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ProteomicsQuantitative proteomic analysis reveals the metabolic characteristics and adaptive mechanism of Cupriavidus oxalaticus in the process of simultaneous nitrogen and phenol removal
The ability of Cupriavidus oxalaticus T2 to simultaneously remove nitrogen and phenol has been confirmed. To explore the metabolic characteristics and adaptive mechanism of Cupriavidus oxalaticus T2 during the simultaneous removal of phenol and nitrogen process, the differences in proteomic profile ...
ORGANISM(S): Cupriavidus Oxalaticus Nbrc 13593 
2021-07-20 | PXD027449 |
TranscriptomicsTranscriptomic profiling of L-rhamnose utilization in Lmo0753 deletion mutant of Listeria monocytogenes EGDe from human foodborne outbreak associated lineage LII
Among the three major genetic lineages of L. monocytogenes (i.e. LI, LII, and LIII), LI and LII are predominantly associated with foodborne listeriosis outbreaks, whereas LIII is rarely implicated in human infections. In a previous study, we identified a Crp/Fnr family transcription factor lmo0753 t...
ORGANISM(S): Listeria monocytogenes 
2013-07-17 | E-GEOD-47721 | biostudies-arrayexpress
ProteomicsAssesing Orthogonality of ER-HRP and cyt-APEX proximity labeling
This project was evaluating the orthogonality of proximity labeling peroxidases that are used to determine partitioning of proteins between the ER and the cytosol.
ORGANISM(S): Homo sapiens (Human) 
2022-05-08 | PXD033764 | Pride
Hek293t Orbitrap velos pro Proximity labeling 
ProteomicsIsolation and determination of PI(4,5)P2 proximal proteins
We screened proteins in close proximity to PI(4,5)P2 in epithelial cells. We established HaCaT cells stably expressing APEX2 N-terminally fused to the PH domain of PLCd1, which specifically binds to PI(4,5)P2. In the presence of hydrogen peroxide and biotin-phenol, proteins proximal to APEX2 are bio...
ORGANISM(S): Homo sapiens (Human) 
2022-03-26 | PXD031266 | Pride
Silac pi(4 5)p2 plcd1 ph 
ProteomicsRBM6 proximity interactions (RBM6-APEX)
We sought to map RBM6 interactome using ascorbate peroxidase (APEX2)-based proximity labelling combined with mass spectrometry. Toward this end, we used CRISPR-cas9 methodology to establish MCF10A cell line expressing APEX2 fused to the N-terminal of RBM6, hereafter called MCF10AAPEX2-RBM6. The pero...
ORGANISM(S): Homo sapiens (Human) 
2021-12-29 | PXD024295 | Pride
Rbm6   apex2   proximity interactions 
TranscriptomicsTranscription profiling of Arabidopsis leaf samples treated with salicylic acid
Arabidopsis plants, ecotype Columbia, were sprayed with surfactant alone (0.01% Silwet) or surfactant and 1mM salicylic acid until all leaves were wet, 3 to 4 weeks after germination (before flowering). Leaves were harvested and frozen in liquid nitrogen. Three biological replicates were obtained ov...
ORGANISM(S): Arabidopsis thaliana 
2007-10-04 | E-GEOD-3984 | biostudies-arrayexpress
ProteomicsNLRP6 controls PTEN stability by promoting autophagic degradation of p85α to drive tumorigenesis
To identify NLRP6-associated proteins in living cells, we applied an APEX2-based labelling method combined with mass spectrometry. In brief, APEX2 was genetically fused to NLRP6. In the presence of hydrogen peroxide, APEX2 catalysed biotin-phenol to become a biotin-phenol radical that covalently bou...
ORGANISM(S): Homo sapiens (Human) 
2023-07-02 | PXD037436 | Pride
Nlrp6 Cell 
ProteomicsNLRP6 controls PTEN stability by promoting autophagic degradation of p85α to drive tumorigenesis
To identify NLRP6-associated proteins in living cells, we applied an APEX2-based labelling method combined with mass spectrometry. In brief, APEX2 was genetically fused to NLRP6. In the presence of hydrogen peroxide, APEX2 catalysed biotin-phenol to become a biotin-phenol radical that covalently bou...
ORGANISM(S): Homo sapiens (Human) 
2023-07-02 | PXD037460 | Pride
Human Lc-ms/ms 
UnknownSimple and Efficient Room-Temperature Release of Biotinylated Nucleic Acids from Streptavidin and Its Application to Selective Molecular Detection.
Not available
S-EPMC6854530 | biostudies-literature
UnknownSignature Fragment Ions of Biotinylated Peptides.
Not available
S-EPMC7199424 | biostudies-literature
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