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ProteomicsIdentification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry
The 26S proteasome is the endpoint of the ubiquitin-proteasome system, an essential pathway for maintaining cellular homeostasis through targeted degradation of misfolded, damaged, and obsolete proteins. Substrates labeled with ubiquitin are directed to the 26S proteasome by binding to one or more u...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2026-06-08 | PXD075114 | Pride
26s proteasome Ubiquitin Ubiquitin receptors 
ProteomicsCross-link MS analysis of human 26S proteasome in complex with RPN13:UCHL5 (without substrate).
This project investigates how the human 26S proteasome recognizes and processes proteins tagged with K11/K48-branched ubiquitin chains, which signal for rapid degradation during cell cycle progression and proteotoxic stress. Using cryo-electron microscopy (cryo-EM), the study uncovers a novel K11-li...
ORGANISM(S): Homo sapiens (Human) 
2025-09-22 | PXD064931 | Pride
Rpn13 Proteasome Uchl5 26s 
ProteomicsEndogenous anti-tumorigenic nitro-fatty acids are a novel type of direct and potent inhibitor of the 26S proteasome
Nitro-fatty acids (NFAs) are endogenous lipid mediators causing a broad spectrum of anti-inflammatory effects by covalent modification of key proteins within inflammatory signaling pathways. Their potential as anti-tumorigenic therapeutics has recently been demonstrated in animal models of solid tum...
ORGANISM(S): Homo sapiens (Human) 
2024-03-26 | PXD041458 | Pride
Nitroalkylation Caco2 26s proteasome Lc-ms/ms 
ProteomicsMS analsysis of phosphoproteins separated by phos-tag diagonal electrophoresis of Human 26S proteasome
Phosphorylation status of human 26S proteasome subunits was analyzed by phos-tag diagonal electrophoresis and GeLC-MS analysis.
ORGANISM(S): Homo Sapiens (human) 
2021-08-03 | PXD020705 | JPOST Repository
ProteomicsMS analsysis of phosphoproteins separated by phos-tag diagonal electrophoresis of yeast 26S proteasome
Phosphorylation status of yeast 26S proteasome subunits was analyzed by phos-tag diagonal electrophoresis and GeLC-MS analysis.
ORGANISM(S): Homo Sapiens (human) 
2021-08-03 | PXD020706 | JPOST Repository
ProteomicsCross-link MS analysis of human 26S proteasome in complex with RPN13:UCHL5 (with substrate).
This project investigates how the human 26S proteasome recognizes and processes proteins tagged with K11/K48-branched ubiquitin chains, which signal for rapid degradation during cell cycle progression and proteotoxic stress. Using cryo-electron microscopy (cryo-EM), the study uncovers a novel K11-li...
ORGANISM(S): Homo sapiens (Human) 
2025-09-22 | PXD064932 | Pride
K11/k48 ubiquitin Rpn13 Proteasome Uchl5 26s Branched ubiquitin 
ProteomicsReversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function
The fundamental importance of the 26S proteasome in health and disease suggests that its function must be finely controlled, and yet our knowledge about proteasome regulation remains limited. Posttranslational modifications, especially phosphorylation, of proteasome subunits have been shown to impac...
ORGANISM(S): Homo Sapiens 
2019-12-08 | PXD016643 |
TranscriptomicsGLA and profiling of proteasome, Spt23 and Mga2
The proteasome can regulate transcription through proteolytic processing of transcription factors and via gene locus binding, but few targets of proteasomal regulation have been identified. Using genome-wide location analysis and transcriptional profiling in Saccharomyces cerevisiae, we have establ...
ORGANISM(S): Saccharomyces cerevisiae 
2006-02-28 | E-GEOD-4272 | biostudies-arrayexpress
TranscriptomicsSpt6 Levels are Modulated by PAAF1 and 26S Proteasome to Regulate the HIV-1 LTR and a Subset of Cellular Genes involved in Cancer.
Effect of PAAF1 and Spt6 knock-down on gene expression. Total RNAs were extracted from HeLa-LTR-Luc cells in which PAAF1 or Spt6 had been knock down by a specific siRNA or HeLa-LTR-Luc cells that had been transfected with a control siRNA (“si Neg”). Differentially expressed genes in PAAF1 knock-down...
ORGANISM(S): Homo sapiens 
2012-05-28 | E-GEOD-32033 | biostudies-arrayexpress
ProteomicsDissecting the molecular effects of cigarette smoke on proteasome function
Proteasome dysfunction is emerging as a novel pathomechanism for the development of chronic obstructive pulmonary disease (COPD), a major leading cause of death in the world. Cigarette smoke is one of the main risk factors for COPD and has been shown to impair proteasome function in vitro and in viv...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2019-01-08 | PXD007148 | Pride
Cigarette smoke Proteasome 
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