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In Saccharomyces cerevisiae histone H2B is ubiquitylated at lysine 123. The SAGA complex component, Ubp8, is one of two proteases that remove this ubiquitin moiety. We analyzed gene expression in a strain containing a variant of histone H2B with lysine 123 converted to arginine to address the mechan...
ORGANISM(S): Saccharomyces cerevisiae 
A combinatorial ubiquitin code degrades substrates protected by deubiquitylation
To survive under adverse conditions, plants form stress granules (SGs) to temporally store mRNA and halt translation as a primary response. Dysregulation in SG disassembly can have detrimental effects on plant survival after stress release, yet the underlying mechanism remains poorly understood in p...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-01-24 | PXD054299 | Pride
To survive under adverse conditions, plants form stress granules (SGs) to temporally store mRNA and halt translation as a primary response. Dysregulation in SG disassembly can have detrimental effects on plant survival after stress release, yet the underlying mechanism remains poorly understood. Usi...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-01-24 | PXD058194 | Pride
Reversibility of protein ubiquitylation play essential roles in cellular protein homeostasis. How substrates stabilized by deubiquitylation are directed for degradation remains largely elusive. Here, we show that the branched ubiquitin chains promote the degradation of the deubiquitylase (DUB) OTUD5...
ORGANISM(S): Homo sapiens 
2025-02-19 | GSE273273 | GEO
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