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ProteomicsExtending the coverage of Lys-C/trypsin-based bottom-up proteomics using cysteine S-aminoethylation
In this study, S-aminoethylation of Cys (AE-Cys) was carried out with 2-bromoethylamine to form pseudo-Lys, which was then digested with Lys-C or trypsin to improve proteome coverage in bottom-up proteomics. A model study with bovine serum albumin showed that the C-terminal side of Cys was successfu...
ORGANISM(S): Homo Sapiens (human) Bos Taurus 
2023-09-27 | PXD045433 | JPOST Repository
ProteomicsUbiquitination at the Parkin ubiquitin-like domain suggests a new mechanism for Parkin activation
The mitochondrial kinase PINK1 and the cytosolic ubiquitin ligase (E3) Parkin is involved in mitochondrial quality control. PINK1, which phosphorylates ubiquitin at serine 65 residue and the ubiquitin-like (Ubl) domain of Parkin at serine 65 residue, promotes the Parkin activation and translocation ...
ORGANISM(S): Homo Sapiens (human) 
2022-08-24 | PXD026554 | JPOST Repository
ProteomicsIn vitro reconstitution of epigenetic reprogramming in the human germ line
M1-BTAG iPSCs or TET1-KO iPSCs were analyzed by 8% SDS-PAGE, followed by trypsin digestion and LC/MS/MS with an Orbitrap Fusion Lumos linked with an Ultimate 3000 pump and HTC-PAL autosampler. Acquired data files were processed using FragPipe v20.0 (MSFragger v3.8, Philosopher v5.0.0, IonQuant v1.9....
ORGANISM(S): Homo Sapiens (human) 
2024-04-25 | PXD048118 | JPOST Repository
ProteomicsPhosphorylation-dependent Regnase-1 interactome
In this study, we exploited interactome-based approach to isolate Regnase-1 protein complexes and found that TLR-ligand, IL-1β, or IL-17 stimulation induces formation of the Regnase-1-14-3-3 or -βTRCP complex in a mutually exclusive manner.
ORGANISM(S): Homo Sapiens (human) 
2021-10-12 | PXD026561 | JPOST Repository
ProteomicsExtending the Separation Space with Trapped Ion Mobility Spectrometry Improves the Accuracy of Isobaric Tag-based Quantitation in Proteomic LC/MS/MS
Two-dimensional separation by nano-LC and trapped ion mobility spectrometry (TIMS) prior to Q-TOF tandem mass spectrometry significantly improves the accuracy of isobaric tag-based quantitation in proteome analysis without the need for additional measurement time for TIMS insertion. The obtained pea...
ORGANISM(S): Cellular Organisms 
2020-05-22 | PXD018650 | JPOST Repository
ProteomicsCoolTip: Low-Temperature Solid-Phase Microextraction Tip for Capturing Hydrophilic Phosphopeptides
We developed a simple temperature controlled desalting strategy to cover from hydrophilic to hydrophobic peptides. Reversed-phase solid-phase extraction (SPE) techniques are commonly used for shotgun-proteomics using liquid chromatography/tandem mass spectrometry. In reversed-phase chromatography, s...
ORGANISM(S): Homo Sapiens (human) 
2021-10-28 | PXD027112 | JPOST Repository
ProteomicsCoolTip: Low-Temperature Solid-Phase Microextraction Tip for Capturing Hydrophilic Phosphopeptides: 2
We developed a simple temperature controlled desalting strategy to cover from hydrophilic to hydrophobic peptides. Reversed-phase solid-phase extraction (SPE) techniques are commonly used for shotgun-proteomics using liquid chromatography/tandem mass spectrometry. In reversed-phase chromatography, s...
ORGANISM(S): Homo Sapiens (human) 
2021-10-28 | PXD028871 | JPOST Repository
ProteomicsTargeted Quantitation of Host Cell Proteins by Capillary LC/IMS/MS/MS in Combination with Rapid Digestion on Immobilized Trypsin Column Under Native Conditions
Host cell protein (HCP) impurities are considered a critical quality attribute of biopharmaceuticals because of their potential to compromise safety and efficacy, and LC/MS-based analytical methods have been developed to identify and quantify individual proteins instead of employing enzyme-linked im...
ORGANISM(S): Cricetulus Griseus 
2025-05-02 | PXD053135 | JPOST Repository
ProteomicsRetention Order Reversal of Phosphorylated and Unphosphorylated Peptides in Reversed-Phase LC/MS
Protein phosphorylation is one of the most ubiquitous post-translational modifications in human, and trypsin-digested phosphorylated peptides have been analyzed by reversed phase LC/MS using C18-silica columns under the acidic conditions to profile human phosphoproteomes. Here, we reported that phos...
ORGANISM(S): Homo Sapiens (human) 
2018-11-11 | PXD010327 | JPOST Repository
ProteomicsNano-scale solid-phase isobaric labeling for multiplexed quantitative phosphoproteomics
We established a workflow for highly sensitive multiplexed quantitative phosphoproteomics using a nano-scale solid-phase tandem mass tag (TMT) labeling reactor. Phosphopeptides were firstly enriched by titanium oxide chromatography and then labeled with isobaric TMT reagents in a StageTip packed wit...
ORGANISM(S): Homo Sapiens (human) 
2021-07-23 | PXD025536 | JPOST Repository
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