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ProteomicsOenothera effect on senescent NDHF
Accumulation of senescent dermal fibroblasts drives skin aging, impairing the integrity of the extracellular matrix (ECM) and the function of neighbouring cells. One of strategies to manipulate cell senescence include the reactivation of proliferation. Here, a data independent mass spectrometry base...
ORGANISM(S): Homo sapiens (Human) 
2023-03-10 | PXD034222 | Pride
Hydrophilic extract of oenothera biennis cell cultures  senescence  proteomics  data independent mass spectrometry  fibroblasts 
UnknownTTC12 Loss-of-Function Mutations Cause Primary Ciliary Dyskinesia and Unveil Distinct Dynein Assembly Mechanisms in Motile Cilia Versus Flagella.
Not available
S-EPMC7011118 | biostudies-literature
ProteomicsProteomic analysis of regulated dendritic cell endosomes reveals dynamic adaptation to antigen uptake and cross-presentation
MHC class I cross-presentation involves final proteolytic peptide processing by the endosomal insulin-regulated aminopeptidase (IRAP). Reasoning that analysis of the IRAP proximal proteome may inform about dynamic remodeling of a key cross-presentation compartment during antigen uptake, we developed...
ORGANISM(S): Mus musculus (Mouse) 
2026-02-09 | PXD067092 | Pride
Endosome Insulin-regulated aminopeptidase Proximity biotinylation Cross-presentation Dendritic cell 
ProteomicsDual proteomics of infected macrophages identifies potential novel players involved in Francisella cell to cell dissemination
dual proteomics, merocytophagy, intracellular parasitism, Francisella tularensis
ORGANISM(S): Mus musculus (Mouse) Francisella tularensis subsp. novicida (strain U112) 
2024-03-29 | PXD035145 | Pride
Merocytophagy Francisella tularensis Dual proteomics Intracellular parasitism 
ProteomicsBiallelic variants in CHCHD4 are associated with combined OXPHOS defect leading to mitochondrial disease
Mitochondrial disorders show remarkable clinical and genetic heterogeneity, and result from genetic variants in either mitochondrial-encoded or nuclear-encoded genes. CHCHD4 is a component of the mitochondrial import and assembly (MIA) pathway that imports small cysteine-containing substrates such a...
ORGANISM(S): Homo sapiens (Human) 
2026-01-21 | PXD069027 | Pride
Chchd4 Timstof ht Evosep Mitochondrial disorders 
ProteomicsRare ADAR1 loss-of-function variants alter RNA editing and drive interferondependent inflammation in psoriasis
In 4 unrelated pedigrees, we report rare heterozygous loss-of-function ADAR1 mutations cosegregating with autosomal dominant, early onset psoriasis and increased type I interferon (IFN)-stimulated gene (ISG) transcripts in skin lesions and/or blood. We identified 6 additional variants in a psoriasis...
ORGANISM(S): Homo sapiens (Human) 
2026-04-27 | PXD065122 | Pride
Keratinocyte Melanocyte Timtof pro Adar1 
ProteomicsCystinosin interactomics - Impact of cystinosin glycosylation on protein stability by differential dynamic SILAC
Cystinosis is a rare autosomal recessive lysosomal storage disorder, characterized by an intra-lysosomal accumulation of cystine. The causative gene for cystinosis is CTNS, which encodes the protein cystinosin, a lysosomal proton-driven cystine transporter. Over 100 mutations are reported, leading t...
ORGANISM(S): Mus musculus (Mouse) 
2017-01-16 | PXD004948 | Pride
Human Rare disease High resolution Lc msms 
UnknownIstore: a project on innovative statistical methodologies to improve rare diseases clinical trials in limited populations.
Not available
S-EPMC10909280 | biostudies-literature
ProteomicsComparison of deep plasma proteome enrichment methods
Plasma is a complex biological fluid containing extracellular vesicles (EVs), residual platelets, and soluble proteins, all of which can serve as biomarkers for pathological conditions. While conventional plasma proteomics typically identifies hundreds of proteins, recent enrichment strategies have ...
ORGANISM(S): Homo sapiens (Human) 
2025-10-17 | PXD063673 | Pride
Enrichplus Proteograph Magnet Timstof Enrichment Plasma Evs Lc-ms/ms 
ProteomicsUnravelling the function of GEXP15, a regulator of Protein Phosphatase type 1, in Plasmodium falciparum
The Protein Phosphatase type 1 catalytic subunit (PP1c) works in combination with an array of regulatory proteins to specifically dephosphorylate a diverse range of substrates in the cell. In the human malaria parasite, Plasmodium falciparum, this phosphatase and its regulators are poorly character...
ORGANISM(S): Mus musculus (Mouse) Plasmodium falciparum (isolate 3D7) 
2023-10-24 | PXD042114 | Pride
Cd2bp2 Malaria Gyf domain Protein phosphatase 1 Ribosome biogenesis Plasmodium Gexp15 
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