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

Assessing the Activation of Tyrosine Kinase KIT through Free Energy Calculations.

Journal of chemical theory and computation - 11 Oct 2022

Sandoval-Pérez Angélica, Winger Beth Apsel, Jacobson Matthew P

Abstract excerpt

KIT is a type 3 receptor tyrosine kinase that plays a crucial role in cellular growth and proliferation. Mutations in KIT can dysregulate its active-inactive equilibrium. Activating mutations drive cancer growth, while deactivating mutations result in the loss of skin and hair pigmentation in a disease known as piebaldism. Here, we propose a method based on molecular dynamics and free energy calculations to...

Read the complete abstract on PubMed

Topics

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

Share to Mast cells and histamine
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to PI3K/AKT/mTOR signaling in cancer

Share to Piebaldism

Share to Proto-Oncogene Mas

Share to Proto-Oncogene Proteins c-kit

Source

Open in PubMed Open full text

Identifiers

PMID: 36166736
DOI: 10.1021/acs.jctc.2c00526
PMCID: PMC9558371

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

Assessing the Activation of Tyrosine Kinase KIT through Free Energy Calculations.PMID 36166736Read ↗

A shift of dynamic equilibrium between the KIT active and inactive states causes drug resistance.Semantic proximity Read ↗

Mutation D816V alters the internal structure and dynamics of c-KIT receptor cytoplasmic region: implications for dimerization and activation mechanisms.Semantic proximity Read ↗

Molecular Mechanisms of KIT Receptor Dimerization and Oncogenic Activation Revealed by Multiscale Simulations.Semantic proximity Read ↗

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

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

A novel approach to study multi-domain motions in JAK1's activation mechanism based on energy landscape.Semantic proximity Read ↗

A Molecular Dynamics Protocol for Rapid Prediction of EGFR Overactivation and Its Application to the Rare Mutations S768I, S768N, D761NSemantic proximity Read ↗

The free energy landscape in translational science: how can somatic mutations result in constitutive oncogenic activation?Semantic proximity Read ↗

Alchemical Free Energy Calculations to Investigate Protein-Protein Interactions: the Case of the CDC42/PAK1 Complex.Semantic proximity Read ↗

Predicting Kinase Inhibitor Resistance: Physics-Based and Data-Driven ApproachesSemantic proximity Read ↗

Role of ELA region in auto-activation of mutant KIT receptor: a molecular dynamics simulation insight.Semantic proximity Read ↗

Q: a molecular dynamics program for free energy calculations and empirical valence bond simulations in biomolecular systems.Semantic proximity Read ↗

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