immunology and Microbial Sciences, The Scripps Research Institute, La Jolla, CA 92037, USA.
Dafna M AbelsonDepartment of Immunology and Microbial Sciences, The Scripps Research Institute, La Jolla, CA 92037, USA.
Sheng LiDepartment of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Malcolm R WoodCore Microscopy Facility, The Scripps Research Institute, La Jolla, CA 92037, USA.
Erica Ollmann SaphireDepartment of Immunology and Microbial Sciences, The Scripps Research Institute, La Jolla, CA 92037, USA; The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: erica@scripps.edu.
Scripps Research Institute · USUniversity of California, San Diego · US

Funding

MOLECULAR BASIS OF VIRAL PATHOGENESIST32AI007354 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI DE LA TORRE, JUAN C. · 1989 to 2020
$5.2M
Function and assembly of the Ebola virus nucleocapsidR01AI118016 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI SAPHIRE, ERICA OLLMANN · 2016 to 2019
$2.0M
Function and assembly of the Ebola virus nucleocapsidR56AI118016 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI SAPHIRE, ERICA OLLMANN · 2015 to 2015
$460k
NIAID NIH HHS 1R56 AI118016-01NIAID NIH HHS 5T32 AI007354-25NIAID NIH HHS R01 AI118016NIAID NIH HHS R56 AI118016NIAID NIH HHS T32 AI007354PHS HHS ACB-12002PHS HHS AGM-12006
6 · The paper itself

Abstract

Ebolavirus NP oligomerizes into helical filaments found at the core of the virion, encapsidates the viral RNA genome, and serves as a scaffold for additional viral proteins within the viral nucleocapsid. We identified a portion of the phosphoprotein homolog VP35 that binds with high affinity to nascent NP and regulates NP assembly and viral genome binding. Removal of the VP35 peptide leads to NP self-assembly via its N-terminal oligomerization arm. NP oligomerization likely causes a conformational change between the NP N- and C-terminal domains, facilitating RNA binding. These functional data are complemented by crystal structures of the NP°-VP35 complex at 2.4 Å resolution. The interactions between NP and VP35 illuminated by these structures are conserved among filoviruses and provide key targets for therapeutic intervention.

Indexed as

Protein MultimerizationAmino Acid SequenceBinding SitesMolecular Sequence DataNucleocapsid ProteinsNucleoproteinsProtein BindingProtein Structure, TertiaryRNAViral Core ProteinsNucleocapsid ProteinsNucleoproteinsnucleoprotein VP35, Ebola virusRNAViral Core Proteins

Identifiers

PMID26119732
PMCPMC4500542
OpenAlexW1620505964

What OpenQuestion holds

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Registered trials

None linked

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.