Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Deciphering the mechanism of HM43239 inhibiting the mutant F691L resistant to gilteritinib in FMS-like tyrosine kinase 3.

Journal of biomolecular structure & dynamics - 1 Jul 2024

Wang Zhiwei, An Yu, Wang Jian, Lu Jinghua

Abstract excerpt

FMS-like tyrosine kinase (FLT3) has become the legitimate molecular therapeutic target for acute myeloid leukemia therapy. Though FLT3 inhibitors have impact on disease progression, drug resistance induced by secondary point mutations is the primary mechanism and urgent to overcome. Herein, we sought to decipher the mechanism of HM43239 inhibiting the mutant F691L resistant to gilteritinib in FLT3. A series of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aniline Compounds
Share to fms-Like Tyrosine Kinase 3

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Molecular Docking Simulation

Share to Molecular Dynamics Simulation

Share to Pyrazines

Share to Thermodynamics

Share to Triazines

Source

Identifiers

PMID: 37382586
DOI: 10.1080/07391102.2023.2229447

Genes

FLT3
DCC

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Deciphering the mechanism of HM43239 inhibiting the mutant F691L resistant to gilteritinib in FMS-like tyrosine kinase 3.PMID 37382586Read ↗

Understanding gilteritinib resistance to FLT3-F691L mutation through an integrated computational strategy.Semantic proximity Read ↗

Exploring the Resistance Mechanisms of Distal D835V Mutation in FLT3 to Inhibitors.Semantic proximity Read ↗

The Structural Effect of FLT3 Mutations at 835th Position and Their Interaction with Acute Myeloid Leukemia Inhibitors: In Silico Approach.Semantic proximity Read ↗

In silico and in vitro study of FLT3 inhibitors and their application in acute myeloid leukemia.Semantic proximity Read ↗

Discovery of a Potent FLT3 Inhibitor (LT-850-166) with the Capacity of Overcoming a Variety of FLT3 Mutations.Semantic proximity Read ↗

A noncanonical FLT3 gatekeeper mutation disrupts gilteritinib binding and confers resistanceSemantic proximity Read ↗

Identification of inhibitors targeting the FLT3-ITD mutation through 4D-QSAR, in vitro, and in silico.Semantic proximity Read ↗

An imidazo[1,2-a]pyridine-pyridine derivative potently inhibits FLT3-ITD and FLT3-ITD secondary mutants, including gilteritinib-resistant FLT3-ITD/F691L.Semantic proximity Read ↗

Characterizing and Overriding the Structural Mechanism of the Quizartinib-Resistant FLT3 "Gatekeeper" F691L Mutation with PLX3397.Semantic proximity Read ↗

Gilteritinib is a clinically active FLT3 inhibitor with broad activity against FLT3 kinase domain mutations.Semantic proximity Read ↗

The Irreversible FLT3 Inhibitor FF-10101 Is Active Against a Diversity of FLT3 Inhibitor Resistance Mechanisms.Semantic proximity Read ↗

Resistance to a tyrosine kinase inhibitor mediated by changes to the conformation space of the kinase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.