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ProteomicsPRM analysis of phosphopeptides of Nab2, Foxk1, HURP, ERK1/2, NPM, and Hspa4 from ΔB-Raf:ER cells.
ΔB-Raf:ER cells were treated with U0126 or 4-HT for 30 min in four biological replicates. Total proteins from cell lysates were digested with Typsin/Lys-C mix, and phosphopeptides were enriched by IMAC using Fe-NTA columns. After data-dependent LC-MS/MS analysis, phosphopeptides of Nab2, Foxk1, HURP...
ORGANISM(S): Mus Musculus (mouse) 
2022-03-03 | PXD028826 | JPOST Repository
ProteomicsIdentification of the components of PRDM14 complex in ESCs
We investigated the N-terminal domain of PRDM14, which has no discernable functional domain, and its contribution to the maintenance of pluripotency. We performed a mass spectrometry analysis of the PRDM14-containing complex to disclose partner molecules that bind to the N-terminal domain of PRDM14.
ORGANISM(S): Mus Musculus (mouse) 
2020-08-03 | PXD020571 | JPOST Repository
ProteomicsTIG-3 quantification of metabolic enzymes set07
Absolute quantification of metabolic enzymes (core metabolic set) was carried out by MRM with internal standard recombinant proteins. Sample digests were labeled with mTRAQdelta0 and internal standard digests were labeled with mTRAQdelta4.
ORGANISM(S): Homo Sapiens (human) 
2016-12-03 | PXD004835 | JPOST Repository
ProteomicsProteomic analysis of NLR proteins.
Immunoprecipitation of NLR proteins followed by mass spectrometry.
ORGANISM(S): Homo Sapiens (human) 
2023-05-22 | PXD037963 | JPOST Repository
ProteomicsTIG-3 quantification of metabolic enzymes set06
Absolute quantification of metabolic enzymes (core metabolic set) was carried out by MRM with internal standard recombinant proteins. Sample digests were labeled with mTRAQdelta0 and internal standard digests were labeled with mTRAQdelta4.
ORGANISM(S): Homo Sapiens (human) 
2016-12-03 | PXD004834 | JPOST Repository
ProteomicsTMT10plex_cTEC_mTEC_beta5tKO-cTEC
TEC cells (K5D1 cTECs in quadruplicate, K5D1 mTECs in triplicate, and K5D1-β5tKO cTECs in triplicate) were lysed in 6 M guanidine-HCl containing 100 mM Tris-HCl, pH 8.0, and 2 mM DTT. The clarified lysates were reduced in 5 mM DTT and alkylated in 27.5 mM iodoacetamide. Proteins were purified by met...
ORGANISM(S): Mus Musculus (mouse) 
2019-10-08 | PXD013132 | JPOST Repository
ProteomicsJPST000068 monolith HILIC-HeLa [Reanalysis: JPST000068]
A meter-scale monolithic silica capillary column modified with urea-functional groups for hydrophilic interaction liquid chromatography (HILIC) was developed for highly efficient separation of biological compounds. We prepared a ureidopropylsilylated monolithic silica capillary column with a minimum...
ORGANISM(S): Homo Sapiens (human) 
2023-04-01 | RPXD034323 | JPOST Repository
ProteomicsMining Missing Protein Landscape in Subcellular Proteome of Human Embryonic Stem Cells
Human embryonic stem cells (hESCs) have capacity of self-renewal and multi-lineage differentiation into derivatives of three germ layers that are of clinical importance for regeneration medicine. Despite the significant progress of hESCs study for clinical application, factors responsible for mainta...
ORGANISM(S): Homo Sapiens (human) 
2019-05-20 | PXD009840 | JPOST Repository
ProteomicsA new tool to reveal bacterial signaling mechanisms in antibiotic treatment and resistance
Antimicrobial resistance is widespread across the globe. Here we presented a dynamic view of protein phosphoregulations during resistance development. Specific phosphorylation motifs and highly conserved phosphorylated residues on transcription factors were identified involving in regulating resista...
ORGANISM(S): Escherichia Coli 
2018-09-21 | PXD008921 | JPOST Repository
ProteomicsSWATH-MS proteomic analysis of liver samples prepared from liver-specific HyD-LIR expressing mice.
HyD-LIR-Venus consists of HyD, a short hydrophobic domain of Aplysia phosphodiesterase 4 short-form; LIR of TP53INP2; and a fluorescent protein, Venus. This protein efficiently binds to LC3-II and GABARAP-II localizing on inner membrane of autophagosomes and does not affect autophagosome formation.L...
ORGANISM(S): Mus Musculus (mouse) 
2020-11-09 | PXD019492 | JPOST Repository
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