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Proteomicsbinding specificity of Native Odorant-Binding Protein isoforms is driven by phosphorylation and O-N-acetylglucosamiylation in the pig (sus scrofa)
In pig, phosphorylation drives binding specificity of recombinant OBP (stricto sensu, referred as OBP in this text) isoforms (Brimau et al., 2010) that are not O-GlcNAcylated, contrary to native OBP, purified from nasal tissue (Nagnan-Le Meillour et al., 2014). In order to precise the role of both P...
ORGANISM(S): Sus scrofa domesticus (domestic pig) 
2019-02-15 | PXD011371 | Pride
Cid-nano-lc-ms/ms Odorant-binding protein Fluorescence spectroscopy Pheromone O-glcnac Phosphorylation 
UnknownImproved identification and relative quantification of sites of peptide and protein oxidation for hydroxyl radical footprinting.
Not available
S-EPMC3814024 | biostudies-literature
UnknownComprehensive Proteomic Analysis of Spider Dragline Silk from Black Widows: A Recipe to Build Synthetic Silk Fibers.
Not available
S-EPMC5037812 | biostudies-literature
ProteomicsMalus x domestica microshoot chloroplast proteome at different growth temperatures
Chloroplasts were purified by centrifugation in Percoll gradient from low temperature (4 C), control (22 C) and high temperature (30 C) grown Malus x domestica microshoots. The proteins were digested using filter aided sample processing (FASP) and analyzed using nano-LC MS/MS. Constant scan rate of ...
ORGANISM(S): Malus domestica 
2019-10-03 | PXD014212 | Pride
Temperature Malus x domestica Chloroplast 
ProteomicsIdentification of Autocrine Growth Factors Secreted by CHO cells for Applications in Single Cell Cloning Media
To identify low abundance autocrine growth factors in CHO cell conditioned media, we utilized a label-free shotgun proteomics approach. CHO cell conditioned media were harvested from fed batch bioreactors and concentrated using methanol/chlorofrom precipitation. Proteins in the samples were then su...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) 
2020-01-22 | PXD000214 | Pride
Secreted proteins Chinese hamster ovary cells Shotgun proteomics Autocrine growth factors 
ProteomicsTi4+-IMAC label-free quantification
We combine high-resolution mass spectrometry with Ti4+-IMAC phosphopeptide enrichment and label-free quantification to monitor the phosphoproteome of Jurkat T-cells following stimulation by Prostaglandin E2. Jurkat T lymphoma cells were grown in RPMI 1640 medium supplemented with 10% fetal bovine se...
ORGANISM(S): Homo sapiens (Human) 
2014-05-22 | PXD000293 | Pride
Label-free phosphoproteomics 
ProteomicsExtracellular Matrix Proteome - Tightly anchored tissue-mimetic matrices as instructive stem cell microenvironments
A major obstacle in defining the exact role of extracellular matrix (ECM) in stem cell niches is the lack of suitable methods that recapitulate complex ECM microenvironments /in vitro/. Here we describe a methodology that permits reliable anchorage of native cell-secreted ECM to culture carriers. We...
ORGANISM(S): Homo sapiens (Human) 
2013-09-12 | PXD000386 | Pride
Extracellular matrix of stem cells 
ProteomicsMolecular effects of Vitamin C treatment in MSC80 cells, a suitable Schwann cell model
Schwann cells (SCs) are not only decisive to produce the axon-wrapping myelin sheath thus ensuring a proper nerve conduction but also exhibit with trophic function and can direct repair mechanisms of the peripheral nervous system. Consequently, suitable and well-characterized SC in vitro models are ...
ORGANISM(S): Mus musculus (Mouse) 
2018-08-13 | PXD006910 | Pride
Protein cataloguing Msc80 Tmx1 Schwann cells 
ProteomicsTrincr1 RNA pull down MS in mESC
Long noncoding RNAs (lncRNAs) have emerged as important components of gene regulatory network in embryonic stem cells (ESCs). However, the function and molecular mechanism of lncRNAs are still largely unknown. Here we identified Trincr1 (TRIM71 interacting long noncoding RNA 1) lncRNA that regulates...
ORGANISM(S): Mus musculus (Mouse) 
2019-02-01 | PXD012493 | Pride
Trincr1 Rna pull down Mesc 
ProteomicsThe six unique histone deacetylase (HDAC) 1 complexes vary greatly in abundance and utilize distinct molecular assemblies.
Histone deacetylase 1 and 2 (HDAC1/2) are highly related enzymes that that regulate histone acetylation levels in all cells, as catalytic and structural components of six unique multi-protein complexes: SIN3, NuRD, CoREST, MIDAC, MIER1 and RERE. Co-immunoprecipitation of HDAC1-Flag followed by mass-...
ORGANISM(S): Mus musculus (Mouse) 
2025-08-22 | PXD060158 | Pride
Acetylation Hdac1 Protein complex Chromatin modification 
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