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ProteomicsProteome and ubiquitinome changes in Huntington’s disease
Huntington’s disease is caused by a polyglutamine repeat expansion at the N-terminus of the huntingtin protein which affects the function and folding of the protein, and results in intracellular protein aggregates. Here, we examined whether this mutation leads to altered ubiquitination of huntingtin...
ORGANISM(S): Mus musculus (Mouse) 
2019-06-05 | PXD010161 | Pride
Ubiquitination Digly Ptms Brain Lfq Mouse Huntington 
ProteomicsProteome-wide ubiquitinome profiling reveals substrate-specific dynamics within the USP7 network
USP7 is a deubiquitylating enzyme, a hub of a multi-nodal network, that is involved in tumor suppression, neuro)development, chromatin regulation and the DNA damage response. How USP7 regulates these diverse pathways is still unclear. Here, we used data-independent acquisition and label free quantit...
ORGANISM(S): Homo sapiens (Human) 
2026-09-07 | PXD071773 | Pride
Neurodevelopment Hao-fountain syndrome Ubiquitin Polycomb Usp7 
ProteomicsDiscovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53
Ubiquitin-specific proteases (USPs) are the largest class of human deubiquitinases (DUBs) and comprise its phylogenetically most distant members USP53 and USP54, which are annotated as catalytically inactive pseudo-enzymes. Conspicuously, mutations in the USP domain of USP53 cause progressive famili...
ORGANISM(S): Homo sapiens (Human) 
2024-11-11 | PXD054748 | Pride
Ubiquitin chain length Dubs Ubiquitin signaling K63 linkage X-ray crystallography Cholestasis Deubiquitinating enzymes Protease mechanism Ubiquitin probes Ubiquitin Polyubiquitin specificity Usp54 Usp53 
ProteomicsImprovement of ubiquitination site detection by Orbitrap mass spectrometry.
We describe a modified workflow to enrich for and detect diGly peptides originating from ubiquitinated proteins using immunopurification. Using a combination of several relatively simple modifications in the sample preparation and mass spectrometric detection protocols, we now routinely detect over ...
ORGANISM(S): Homo sapiens (Human) 
2017-11-14 | PXD007101 | Pride
Ubiquitinome Silac Hela Ubiquitination U2os Ubiquitin Orbitrap lumos Digly peptides Mouse brain tissue 
UnknownActivin A suppresses osteoblast mineralization capacity by altering extracellular matrix (ECM) composition and impairing matrix vesicle (MV) production.
Not available
S-EPMC3790298 | biostudies-literature
UnknownCombgap contributes to recruitment of Polycomb group proteins in Drosophila.
Not available
S-EPMC4833261 | biostudies-literature
UnknownGlobal Proteome and Ubiquitinome Changes in the Soluble and Insoluble Fractions of Q175 Huntington Mice Brains.
Not available
S-EPMC6731087 | biostudies-literature
TranscriptomicsdKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing.
Transcription regulation involves enzyme-mediated changes in chromatin structure. Here, we describe a novel mode of histone crosstalk during gene silencing, in which histone H2A monoubiquitylation is coupled to the removal of histone H3 Lys 36 dimethylation (H3K36me2). This pathway was uncovered thr...
ORGANISM(S): Drosophila melanogaster 
2011-12-13 | E-GEOD-34390 | biostudies-arrayexpress
ProteomicsA ubiquitinome analysis to study the functional roles of the proteasome associated deubiquitinating enzymes USP14 and UCH37
The removal of (poly)ubiquitin (Ub) chains at the proteasome is a key step in the protein degradation pathway that determines which proteins are degraded and ultimately decides cell fate. Specific polyubiquitin linkages may lead to distinct cellular effects, with several linkage types associated wit...
ORGANISM(S): Homo sapiens (Human) 
2022-06-30 | PXD030714 | Pride
Ubiquitinome Ubiquitinomics Silac Quantitative mass spectrometry Usp14 Parallel reaction monitoring Proteasome Deubiquitinase (dub) Ubiquitin Uch37/uchl5 
ProteomicsUbiquitinome UPS - Quantitative proteomics reveals extensive changes in the ubiquitinome after perturbation of the proteasome by targeted dsRNA mediated subunit knockdown in Drosophila
In eukaryotic cells, short-lived, regulatory and misfolded or denatured proteins are degraded by the ubiquitin–proteasome system (UPS), a highly regulated mechanism including the active marking of proteins for proteasomal degradation by ubiquitin. The UPS is critical in regulating proteostasis and d...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2017-07-03 | PXD002552 | Pride
Ubiquitinome Digly Silac Proteasome Lc-ms/ms 
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