Genomic architecture of FGFR2 fusions in cholangiocarcinoma and its implication for molecular testing

[1]  Bahar Yilmazel,et al.  Validation and Characterization of FGFR2 Rearrangements in Cholangiocarcinoma With Comprehensive Genomic Profiling. , 2022, The Journal of molecular diagnostics : JMD.

[2]  R. Verhaak,et al.  HUGO Gene Nomenclature Committee (HGNC) recommendations for the designation of gene fusions , 2021, Leukemia.

[3]  Joon-Oh Park,et al.  Futibatinib, an Irreversible FGFR1–4 Inhibitor, in Patients with Advanced Solid Tumors Harboring FGF/FGFR Aberrations: A Phase I Dose-Expansion Study , 2021, Cancer discovery.

[4]  P. Philip,et al.  Infigratinib (BGJ398) in previously treated patients with advanced or metastatic cholangiocarcinoma with FGFR2 fusions or rearrangements: mature results from a multicentre, open-label, single-arm, phase 2 study. , 2021, The lancet. Gastroenterology & hepatology.

[5]  S. Fröhling,et al.  Accurate and efficient detection of gene fusions from RNA sequencing data , 2021, Genome research.

[6]  D. Melisi,et al.  Clinicogenomic analysis of FGFR2-rearranged cholangiocarcinoma identifies correlates of response and mechanisms of resistance to pemigatinib. , 2020, Cancer discovery.

[7]  W. Weichert,et al.  NTRK testing: First results of the QuiP‐EQA scheme and a comprehensive map of NTRK fusion variants and their diagnostic coverage by targeted RNA‐based NGS assays , 2020, Genes, chromosomes & cancer.

[8]  B. Teh,et al.  Lack of Targetable FGFR2 Fusions in Endemic Fluke-Associated Cholangiocarcinoma , 2020, JCO global oncology.

[9]  E. Van Cutsem,et al.  Pemigatinib for previously treated, locally advanced or metastatic cholangiocarcinoma: a multicentre, open-label, phase 2 study. , 2020, The Lancet. Oncology.

[10]  G. Brandi,et al.  Targeting BRAF-Mutant Biliary Tract Cancer: Recent Advances and Future Challenges , 2020, Cancer control : journal of the Moffitt Cancer Center.

[11]  D. Donoghue,et al.  Functions of FGFR2 corrupted by translocations in intrahepatic cholangiocarcinoma. , 2019, Cytokine & growth factor reviews.

[12]  Peter Schirmacher,et al.  The 2019 WHO classification of tumours of the digestive system , 2019, Histopathology.

[13]  P. Schirmacher,et al.  RNA-Based Detection of Gene Fusions in Formalin-Fixed and Paraffin-Embedded Solid Cancer Samples , 2019, Cancers.

[14]  V. Miller,et al.  Profiling of 3,634 cholangiocarcinomas (CCA) to identify genomic alterations (GA), tumor mutational burden (TMB), and genomic loss of heterozygosity (gLOH). , 2019, Journal of Clinical Oncology.

[15]  B. Goeppert,et al.  Anatomical, histomorphological and molecular classification of cholangiocarcinoma , 2019, Liver international : official journal of the International Association for the Study of the Liver.

[16]  Y. Zen,et al.  Histological and molecular characterization of intrahepatic bile duct cancers suggests an expanded definition of perihilar cholangiocarcinoma. , 2019, HPB : the official journal of the International Hepato Pancreato Biliary Association.

[17]  M. Katoh Fibroblast growth factor receptors as treatment targets in clinical oncology , 2018, Nature Reviews Clinical Oncology.

[18]  A. Krasinskas Cholangiocarcinoma. , 2018, Surgical pathology clinics.

[19]  Kenneth L. Jones,et al.  Comparison of Molecular Testing Modalities for Detection of ROS1 Rearrangements in a Cohort of Positive Patient Samples , 2017, Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer.

[20]  Hiromi Nakamura,et al.  Genomic spectra of biliary tract cancer , 2015, Nature Genetics.

[21]  A. N. Meyer,et al.  Functions of Fibroblast Growth Factor Receptors in cancer defined by novel translocations and mutations. , 2015, Cytokine & growth factor reviews.

[22]  F. Couch,et al.  Fibroblast growth factor receptor 2 translocations in intrahepatic cholangiocarcinoma. , 2014, Human pathology.

[23]  Y. Jeng,et al.  Morphological subclassification of intrahepatic cholangiocarcinoma: etiological, clinicopathological, and molecular features , 2014, Modern Pathology.

[24]  Y. Totoki,et al.  Fibroblast growth factor receptor 2 tyrosine kinase fusions define a unique molecular subtype of cholangiocarcinoma , 2014, Hepatology.

[25]  Nickolay A. Khazanov,et al.  Identification of targetable FGFR gene fusions in diverse cancers. , 2013, Cancer discovery.

[26]  Jesse S. Voss,et al.  Isocitrate dehydrogenase 1 and 2 mutations in cholangiocarcinoma. , 2012, Human pathology.

[27]  S. Arold,et al.  Inhibition of Basal FGF Receptor Signaling by Dimeric Grb2 , 2012, Cell.

[28]  B. Yoong,et al.  Survival analysis of cholangiocarcinoma: a 10-year experience in Malaysia. , 2012, World journal of gastroenterology.

[29]  Jeffrey W. Clark,et al.  Frequent mutation of isocitrate dehydrogenase (IDH)1 and IDH2 in cholangiocarcinoma identified through broad-based tumor genotyping. , 2012, The oncologist.

[30]  Helga Thorvaldsdóttir,et al.  Integrative Genomics Viewer , 2011, Nature Biotechnology.

[31]  J. Ladbury,et al.  Direct binding of Grb2 SH3 domain to FGFR2 regulates SHP2 function. , 2010, Cellular signalling.

[32]  C. Der,et al.  Aberrant Receptor Internalization and Enhanced FRS2-dependent Signaling Contribute to the Transforming Activity of the Fibroblast Growth Factor Receptor 2 IIIb C3 Isoform* , 2009, Journal of Biological Chemistry.

[33]  S. Ethier,et al.  Differential signal transduction of alternatively spliced FGFR2 variants expressed in human mammary epithelial cells , 2007, Journal of cellular physiology.

[34]  Tom H. Pringle,et al.  The human genome browser at UCSC. , 2002, Genome research.

[35]  M. Makuuchi,et al.  Deletion of the carboxyl-terminal exons of K-sam/FGFR2 by short homology-mediated recombination, generating preferential expression of specific messenger RNAs. , 1999, Cancer research.

[36]  R. Friesel,et al.  Ligand-independent Activation of Fibroblast Growth Factor Receptors by Point Mutations in the Extracellular, Transmembrane, and Kinase Domains* , 1996, The Journal of Biological Chemistry.

[37]  H. Ishii,et al.  Preferential alternative splicing in cancer generates a K-sam messenger RNA with higher transforming activity. , 1994, Cancer research.