Evidence map›Paper›PMID 35654936›Full record

ArticleJournal of molecular neuroscience : MN2022

Combined in Silico Prediction Methods, Molecular Dynamic Simulation, and Molecular Docking of FOXG1 Missense Mutations: Effect on FoxG1 Structure and Its Interactions with DNA and Bmi-1 Protein.

Marwa Kharrat, Chahnez Charfi Triki, Olfa Alila-Fersi, Olfa Jallouli, Bassem Khemakham, Salma Mallouli, Marwa Maalej, Marwa Ammar, Fakher Frikha, Fatma Kamoun and 1 more

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Article in Journal of molecular neuroscience : MN, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
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

11 authors at 2 institutions in 1 country.

Marwa KharratLaboratory of Molecular and Functional Genetics, Faculty of Science, Sfax University, Sfax, Tunisia. marwa.kharrat.feki@gmail.com.
Chahnez Charfi TrikiChild Neurology Department, Hedi Chaker Hospital, Sfax, Tunisia.
Olfa Alila-FersiLaboratory of Molecular and Functional Genetics, Faculty of Science, Sfax University, Sfax, Tunisia.
Olfa JallouliChild Neurology Department, Hedi Chaker Hospital, Sfax, Tunisia.
Bassem KhemakhamLaboratory of Plant Biotechnology, Faculty of Sciences of Sfax, Sfax University, Sfax, Tunisia.
Salma MallouliChild Neurology Department, Hedi Chaker Hospital, Sfax, Tunisia.
Marwa MaalejLaboratory of Molecular and Functional Genetics, Faculty of Science, Sfax University, Sfax, Tunisia.
Marwa AmmarLaboratory of Molecular and Functional Genetics, Faculty of Science, Sfax University, Sfax, Tunisia.
Fakher FrikhaLaboratory of Molecular and Cellular Screening Processes, Center of Biotechnology of Sfax, University of Sfax, Sfax, Tunisia.
Fatma KamounChild Neurology Department, Hedi Chaker Hospital, Sfax, Tunisia.
Faiza FakhfakhLaboratory of Molecular and Functional Genetics, Faculty of Science, Sfax University, Sfax, Tunisia. faiza.fakhfakh02@gmail.com.
University of Sfax · TNHopital Universitaire Hedi Chaker · TN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FoxG1 encoded by FOXG1 gene is a transcriptional factor interacting with the DNA of targeted genes as well as with several proteins to regulate the forebrain development. Mutations in the FOXG1 gene have been shown to cause a wide spectrum of brain disorders, including the congenital variant of Rett syndrome. In this study, the direct sequencing of FOXG1 gene revealed a novel c.645C > A (F215L) variant in the patient P1 and a de novo known one c.755G > A (G252D) in the patient P2. To investigate the putative impact of FOXG1 missense variants, a computational pipeline by the application of in silico prediction methods, molecular dynamic simulation, and molecular docking approaches was used. Bioinformatics analysis and molecular dynamics simulation have demonstrated that F215L and G252D variants found in the DNA binding domain are highly deleterious mutations that may cause the protein structure destabilization. On the other hand, molecular docking revealed that F215L mutant is likely to have a great impact on destabilizing the protein structure and the disruption of the Bmi-1 binding site quite significantly. Regarding G252D mutation, it seems to abolish the ability of FoxG1 to bind DNA target, affecting the transcriptional regulation of targeted genes. Our study highlights the usefulness of combined computational approaches, molecular dynamic simulation, and molecular docking for a better understanding of the dysfunctional effects of FOXG1 missense mutations and their role in the etiopathogenesis as well as in the genotype-phenotype correlation.

Indexed as

Molecular Dynamics SimulationMutation, MissenseDNAForkhead Transcription FactorsMolecular Docking SimulationMutationNerve Tissue ProteinsDNAForkhead Transcription FactorsNerve Tissue ProteinsCongenital Rett syndromeFoxG1Missense mutationsMolecular dockingMolecular dynamic simulation

Identifiers

PMID35654936
OpenAlexW4281676694

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.