Evidence map›Paper›PMID 39514082›Full record

ArticleBiochemical genetics2025

A Novel NRAS Variant Near the Splice Junction in Moroccan Childhood Acute Lymphoblastic Leukemia: A Molecular Dynamics Study.

Hanaa Skhoun, Meriem El Fessikh, Mohammed Khattab, Basma Mchich, Aomar Agadr, Rachid Abilkassem, Nadia Dakka, Delphine Flatters, Anne-Claude Camproux, Zohra Ouzzif and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Biochemical genetics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Hanaa SkhounGenetics Unit, Military Hospital Mohammed V, Rabat, Morocco.ORCID https://orcid.org/0000-0002-4081-1604
Meriem El FessikhGenetics Unit, Military Hospital Mohammed V, Rabat, Morocco.ORCID https://orcid.org/0000-0001-9237-1156
Mohammed KhattabPediatric Hematology and Oncology Center, Children's Hospital, Rabat, Morocco.
Basma MchichUnité de Biologie Fonctionnelle Et Adaptative, Université Paris Cité, CNRS, INSERM, Paris, France.
Aomar AgadrDepartment of Pediatrics, Military Hospital Mohammed V, Faculty of Medicine and Pharmacy, University Mohammed V, Rabat, Morocco.
Rachid AbilkassemDepartment of Pediatrics, Military Hospital Mohammed V, Faculty of Medicine and Pharmacy, University Mohammed V, Rabat, Morocco.
Nadia DakkaLaboratory of Human Pathologies Biology and Genomic Center of Human Pathologies, Department of Biology, Faculty of Sciences, Mohammed V University, Rabat, Morocco.ORCID https://orcid.org/0000-0002-8265-5689
Delphine FlattersUnité de Biologie Fonctionnelle Et Adaptative, Université Paris Cité, CNRS, INSERM, Paris, France.ORCID https://orcid.org/0000-0003-2273-3259
Anne-Claude CamprouxUnité de Biologie Fonctionnelle Et Adaptative, Université Paris Cité, CNRS, INSERM, Paris, France.ORCID https://orcid.org/0000-0001-8821-9952
Zohra OuzzifLaboratories Pole, Military Hospital Mohammed V, Rabat, Morocco.
Jamila El BaghdadiGenetics Unit, Military Hospital Mohammed V, Rabat, Morocco. baghdadijamila@yahoo.fr.ORCID https://orcid.org/0000-0002-1920-2310

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RAS genes are importantly implicated in oncogenesis and are frequently mutated in childhood acute lymphoblastic leukemia. This study is the first to our knowledge, to determine the mutational status of NRAS and KRAS genes in Moroccan pediatric acute lymphoblastic leukemia (ALL). Polymerase chain reaction and Sanger sequencing were performed for 45 ALL samples to explore the coding exons. The functional effect of the mutation was evaluated using in silico prediction tools and molecular modeling. We identified a novel variant c.290 G > C p.Arg97Thr within NRAS gene in a patient with T-ALL, which is a rare missense point mutation affecting the last base of exon 3. Analyses revealed that p.Arg97Thr impairs the adjacent splice site efficiency. Moreover, it leads to structural modifications at local and global levels of the protein through the loss of hydrogen bonds. Additionally, the molecular dynamics (MD) simulation showed that it slightly increases the stability of NRAS protein by locally decreasing the flexibility of the mutated region. No variant was detected within KRAS gene. R97 at NRAS gene is an overlapping splice site residue. Our findings suggest that the NRAS p.Arg97Thr variant may disrupt the splicing machinery and functions of the protein, thus playing a vital role in leukemogenesis. In addition, the highly druggable pocket may possibly be studied for its therapeutic implications.

Indexed as

GTP PhosphohydrolasesMembrane ProteinsPrecursor Cell Lymphoblastic Leukemia-LymphomaRNA Splice SitesChildChild, PreschoolExonsFemaleHumansMaleMolecular Dynamics SimulationMoroccoMutation, MissenseProto-Oncogene Proteins p21(ras)GTP PhosphohydrolasesKRAS protein, humanMembrane ProteinsNRAS protein, humanProto-Oncogene Proteins p21(ras)RNA Splice SitesChanges in protein structureChildhood acute lymphoblastic leukemiaIn silico analysesNovel NRAS variantSplicing disruption

Identifiers

What Socratic holds

Textmetadata
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 Socratic graph.