Associated Papers
Saturation mutagenesis identifies activating and resistance-inducing FGFR kinase domain mutations.
Tangermann C et al.
Nature Genetics, 2026
41361008 (PubMed )
Supplement: 41588_2025_2431_MOESM3_ESM.xlsx › S10_Screen_data_table
Discovery of TYRA-300: First Oral Selective FGFR3 Inhibitor for the Treatment of Urothelial Cancers and Achondroplasia.
Hudkins RL et al.
Journal of Medicinal Chemistry, 2024
39258897 (PubMed )
Supplement: jm4c01531_si_001.pdf
Structural basis and selectivity of sulfatinib binding to FGFR and CSF-1R.
Lin Q et al.
Communications Chemistry, 2024
Characterization of the cholangiocarcinoma drug pemigatinib against FGFR gatekeeper mutants.
Lin Q et al.
Communications Chemistry, 2022
Molecular basis for receptor tyrosine kinase A-loop tyrosine transphosphorylation.
Chen L et al.
Nature Chemical Biology, 2020
Structural insights and activating mutations in diverse pathologies define mechanisms of deregulation for phospholipase C gamma enzymes.
Liu Y et al.
Ebiomedicine, 2020
Rotational Freedom, Steric Hindrance, and Protein Dynamics Explain BLU554 Selectivity for the Hinge Cysteine of FGFR4.
Lin X et al.
Acs Medicinal Chemistry Letters, 2019
31413803 (PubMed )
Supplement: ml9b00196_si_001.pdf
An overview of the binding models of FGFR tyrosine kinases in complex with small molecule inhibitors.
Cheng W et al.
European Journal of Medicinal Chemistry, 2017
Structural analysis of the mechanism of phosphorylation of a critical autoregulatory tyrosine residue in FGFR1 kinase domain.
Kobashigawa Y et al.
Genes to Cells : Devoted to Molecular & Cellular Mechanisms, 2015
Structural and dynamic insights into the energetics of activation loop rearrangement in FGFR1 kinase.
Klein T et al.
Nature Communications, 2015
Illuminating the molecular mechanisms of tyrosine kinase inhibitor resistance for the FGFR1 gatekeeper mutation: the Achilles' heel of targeted therapy.
Sohl CD et al.
Acs Chemical Biology, 2015
The 1.65 Å resolution structure of the complex of AZD4547 with the kinase domain of FGFR1 displays exquisite molecular recognition.
Yosaatmadja Y et al.
Acta Crystallographica. Section D, Biological Crystallography, 2015
NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
Vajpai N et al.
Biomolecular Nmr Assignments, 2014
Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation.
Bunney TD et al.
Structure (london, England : 1993), 2012
23063561 (PubMed )
Supplement: mmc1.pdf
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