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ProteomicsA lysine residue at the C-terminus of MHC class I ligands correlates with low C-terminal proteasomal cleavage probability
The majority of peptides presented by MHC class I results from proteasomal protein turnover. The specialized immunoproteasome, which is induced during inflammation, plays a major role in antigenic peptide generation. However, other cellular proteases can, either alone or together with the proteasome...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD044235 | Pride
Immunopeptidomics  proteasome-independent  non-canonical mhc class i ligands  hla-a*03:01  hla-a*11:01  hla-a*30:01  proteasomal cleavage probability  peptide origin  peptide processing 
UnknownA Lysine Residue at the C-Terminus of MHC Class I Ligands Correlates with Low C-Terminal Proteasomal Cleavage Probability.
Not available
S-EPMC10527444 | biostudies-literature
ProteomicsCalpain activity is regulated by a KCTD7–cullin 3 complex via non-degradative ubiquitination
Calpains are a class of non-lysosomal cysteine proteases that exert their regulatory functions via limited proteolysis of their substrates. Similar to the lysosomal and proteasomal systems, calpain dysregulation is implicated in the pathogenesis of neurodegenerative disease and cancer. Despite inten...
ORGANISM(S): Homo sapiens (Human) 
2023-05-10 | PXD038842 | Pride
Human Pasef Calpain 
ProteomicsUSP9X promotes the degradation of trapped translation factors on collided ribosomes
Various ribosome-associated quality control pathways safeguard translation fidelity by detecting and resolving aberrant translation events. Recently, a pathway that senses stalled ribosomes with an occluded A-site has been described. The small molecules NVS1.1 and Ternatin-4 induce ribosome stalling...
ORGANISM(S): Homo sapiens (Human) 
2026-09-22 | PXD079916 | Pride
Usp9x  rqc  ribosome collisions  erf1  proteasomal degradation  eef1a1  ubiquitination  nvs1.1  ternatin-4 
UnknownMulti-epitope vaccine design of African swine fever virus considering T cell and B cell immunogenicity.
Not available
S-EPMC11365882 | biostudies-literature
ProteomicsCBL ubiquitin ligase targets translation as a degrader E3
Proteolysis Targeting Chimeras (PROTACs) are heterobifunctional molecules that recruits an ubiquitin ligase (E3) and a neo-substrate into a ternary complex, enabling selective protein degradation. Despite the presence of over 600 E3s, only a handful are utilized in PROTAC application, potentially l...
ORGANISM(S): Homo sapiens (Human) Escherichia coli Bacteria 
2026-01-19 | PXD063494 | Pride
Cbl Protac Targeted protein degradation Ubiquitin Mrna Translation Eif4e 
ProteomicsEndogenous, in vivo, and site-specific characterization of the SUMO architecture across species and organs
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications that play crucial roles in most cellular processes. While methods exist to study exogenous SUMOylation, large-scale characterization of endogenous SUMO has remained technically daunting. Here, we describe a proteomics approa...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2018-06-26 | PXD008003 | Pride
Tissue Sumo In vivo Endogenous Human Mouse Cells 
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