Evidence map›Paper›PMID 27294109›Full record

ArticleBioMed research international2016

Predicted 3D Model of the Rabies Virus Glycoprotein Trimer.

Bastida-González Fernando, Celaya-Trejo Yersin, Correa-Basurto José, Zárate-Segura Paola

Open access · hybridAbstract read
In one paragraph

Article in BioMed research international, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

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  5. Monocyte-Macrophage Lineage Cell Fusion.International journal of molecular sciences · 2022
    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

4 authors at 1 institution in 1 country.

Bastida-González FernandoLaboratorio de Medicina Traslacional, Escuela Superior de Medicina, Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón s/n, Santo Tomas, Miguel Hidalgo, 11340 Ciudad de México, DF, Mexico; Laboratorio de Biología Molecular, Laboratorio Estatal de Salud Pública del Estado de México, Paseo Tollocan s/n, La moderna de la cruz, 50180 Toluca, MEX, Mexico.
Celaya-Trejo YersinLaboratorio de Medicina Traslacional, Escuela Superior de Medicina, Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón s/n, Santo Tomas, Miguel Hidalgo, 11340 Ciudad de México, DF, Mexico.
Correa-Basurto JoséLaboratorio de Modelado Molecular y Bioinformática, Escuela Superior de Medicina, Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón s/n, Santo Tomas, Miguel Hidalgo, 11340 Ciudad de México, DF, Mexico.
Zárate-Segura PaolaLaboratorio de Medicina Traslacional, Escuela Superior de Medicina, Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón s/n, Santo Tomas, Miguel Hidalgo, 11340 Ciudad de México, DF, Mexico; Departamento de Bioprocesos, Unidad Profesional Interdisciplinaria de Biotecnología, Instituto Politécnico Nacional, Avenida Acueducto de Guadalupe s/n, Ticoman, Gustavo A. Madero, 07340 Ciudad de México, DF, Mexico.
Instituto Politécnico Nacional · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RABVG ectodomain is a homotrimer, and trimers are often called spikes. They are responsible for the attachment of the virus through the interaction with nicotinic acetylcholine receptors, neural cell adhesion molecule (NCAM), and the p75 neurotrophin receptor (p75NTR). This makes them relevant in viral pathogenesis. The antigenic structure differs significantly between the trimers and monomers. Surfaces rich in hydrophobic amino acids are important for trimer stabilization in which the C-terminal of the ectodomain plays an important role; to understand these interactions between the G proteins, a mechanistic study of their functions was performed with a molecular model of G protein in its trimeric form. This verified its 3D conformation. The molecular modeling of G protein was performed by a I-TASSER server and was evaluated via a Rachamandran plot and ERRAT program obtained 84.64% and 89.9% of the residues in the favorable regions and overall quality factor, respectively. The molecular dynamics simulations were carried out on RABVG trimer at 310 K. From these theoretical studies, we retrieved the RMSD values from Cα atoms to assess stability. Preliminary model of G protein of rabies virus stable at 12 ns with molecular dynamics was obtained.

Indexed as

Rabies virusAlgorithmsAntigens, ViralCD56 AntigenGlycoproteinsImaging, Three-DimensionalImmune SystemMolecular Dynamics SimulationNerve Tissue ProteinsProtein DomainsProtein MultimerizationProtein Structure, SecondaryReceptors, Nerve Growth FactorViral Envelope ProteinsAntigens, ViralCD56 Antigenglycoprotein G, Rabies virusGlycoproteinsNCAM1 protein, humanNerve Tissue ProteinsNGFR protein, humanReceptors, Nerve Growth FactorViral Envelope Proteins

Identifiers

PMID27294109
PMCPMC4879324
OpenAlexW2342208513

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.