ArticleInternational journal of molecular sciences2021
The Structural Effect of FLT3 Mutations at 835th Position and Their Interaction with Acute Myeloid Leukemia Inhibitors: In Silico Approach.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- XY0206 targets FLT3-dependent resistance states in acute myeloid leukemia.The Journal of clinical investigation · 2026Article
- Review
- Theoretical investigation of AKT1 mutations in breast cancer: a computational approach to structural and functional insights.Journal of computer-aided molecular design · 2025Article
- Understanding the characteristic behaviour of the wild-type and mutant structure of FLT3 protein by computational methods.Computational and structural biotechnology journal · 2025Article
- SPEAR: CRISPR-mediated ultrasensitive, specific and rapid one-pot detection strategy for cancer-related SNPs.Theranostics · 2025Article
- Article
- Prediction of Cholecystokinin-Secretory Peptides Using Bidirectional Long Short-term Memory Model Based on Transfer Learning and Hierarchical Attention Network Mechanism.Biomolecules · 2023Article
- How ITD Insertion Sites Orchestrate the Biology and Disease of FLT3-ITD-Mutated Acute Myeloid Leukemia.Cancers · 2023Review
- In Silico-Based Structural Evaluation to Categorize the Pathogenicity of Mutations Identified in the RAD Class of Proteins.ACS omega · 2023Article
- Molecular interaction of a putative inhibitor with bacterial SHV, an enzyme associated with antibiotic resistance.Royal Society open science · 2023Article
- Unraveling the molecular mechanism of novel leukemia mutations on NTRK2 (A203T & R458G) and NTRK3 (E176D & L449F) genes using molecular dynamics simulations approach.F1000Research · 2023Article
- Molecular dynamics of the ERRγ ligand-binding domain bound with agonist and inverse agonist.PloS one · 2023Article
- Discovery of Hepatotoxic Equivalent Markers and Mechanism ofMolecules (Basel, Switzerland) · 2022Article
- FLT3-targeted treatment for acute myeloid leukemia.International journal of hematology · 2022Review
- Understanding gilteritinib resistance to FLT3-F691L mutation through an integrated computational strategy.Journal of molecular modeling · 2022Article
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2 authors.
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Abstract
FMS-like tyrosine kinase 3 (FLT3) gene mutations have been found in more than one-third of Acute Myeloid Leukemia (AML) cases. The most common point mutation in FLT3 occurs at the 835th residue (D835A/E/F/G/H/I/N/V/Y), in the activation loop region. The D835 residue is critical in maintaining FLT3 inactive conformation; these mutations might influence the interaction with clinically approved AML inhibitors used to treat the AML. The molecular mechanism of each of these mutations and their interactions with AML inhibitors at the atomic level is still unknown. In this manuscript, we have investigated the structural consequence of native and mutant FLT-3 proteins and their molecular mechanisms at the atomic level, using molecular dynamics simulations (MDS). In addition, we use the molecular docking method to investigate the binding pattern between the FLT-3 protein and AML inhibitors upon mutations. This study apparently elucidates that, due to mutations in the D835, the FLT-3 structure loses its conformation and becomes more flexible compared to the native FLT3 protein. These structural changes are suggested to contribute to the relapse and resistance responses to AML inhibitors. Identifying the effects of FLT3 at the molecular level will aid in developing a personalized therapeutic strategy for treating patients with FLT-3-associated AML.
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