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UnknowniTRAQ-Based Quantitative Proteomic Comparison of 2D and 3D Adipocyte Cell Models Co-cultured with Macrophages Using Online 2D-nanoLC-ESI-MS/MS.
Not available
S-EPMC6856061 | biostudies-literature
ProteomicsiTRAQ-Based Quantitative Proteomic Comparison of 2D and 3D Adipocyte Cell Models Co-cultured with Macrophages Using Online 2D-nanoLC-ESI-MS/MS
The demand for novel three-dimensional (3D) cell culture models of adipose tissue has been increasing, and proteomic investigations are important for determining the underlying causes of obesity, type II diabetes, and metabolic disorders. In this study, we performed global quantitative proteomic pro...
ORGANISM(S): Mus musculus (Mouse) 
2020-05-26 | PXD014437 | Pride
3d-culture Macrophages Adipocytes Proteomic quantification Itraq 
ProteomicsAge-related cleavages of crystallins in human lens cortical fibre cells generate a plethora of low molecular weight peptides and cross-linked crystallin complexes
A large variety of low molecular weight (LMW) peptides, derived from the breakdown of crystallins, have been reported in middle to old age human lenses. The proliferation of these LMW peptides coincides with the earliest stages of cataract formation, suggesting that the protein cleavages involved ma...
ORGANISM(S): Homo sapiens (Human) 
2016-09-29 | PXD001593 | Pride
Human lens Crystallin Endogeneuous peptideslens aging  crystallin  cataract  mass spectrometry  endogenous peptides  2-d gel electrophoresis  nanolc-esi-ms/ms  trypsin-like cleavage 
ProteomicsWhite body nanoLC ESI-MS/MS analysis in the cephalopod Sepia officinalis
Cephalopods, like other Protostomes, lack an adaptive immune system and only rely on an innate immune system. The main immune cells are haemocytes, able to respond to pathogens and external attacks. First reports based on morphological observations suggested that the white body located in the optic ...
ORGANISM(S): Sepia officinalis 
2020-07-10 | PXD017509 | Pride
Cuttlefish White body Esi-ms/ms 
ProteomicsProfiling of Subclass-Specific IgG Glycosylation in Gastric Cancer by nanoLC-ESI-MS/MS
Background:Gastric cancer (GC) is one of the most aggressive gastrointestinal malignancy and leading cause of cancer related deaths worldwide,warranting the urgent discovery of biomarkers for early detection. IgG glycosylation is strongly related to disease progression and specific IgG glycans have ...
ORGANISM(S): Homo sapiens (Human) 
2025-05-06 | PXD027475 | Pride
Human Gastric cancer Serum igg Subclass specific Lc-ms 
ProteomicsOVA N-glycans PGC-LC-MSMS - Large-scale identification and visualization of N-glycans with primary structures using GlySeeker
With PNGase F digestion, PGC enrichment,OVA N-glycans were analyzed using PGC nanoLC-ESI-MS/MS.Datasets were analyzed by the N-glycan database search engine called GlycanGoggle developed in our group.
ORGANISM(S): Gallus gallus (Chicken) 
2019-01-17 | PXD006400 | Pride
Pgc-lc-msms Ova N-glycans 
ProteomicsComplementary metaproteomic approaches to assess marine bacteriopankton response towards algal bloom
In this project, the metaproteome of the marine bacterioplankton was analyzed to assess its respone towards an algal bloom in the southern North Sea in spring 2010. Proteins were extracted applying two different methods: (i) applying chemical cell lysis using trifluoroethanol in combination with in-...
ORGANISM(S): environmental samples 
2017-04-11 | PXD004944 | Pride
Metaproteome Algal bloom Marine bacterioplankton 
UnknownSensitive and fast characterization of site-specific protein glycosylation with capillary electrophoresis coupled to mass spectrometry.
Not available
S-EPMC5763510 | biostudies-literature
ProteomicsInvestigation of the aging process of C. elegans using integrated quantitative proteomics and N-glycoproteomics
N-glycosylation, a highly diverse and abundant post-translational modification, critically regulates organismal aging. Leveraging the Caenorhabditis elegans (C. elegans) model, which exhibits distinctive N-glycosylation features including highly fucosylated core structures, bisecting β1,4-galactose,...
ORGANISM(S): Caenorhabditis elegans 
2026-09-14 | PXD067150 | Pride
Aging process Nanolc-esi-ms/ms N-glycosylation Caenorhabditis elegans 
UnknownHinge-Region O-Glycosylation of Human Immunoglobulin G3 (IgG3).
Not available
S-EPMC4424406 | biostudies-literature
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