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Journal of the American Chemical Society|May 20, 2026
Intermolecular β-sheet Formation Guides the Interaction between Ubiquitin-like Modifier FAT10 and Adapter Protein NUB1LCharlotte Weiss, Sarah Overall, Nicola Catone, et al.Life Science Alliance|May 15, 2023
FAT10 and NUB1L cooperate to activate the 26S proteasomeFlorian Brockmann, Nicola Catone, Christine Wünsch, et al.Journal of Cell Science|July 17, 2012
The proteomic analysis of endogenous FAT10 substrates identifies p62/SQSTM1 as a substrate of FAT10ylationAnnette Aichem, Birte Kalveram, Valentina Spinnenhirn, et al.Nature Communications|October 27, 2010
USE1 is a bispecific conjugating enzyme for ubiquitin and FAT10, which FAT10ylates itself in cisAnnette Aichem, Christiane Pelzer, Sebastian Lukasiak, et al.Nature Communications|October 3, 2019
The ubiquitin-like modifier FAT10 interferes with SUMO activationAnnette Aichem, Carolin Sailer, Stella Ryu, et al.The Journal of Biological Chemistry|August 21, 2020
The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradationAnnika N Boehm, Johanna Bialas, Nicola Catone, et al.Life Science Alliance|November 8, 2023
FAT10 is phosphorylated by IKKβ to inhibit the antiviral type-I interferon responseKritika Saxena, Nicola Domenico Roverato, Melody Reithmann, et al.Human Molecular Genetics|October 4, 2017
The integrity and organization of the human AIPL1 functional domains is critical for its role as a HSP90-dependent co-chaperone for rod PDE6Almudena Sacristan-Reviriego, James Bellingham, Chrisostomos Prodromou, et al.Nature Communications|August 22, 2018
The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradationAnnette Aichem, Samira Anders, Nicola Catone, et al.Nature Communications|November 4, 2018
Author Correction: The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradationAnnette Aichem, Samira Anders, Nicola Catone, et al.Pageof 4