Resources

Proteomics Databases



Metabolomics Databases

• • Advantages and Disadvantages of Top-Down Mass Spectrometry in PTMs Analysis

  Post-translational modifications (PTMs) are critical biochemical processes that regulate protein function, structure, and interactions. PTMs include phosphorylation, acetylation, ubiquitination, and others, which influence biological processes such as cell signaling, gene expression, and metabolism by altering the physicochemical properties of proteins. Given their pivotal role, precise PTM analysis is essential for understanding protein functionality and disease mechanisms.

• • Workflow of PTMs Characterization Using Top-Down Mass Spectrometry

  Proteins are the fundamental executors of life activities, and post-translational modifications (PTMs) play a critical role in regulating protein function and activity. PTMs, including phosphorylation, acetylation, glycosylation, and methylation, can significantly influence protein structure, function, and interactions. Accurately and efficiently characterizing PTMs is essential for understanding protein biological functions and disease mechanisms.

• • Principle of Top-Down Proteomics in PTMs Characterization

  Proteins are the core molecules of life, and their functions are not solely determined by their amino acid sequences but are also regulated by post-translational modifications (PTMs). PTMs refer to a series of chemical modifications that occur after protein synthesis, significantly altering protein functions, stability, localization, and interactions. Characterizing PTMs in proteomics is crucial for understanding the mechanisms underlying protein functions.

• • Application of S-Nitrosylation Analysis in Disease Research

  S-nitrosylation refers to the modification of protein cysteine residues by the attachment of a nitric oxide (NO) group to form S-nitrosothiol (SNO). As an important post-translational modification, S-nitrosylation plays a pivotal role in cellular processes such as signal transduction, metabolic regulation, and the response to oxidative stress.

• • Mechanism of Protein S-Nitrosylation Regulation

  Protein S-nitrosylation refers to the covalent modification of cysteine thiol groups (–SH) by a nitrosyl group (–NO), facilitated by nitric oxide (NO), forming S-nitrosothiols. This reversible post-translational modification is crucial for intracellular signaling, protein function regulation, and numerous pathophysiological processes.

• • Workflow of S-Nitrosylation Detection Based on HPLC-MS

  S-nitrosylation refers to the covalent attachment of a nitric oxide (NO) group to the thiol group of cysteine residues in proteins, forming an S-nitrosothiol (SNO). This post-translational modification plays a crucial role in regulating various cellular signaling pathways, including metabolism, apoptosis, and immune responses. Aberrant S-nitrosylation is implicated in numerous diseases, such as cardiovascular and neurodegenerative disorders.

• • Principle of S-Nitrosylation Analysis

  S-Nitrosylation is a significant post-translational modification (PTM) that regulates protein function by attaching a nitric oxide (NO) group to cysteine residues in proteins. This modification plays a key role in various biological processes, including signal transduction, enzyme activity regulation, and redox balance within cells. Understanding the impact of S-nitrosylation on biological systems is crucial for elucidating its role in both physiological and pathological contexts.

• • Workflow of Multi-Pathway Phosphoproteomics Using NanoLC-MS

  Protein phosphorylation is a key post-translational modification (PTM) involved in cellular signal transduction, metabolic regulation, and various other biological processes. To gain a comprehensive understanding of intracellular phosphorylation events, phosphoproteomics has become a major focus in modern life sciences research.

• • Application of Multi-Pathway Phosphoproteomics in Disease Research

  Protein phosphorylation is a common post-translational modification that plays a crucial role in regulating cell signaling, metabolism, proliferation, and apoptosis through the coordinated actions of kinases and phosphatases. Recent advances in mass spectrometry, especially in multi-pathway phosphoproteomics, have provided new insights into the mechanisms of complex diseases.

• • Principle of Multi-Pathway Phosphoproteomics in Protein Analysis

  Phosphorylation, as one of the major post-translational modifications of proteins, plays a crucial role in regulating biological processes such as cell signaling, metabolic pathways, and the cell cycle. Through the study of phosphoproteomics, scientists can uncover the dynamic regulatory networks within cells, providing in-depth insights into disease development and progression.