Glycosylation is one of the most common post-translational modifications, with over 50% of human proteins having been reported to be glycosylated. The identification and functional validation of complex glycoproteins are important to revealing the role of glycoproteins in biological processes. Due to the complexity of glycosylation (micro- and macro-heterogeneity), it is challenging to comprehensively identify and analyze glycoproteins which include the glycosites, glycan compositions, as well as the site- and structure-specific glycosylation. In the past decade, analytical strategies for glycoprotein characterization, especially mass spectrometry-based methods, have been widely developed. However, until now, fewer than 1,300 glycoproteins in human have been identified, while nearly 5,000 proteins have been predicted to be glycoproteins in Uniprot and thousands of glycoproteins still need to be characterized. Therefore, comprehensive, rapid and sensitive methodology to map the protein glycosylation event is required more than ever.
The biosynthesis of glycans is different from the biosynthesis of nucleic acid and proteins, which is a non-template-driven process. It is regulated by several heterogeneous factors, from cell types, to the species which cause the complex nature of protein glycosylation. Mass spectrometry (MS)is the most powerful tool for glycoprotein identification. However, the low abundance and poor ionization efficiency of glyco-proteins/peptides are the main obstacle in Mass Spectrometry-based glycosylation analysis. With the goal to understand and characterize protein glycosylation, we would like to encourage scientific discoveries, such as (1) novel glycan structure analysis and glycoprotein characterization methods, (2) protein glycosylation related databases and search engine development and (3) low organism protein glycosylation analysis, as well as (4) biological function analysis of protein glycosylation in disease.
We welcome Original Research, Review, Mini Review and Perspective articles on themes including, but not limited to:
• Glycan modification analysis on glycoproteins, such as phosphorylation (Man6P) or sulfation
• Advanced characterization of O-glycosylated proteins, such as mucin-type O-glycosylation and O-GlcNAcylation
• Studies on the relationship between protein glycosylation and diseases, like 2019-nCov and cancer
• Reviews on glycoprotein characterization and glycan analysis using analytical techniques.
• Advanced analytical strategies for the high-throughput and automated characterization of site- or structure- specific glycosylation of proteins, like intact glycopeptide analysis, DIA method in glycoprotein analysis, and top-down glycoproteomics.
• Novel methodology for glycan-precise structure analysis
• Protein glycosylation analysis of low organisms, such as insects, plants and animals
• Development of glyco-related databases and search engines
Glycosylation is one of the most common post-translational modifications, with over 50% of human proteins having been reported to be glycosylated. The identification and functional validation of complex glycoproteins are important to revealing the role of glycoproteins in biological processes. Due to the complexity of glycosylation (micro- and macro-heterogeneity), it is challenging to comprehensively identify and analyze glycoproteins which include the glycosites, glycan compositions, as well as the site- and structure-specific glycosylation. In the past decade, analytical strategies for glycoprotein characterization, especially mass spectrometry-based methods, have been widely developed. However, until now, fewer than 1,300 glycoproteins in human have been identified, while nearly 5,000 proteins have been predicted to be glycoproteins in Uniprot and thousands of glycoproteins still need to be characterized. Therefore, comprehensive, rapid and sensitive methodology to map the protein glycosylation event is required more than ever.
The biosynthesis of glycans is different from the biosynthesis of nucleic acid and proteins, which is a non-template-driven process. It is regulated by several heterogeneous factors, from cell types, to the species which cause the complex nature of protein glycosylation. Mass spectrometry (MS)is the most powerful tool for glycoprotein identification. However, the low abundance and poor ionization efficiency of glyco-proteins/peptides are the main obstacle in Mass Spectrometry-based glycosylation analysis. With the goal to understand and characterize protein glycosylation, we would like to encourage scientific discoveries, such as (1) novel glycan structure analysis and glycoprotein characterization methods, (2) protein glycosylation related databases and search engine development and (3) low organism protein glycosylation analysis, as well as (4) biological function analysis of protein glycosylation in disease.
We welcome Original Research, Review, Mini Review and Perspective articles on themes including, but not limited to:
• Glycan modification analysis on glycoproteins, such as phosphorylation (Man6P) or sulfation
• Advanced characterization of O-glycosylated proteins, such as mucin-type O-glycosylation and O-GlcNAcylation
• Studies on the relationship between protein glycosylation and diseases, like 2019-nCov and cancer
• Reviews on glycoprotein characterization and glycan analysis using analytical techniques.
• Advanced analytical strategies for the high-throughput and automated characterization of site- or structure- specific glycosylation of proteins, like intact glycopeptide analysis, DIA method in glycoprotein analysis, and top-down glycoproteomics.
• Novel methodology for glycan-precise structure analysis
• Protein glycosylation analysis of low organisms, such as insects, plants and animals
• Development of glyco-related databases and search engines
