REFERENCES
1. Komander D, Clague MJ, Urbé S. Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol. 2009;10:550-63.
2. Mofers A, Pellegrini P, Linder S, D’Arcy P. Proteasome-associated deubiquitinases and cancer. Cancer Metast Rev. 2017;36:635-53.
3. Harrigan JA, Jacq X, Martin NM, Jackson SP. Deubiquitylating enzymes and drug discovery: emerging opportunities. Nat Rev Drug Discov. 2018;17:57-78.
4. Schauer NJ, Magin RS, Liu X, Doherty LM, Buhrlage SJ. Advances in discovering deubiquitinating enzyme (DUB) inhibitors. J Med Chem. 2020;63:2731-50.
6. Liu B, Ruan J, Chen M, et al. Deubiquitinating enzymes (DUBs): decipher underlying basis of neurodegenerative diseases. Mol Psychiatry. 2022;27:259-68.
7. Pozhidaeva A, Bezsonova I. USP7: structure, substrate specificity, and inhibition. DNA Repair. 2019;76:30-9.
8. Li M, Brooks CL, Kon N, Gu W. A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol Cell. 2004;13:879-86.
9. Corno C, D’Arcy P, Bagnoli M, et al. The deubiquitinase USP8 regulates ovarian cancer cell response to cisplatin by suppressing apoptosis. Front Cell Dev Biol. 2022;10:1055067.
10. Colombo D, Gatti L, Sjöstrand L, et al. Caffeic acid phenethyl ester targets ubiquitin-specific protease 8 and synergizes with cisplatin in endometrioid ovarian carcinoma cells. Biochem Pharmacol. 2022;197:114900.
11. Beretta GL, Costantino M, Mirra L, Pettinari P, Perego P. Deubiquitinases in ovarian cancer: role in drug resistance and tumor aggressiveness. Int J Biol Sci. 2024;20:5208-22.
12. Konstantinopoulos PA, Matulonis UA. Clinical and translational advances in ovarian cancer therapy. Nat Cancer. 2023;4:1239-57.
13. Rottenberg S, Disler C, Perego P. The rediscovery of platinum-based cancer therapy. Nat Rev Cancer. 2021;21:37-50.
14. Gatti L, Cassinelli G, Zaffaroni N, Lanzi C, Perego P. New mechanisms for old drugs: Insights into DNA-unrelated effects of platinum compounds and drug resistance determinants. Drug Resist Updat. 2015;20:1-11.
15. Kane RC, Bross PF, Farrell AT, Pazdur R. Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy. Oncologist. 2003;8:508-13.
16. D’Arcy P, Linder S. Proteasome deubiquitinases as novel targets for cancer therapy. Int J Biochem Cell Biol. 2012;44:1729-38.
17. Zhang N, Zhang H, Yang X, et al. USP14 exhibits high expression levels in hepatocellular carcinoma and plays a crucial role in promoting the growth of liver cancer cells through the HK2/AKT/P62 axis. BMC Cancer. 2024;24:237.
18. Liu C, Zhou S, Tang W. USP14 promotes the cancer stem-like cell properties of OSCC via promoting SOX2 deubiquitination. Oral Dis. 2024;30:4255-65.
19. Zhang S, Zou S, Yin D, et al. USP14-regulated allostery of the human proteasome by time-resolved cryo-EM. Nature. 2022;605:567-74.
20. Kim HT, Goldberg AL. UBL domain of Usp14 and other proteins stimulates proteasome activities and protein degradation in cells. Proc Natl Acad Sci U S A. 2018;115:E11642-50.
21. D’Arcy P, Brnjic S, Olofsson MH, et al. Inhibition of proteasome deubiquitinating activity as a new cancer therapy. Nat Med. 2011;17:1636-40.
22. Wang X, D’Arcy P, Caulfield TR, et al. Synthesis and evaluation of derivatives of the proteasome deubiquitinase inhibitor b-AP15. Chem Biol Drug Des. 2015;86:1036-48.
23. Rowinsky EK, Paner A, Berdeja JG, et al. Phase 1 study of the protein deubiquitinase inhibitor VLX1570 in patients with relapsed and/or refractory multiple myeloma. Invest New Drugs. 2020;38:1448-53.
24. Perego P, Giarola M, Righetti SC, et al. Association between cisplatin resistance and mutation of p53 gene and reduced bax expression in ovarian carcinoma cell systems. Cancer Res. 1996;56:556-62.
25. Cossa G, Lanzi C, Cassinelli G, et al. Differential outcome of MEK1/2 inhibitor-platinum combinations in platinum-sensitive and -resistant ovarian carcinoma cells. Cancer Lett. 2014;347:212-24.
26. Lee BH, Finley D, King RW. A high-throughput screening method for identification of inhibitors of the deubiquitinating enzyme USP14. Curr Protoc Chem Biol. 2012;4:311-30.
27. Friesner RA, Banks JL, Murphy RB, et al. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem. 2004;47:1739-49.
28. Corso G, Stärk H, Jing B, Barzilay R, Jaakkola T. DiffDock: diffusion steps, twists, and turns for molecular docking. arXiv. 2023;arXiv:2210.01776. Available from https://doi.org/10.48550/arXiv.2210.01776 [accessed 18 September 2025].
29. Wang F, Ning S, Yu B, Wang Y. USP14: structure, function, and target inhibition. Front Pharmacol. 2021;12:801328.
30. Wang Y, Jiang Y, Ding S, et al. Small molecule inhibitors reveal allosteric regulation of USP14 via steric blockade. Cell Res. 2018;28:1186-94.
31. Abraham MJ, Murtola T, Schulz R, et al. GROMACS: high performance molecular simulations through multilevel parallelism from laptops to supercomputers. SoftwareX. 2015;1-2:19-25.
32. Bouysset C, Fiorucci S. ProLIF: a library to encode molecular interactions as fingerprints. J Cheminform. 2021;13:72.
33. Tian C, Kasavajhala K, Belfon KAA, et al. ff19SB: amino-acid-specific protein backbone parameters trained against quantum mechanics energy surfaces in solution. J Chem Theory Comput. 2020;16:528-52.
34. der Spoel D, van Maaren PJ. The origin of layer structure artifacts in simulations of liquid water. J Chem Theory Comput. 2006;2:1-11.
35. Frisch MJ, Trucks GW, Schlegel HB, et al. Gaussian-09. Gaussian, Inc.: 340 Quinnipiac St Bldg 40, Wallingford, CT 06492, USA. Available from https://gaussian.com/g09citation [accessed 18 September 2025].
36. Wang J, Wang W, Kollman PA, Case DA. Automatic atom type and bond type perception in molecular mechanical calculations. J Mol Graph Model. 2006;25:247-60.
37. Wang J, Wolf RM, Caldwell JW, Kollman PA, Case DA. Development and testing of a general amber force field. J Comput Chem. 2004;25:1157-74.
38. He X, Man VH, Yang W, Lee TS, Wang J. A fast and high-quality charge model for the next generation general AMBER force field. J Chem Phys. 2020;153:114502.
39. Jo S, Kim T, Iyer VG, Im W. CHARMM-GUI: a web-based graphical user interface for CHARMM. J Comput Chem. 2008;29:1859-65.
40. Marino D, Achsel T, Lacoux C, Falconi M, Bagni C. Molecular dynamics simulations show how the FMRP Ile304Asn mutation destabilizes the KH2 domain structure and affects its function. J Biomol Struct Dyn. 2014;32:337-50.
42. Meng EC, Goddard TD, Pettersen EF, et al. UCSF ChimeraX: tools for structure building and analysis. Protein Sci. 2023;32:e4792.
43. Corno C, Gatti L, Arrighetti N, et al. Axl molecular targeting counteracts aggressiveness but not platinum-resistance of ovarian carcinoma cells. Biochem Pharmacol. 2017;136:40-50.
44. Lee BH, Lee MJ, Park S, et al. Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature. 2010;467:179-84.
45. Di Fruscia P, Carbone A, Bottegoni G, et al. Discovery and SAR evolution of pyrazole azabicyclo[3.2.1]octane sulfonamides as a novel class of non-covalent N-acylethanolamine-hydrolyzing acid amidase (NAAA) inhibitors for oral administration. J Med Chem. 2021;64:13327-55.
46. Wang Y, Wang J, Zhong J, et al. Ubiquitin-specific protease 14 (USP14) regulates cellular proliferation and apoptosis in epithelial ovarian cancer. Med Oncol. 2015;32:379.
47. Shen J, Hong L, Chen L. Ubiquitin-specific protease 14 regulates ovarian cancer cisplatin-resistance by stabilizing BCL6 oncoprotein. Biochem Biophys Res Commun. 2020;524:683-8.
48. Boselli M, Lee BH, Robert J, et al. An inhibitor of the proteasomal deubiquitinating enzyme USP14 induces tau elimination in cultured neurons. J Biol Chem. 2017;292:19209-25.
