This review focus on discussing key mechanisms in disease pathogenesis mediated by the protein post-translational modification, citrullination. These processes are discussed in depth in the context of complex diseases such… Click to show full abstract
This review focus on discussing key mechanisms in disease pathogenesis mediated by the protein post-translational modification, citrullination. These processes are discussed in depth in the context of complex diseases such as, rheumatoid arthritis, cancer, central nervous system disorders, and cardiovascular disease. Additionally, a critical evaluation of challenges in laboratory-detection of citrullination sites is also outlined. In this context, the role of mass spectrometry is discussed with a focus on contemporary techniques that offer promising options to detect the exact site of protein citrullination. Novel methods described in the paper have the potential to detect and quantify the occurrence of post-translational modification sites for diagnosis and therapeutic purposes with a high degree of specificity and sensitivity. Furthermore, they offer much faster performance than traditional techniques making them ideal for large-scale experimentation.
               
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