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A composition of proteasome complexes in WT yeast, and the changes these complexes undergo upon the deletion of Pre9 (Δα3) or of Sem1 (ΔSem1) based on whole-cell proteomic analysis and to activity-guided proteasome profiling of indicates that the amounts of proteasomal proteins and proteasome intera...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-02-15 | PXD045047 | Pride
A composition of proteasome complexes in WT yeast, and the changes these complexes undergo upon the deletion of Pre9 (Δα3) or of Sem1 (ΔSem1) based on whole-cell proteomic analysis and to activity-guided proteasome profiling of indicates that the amounts of proteasomal proteins and proteasome intera...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-02-15 | PXD045051 | Pride
This experiment compared the impact of protein extraction conditions on the identification and quantification of proteasome subunits in WT yeast. It involved comparing proteins extracted from identical WT yeast samples under two different conditions: native and denaturing (in the presence of SDS and...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-02-15 | PXD048380 | Pride
Proteins' N-termini contain information about their biochemical properties and functions, and they can undergo co- or post-translational modifications, as well as be processed by proteases. To expand the coverage of the N-terminome, we have developed LATE (LysN Amino Terminal Enrichment), a method t...
ORGANISM(S): Homo sapiens (Human) 
2023-06-27 | PXD040732 | Pride
Proteins' N-termini contain information about their biochemical properties and functions, and they can undergo co- or post-translational modifications, as well as be processed by proteases. To expand the coverage of the N-terminome, we have developed LATE (LysN Amino Terminal Enrichment), a method t...
ORGANISM(S): Homo sapiens (Human) 
2023-06-27 | PXD036648 | Pride
Proteins' N-termini contain information about their biochemical properties and functions, and they can undergo co- or post-translational modifications, as well as be processed by proteases. To expand the coverage of the N-terminome, we have developed LATE (LysN Amino Terminal Enrichment), a method t...
ORGANISM(S): Homo sapiens (Human) 
2023-06-27 | PXD036593 | Pride
Virophages are small dsDNA viruses dependent on a nucleocytoplasmic large-DNA virus infection of a cellular host for replication. Putative virophages infecting algal hosts are classified together with Polinton-like viruses, transposable elements widely found in algal genomes, yet the lack of isolate...
ORGANISM(S): Phaeocystis globosa virus virophage Phaeocystis globosa virus Phaeocystis globosa Phaeocystis globosa virus 14T 
2023-02-11 | PXD036892 | Pride
Dipeptidyl peptidase 9 (DPP9) is an amino peptidase with the unusual ability to cleave a peptide bond post-proline. Its function affects immunity, DNA-repair, cell signaling, memory and neonatal survival; its dysregulation is linked to cancer and immune-related disorders. While most studies focus on...
ORGANISM(S): Homo sapiens (Human) 
2026-08-31 | PXD067345 | Pride
A systematic and comparative study of the proteolysis products generated by purified human 26S and 20S proteasome following the in vitro cleavage of non-modified (naked), mono-ubiquitinated and poly-ubiquitinated cyclin B.
ORGANISM(S): Homo sapiens (Human) 
2021-11-02 | PXD018711 | Pride
Careful removal of unwanted proteins is necessary for cell survival. The primary constitutive intracellular protease is the 26S proteasome complex, very often found in equilibrium with its catalytic core particle – the 20S subcomplex. Protein degradation by the former is tightly regulated due to pri...
ORGANISM(S): Homo sapiens (Human) 
2021-11-02 | PXD018722 | Pride
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