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

Discovery of novel 2-aminopyridine derivatives as ROS1 and ALK dual inhibitors to combat drug-resistant mutants including ROS1G2032R and ALKG1202R.

Journal of enzyme inhibition and medicinal chemistry - 1 Dec 2023

Liu Siming, Huang Chuan, Huang Chunhui, Huang Yaqi, Yu Yonghuan, Wu Guowu, Guo Fengqiu, Jiang Ying, Wan Shanhe, Zhu Zhengguang, Tian Yuanxin, Zhu Jianghua, Zhang Jiajie

Abstract excerpt

Clinical treatment by FDA-approved ROS1/ALK inhibitor Crizotinib significantly improved the therapeutic outcomes. However, the emergence of drug resistance, especially driven by acquired mutations, have become an inevitable problem and worsened the clinical effects of Crizotinib. To combat drug resistance, some novel 2-aminopyridine derivatives were designed rationally based on molecular simulation, then...

Read the complete abstract on PubMed

Topics

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

Share to Anaplastic Lymphoma Kinase
Share to Cell Line, Tumor

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crizotinib

Share to Drug Resistance, Neoplasm

Share to Lung Neoplasms

Share to Protein Kinase Inhibitors

Share to Protein-Tyrosine Kinases

Share to Proto-Oncogene Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 37349867
DOI: 10.1080/14756366.2023.2227779
PMCID: PMC10288926

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Discovery of novel 2-aminopyridine derivatives as ROS1 and ALK dual inhibitors to combat drug-resistant mutants including ROS1G2032R and ALKG1202R.PMID 37349867Read ↗

Fragment-based modification of 2,4-diarylaminopyrimidine derivatives as ALK and ROS1 dual inhibitors to overcome secondary mutants.Semantic proximity Read ↗

Discovery of novel 2,4-diarylaminopyrimidine analogues as ALK and ROS1 dual inhibitors to overcome crizotinib-resistant mutants including G1202R.Semantic proximity Read ↗

Comprehensive Review of ROS1 Tyrosine Kinase Inhibitors-Classified by Structural Designs and Mutation Spectrum (Solvent Front Mutation [G2032R] and Central β-Sheet 6 [Cβ6] Mutation [L2086F]).Semantic proximity Read ↗

Structural insight into selectivity and resistance profiles of ROS1 tyrosine kinase inhibitorsSemantic proximity Read ↗

Virtual screening of novel alkaloids as potent inhibitors for G2032R-mutant ROS1 kinase in non-small-cell lung cancer.Semantic proximity Read ↗

P-loop conformation governed crizotinib resistance in G2032R-mutated ROS1 tyrosine kinase: clues from free energy landscape.Semantic proximity Read ↗

Structure-based optimization identified novel furyl-containing 2,4-diarylaminopyrimidine analogues as ALK/ROS1 dual inhibitors with anti-mutation effects.Semantic proximity Read ↗

The new-generation selective ROS1/NTRK inhibitor DS-6051b overcomes crizotinib resistant ROS1-G2032R mutation in preclinical modelsSemantic proximity Read ↗

Investigation on the binding mechanism of loratinib with the c-ros oncogene 1 (ROS1) receptor tyrosine kinase via molecular dynamics simulation and binding free energy calculations.Semantic proximity Read ↗

PF-06463922 is a potent and selective next-generation ROS1/ALK inhibitor capable of blocking crizotinib-resistant ROS1 mutations.Semantic proximity Read ↗

Discovery and preclinical evaluations of WX-0593, a novel ALK inhibitor targeting crizotinib-resistant mutations.Semantic proximity Read ↗

Resistance Profile and Structural Modeling of Next-Generation ROS1 Tyrosine Kinase InhibitorsSemantic proximity Read ↗

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