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Article

Allosteric enhancement of the BCR-Abl1 kinase inhibition activity of nilotinib by cobinding of asciminib.

The Journal of biological chemistry - 1 Aug 2022

Oruganti Baswanth, Lindahl Erik, Yang Jingmei, Amiri Wahid, Rahimullah Rezwan, Friedman Ran

Abstract excerpt

Inhibitors that bind competitively to the ATP binding pocket in the kinase domain of the oncogenic fusion protein BCR-Abl1 are used successfully in targeted therapy of chronic myeloid leukemia (CML). Such inhibitors provided the first proof of concept that kinase inhibition can succeed in a clinical setting. However, emergence of drug resistance and dose-dependent toxicities limit the effectiveness of these...

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Share to Adenosine Triphosphate
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Resistance, Neoplasm

Share to Fusion Proteins, bcr-abl

Share to Leukemia, Myelogenous, Chronic, BCR-ABL Positive

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Source

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Identifiers

PMID: 35809644
DOI: 10.1016/j.jbc.2022.102238
PMCID: PMC9386466

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

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Allosteric enhancement of the BCR-Abl1 kinase inhibition activity of nilotinib by cobinding of asciminib.PMID 35809644Read ↗

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