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ProteomicsTop-down proteomics of membrane proteoforms from HeLa cells and mouse hippocampus
Comprehensive characterization of membrane proteins at the level of proteoforms in complex biological samples by top-down mass spectrometry is of vital importance in revealing their precise functions. Based on a novel membrane protein separation technology, we obtained a dataset of membrane proteofo...
ORGANISM(S): Homo Sapiens Mus Musculus 
2023-02-08 | PXD039949 |
ProteomicsA multiplex fragment ion-based method for accurate proteome quantification
We developed a multiplex pseudo-isobaric dimethyl labeling (m-pIDL) method for proteome quantification to extend the capacity of the fragment ion-based method to 6-plex by one-step dimethyl labeling with several millidalton and dalton mass differences between precursor ions and enlarging the isolati...
ORGANISM(S): Homo Sapiens Escherichia Coli 
2019-01-22 | PXD012457 |
ProteomicsProteoform Imaging by Combining MALDI MSI and High-sensitivity Top-down Proteomics
Spatially resolved characterization of proteoforms has great potential to significantly advance our understanding of physiological and disease mechanisms. However, it faces challenges regarding throughput and coverage. Herein, we developed a robust method for high-throughput proteoform imaging (HTPi...
ORGANISM(S): Mus Musculus 
2024-12-03 | PXD058552 |
ProteomicsIn-vivo crosslinking based affinity purification-mass spectrometry for targeting intracellular protein-protein interactions
Comprehensive interactome analysis of targeted proteins is of great significance to understand how pro-teins work together for functional regulation. Until now, affinity purification strategy with mass spec-trometry (AP-MS) has been recognized as the most widely used technique for studying protein-p...
ORGANISM(S): Homo Sapiens 
2022-12-01 | PXD038473 |
ProteomicsA Glycosidic-Bond-Based Mass-Spectrometry-Cleavable Cross-linker Enables In Vivo Cross-linking for Protein Complex Analysis
Chemical cross-linking mass spectrometry (CXMS) has emerged as a powerful technology to analyze protein complex structure and interaction. However, the spectral fragmentation behavior and spectral data retrieval of cross-linked peptides are more complex than single peptides. In this study, we design...
ORGANISM(S): Homo Sapiens Saccharomyces Cerevisiae 
2023-12-06 | PXD047554 |
ProteomicsAnalysis of Nucleocytoplasmic Protein Separation in DPST-Crosslinked Human Neuroblastoma SY5Y Cells
Following DPST crosslinking of human neuroblastoma cells, nuclear-cytoplasmic fractionation was performed using hypotonic lysis to obtain cytoplasmic and nuclear protein compartments. Through systematic analysis of crosslinking mass spectrometry data, we elucidated how subcellular compartmentalized ...
ORGANISM(S): Homo Sapiens 
2025-04-14 | PXD062913 |
ProteomicsCleavable Hydrophobic Derivatization Strategy for Enrichment and Identification of Phosphorylated Lysine Peptides
Herein, a cleavable hydrophobic derivatization (CHD) strategy was established for the enrichment and identification of pLys peptides. By CHD, 2,5-dioxopyrrolidin-1-yl-3-(decyldisulfanyl)propanoate (Dec-disulf-NHS) was synthesized to react with lysine dephosphorylated peptides, and then the derived p...
ORGANISM(S): Escherichia Coli 
2019-02-12 | PXD012682 |
ProteomicsAffinity peptide ligands: New tools for chasing non-canonical N-phosphoproteome
Protein N-phosphorylation enrichment is faced with great difficulties due to the intrinsic instability of the N-P bond, which has seriously hindered its biological function unraveling. Current methods for N-phosphopeptides enrichment are challenging to fulfil high selectivity for all types of N-phos...
ORGANISM(S): Homo Sapiens Escherichia Coli Mus Musculus 
2024-12-12 | PXD058797 |
ProteomicsBis(zinc(II)-dipicolylamine) functionalized sub-2 μm core-shell microspheres enabled comprehensive analysis of N-phosphoproteome
Herein, bis(zinc(II)-dipicolylamine) functionalized sub-2 μm core-shell silica microspheres (SiO2@DpaZn) were tailored for N-phosphopeptide enrichment at pH 7.7. Contributed by the coordination bonding between Zn(II) and phosphate groups with the KD value of 13.14 μM, N-phosphopeptides could be capt...
ORGANISM(S): Escherichia Coli 
2020-02-07 | PXD017423 |
ProteomicsBis(zinc(II)-dipicolylamine) functionalized sub-2 μm core-shell microspheres for analysis of N-phosphoproteome-
Herein, bis(zinc(II)-dipicolylamine) functionalized sub-2 μm core-shell silica microspheres (SiO2@DpaZn) were tailored for N-phosphopeptide enrichment at pH 7.7. Contributed by the coordination bonding between Zn(II) and phosphate groups with the KD value of 13.14 μM, N-phosphopeptides could be capt...
ORGANISM(S): Homo Sapiens 
2020-08-22 | PXD021067 |
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