Analysis of modification and proteolytic targeting by the ubiquitin-like modifier FAT10
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Elsevier
Reference30 articles.
1. The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation;Aichem;Nature Communications,2018
2. Investigations into the auto-FAT10ylation of the bispecific E2 conjugating enzyme UBA6-specific E2 enzyme 1;Aichem;The FEBS Journal,2014
3. Detection and analysis of FAT10 modification;Aichem;Methods in Molecular Biology,2012
4. The ubiquitin-like modifier FAT10 in cancer development;Aichem;The International Journal of Biochemistry & Cell Biology,2016
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1. FAT10 inhibits TRIM21 to down-regulate antiviral type-I interferon secretion;Life Science Alliance;2024-07-08
2. FAT10 is phosphorylated by IKKβ to inhibit the antiviral type-I interferon response;Life Science Alliance;2023-11-08
3. Tumor necrosis factor mediates USE1-independent FAT10ylation under inflammatory conditions;Life Science Alliance;2023-08-21
4. The ubiquitin-like modifier FAT10 covalently modifies HUWE1 and strengthens the interaction of AMBRA1 and HUWE1;PLOS ONE;2023-08-14
5. FAT10 and NUB1L cooperate to activate the 26S proteasome;Life Science Alliance;2023-05-15
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