Affiliation:
1. Medical Science and Technology Innovation Center, Shandong Key Laboratory of Radiation Oncology, Shandong Cancer Hospital and Institute Shandong First Medical University & Shandong Academy of Medical Sciences Shandong Jinan People's Republic of China
2. Key Laboratory of Cancer Proteomics of Chinese Ministry of Health Central South University Changsha Hunan People's Republic of China
Abstract
AbstractTyrosine phosphorylation is a crucial posttranslational modification that is involved in various aspects of cell biology and often has functions in cancers. It is necessary not only to identify the specific phosphorylation sites but also to quantify their phosphorylation levels under specific pathophysiological conditions. Because of its high sensitivity and accuracy, mass spectrometry (MS) has been widely used to identify endogenous and synthetic phosphotyrosine proteins/peptides across a range of biological systems. However, phosphotyrosine‐containing proteins occur in extremely low abundance and they degrade easily, severely challenging the application of MS. This review highlights the advances in both quantitative analysis procedures and enrichment approaches to tyrosine phosphorylation before MS analysis and reviews the differences among phosphorylation, sulfation, and nitration of tyrosine residues in proteins. In‐depth insights into tyrosine phosphorylation in a wide variety of biological systems will offer a deep understanding of how signal transduction regulates cellular physiology and the development of tyrosine phosphorylation‐related drugs as cancer therapeutics.
Subject
Spectroscopy,General Biochemistry, Genetics and Molecular Biology,Condensed Matter Physics,Analytical Chemistry
Cited by
2 articles.
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