scholarly journals Global and site‐specific analysis of protein glycosylation in complex biological systems with Mass Spectrometry

2019 ◽  
Vol 38 (4-5) ◽  
pp. 356-379 ◽  
Author(s):  
Haopeng Xiao ◽  
Fangxu Sun ◽  
Suttipong Suttapitugsakul ◽  
Ronghu Wu
Keyword(s):  
Mass Spectrometry ◽  
Biological Systems ◽  
Protein Glycosylation ◽  
Site Specific ◽  
Specific Analysis

scholarly journals Sensitive and fast characterization of site-specific protein glycosylation with capillary electrophoresis coupled to mass spectrometry

Talanta ◽  
2018 ◽  
Vol 179 ◽  
pp. 22-27 ◽  
Author(s):  
Yanyan Qu ◽  
Liangliang Sun ◽  
Guijie Zhu ◽  
Zhenbin Zhang ◽  
Elizabeth H. Peuchen ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Capillary Electrophoresis ◽  
Specific Protein ◽  
Protein Glycosylation ◽  
Site Specific

Quantitative site-specific analysis of protein glycosylation by LC-MS using different glycopeptide-enrichment strategies

2009 ◽  
Vol 395 (2) ◽  
pp. 178-188 ◽  
Author(s):  
Jessica Wohlgemuth ◽  
Michael Karas ◽  
Thomas Eichhorn ◽  
Robertus Hendriks ◽  
Sven Andrecht
Keyword(s):  
Protein Glycosylation ◽  
Site Specific ◽  
Glycopeptide Enrichment ◽  
Specific Analysis

scholarly journals GlypNirO: An automated workflow for quantitative N- and O-linked glycoproteomic data analysis

2020 ◽  
Author(s):  
Toan K. Phung ◽  
Cassandra L. Pegg ◽  
Benjamin L. Schulz
Keyword(s):  
Mass Spectrometry ◽  
Hepatocellular Carcinoma ◽  
Data Analysis ◽  
High Throughput ◽  
Protein Glycosylation ◽  
Software Pipeline ◽  
Site Specific ◽  
Proteome Discoverer ◽  
Automated Software

AbstractMass spectrometry glycoproteomics is rapidly maturing, allowing unprecedented insights into the diversity and functions of protein glycosylation. However, quantitative glycoproteomics remains challenging. We developed GlypNirO, an automated software pipeline which integrates the complementary outputs of Byonic and Proteome Discoverer to allow high-throughput automated quantitative glycoproteomic data analysis. The output of GlypNirO is clearly structured, allowing manual interrogation, and is also appropriate for input into diverse statistical workflows. We used GlypNirO to analyse a published plasma glycoproteome dataset and identified changes in site-specific N- and O-glycosylation occupancy and structure associated with hepatocellular carcinoma as putative biomarkers of disease.

scholarly journals GlypNirO: An automated workflow for quantitative N- and O-linked glycoproteomic data analysis

2020 ◽  
Vol 16 ◽  
pp. 2127-2135 ◽  
Author(s):  
Toan K Phung ◽  
Cassandra L Pegg ◽  
Benjamin L Schulz
Keyword(s):  
Mass Spectrometry ◽  
Hepatocellular Carcinoma ◽  
Data Analysis ◽  
High Throughput ◽  
Protein Glycosylation ◽  
Software Pipeline ◽  
Site Specific ◽  
Proteome Discoverer ◽  
Automated Software

Mass spectrometry glycoproteomics is rapidly maturing, allowing unprecedented insights into the diversity and functions of protein glycosylation. However, quantitative glycoproteomics remains challenging. We developed GlypNirO, an automated software pipeline which integrates the complementary outputs of Byonic and Proteome Discoverer to allow high-throughput automated quantitative glycoproteomic data analysis. The output of GlypNirO is clearly structured, allowing manual interrogation, and is also appropriate for input into diverse statistical workflows. We used GlypNirO to analyse a published plasma glycoproteome dataset and identified changes in site-specific N- and O-glycosylation occupancy and structure associated with hepatocellular carcinoma as putative biomarkers of disease.

scholarly journals Multilayered N-glycoproteomics reveals impaired N-glycosylation promoting Alzheimer’s disease

2019 ◽  
Author(s):  
Pan Fang ◽  
Juan-Juan Xie ◽  
Shao-Ming Sang ◽  
Lei Zhang ◽  
Ming-Qi Liu ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Wild Type Mouse ◽  
Specific Protein ◽  
Protein Glycosylation ◽  
Functional Study ◽  
Wild Type ◽  
Site Specific ◽  
Specific Analysis ◽  
Quantitative Analyses

ABSTRACTAlzheimer’s disease (AD) is one of the most common neurodegenerative diseases that currently lacks clear pathogenesis and effective treatment. Protein glycosylation is ubiquitous in brain tissue and site-specific analysis of N-glycoproteome, which is technically challenging, can advance our understanding of the glycoproteins’ role in AD. In this study, we profiled the multilayered variations in proteins, N-glycosites, N-glycans, and in particular site-specific N-glycopeptides in the APP/PS1 and wild type mouse brain through combining pGlyco 2.0 strategy with other quantitative N-glycoproteomic strategies. The comprehensive brain N-glycoproteome landscape was constructed, and rich details of the heterogeneous site-specific protein N-glycosylations were exhibited. Quantitative analyses explored generally downregulated N-glycosylation involving proteins such as glutamate receptors, as well as fucosylated and oligo-mannose type glycans in APP/PS1 mice versus wild type mice. Moreover, our preliminary functional study revealed that N-glycosylation was crucial for the membrane localization of NCAM1 and for maintaining the excitability and viability of neuron cells. Our work offered a panoramic view of the N-glycoproteomes in Alzheimer’s disease and revealed that generally impaired N-glycosylation promotes Alzheimer’s disease progression.

Site-specific analysis of theN-glycans on murine polymeric immunoglobulin A using liquid chromatography/electrospray mass spectrometry

1995 ◽  
Vol 30 (12) ◽  
pp. 1679-1686 ◽  
Author(s):  
Eddy A. Kragten ◽  
Aldert A. Bergwerff ◽  
Jan van Oostrum ◽  
Dieter R. Müller ◽  
Wilhelm J. Richter
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Electrospray Mass Spectrometry ◽  
Immunoglobulin A ◽  
Site Specific ◽  
Specific Analysis
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