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

Molecular interactions of c-ABL mutants in complex with imatinib/nilotinib: a computational study using linear interaction energy (LIE) calculations.

Journal of molecular modeling - 1 Sept 2012

Pereira Elen Gomes, Moreira Miguel Angelo Martins, Caffarena Ernesto Raúl

Abstract excerpt

In spite of the effectiveness of Imatinib for chronic myeloid leukemia (CML) treatment, resistance has repeatedly been reported and is associated with point mutations in the BCR-ABL chimeric gene. To overcome this resistance, several inhibitors of BCR-ABL tyrosine kinase activity were developed. In this context, computational simulations have become a powerful tool for understanding drug-protein interactions....

Read the complete abstract on PubMed

Topics

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

Share to Benzamides
Share to Imatinib Mesylate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutant Proteins

Share to Piperazines

Share to Proto-Oncogene Proteins c-abl

Share to Pyrimidines

Source

Identifiers

PMID: 22570081
DOI: 10.1007/s00894-012-1436-x

Genes

BCR

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

Molecular interactions of c-ABL mutants in complex with imatinib/nilotinib: a computational study using linear interaction energy (LIE) calculations.PMID 22570081Read ↗

T315I-mutated Bcr-Abl in chronic myeloid leukemia and imatinib: insights from a computational studySemantic proximity Read ↗

Molecular basis explanation for imatinib resistance of BCR-ABL due to T315I and P-loop mutations from molecular dynamics simulations.Semantic proximity Read ↗

Basis for resistance to imatinib in 16 BCR-ABL mutants as determined using molecular dynamics.Semantic proximity Read ↗

Discovery and Protein Modeling Studies of Novel Compound Mutations Causing Resistance to Multiple Tyrosine Kinase Inhibitors in Chronic Myeloid Leukemia.Semantic proximity Read ↗

Identification of new dasatinib analogues targeting mutated BCR-ABL1: virtual screening, molecular docking, and dynamics simulations studies.Semantic proximity Read ↗

Towards a Molecular Understanding of the Link between Imatinib Resistance and Kinase Conformational DynamicsSemantic proximity Read ↗

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

Dual Drug Targeting of Mutant Bcr-Abl Induces Inactive Conformation: New Strategy for the Treatment of Chronic Myeloid Leukemia and Overcoming Monotherapy Resistance.Semantic proximity Read ↗

A combined computational and experimental strategy identifies mutations conferring resistance to drugs targeting the BCR-ABL fusion protein.Semantic proximity Read ↗

Insight on Mutation-Induced Resistance from Molecular Dynamics Simulations of the Native and Mutated CSF-1R and KIT.Semantic proximity Read ↗

Predicting resistance of clinical Abl mutations to targeted kinase inhibitors using alchemical free-energy calculationsSemantic proximity Read ↗

Hierarchical modeling of activation mechanisms in the ABL and EGFR kinase domains: thermodynamic and mechanistic catalysts of kinase activation by cancer mutations.Semantic proximity Read ↗

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