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ProteomicsMouse lung N-glycoproteome, phosphoproteome, and M6P glycoproteome
This is the raw data and Byonic search results of mouse mouse lung N-glycoproteome, phosphoproteome, and Mannose-6-Phosphate glycoproteome.
ORGANISM(S): Mus musculus (Mouse) 
2022-01-11 | PXD020196 | Pride
Mannose-6-phosphate glycosylation Phosphoproteome Mouse Lung Glycoproteome 
ProteomicsMultilayered N-glycoproteome Profiling Reveals Highly Heterogeneous and Dysregulated Protein N-glycosylations Related to Alzheimer’s Disease
Protein N-glycosylation is ubiquitous in brain and closely related to cognition and memory. Alzheimer's disease (AD) is a multifactorial disorder that lacks clear pathogenesis and treatment. Aberrant N-glycosylation has been suggested to be involved in AD pathology. While the systematic variations o...
ORGANISM(S): Mus musculus (Mouse) 
2019-11-25 | PXD015335 | Pride
Glycoproteomics alzheimer's disease 
ProteomicsUltradeep N-glycoproteome Atlas of Mouse Reveals Spatiotemporal Signatures of Brain Aging and Neurodegenerative Diseases
The current depth of site-specific N-glycoproteomics is insufficient to fully characterize glycosylation events in biological samples. Herein, we achieved an ultradeep and precision analysis of the N-glycoproteome of mouse tissues by integrating multiple workflows. The largest N-glycoproteomic datas...
ORGANISM(S): Mus Musculus 
2025-03-04 | PXD061436 |
ProteomicsNovel Proteome and N-glycoproteome of the Thermophilic Fungus Chaetomium thermophilugm in Response to High Temperature
Thermophilic fungi are eukaryotic species that grow at high temperatures, but little is known about the thermophily of thermophilic fungi. Here the proteome and N-glycoproteome of Chaetomium thermophilum at varying culture temperatures (30℃, 50℃, and 55℃) were studied using hydrophilic interaction l...
ORGANISM(S): Chaetomium thermophilum 
2021-05-17 | PXD023311 | Pride
Glycosylation Chaetomium thermophilum Thermophily N-glycoproteome Proteome 
ProteomicsN-Glycome and N-Glycoproteome of a Hematophagous Parasitic Nematode Haemonchus
N-glycosylation is a physiologically vital post-translational modification of proteins in eukaryotic organisms. Initial work on Haemonchus contortus – an economically-important blood-sucking nematode of ruminants with a broad geographical distribution – has shown that the parasite harbors N-glycans ...
ORGANISM(S): Haemonchus contortus (Barber pole worm) 
2021-09-09 | PXD023379 | Pride
Haemonchus contortus N-glycan Mass spectrometry Glycopeptide N-glycosylation 
ProteomicsA comprehensive landscape of human organ N-glycoproteome
N-glycosylation, as a common post-translational modification with enormous structures, plays key roles in protein folding, cellular recognition and signaling pathways. State-of-the-art mass spectrometry-based N-glycoproteomics has enabled deep N-glycoproteome characterization of various human organs...
ORGANISM(S): Homo sapiens (Human) 
2026-05-13 | PXD070547 | Pride
Tissue Human N-glycosylation Profile 
ProteomicsVenom profiling of the insular species Bothrops alcatraz: characterization of proteome, glycoproteome, and N-terminome using Terminal Amine Isotopic Labeling of Substrates.
In this study we applied mass spectrometric approaches to characterize the proteome and glycoproteome of B. alcatraz venom, and to show for the first time the use of the TAILS method to profile a snake venom N-terminome.
ORGANISM(S): Bothrops alcatraz 
2021-01-13 | PXD021561 | Pride
Bothrops alcatraz  snake venom  proteome  glycoproteome  n-terminome  proteolytic processing 
UnknownCapturing site-specific heterogeneity with large-scale N-glycoproteome analysis.
Not available
S-EPMC6428843 | biostudies-literature
UnknownComprehensive Plasma N-Glycoproteome Profiling Based on EThcD-sceHCD-MS/MS.
Not available
S-EPMC9251008 | biostudies-literature
ProteomicsComprehensive human plasma N-glycoproteome profiling based on EThcD-sceHCD-MS/MS
N-glycoproteins are involved in various biological processes. More than one-third of plasma tumor protein biomarkers approved by the Food and Drug Administration (FDA) are glycoproteins which would enhance the specificity and/or sensitivity of cancer diagnosis. Therefore, the characterization of pla...
ORGANISM(S): Homo sapiens (Human) 
2022-08-12 | PXD030622 | Pride
Mass spectrometry  human plasma  n-glycoproteomics  combinatorial peptide ligands library  ethcd-scehcd 
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