ArticleNature communications2015
Structural and dynamic insights into the energetics of activation loop rearrangement in FGFR1 kinase.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed, 74 citations in OpenAlex.
- The role of FGFR signaling in SCLC and NSCLC: Current insights and therapeutic perspectives.iScience · 2026Review
- The rise and fall of SARM1 base-exchange inhibitors.Communications chemistry · 2026Article
- Protein-Ligand Interactions in Cardiometabolic Drug Targets: Focus on Weight Loss and Cardioprotection.Molecules (Basel, Switzerland) · 2025Review
- MolPrompt: improving multi-modal molecular pre-training with knowledge prompts.Bioinformatics (Oxford, England) · 2025Article
- Development and Characterization of Three Novel FGFR Inhibitor Resistant Cervical Cancer Cell Lines to Help Drive Cervical Cancer Research.International journal of molecular sciences · 2025Article
- Exploring the Impact of Protein Chain Selection in Binding Energy Calculations with DFT.Chemphyschem : a European journal of chemical physics and physical chemistry · 2024Article
- Multiple allostery in the regulation of PDGFR beta kinase activities.Acta biochimica et biophysica Sinica · 2024Article
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- A knowledge-guided pre-training framework for improving molecular representation learning.Nature communications · 2023Article
- Optimization of a Protein-Targeted Medicine into an RNA-Specific Small Molecule.ACS chemical biology · 2023Article
- Online Fully Automated System for Hydrogen/Deuterium-Exchange Mass Spectrometry with Millisecond Time Resolution.Analytical chemistry · 2023Article
- Reduced Cardiotoxicity of Ponatinib-Loaded PLGA-PEG-PLGA Nanoparticles in Zebrafish Xenograft Model.Materials (Basel, Switzerland) · 2022Article
- DNA repair glycosylase hNEIL1 triages damaged bases via competing interaction modes.Nature communications · 2021Article
- Utilizing Stimulated Raman Scattering Microscopy To Study Intracellular Distribution of Label-Free Ponatinib in Live Cells.Journal of medicinal chemistry · 2020Article
- A combined computational and experimental strategy identifies mutations conferring resistance to drugs targeting the BCR-ABL fusion protein.Communications biology · 2020Article
- A Dynamic Switch in Inactive p38γ Leads to an Excited State on the Pathway to an Active Kinase.Biochemistry · 2019Article
- Application of a Substrate-Mediated Selection with c-Src Tyrosine Kinase to a DNA-Encoded Chemical Library.Molecules (Basel, Switzerland) · 2019Article
- Review
- A class of highly selective inhibitors bind to an active state of PI3Kγ.Nature chemical biology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 2 institutions in 1 country.
Funding
Abstract
Protein tyrosine kinases differ widely in their propensity to undergo rearrangements of the N-terminal Asp-Phe-Gly (DFG) motif of the activation loop, with some, including FGFR1 kinase, appearing refractory to this so-called 'DFG flip'. Recent inhibitor-bound structures have unexpectedly revealed FGFR1 for the first time in a 'DFG-out' state. Here we use conformationally selective inhibitors as chemical probes for interrogation of the structural and dynamic features that appear to govern the DFG flip in FGFR1. Our detailed structural and biophysical insights identify contributions from altered dynamics in distal elements, including the αH helix, towards the outstanding stability of the DFG-out complex with the inhibitor ponatinib. We conclude that the αC-β4 loop and 'molecular brake' regions together impose a high energy barrier for this conformational rearrangement, and that this may have significance for maintaining autoinhibition in the non-phosphorylated basal state of FGFR1.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.