1 Khan, S. A., Tavolari, S. & Brandi, G. Cholangiocarcinoma: Epidemiology and risk factors. Liver international : official journal of the International Association for the Study of the Liver39 Suppl 1, 19-31, doi:10.1111/liv.14095 (2019).
2 Srivastava, A. K. et al. Human genome meeting 2016 : Houston, TX, USA. 28 February - 2 March 2016. Human genomics10 Suppl 1, 12, doi:10.1186/s40246-016-0063-5 (2016).
3 Belfiore, M. P. et al. Preliminary results in unresectable cholangiocarcinoma treated by CT percutaneous irreversible electroporation: feasibility, safety and efficacy. Medical oncology (Northwood, London, England)37, 45, doi:10.1007/s12032-020-01360-2 (2020).
4 Cai, Y. et al. The current management of cholangiocarcinoma: A comparison of current guidelines. Bioscience trends10, 92-102, doi:10.5582/bst.2016.01048 (2016).
5 Ulstrup, T. & Pedersen, F. M. [Photodynamic therapy of cholangiocarcinomas]. Ugeskrift for laeger175, 579-582 (2013).
6 Bristow, R. E. et al. Recurrent micropapillary serous ovarian carcinoma. Cancer95, 791-800, doi:10.1002/cncr.10789 (2002).
7 Chun, Y. S. & Javle, M. Systemic and Adjuvant Therapies for Intrahepatic Cholangiocarcinoma. Cancer control : journal of the Moffitt Cancer Center24, 1073274817729241, doi:10.1177/1073274817729241 (2017).
8 Laurent, S. et al. Update on liver transplantation for cholangiocarcinoma : a review of the recent literature. Acta gastro-enterologica Belgica82, 417-420 (2019).
9 Murtaza, M., Jolly, L. A., Gecz, J. & Wood, S. A. La FAM fatale: USP9X in development and disease. Cellular and molecular life sciences : CMLS72, 2075-2089, doi:10.1007/s00018-015-1851-0 (2015).
10 Li, H. & Zheng, B. Overexpression of the Ubiquitin-Specific Peptidase 9 X-Linked (USP9X) Gene is Associated with Upregulation of Cyclin D1 (CCND1) and Downregulation of Cyclin-Dependent Inhibitor Kinase 1A (CDKN1A) in Breast Cancer Tissue and Cell Lines. Medical science monitor : international medical journal of experimental and clinical research25, 4207-4216, doi:10.12659/msm.914742 (2019).
11 Li, Z. et al. USP9X controls translation efficiency via deubiquitination of eukaryotic translation initiation factor 4A1. Nucleic acids research46, 823-839, doi:10.1093/nar/gkx1226 (2018).
12 Paemka, L. et al. Seizures are regulated by ubiquitin-specific peptidase 9 X-linked (USP9X), a de-ubiquitinase. PLoS genetics11, e1005022, doi:10.1371/journal.pgen.1005022 (2015).
13 Habata, S. et al. BAG3-mediated Mcl-1 stabilization contributes to drug resistance via interaction with USP9X in ovarian cancer. International journal of oncology49, 402-410, doi:10.3892/ijo.2016.3494 (2016).
14 Johnson, B. V. et al. Partial Loss of USP9X Function Leads to a Male Neurodevelopmental and Behavioral Disorder Converging on Transforming Growth Factor β Signaling. Biological psychiatry87, 100-112, doi:10.1016/j.biopsych.2019.05.028 (2020).
15 Spinella, J. F. et al. Genomic characterization of pediatric T-cell acute lymphoblastic leukemia reveals novel recurrent driver mutations. Oncotarget7, 65485-65503, doi:10.18632/oncotarget.11796 (2016).
16 Zhao, Y. et al. Noncanonical regulation of alkylation damage resistance by the OTUD4 deubiquitinase. The EMBO journal34, 1687-1703, doi:10.15252/embj.201490497 (2015).
17 Kim, S. et al. WP1130 Enhances TRAIL-Induced Apoptosis through USP9X-Dependent miR-708-Mediated Downregulation of c-FLIP. Cancers11, doi:10.3390/cancers11030344 (2019).
18 Kloosterman, W. P. et al. A Systematic Analysis of Oncogenic Gene Fusions in Primary Colon Cancer. Cancer research77, 3814-3822, doi:10.1158/0008-5472.Can-16-3563 (2017).
19 Peng, J. et al. USP9X expression correlates with tumor progression and poor prognosis in esophageal squamous cell carcinoma. Diagnostic pathology8, 177, doi:10.1186/1746-1596-8-177 (2013).
20 Jaakkola, P. M. & Rantanen, K. The regulation, localization, and functions of oxygen-sensing prolyl hydroxylase PHD3. Biological chemistry394, 449-457, doi:10.1515/hsz-2012-0330 (2013).
21 Xia, Y. J. et al. PHD3 affects gastric cancer progression by negatively regulating HIF1A. Molecular medicine reports16, 6882-6889, doi:10.3892/mmr.2017.7455 (2017).
22 Chu, H. X. & Jones, N. M. Changes in Hypoxia-Inducible Factor-1 (HIF-1) and Regulatory Prolyl Hydroxylase (PHD) Enzymes Following Hypoxic-Ischemic Injury in the Neonatal Rat. Neurochemical research41, 515-522, doi:10.1007/s11064-015-1641-y (2016).
23 Luo, W. et al. Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1. Cell145, 732-744, doi:10.1016/j.cell.2011.03.054 (2011).
24 Schlisio, S. et al. The kinesin KIF1Bbeta acts downstream from EglN3 to induce apoptosis and is a potential 1p36 tumor suppressor. Genes & development22, 884-893, doi:10.1101/gad.1648608 (2008).
25 Frank, D. et al. MicroRNA-20a inhibits stress-induced cardiomyocyte apoptosis involving its novel target Egln3/PHD3. Journal of molecular and cellular cardiology52, 711-717, doi:10.1016/j.yjmcc.2011.12.001 (2012).
26 Hatzimichael, E. et al. The prolyl-hydroxylase EGLN3 and not EGLN1 is inactivated by methylation in plasma cell neoplasia. European journal of haematology84, 47-51, doi:10.1111/j.1600-0609.2009.01344.x (2010).
27 Lee, S. et al. Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: developmental culling and cancer. Cancer cell8, 155-167, doi:10.1016/j.ccr.2005.06.015 (2005).
28 Li, S. et al. EglN3 hydroxylase stabilizes BIM-EL linking VHL type 2C mutations to pheochromocytoma pathogenesis and chemotherapy resistance. Proceedings of the National Academy of Sciences of the United States of America116, 16997-17006, doi:10.1073/pnas.1900748116 (2019).
29 Walmsley, S. R. et al. Prolyl hydroxylase 3 (PHD3) is essential for hypoxic regulation of neutrophilic inflammation in humans and mice. The Journal of clinical investigation121, 1053-1063, doi:10.1172/jci43273 (2011).
30 Wang, J. et al. Comparison of the time courses of selective gene expression and dopaminergic depletion induced by MPP+ in MN9D cells. Neurochemistry international52, 1037-1043, doi:10.1016/j.neuint.2007.10.017 (2008).
31 Högel, H., Rantanen, K., Jokilehto, T., Grenman, R. & Jaakkola, P. M. Prolyl hydroxylase PHD3 enhances the hypoxic survival and G1 to S transition of carcinoma cells. PloS one6, e27112, doi:10.1371/journal.pone.0027112 (2011).
32 Wang, Y. et al. MicroRNA-1205, encoded on chromosome 8q24, targets EGLN3 to induce cell growth and contributes to risk of castration-resistant prostate cancer. Oncogene38, 4820-4834, doi:10.1038/s41388-019-0760-3 (2019).
33 Wang, Z. C. et al. Genetic polymorphism of the kinesin-like protein KIF1B gene and the risk of hepatocellular carcinoma. PloS one8, e62571, doi:10.1371/journal.pone.0062571 (2013).
34 Yang, S. Z. et al. Downregulation of KIF1B mRNA in hepatocellular carcinoma tissues correlates with poor prognosis. World journal of gastroenterology21, 8418-8424, doi:10.3748/wjg.v21.i27.8418 (2015).
35 Shi, T. Y. et al. Polymorphisms in the kinesin-like factor 1 B gene and risk of epithelial ovarian cancer in Eastern Chinese women. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine36, 6919-6927, doi:10.1007/s13277-015-3394-2 (2015).
36 Byrling, J. et al. Mass spectrometry-based analysis of formalin-fixed, paraffin-embedded distal cholangiocarcinoma identifies stromal thrombospondin-2 as a potential prognostic marker. Journal of translational medicine18, 343, doi:10.1186/s12967-020-02498-3 (2020).
37 Bagante, F. et al. Intrahepatic cholangiocarcinoma tumor burden: A classification and regression tree model to define prognostic groups after resection. Surgery166, 983-990, doi:10.1016/j.surg.2019.06.005 (2019).
38 Ebata, T. et al. Surgical resection for Bismuth type IV perihilar cholangiocarcinoma. The British journal of surgery105, 829-838, doi:10.1002/bjs.10556 (2018).
39 Blechacz, B. Cholangiocarcinoma: Current Knowledge and New Developments. Gut and liver11, 13-26, doi:10.5009/gnl15568 (2017).
40 Rahnemai-Azar, A. A., Weisbrod, A., Dillhoff, M., Schmidt, C. & Pawlik, T. M. Intrahepatic cholangiocarcinoma: Molecular markers for diagnosis and prognosis. Surgical oncology26, 125-137, doi:10.1016/j.suronc.2016.12.009 (2017).
41 Zheng, S. et al. Liver fluke infection and cholangiocarcinoma: a review. Parasitology research116, 11-19, doi:10.1007/s00436-016-5276-y (2017).
42 Doherty, B., Nambudiri, V. E. & Palmer, W. C. Update on the Diagnosis and Treatment of Cholangiocarcinoma. Current gastroenterology reports19, 2, doi:10.1007/s11894-017-0542-4 (2017).
43 Rizvi, S. & Gores, G. J. Pathogenesis, diagnosis, and management of cholangiocarcinoma. Gastroenterology145, 1215-1229, doi:10.1053/j.gastro.2013.10.013 (2013).
44 Shaib, Y. & El-Serag, H. B. The epidemiology of cholangiocarcinoma. Seminars in liver disease24, 115-125, doi:10.1055/s-2004-828889 (2004).
45 Fabris, L. et al. The tumour microenvironment and immune milieu of cholangiocarcinoma. Liver international : official journal of the International Association for the Study of the Liver39 Suppl 1, 63-78, doi:10.1111/liv.14098 (2019).
46 Lübbert, C. & Schneitler, S. Parasitic and infectious diseases of the biliary tract in migrants and international travelers. Expert review of gastroenterology & hepatology10, 1211-1225, doi:10.1080/17474124.2016.1240614 (2016).
47 Labib, P. L., Goodchild, G. & Pereira, S. P. Molecular Pathogenesis of Cholangiocarcinoma. BMC cancer19, 185, doi:10.1186/s12885-019-5391-0 (2019).
48 Hill, M. A. et al. Kras and Tp53 Mutations Cause Cholangiocyte- and Hepatocyte-Derived Cholangiocarcinoma. Cancer research78, 4445-4451, doi:10.1158/0008-5472.Can-17-1123 (2018).
49 Mahipal, A., Tella, S. H., Kommalapati, A., Anaya, D. & Kim, R. FGFR2 genomic aberrations: Achilles heel in the management of advanced cholangiocarcinoma. Cancer treatment reviews78, 1-7, doi:10.1016/j.ctrv.2019.06.003 (2019).
50 Liu, Q. et al. Broad and diverse mechanisms used by deubiquitinase family members in regulating the type I interferon signaling pathway during antiviral responses. Science advances4, eaar2824, doi:10.1126/sciadv.aar2824 (2018).
51 Mapa, C. E., Arsenault, H. E., Conti, M. M., Poti, K. E. & Benanti, J. A. A balance of deubiquitinating enzymes controls cell cycle entry. Molecular biology of the cell29, 2821-2834, doi:10.1091/mbc.E18-07-0425 (2018).
52 Pruneda, J. N. & Komander, D. Evaluating enzyme activities and structures of DUBs. Methods in enzymology618, 321-341, doi:10.1016/bs.mie.2019.01.001 (2019).
53 Leznicki, P. & Kulathu, Y. Mechanisms of regulation and diversification of deubiquitylating enzyme function. Journal of cell science130, 1997-2006, doi:10.1242/jcs.201855 (2017).
54 Chen, X. et al. Targeting USP9x/SOX2 axis contributes to the anti-osteosarcoma effect of neogambogic acid. Cancer letters469, 277-286, doi:10.1016/j.canlet.2019.10.015 (2020).
55 Wang, S. et al. Ablation of the oncogenic transcription factor ERG by deubiquitinase inhibition in prostate cancer. Proceedings of the National Academy of Sciences of the United States of America111, 4251-4256, doi:10.1073/pnas.1322198111 (2014).
56 Zhu, C. et al. Deubiquitylase USP9X suppresses tumorigenesis by stabilizing large tumor suppressor kinase 2 (LATS2) in the Hippo pathway. The Journal of biological chemistry293, 1178-1191, doi:10.1074/jbc.RA117.000392 (2018).
57 Khan, O. M. et al. The deubiquitinase USP9X regulates FBW7 stability and suppresses colorectal cancer. The Journal of clinical investigation128, 1326-1337, doi:10.1172/jci97325 (2018).
58 Lu, Q., Zhang, F. L., Lu, D. Y., Shao, Z. M. & Li, D. Q. USP9X stabilizes BRCA1 and confers resistance to DNA-damaging agents in human cancer cells. Cancer medicine8, 6730-6740, doi:10.1002/cam4.2528 (2019).
59 Oosterkamp, H. M. et al. USP9X downregulation renders breast cancer cells resistant to tamoxifen. Cancer research74, 3810-3820, doi:10.1158/0008-5472.Can-13-1960 (2014).
60 Taylor, M. S. Characterization and comparative analysis of the EGLN gene family. Gene275, 125-132, doi:10.1016/s0378-1119(01)00633-3 (2001).
61 Chang, E. et al. 18F-FAZA PET imaging response tracks the reoxygenation of tumors in mice upon treatment with the mitochondrial complex I inhibitor BAY 87-2243. Clinical cancer research : an official journal of the American Association for Cancer Research21, 335-346, doi:10.1158/1078-0432.Ccr-14-0217 (2015).
62 Dopeso, H. et al. PHD3 Controls Lung Cancer Metastasis and Resistance to EGFR Inhibitors through TGFα. Cancer research78, 1805-1819, doi:10.1158/0008-5472.Can-17-1346 (2018).
63 Garvalov, B. K. et al. PHD3 regulates EGFR internalization and signalling in tumours. Nature communications5, 5577, doi:10.1038/ncomms6577 (2014).
64 Högel, H., Miikkulainen, P., Bino, L. & Jaakkola, P. M. Hypoxia inducible prolyl hydroxylase PHD3 maintains carcinoma cell growth by decreasing the stability of p27. Molecular cancer14, 143, doi:10.1186/s12943-015-0410-5 (2015).