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  1. Article

    Open Access

    The ubiquitin-like modifier FAT10 interferes with SUMO activation

    The covalent attachment of the cytokine-inducible ubiquitin-like modifier HLA-F adjacent transcript 10 (FAT10) to hundreds of substrate proteins leads to their rapid degradation by the 26 S proteasome independ...

    Annette Aichem, Carolin Sailer, Stella Ryu, Nicola Catone in Nature Communications (2019)

  2. Article

    Open Access

    Author Correction: The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

    The original version of the Supplementary Information associated with this Article inadvertently omitted Supplementary Table 3. The HTML version of the Article has been updated to include a corrected version o...

    Annette Aichem, Samira Anders, Nicola Catone, Philip Rößler in Nature Communications (2018)

  3. Article

    Open Access

    The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

    FAT10 is a ubiquitin-like modifier that directly targets proteins for proteasomal degradation. Here, we report the high-resolution structures of the two individual ubiquitin-like domains (UBD) of FAT10 that ar...

    Annette Aichem, Samira Anders, Nicola Catone, Philip Rößler in Nature Communications (2018)

  4. No Access

    Article

    FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis

    FAT10 is the only ubiquitin-like modifier that can target proteins for degradation by the proteasome in a ubiquitin-independent manner. The degradation of FAT10-linked proteins by the proteasome is strongly ac...

    Neha Rani, Annette Aichem, Gunter Schmidtke, Stefan G. Kreft in Nature Communications (2012)

  5. No Access

    Article

    USE1 is a bispecific conjugating enzyme for ubiquitin and FAT10, which FAT10ylates itself in cis

    The ubiquitin-like modifier FAT10 targets proteins for degradation by the proteasome and is activated by the E1 enzyme UBA6. In this study, we identify the UBA6-specific E2 enzyme (USE1) as an interaction part...

    Annette Aichem, Christiane Pelzer, Sebastian Lukasiak in Nature Communications (2010)

  6. No Access

    Protocol

    Identification of Homozygous Transgenic Mice by Genomic Real-Time PCR

    The 26S proteasome is the executing protease of the ubiquitin-dependent degradation system. It consists of one or two 19S regulatory sub-complexes and one 20S proteolytic sub-complex (1). The 20S proteasome is a ...

    Gunter Schmidtke, Marcus Groettrup in Molecular Beacons: Signalling Nucleic Acid… (2008)

  7. No Access

    Protocol

    Quantitative Analysis of Gene Expression Relative to 18S rRNA in Carcinoma Samples Using the LightCycler® Instrument and a SYBR GreenI-based Assay: Determining FAT10 mRNA Levels in Hepatocellular Carcinoma

    Due to the fact that mutations and up- or downregulation of genes can lead to the development of cancer, quantitative comparison of relative gene expression in healthy and cancerous tissue can gain valuable in...

    Sebastian Lukasiak, Kai Breuhahn in Molecular Beacons: Signalling Nucleic Acid… (2008)

  8. No Access

    Chapter

    Effects of the HIV-1 Protease Inhibitor Ritonavir on Proteasome Activity and Antigen Presentation

    Ritonavir is a potent inhibitor of the protease encoded by the human immunodeficiency virus (HIV)-1 and is clinically applied to suppress HIV-1 replication in AIDS patients. When following up clinical hints po...

    Marcus Groettrup, Rita de Giuli in Proteasome Inhibitors in Cancer Therapy (2004)

  9. No Access

    Article

    Structure and structure formation of the 20S proteasome

    Eukaryotic 20S proteasomes are complex oligomeric proteins. The maturation process of the 14 different α- and β-subunits has to occur in a highly coordinate manner. In addition β-subunits are synthesized as pr...

    Marion Schmidt, Gunter Schmidtke, Peter-M. Kloetzel in Molecular Biology Reports (1997)