Resources

Proteomics Databases



Metabolomics Databases

• • Mechanism of Tyrosine Phosphorylation Detection via Mass Spectrometry

  Tyrosine phosphorylation is a critical post-translational modification (PTM) involved in regulating various cellular processes such as signal transduction, proliferation, differentiation, and metabolic control. The dynamic nature of tyrosine phosphorylation modulates protein functions and protein-protein interactions, and dysregulation of this process is closely associated with numerous diseases, including cancer, autoimmune disorders, and neurodegenerative diseases.

• • Application of Quantitative Tyrosine Phosphoproteomics in Cancer Research

  Tyrosine phosphorylation is a critical post-translational modification that plays a significant role in cellular processes such as signal transduction, differentiation, proliferation, and apoptosis. Aberrant tyrosine phosphorylation is often associated with cancer initiation, progression, and metastasis. Thus, quantitative tyrosine phosphoproteomics has become a vital tool for studying cancer mechanisms and identifying potential biomarkers.

• • Quantification of Ubiquitinated Proteins Using Orbitrap Fusion Mass Spectrometry

  Ubiquitination is a fundamental biological process that regulates the degradation and stability of proteins via the covalent attachment of ubiquitin, a small regulatory protein. Abnormal ubiquitination is often implicated in various diseases, such as cancer and neurodegenerative disorders. Consequently, understanding ubiquitinated proteins and their modifications holds great significance in biomedical research.

• • Detection of Ubiquitinated Proteins by Nano-LC-MS/MS

  Ubiquitination is a key post-translational modification that regulates various cellular processes, such as protein degradation, activation, and subcellular localization, by covalently attaching the small protein ubiquitin to target proteins. Investigating the mechanisms of ubiquitination and identifying ubiquitinated proteins is crucial for understanding the pathogenesis of numerous diseases, including cancer and neurodegenerative disorders.

• • Detection of Protein Oxidative Modifications Based on Obitrap Fusion Lumos Mass Spectrometry

  Protein oxidative modifications (OM) refer to the chemical modifications of protein amino acid residues induced by reactive oxygen species (ROS) and other reactive molecules under oxidative stress conditions. These modifications play significant roles in various biological processes, such as cell signaling, inflammation, and aging. Detecting protein oxidative modifications is crucial for understanding their functions in pathological and physiological processes.

• • Detection of Protein Modifications by Top-Down Proteomics

  Protein modification is a vital regulatory mechanism of protein function and activity within organisms. Post-translational modifications (PTMs), such as phosphorylation, acetylation, methylation, and ubiquitination, allow precise control over protein functions. These modifications not only play crucial roles in cellular signaling, metabolic regulation, and disease development, but also open new avenues for drug discovery and biomarker identification.

• • Quantitative Analysis of Protein Oxidative Modifications Using Mass Spectrometry

  Protein oxidative modifications are a common form of post-translational modification, playing crucial roles in regulating protein function, cellular signaling, and the pathogenesis of various diseases. Therefore, understanding and quantifying protein oxidative modifications are key to elucidating the mechanisms of redox balance in cells and their implications for disease.

• • MS Analysis of Unknown Protein Identification

  Mass spectrometry (MS) serves as a highly sensitive and high-resolution analytical technique, playing a crucial role in the identification of unknown proteins.

• • Analytical Techniques for Unknown Protein Identification

  The identification of unknown proteins is crucial in modern biological research. With advancements in genomics and proteomics, a vast amount of protein sequence data is available, yet understanding these proteins' functions remains challenging. This paper explores major analytical techniques used in protein identification, including mass spectrometry, X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and bioinformatics methods, highlighting their advantages and limitations.

• • Workflow of Quantitative Tyrosine Phosphoproteomics Analysis

  Protein phosphorylation is a critical modification in cellular signaling, metabolic regulation, and other biological processes. Tyrosine phosphorylation, in particular, plays a significant role in various biological contexts, including cell growth, differentiation, and cancer. Quantitative tyrosine phosphorylation proteomics is a powerful technique for comprehensively studying the levels and dynamics of tyrosine phosphorylation.