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Quantification of ubiquitin chain linkage of uS10. Quantification of ubiquitin chain linkage of uS10in UbiR54A mutant strain.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2025-09-18 | PXD052346 | Pride
This experiment aimed to characterise ubiquitin chain linkage preferences generated and autoubiquitination sistes during ZNFX1 E3 reactions using diGly remnant mass spectrometry. GlyGly-modified lysine residues were identified as a qualitative proxy for ubiquitin linkage types. Spectral counts of ra...
ORGANISM(S): Homo sapiens (Human) 
2026-05-22 | PXD073484 | Pride
Mass spectrometry-based proteomics has become an integral approach for characterising ubiquitin chain-linkage compositions and architectures. In this study, we optimised sample preparation and chromatographic separation of Ubiquitin peptides for Absolute Quantification by Parallel Reaction Monitorin...
ORGANISM(S): Mus musculus (Mouse) 
2020-09-28 | PXD017754 | Pride
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002201 | Pride
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002202 | Pride
Linkage-specific ubiquitin (Ub) chains dictate the functional outcome of many critical Ub-dependent signaling processes. However, the functions and targets of several poly-Ub topologies remain poorly understood due to a lack of tools for their specific detection and manipulation. To remedy this know...
ORGANISM(S): Homo sapiens (Human) 
2025-09-18 | PXD056493 | Pride
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002197 | Pride
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002200 | Pride
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002198 | Pride
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002199 | Pride
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