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ProteomicsStructural- and Site-specific N-glycosylation Characterization of COVID-19 Virus Spike with StrucGP
Spike (S) protein plays a key role in COVID-19 (SARS-CoV-2) infection and host-cell entry. Previous studies have systematically analyzed site-specific glycans compositions of S protein. Here, we further provide structure-clear N-glycosylation of S protein at site-specific level by using our recently...
ORGANISM(S): Homo sapiens (Human) 
2022-10-13 | PXD034086 | Pride
Covid-19 Lc-msms Strucgp Spike Glycopeptides 
ProteomicsThe identification result of MAP-Match and conventional method
The comparison of GPSMs that's identified by StrucGP in 24 MouseBrain raw files, using MAP-Match and the conventional calibration method saparately.
ORGANISM(S): Mus musculus (Mouse) 
2025-08-08 | PXD052777 | Pride
Strucgp Mousebrain 
ProteomicsPrecision mapping of glycosite-specific glycans reveals distinctive N-glycosylation on human spermatozoa
In this study, we applied the recently developed software, StrucGP to large-scale characterize glycoproteins, and IGPs, as well as precise site-specific glycan structures in human spermatozoa. Furthermore, bioinformatical analyses were conducted to systematically describe the potential functions of ...
ORGANISM(S): Homo sapiens (Human) 
2022-05-19 | PXD026649 | Pride
Spermatozoa Glycan structures Mass spectrometry 
UnknownIdentifying intact N-glycopeptides from tandem mass spectrometry data using StrucGP.
Not available
S-EPMC10166508 | biostudies-literature
ProteomicsStructural Interpretation of Glycosite-specific N-Glycans Using Tandem Mass Spectrometry
In this project we developed a new algorithm termed StrucGP, for large-scale interpretation of N-glycan structures on intact glycopeptides from tandem mass spectrometry data. StrucGP is able to reveal the glycan structure heterogeneity for individual glycosites. The StrucGP also has high performance...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) Mus musculus (Mouse) Gallus gallus (Chicken) 
2021-07-07 | PXD025859 | Pride
N-glycans Intact glycopeptides Glycan structure 
ProteomicsSite-specific N-glycoproteomic analysis of four M2 macrophage subtypes derived from human THP-1 cells
In this study, we performed site-specific N-glycoproteomic analysis of THP-1 derived four M2 macrophage subtypes (M2a, M2b, M2c, and M2d) by StrucGP method combined with 2D-LC-MS/MS analysis, and revealed the distribution regularities and characters of N-glycans.
ORGANISM(S): Homo sapiens (Human) 
2025-12-23 | PXD048964 | Pride
Glycoproteome M2 subtypes Macrophage 
ProteomicsProfiling of human spermatozoa glycoproteins by LC/MS/MS
N-linked glycoproteins are known to be important for spermatozoa development and gametes fusion. However, little is known about detailed information of these glycoproteins, particularly the glycosylation sites and its corresponding glycan structures in human spermatozoa. In present study, an in hous...
ORGANISM(S): Homo sapiens (Human) 
2023-03-04 | PXD020286 | Pride
Human Lc/ms/ms Glycan structures Spermatozoa 
ProteomicsPrecision structural interpretation of site-specific N-glycans in seminal plasma
This study is aimed to comprehensively and globally characterize seminal plasma glycoproteins in a site-specific manner with information of N-glycosites and corresponding glycan structures, as well as glycan isomers using mass spectrometry. Furthermore, the function of specific glycan structures is ...
ORGANISM(S): Homo sapiens (Human) 
2023-03-04 | PXD030804 | Pride
Seminal plasma Glycoproteomics Glycan structures Mass spectrometry Intact glycopeptides 
ProteomicsGlycoproteomics of human THP-1-derived M0, M1 and M2 macrophages
In this study, we used human THP-1-derived macrophages as an immune cell model, and systematically performed glycoproteomics of three subtypes of macrophages by StrucGP.To study the N‑Glycoproteomic of them, the intact glycopeptides were first enriched and identified using triplicate mass spectromet...
ORGANISM(S): Homo sapiens (Human) 
2023-10-19 | PXD030277 | Pride
Macrophages Glycoproteomics Lc-ms/ms 
ProteomicsPrecision Characterization of Site-specific O-Acetylated Sialic Acids on N-Glycoproteins
O-Acetylation is a common modification of sialic acid, playing a significant role in glycoprotein stability, immune response, and cell development. The lack of efficient methods for direct analysis of O-acetylated sialoglycopeptides (O-AcSGPs) made the majority of identified O-acetylated sialic acid...
ORGANISM(S): Mus musculus (Mouse) 
2023-01-13 | PXD037161 | Pride
Glycoproteomics Strucgp Mouse serum O-acetylated sialic acids 
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