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ProteomicsComplexome profiling of nuclear lysates from control and USP39-depleted HeLa cells
RNA splicing and protein degradation systems allow the functional adaptation of the proteome in response to changing cellular contexts. However, the regulatory mechanisms connecting these processes remain poorly understood. Here, we show that impaired spliceosome assembly caused by USP39 deficiency ...
ORGANISM(S): Homo sapiens (Human) 
2024-09-25 | PXD050738 | Pride
Hela cells Complexome profiling Usp39 Nucleus Spliceosome 
ProteomicsIdentification of interacting proteins with U4 snRNA with and without USP39
RNA splicing and protein degradation systems allow the functional adaptation of the proteome in response to changing cellular contexts. However, the regulatory mechanisms connecting these processes remain poorly understood. Here, we show that impaired spliceosome assembly caused by USP39 deficiency ...
ORGANISM(S): Homo sapiens (Human) 
2024-09-25 | PXD050688 | Pride
Human U4 snrna Spliceosome Usp39 As oligo pulldown 
ProteomicsThe Plastid Proteome of the Nonphotosynthetic Chlorophycean Alga Polytomella parva
The unicellular, free-living, nonphotosynthetic chlorophycean alga Polytomella parva, closely related to Chlamydomonas reinhardtii and Volvox carteri, contains colorless, starch-storing plastids. The P. parva plastids lack all light-dependent processes but maintain crucial metabolic pathways. The co...
ORGANISM(S): Polytomella parva 
2020-12-10 | PXD022051 | Pride
Chlorophycean algae Amyloplast Q exactive Plastid proteome Polytomella parva Chlamydomonas reinhardtii Nonphotosynthetic algae 
ProteomicsMitochondrial super complexes in the colorless chlorophycean alga Polytomella parva
Chlorophycean algae of the genera Chlamydomonas and Polytomella share a common photosynthetic ancestor. However, members of the Polytomella lineage have adopted a heterotrophic lifestyle, having lost the photosynthetic apparatus and relying instead on acetate or ethanol as carbon sources, with energ...
ORGANISM(S): Polytomella parva 
2026-06-01 | PXD075371 | Pride
Oxidative phosphorylation F1fo atp synthase Mitochondrial supercomplexes Oligomeric complex v Chlorophycean algae 
ProteomicsEnhancing KLF15 Activity in Cardiomyocytes: A Novel Approach to Prevent Pathological Reprogramming and Fibrosis via Nuclease-Deficient dCas9VPR
Transcriptional activity perturbation holds promise for selectively modulating harmful transcriptional networks, but its therapeutic potential remains largely unexplored. We employed a network-based analysis of single-cell heart transcriptomes to identify transcription factor activities linked to pa...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2026-03-09 | PXD072456 | Pride
ProteomicsNovel genetic mutations in pyrimidine salvage pathway enzymes from Cryptococcus neoformans contribute to reduced susceptibility against 5-fluorocytosine
The most common cause of cryptococcal meningitis is Cryptococcus neoformans. The addition of 5-fluorocytosine to the treatment of patient with this potentially fatal infection significantly improves disease outcome. However, developing resistance to this drug is a serious problem in patient manageme...
ORGANISM(S): Cryptococcus neoformans var. grubii Cryptococcus neoformans var. neoformans 
2024-07-29 | PXD044249 | Pride
Pyrimidine salvage pathway Proteomics Cryptococcus neoformans Resistance 5-fluorocytosine 
ProteomicsThe transaminase-ω-amidase pathway is a redox switch in glutamine metabolism that generates α-ketoglutarate
Oxidative stress is caused by short-lived molecules and metabolic changes belong to the fastest cellular responses. Here we studied how the endothelial cell metabolome reacts to acute oxidative challenges (menadione or H2O2) to identify redox-sensitive metabolic enzymes. H2O2 selectively increased α...
ORGANISM(S): Homo sapiens (Human) 
2025-09-22 | PXD055885 | Pride
Glutamine metabolism  oxidative stress  ω-amidase  reactive oxygen species  endothelial cells  α-ketoglutarate  α-ketoglutaramate  salvage pathway  kynurenine aminotransferases  nitrilase 
ProteomicsBiallelic variants in the mitochondrial ribosomal protein MRPL49 cause combined oxidative phosphorylation deficiency
Combined oxidative phosphorylation deficiency (COXPD) is a rare, multisystem disorder that exhibits significant clinical and genetic heterogeneity. Through genome sequencing, we identified biallelic variants in MRPL49 in individuals from five unrelated families. These individuals presented a spectru...
ORGANISM(S): Homo sapiens (Human) 
2025-03-04 | PXD056347 | Pride
Perrault syndrome Rare disease Mitochondrial large ribosomal subunit Mrpl49 Mitoribosome Combined oxidative phosphorylation deficiency 
ProteomicsThe AMIGa complex is at the crossroads of cytochrome c oxidase and ATP synthase biogenesis
Cytochrome c oxidase (CIV) and ATP synthase are part of the oxidative phosphorylation machinery. Their modular, highly regulated assembly requires specific factors and is coordinated through a common intermediate, the Atco complex, composed of the Atp9 ring and Cox6. By high-throughput analysis, it ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2026-09-16 | PXD075467 | Pride
Aim11 Mtc3 Biogenesis Gep7 Yeast Cytochrome c oxidase Iai11 
UnknownThe AMIGa complex is at the crossroads of cytochrome c oxidase and ATP synthase biogenesis
Not available
S-SCDT-10_1038-S44319-026-00946-7 | biostudies-other
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