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ProteomicsEvaluation and Optimization of High-Field Asymmetric Waveform Ion Mobility Spectrometry for Multiplexed Quantitative Site-specific N-glycoproteomics
The heterogeneity and complexity of glycosylation hinder the depth of site-specific glycoproteomics analysis. High-field asymmetric-waveform ion-mobility spectrometry (FAIMS) has shown to improve the scope of bottom-up proteomics. The benefits of FAIMS for quantitative N-glycoproteomics have not bee...
ORGANISM(S): Homo sapiens (Human) 
2021-05-05 | PXD023951 | Pride
Faims n-glycoproteomics 
ProteomicsIMPROVED N- AND O-GLYCOPEPTIDE IDENTIFICATION USING HIGH-FIELD ASYMMETRIC WAVEFORM ION MOBILITY SPECTROMETRY (FAIMS)
Mass spectrometry is the premier tool for identifying and quantifying site-specific protein glycosylation globally. Analysis of intact glycopeptides often requires an enrichment step, after which the samples remain highly complex and exhibit a broad dynamic range of abundance. Here, we evaluated th...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD038673 | Pride
Faims N-glycopeptides Mass spectrometry O-glycopeptides Glycoproteomics 
ProteomicsFalse positive glycopeptide identification through in-FAIMS glycan fragmentation.
Glycosylation is an important post-translational modification characterized by extensive heterogeneity. While mass spectrometry (MS) is the premier technique to characterize glycoproteins, the study of intact glycopeptides presents challenges often not observed in the study of unmodified species. Hi...
ORGANISM(S): Homo sapiens (Human) 
2023-09-11 | PXD041217 | Pride
Glycoproteomics Mucinomics faims Mucin-domain glycoproteomics Enrichment. Ion mobility separation 
UnknownFalse-Positive Glycopeptide Identification via In-FAIMS Fragmentation.
Not available
S-EPMC10523363 | biostudies-literature
ProteomicsCombining FAIMS based Glycoproteomic and DIA Proteomic of reveals widespread proteome alteration in response to changes in N. gonorrhoeae glycosylation.- FAIMS pglO alleles
Protein glycosylation is increasingly recognized as a common protein modification across bacterial species. Within members of the Neisseria genus O-linked protein glycosylation plays important roles in virulence and antigenic variation yet our understanding of the substrates of glycosylation are lim...
ORGANISM(S): Neisseria gonorrhoeae MS11 
2024-02-01 | PXD044666 | Pride
Faims Dia Glycosylation Neisseria gonorrhoeae Post-translational modifications Proteomics 
ProteomicsCombining FAIMS based Glycoproteomic and DIA Proteomic of reveals widespread proteome alteration in response to changes in N. gonorrhoeae glycosylation.
Protein glycosylation is increasingly recognized as a common protein modification across bacterial species. Within members of the Neisseria genus O-linked protein glycosylation plays important roles in virulence and antigenic variation yet our understanding of the substrates of glycosylation are lim...
ORGANISM(S): Neisseria gonorrhoeae MS11 
2024-02-01 | PXD044665 | Pride
Faims Dia Glycosylation Neisseria gonorrhoeae Post-translational modifications Proteomics 
ProteomicsAGP nLC-MS/MS and nLC-FAIMS-MS/MS
Bottom-up nLC-MS/MS glycoprotein mass spectrometry workflows rely on the generation of a mixture of unmodified and glycosylated peptides via proteolysis. Such methods are challenged by suppression of hydrophilic glycopeptide ions by more abundant, hydrophobic, and readily ionizable unmodified peptid...
ORGANISM(S): Homo sapiens (Human) 
2023-03-11 | PXD036667 | Pride
N-glycopeptide High-field asymmetric waveform ion mobility spectrometry Glycoproteomics Agp Alpha-1-acid glycoprotein Faims 
ProteomicsExploring the glycosylation state of the Cryptosporidium parvum CpTSP protein family-HILIC glycopeptide enrichment
Cryptosporidium parvum is a zoonotic apicomplexan parasite and a common cause of diarrheal disease worldwide. The development of vaccines to prevent or limit infection remains an important goal for tackling these diarrheal diseases, which are a significant cause of infant morbidity in the developing...
ORGANISM(S): Cryptosporidium parvum Iowa II 
2023-01-12 | PXD023936 | Pride
Cryptosporidium Glycosylation Thrombospondin repeat 
ProteomicsGlycan-tailored glycoproteomic analysis reveals Serine is the sole residue subjected to O-linked glycosylation in Acinetobacter baumannii
Protein glycosylation is a ubiquitous process observed across all domains of life. Within the human pathogen Acinetobacter baumannii, O-linked glycosylation is required for virulence however the targets and conservation of glycosylation events remains poorly defined. Within this work we expand our u...
ORGANISM(S): Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 
2024-07-12 | PXD050066 | Pride
Glycosylation Acinetobacter baumannii Glycoproteomics Post-translational modifications Pgll 
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