Resources

• • Mechanism of N-Glycan Modification in Cancer Diagnosis

  N-glycosylation is a protein modification process where N-acetylglucosamine (GlcNAc) is added to specific amino acid residues. This modification significantly influences the structure, stability, and function of proteins. Recent studies have highlighted N-glycosylation's critical role in cancer progression, positioning it as a valuable focus for cancer diagnosis.

• • Application of N-Glycan Modification and Site Analysis in Biomarker Discovery

  N-glycosylation is a pivotal post-translational modification that significantly influences protein function and stability. In the realm of biomarker discovery, N-glycosylation and its site analysis have become critical research focal points.

• • Workflow of N-Glycan Modification and Site Analysis

  N-glycosylation refers to the attachment of sugar chains to the nitrogen atom of amino acid residues in proteins, primarily asparagine or lysine. This modification plays a vital role in protein structure and function, influencing processes like cell signaling, immune response, and intercellular interactions.

• • Principle of N-Glycan Modification and Site Analysis

  N-glycosylation is a post-translational modification where sugar molecules attach to proteins via nitrogen atoms, specifically through asparagine residues. This modification is crucial in determining protein structure, stability, and functionality, influencing various biological processes, including cell signaling, immune response, and cellular interactions.

• • Mechanism of O-Glycan Cleavage and Methylation Analysis

  O-glycosylation refers to the addition of glycans to hydroxyl amino acid residues in proteins, an important post-translational modification that affects protein function, stability, and cellular recognition. The analysis of O-glycan cleavage and methylation is crucial for understanding the roles of O-glycosylation in biological systems.

• • Workflow of O-Glycan Site-Specific Modification Analysis

  O-glycosylation is an important post-translational modification widely present in various biomolecules, such as glycoproteins and glycolipids. It affects protein function, stability, and cell signaling, playing a crucial role in biomedical applications.

• • Application of Mass Spectrometry in O-Glycan Site Analysis

  O-glycosylation is a significant form of post-translational modification of proteins, prevalent in membrane proteins, secreted proteins, and their derivatives. O-glycosylation plays a crucial role in various biological processes, including cell signaling, immune responses, and cell recognition. Therefore, quantitative analysis of O-glycosylation sites is vital for understanding their biological functions.

• • Principle of O-Glycan Modification and Site Identification

  O-glycosylation is the process by which sugar chains are added to serine (Ser) or threonine (Thr) residues on proteins through glycosylation reactions. This modification significantly influences protein function, stability, and cellular signaling. Understanding the principles of O-glycosylation and methods for site identification is thus crucial for biological research and its applications.

• • Mechanism of O-Glycosylation and Its Impact on Biological Products

  O-glycosylation refers to the process where sugar molecules bind to the hydroxyl groups of amino acids through ester or ether bonds, forming O-glycosidic bonds. This modification plays a vital role in numerous biological processes within organisms, affecting the functionality and stability of proteins.

• • Application of O-Glycosylation Site Analysis in Biological Products

  O-glycosylation is a crucial form of post-translational modification of proteins, widely present in various organisms, especially in bioproducts. This modification not only affects the structure and function of proteins but also closely relates to many physiological and pathological processes in organisms. Therefore, analyzing O-glycosylation sites in bioproducts can provide important information regarding their biological functions and potential applications.