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ProteomicsMS characterization of spidroin-1
For MS characterization of major ampullate spidroin-1 from the three species of Nephila clavipes, edulis and madagascariensis, an experimental approach was developed combining 2-DE with multiple proteolytic in-gel digestion (trypsin, chymotrypsin, pepsin, proteinase K, subtilisin and proteinase 1...
ORGANISM(S): Nephila clavipes (Golden silk orbweaver) 
2022-02-22 | PXD000057 | Pride
Major ampullate silk Nephila sp. Post-translational modifications Phosphorylation Nanolc-esi-cid/etd-ms/ms Spidroin-1 
UnknownHistone variants and their post-translational modifications in primary human fat cells.
Not available
S-EPMC3017551 | biostudies-literature
ProteomicsAgonist-selective NOP receptor phosphorylation correlates in vitro and in vivo and reveals differential post-activation signaling by chemically diverse agonists
Agonists for the nociceptin/orphanin FQ opioid peptide NOP receptor, a member of the opioid receptor family, are under active investigation as novel analgesics, but their modes of signaling are less well characterized than those for other members of the opioid receptor family. Therefore, we investig...
ORGANISM(S): Mus musculus (Mouse) 
2020-05-26 | PXD012908 | Pride
Brain Opioid receptor family Mouse Biological Pharmacology Post-translational modification Nanolc-ms/ms cid/etd Phosphorylation 
ProteomicsHA-MOP knockin mice express the canonical µ-opioid receptor but lack detectable splice variants
G protein-coupled receptors (GPCRs) are notoriously difficult to detect in native tissues. In an effort to resolve this problem, we have developed a novel mouse model by fusing the hemagglutinin (HA)-epitope tag sequence to the amino-terminus of the µ-opioid receptor (MOP). Although HA-MOP knock-in ...
ORGANISM(S): Mus musculus (Mouse) 
2022-12-07 | PXD027825 | Pride
Brain Mouse Pharmacology Mop splice variants Opioid receptor family Nanolc-ms/ms cid/etd Phosphorylation 
ProteomicsAn integrated global analysis of compartmentalized HRAS signaling - Phosphoproteomics
Modern omics technologies allow us obtaining global information on different types of biological networks. However, integrating these different types of analyzes into a coherent framework for a comprehensive biological interpretation remains challenging. Here, we present a conceptual framework that ...
ORGANISM(S): Homo sapiens (Human) 
2019-03-08 | PXD012506 | Pride
Ras phosphoproteomics minetei localisation 
ProteomicsGSK3 phosphorylation sites in Lpd
Neural crest cells are multipotent cells that delaminate from the neuroepithelium, migrating throughout the embryo. Aberrant migration causes developmental defects. Animal models are improving our understanding of neural crest anomalies, but in vivo migration behaviours are poorly understood. Here, ...
ORGANISM(S): Homo sapiens (Human) 
2023-10-05 | PXD044150 | Pride
Gsk3 Phosphorylation Cid/etd tandem mass spectrometry Lpd 
ProteomicsThe haemolymph proteome of Mytilus edulis: insights into the circulatory system and innate immunity of marine mussels
Mussels are a group of sessile and filter-feeding invertebrates, and are key structural elements of many marine and freshwater ecosystems. The mussel haemolymph is the first defense line to pathogen infection and inflammation with an innate immune response. Despite the importance of this body fluid ...
ORGANISM(S): Mytilus edulis (Blue mussel) 
2015-09-14 | PXD001951 | Pride
Innate immunity Shotgun proteomics Mytilus edulis Haemolymph Biomarker 
ProteomicsPhosphoproteome of Magnaporthe oryzae
Rice blast caused by Magnaporthe oryzae is the most devastating disease of cultivated rice. Several protein kinase cascades have been known to be essential to pathogenesis or important for response to stress, mycelial growth and conidiation in M. oryzae. However, phosphoproteins and their phosphoryl...
ORGANISM(S): Magnaporthe oryzae (strain P131) (Rice blast fungus) (Pyricularia oryzae) 
2017-07-17 | PXD002364 | Pride
Mycelium Phosphorylation Pathogensis Rice blast fungus 
ProteomicsSite mapping of PGK1 O-GlcNAcylation
To identify the site(s) of O-GlcNAcylation on PGK1, we transiently co-expressed Flag-tagged PGK1 and OGT in HEK293T cells. After immunoprecipitation using anti-Flag M2 beads and in-gel trypsin digestion, resulted peptides were subjected to mass spectrometry analysis
ORGANISM(S): Homo sapiens (Human) 
2019-11-06 | PXD015659 | Pride
Pgk1 
ProteomicsPhosphopeptide enrichment on synthetic libraries and HeLa cells digest
2 phosphopeptide enrichment methods (TiO2 and Ti-IMAC) were evaluated on synthetic libraries and HeLa cells digest. The resulting peptides were compared to the ones without enrichment with regards to the nature of the phosphorylation site (serine, threonine, tyrosine) and the characteristics of the ...
ORGANISM(S): Homo sapiens (Human) 
2014-08-11 | PXD000759 | Pride
Phosphopeptide enrichment Tio2 Ti-imac Hela Synthetic library 
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