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 › S12_Cell_lines
Discriminating activating, deactivating and resistance variants in protein kinases.
Singh G et al.
Genome Medicine, 2025
41152984 (PubMed )
Supplement: 13073_2025_1564_MOESM2_ESM.xlsx › Table_S6
Elucidating the Role of Wildtype and Variant FGFR2 Structural Dynamics in (Dys)Function and Disorder.
Lian Y et al.
International Journal of Molecular Sciences, 2024
Truncated FGFR2 is a clinically actionable oncogene in multiple cancers.
Zingg D et al.
Nature, 2022
35948633 (PubMed )
Supplement: 41586_2022_5066_MOESM16_ESM.xlsx › ED_Fig._2a
Elucidation of a four-site allosteric network in fibroblast growth factor receptor tyrosine kinases.
Chen H et al.
Elife, 2017
Cracking the molecular origin of intrinsic tyrosine kinase activity through analysis of pathogenic gain-of-function mutations.
Chen H et al.
Cell Reports, 2013
Decoupling the dynamic mechanism revealed by FGFR2 mutation-induced population shift.
Zhang Y et al.
Journal of Biomolecular Structure & Dynamics, 0
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