Evidence map›Paper›PMID 28917841›Full record

ArticleBiochemical and biophysical research communications2017

Graphene-VP40 interactions and potential disruption of the Ebola virus matrix filaments.

Jeevan B Gc, Rudramani Pokhrel, Nisha Bhattarai, Kristen A Johnson, Bernard S Gerstman, Robert V Stahelin, Prem P Chapagain

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
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  5. Article
  6. Graphene: A Disruptive Opportunity for COVID-19 and Future Pandemics?Advanced materials (Deerfield Beach, Fla.) · 2021
    Article
  7. Review
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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

7 authors at 2 institutions in 1 country.

Jeevan B GcDepartment of Physics, Florida International University, Miami, FL 33199, United States.
Rudramani PokhrelDepartment of Physics, Florida International University, Miami, FL 33199, United States.
Nisha BhattaraiDepartment of Physics, Florida International University, Miami, FL 33199, United States.
Kristen A JohnsonDepartment of Chemistry and Biochemistry, The Eck Institute for Global Health, The Boler-Parseghian Center for Rare and Neglected Diseases, University of Notre Dame, Notre Dame, IN 46556, United States.
Bernard S GerstmanDepartment of Physics, Florida International University, Miami, FL 33199, United States; Biomolecular Sciences Institute, Florida International University, Miami, FL 33199, United States.
Robert V StahelinDepartment of Chemistry and Biochemistry, The Eck Institute for Global Health, The Boler-Parseghian Center for Rare and Neglected Diseases, University of Notre Dame, Notre Dame, IN 46556, United States; Department of Biochemistry and Molecular Biology, Indiana University School of Medicine-South Bend, South Bend, IN 46617, United States.
Prem P ChapagainDepartment of Physics, Florida International University, Miami, FL 33199, United States; Biomolecular Sciences Institute, Florida International University, Miami, FL 33199, United States. Electronic address: chapagap@fiu.edu.
Florida International University · USUniversity of Notre Dame · US

Funding

LIPID-PROTEIN INTERACTIONS IN VIRAL ASSEMBLY AND VIRUS LIKE PARTICLE FORMATIONR01AI081077 · NIAID · PURDUE UNIVERSITY · PI STAHELIN, ROBERT VIRGIL · 2009 to 2019
$3.5M
NIAID NIH HHS R01 AI081077
6 · The paper itself

Abstract

Ebola virus infections cause hemorrhagic fever that often results in very high fatality rates. In addition to exploring vaccines, development of drugs is also essential for treating the disease and preventing the spread of the infection. The Ebola virus matrix protein VP40 exists in various conformational and oligomeric forms and is a potential pharmacological target for disrupting the virus life-cycle. Here we explored graphene-VP40 interactions using molecular dynamics simulations and graphene pelleting assays. We found that graphene sheets associate strongly with VP40 at various interfaces. We also found that the graphene is able to disrupt the C-terminal domain (CTD-CTD) interface of VP40 hexamers. This VP40 hexamer-hexamer interface is crucial in forming the Ebola viral matrix and disruption of this interface may provide a method to use graphene or similar nanoparticle based solutions as a disinfectant that can significantly reduce the spread of the disease and prevent an Ebola epidemic.

Indexed as

Binding SitesGraphiteMolecular Dynamics SimulationNucleoproteinsProtein BindingProtein ConformationProtein MultimerizationViral Core ProteinsViral Matrix ProteinsGraphiteNucleoproteinsnucleoprotein VP40, Ebola virusViral Core ProteinsViral Matrix ProteinsVP40 protein, virusEbola virusGraphene sheetMatrix filamentsNanotherapyVP40

Identifiers

PMID28917841
PMCPMC5636687
OpenAlexW2755350459

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.