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

Structural study of ponatinib in inhibiting SRC kinase.

Biochemical and biophysical research communications - 2 Apr 2022

Guo Ming, Duan Yankun, Dai Shuyan, Li Jun, Chen Xiaojuan, Qu Lingzhi, Chen Zhuchu, Wei Hudie, Jiang Longying, Chen Yongheng

Abstract excerpt

Ponatinib is a multi-target tyrosine kinase inhibitor that targets ABL, SRC, FGFR, and so on. It was designed to overcome the resistance of BCR-ABL mutation to imatinib, especially the gatekeeper mutation ABLT315I. The molecular mechanism by which ponatinib overcomes mutations of BCR-ABL and some other targets has been explained, but little information is known about the characteristics of ponatinib binding to...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Imidazoles

Share to Protein Conformation

Share to Protein Domains

Share to Protein Kinase Inhibitors

Share to Pyridazines

Share to src-Family Kinases

Source

Identifiers

PMID: 35151199
DOI: 10.1016/j.bbrc.2022.02.001

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

Structural study of ponatinib in inhibiting SRC kinase.PMID 35151199Read ↗

Structural mechanism of the Pan-BCR-ABL inhibitor ponatinib (AP24534): lessons for overcoming kinase inhibitor resistance.Semantic proximity Read ↗

Computational biophysical characterization of the effect of gatekeeper mutations on the binding of ponatinib to the FGFR kinase.Semantic proximity Read ↗

Structure optimization, synthesis and bioactivity evaluation of novel BCR-ABL tyrosine kinase inhibitor targeting T315I mutation.Semantic proximity Read ↗

T315L: a novel mutation within BCR-ABL kinase domain confers resistance against ponatinib.Semantic proximity Read ↗

Activation of tyrosine kinases by mutation of the gatekeeper threonine.Semantic proximity Read ↗

DFG-out mode of inhibition by an irreversible type-1 inhibitor capable of overcoming gate-keeper mutations in FGF receptors.Semantic proximity Read ↗

BCR-ABL1 compound mutations drive ponatinib resistance.Semantic proximity Read ↗

Resistant mutations in CML and Ph+ALL &ndash; role of ponatinibSemantic proximity Read ↗

Advances in Targeting BCR-ABLT315I Mutation with Imatinib Derivatives and Hybrid Anti-Leukemic Molecules.Semantic proximity Read ↗

Profiling of the drug resistance of thousands of Src tyrosine kinase mutants uncovers a regulatory network that couples autoinhibition to catalytic domain dynamicsSemantic proximity Read ↗

Ponatinib--a step forward in overcoming resistance in chronic myeloid leukemia.Semantic proximity Read ↗

Discovery of 5-(arenethynyl) hetero-monocyclic derivatives as potent inhibitors of BCR-ABL including the T315I gatekeeper mutant.Semantic proximity Read ↗

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