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TranscriptomicsImmunoproteasome dysfunction augments alternative polarization of alveolar macrophages
The proteasome is a central regulatory hub for intracellular signaling by degrading numerous signaling mediators. Immunoproteasomes are specialized types of proteasomes known to be involved in shaping adaptive immune responses, but their role for innate immune signaling is elusive. Here, we analyzed...
ORGANISM(S): Mus musculus 
2016-06-29 | E-GEOD-72000 | biostudies-arrayexpress
GenomicsCaffeine modulates immunoproteasome activity and content in colorectal adenocarcinoma cells
Caffeine modulates immunoproteasome activity and content in colorectal adenocarcinoma cells
PRJNA1174712 | ENA
ProteomicsColonic proteome signature in immunoproteasome-deficient stressed mice and its relevance for irritable bowel syndrome
A role for immunoproteasome in the regulation of intestinal permeability has been previously suggested both in mice during water avoidance stress (WAS) and in patients with irritable bowel syndrome (IBS). We thus aimed (i) to evaluate the colonic proteome in wild-type (wt) and β2i immunoproteasome s...
ORGANISM(S): Mus musculus (Mouse) 
2018-12-05 | PXD011199 | Pride
Colonic proteome  immunoproteasome  irritable bowel syndrome  water avoidance stress. 
ProteomicsInduction of the immunoproteasome subunit Lmp7 links proteostasis and immunity in α-synuclein aggregation disorders
Accumulation of aggregated α-synuclein into Lewy bodies is thought to contribute to the onset and progression of dopaminergic neuron degeneration in Parkinson’s disease (PD) and related disorders. Although protein aggregation is associated with perturbation of proteostasis, how α-synuclein aggregat...
ORGANISM(S): Mus musculus (Mouse) 
2018-05-18 | PXD009647 | Pride
Proteomics Immunoproteasome Phosphoproteomics Α-synuclein 
ProteomicsInduction of the immunoproteasome subunit Lmp7 links proteostasis and immunity in α-synuclein aggregation disorders, part 2
Accumulation of aggregated α-synuclein into Lewy bodies is thought to contribute to the onset and progression of dopaminergic neuron degeneration in Parkinson’s disease (PD) and related disorders. Although protein aggregation is associated with perturbation of proteostasis, how α-synuclein aggregat...
ORGANISM(S): Mus musculus (Mouse) 
2018-05-18 | PXD009718 | Pride
Proteomics Immunoproteasome Phosphoproteomics Α-synuclein 
ProteomicsInduction of the immunoproteasome subunit Lmp7 links proteostasis and immunity in α-synuclein aggregation disorders, part 1
Accumulation of aggregated α-synuclein into Lewy bodies is thought to contribute to the onset and progression of dopaminergic neuron degeneration in Parkinson’s disease (PD) and related disorders. Although protein aggregation is associated with perturbation of proteostasis, how α-synuclein aggregat...
ORGANISM(S): Mus musculus (Mouse) 
2018-05-18 | PXD009717 | Pride
Phosphoproteome Immunoproteasome Α-synuclein Proteomoe 
ProteomicsImmunoproteasome expression is associated with better prognosis and response to checkpoint therapies in melanoma
Predicting the outcome of immunotherapy treatment in melanoma patients is challenging. Alterations in genes involved in antigen presentation and the interferon gamma (IFN) pathway play an important role in the immune response to tumors. We describe here that the overexpression of PSMB8 and PSMB9, tw...
ORGANISM(S): Homo sapiens (Human) 
2020-02-18 | PXD015957 | Pride
Immunoproteasome Neoantigens Melanoma Tumor associated antigens Hla peptidomics 
ProteomicsImmunoproteasome function maintains oncogenic gene expression in KMT2A-complex driven leukemia
Pharmacologic targeting of epigenetic protein complexes has shown significant in vitro responses in acute myeloid leukemia (AML). Early clinical trials in KMT2A-rearranged leukemia indicate rather transient responses and development of resistance. In an effort to define functional dependencies of KM...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD041245 | Pride
Aml Mll-fusion Kmt2a Immunoproteasome Leukemia Proteome 
GenomicsTargeting an alternate Wilms Tumor Antigen-1 peptide bypasses immunoproteasome dependency
Targeting an alternate Wilms Tumor Antigen-1 peptide bypasses immunoproteasome dependency
PRJNA787299 | ENA
UnknownImmunoproteasome Activity in Chronic Lymphocytic Leukemia as a Target of the Immunoproteasome-Selective Inhibitors.
Not available
S-EPMC8909520 | biostudies-literature
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