Publikationen Nicola Catone

  • Roverato ND, Sailer C, Catone N, Aichem A, Stengel F, Groettrup M. 2021. Parkin is an E3 ligase for the ubiquitin-like modifier FAT10, which inhibits Parkin activation and mitophagy. Cell Rep Mar 16;34(11):108857. doi: 10.1016/j.celrep.2021.108857.
  • Boehm AN, Bialas J, Catone N, Sacristan-Reviriego A, van der Spuy J, Groettrup M, Aichem A. 2020. The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation. JBC Aug 14;jbc.RA120.013873. doi: 10.1074/jbc.RA120.013873. Online ahead of print.
  • Aichem A, Sailer C, Ryu S, Catone N, Stankovic-Valentin N, Schmidtke G, Melchior F, Stengel F, Groettrup M. 2019. The ubiquitin-like modifier FAT10 interferes with SUMO activation. Nat Commun Oct 1;10(1):4452. doi: 10.1038/s41467-019-12430-z.
  • Bialas J, Boehm AN, Catone N, Aichem A, Groettrup M. 2019. The ubiquitin-like modifier FAT10 stimulates the activity of the deubiquitylating enzyme OTUB1. J Biol Chem Feb 4. pii: jbc.RA118.005406. doi: 10.1074/jbc.RA118.005406. [Epub ahead of print].
  • Aichem A, Boehm AN, Catone N, Schmidtke G, Groettrup M. 2019. Analysis of modification and proteolytic targeting by the ubiquitin-like modifier FAT10. Methods Enzymol 618:229-256. doi: 10.1016/bs.mie.2018.12.040. Epub 2019 Feb 83.
  • Aichem A, Anders S, Catone N, Rößler P, Stotz S, Berg A, Schwab R, Scheuermann S, Bialas J, Schütz-Stoffregen MC, Schmidtke G, Peter C, Groettrup M, Wiesner S. 2018. The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation. Nat Commun Aug 20;9(1):3321. doi: 10.1038/s41467-018-05776-3.
  • Aichem A, Catone N, Groettrup M. 2014. Investigations into the auto-FAT10ylation of the bispecific E2 conjugating enzyme USE1.FEBS J doi: 10.1111/febs.12745. [Epub ahead of print].
  • Aichem A, Kalveram B, Spinnenhirn V, Kluge K, Catone N, Johansen T, Groettrup M. 2012. The proteomic analysis of FAT10 substrates identifies p62/SQSTM1 as a substrate of FAT10ylation.J Cell Sci 125(19):4576-4585.