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

Unbinding Pathways of VEGFR2 Inhibitors Revealed by Steered Molecular Dynamics

9 Oct 2014

Abstract excerpt

A detailed atomistic description of the unbinding process of sorafenib and sunitinib, two known VEGFR2 inhibitors clinically used to treat renal cell carcinoma, was unraveled by using steered molecular dynamics (SMD) simulations. While sunitinib is a fast-dissociating binder, sorafenib exhibits quite a long residence time at this enzyme, which might impact its duration of action in vivo. In order to gain insights...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme function and inhibition
Share to Mathematical Biology Tumor Growth
Share to Renal cell carcinoma treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25299731
DOI: 10.1021/ci500527j

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

Unbinding Pathways of VEGFR2 Inhibitors Revealed by Steered Molecular DynamicsPMID 25299731Read ↗

Microsecond Molecular Dynamics Simulation to Gain Insight Into the Binding of MRTX1133 and Trametinib With KRASG12D Mutant Protein for Drug Repurposing.Semantic proximity Read ↗

Structural dynamics and kinase inhibitory activity of three generations of tyrosine kinase inhibitors against wild-type, L858R/T790M, and L858R/T790M/C797S forms of EGFR.Semantic proximity Read ↗

Investigation of molecular mechanism leading to gefitinib and osimertinib resistance against EGFR tyrosine kinase: molecular dynamics and binding free energy calculation.Semantic proximity Read ↗

Contact Map Fingerprints of Protein-Ligand Unbinding Trajectories Reveal Mechanisms Determining Residence Times Computed from Scaled Molecular DynamicsSemantic proximity Read ↗

Structure-Based Virtual Screening, Molecular Docking, Molecular Dynamics Simulation of EGFR for the clinical treatment of GlioblastomaSemantic proximity Read ↗

Exhaustively Exploring the Prevalent Interaction Pathways of Ligands Targeting the Ligand-Binding Pocket of Farnesoid X Receptor via Combined Enhanced SamplingSemantic proximity Read ↗

Combining Molecular Dynamics and Machine Learning to Predict Drug Resistance Causing Variants of BRAF in Colorectal CancerSemantic proximity Read ↗

Unveiling KRAS G12D inhibition: from molecular dynamics to therapeutic strategies.Semantic proximity Read ↗

Molecular Dynamics Simulations in Designing DARPins as Phosphorylation-Specific Protein Binders of ERK2.Semantic proximity Read ↗

Unleashing Nature’s potential: a computational approach to discovering novel VEGFR-2 inhibitors from African natural compound using virtual screening, ADMET analysis, molecular dynamics, and MMPBSA calculationsSemantic proximity Read ↗

Gefitinib derivatives and drug-resistance: A perspective from molecular dynamics simulations.Semantic proximity Read ↗

Dynamics of human protein kinases linked to drug selectivitySemantic proximity Read ↗

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