Abstract
Post-translational modifications (PTMs) are the alteration of amino acids in proteins after their synthesis. Such alteration significantly affects the stability, function, and structure of proteins. These modifications, in turn, regulate diverse cellular processes. Ubiquitination is an important post-translational modification that involved in the regulation of many signaling pathways. It is a multi-step enzymatic reaction that leads to the attachment of ubiquitin molecules to the substrate proteins. Aberrant ubiquitin signaling is known to be a molecular causality of several immune, cancer, neurodegenerative, and cardiovascular diseases. Thus, detection and analysis of PTMs are of immense significance in understanding the pathological mechanism of the diseases and developing new therapeutic strategies. In this chapter, we describe the advancement of the methods for the detection of protein post-translational modifications with particular reference to ubiquitination.
Original language | English (US) |
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Title of host publication | Advances in Protein Molecular and Structural Biology Methods |
Publisher | Elsevier |
Pages | 635-640 |
Number of pages | 6 |
ISBN (Electronic) | 9780323902649 |
ISBN (Print) | 9780323902656 |
DOIs | |
State | Published - Jan 1 2022 |
Keywords
- Deubiquitinating enzymes
- E3 ligase
- Post-translational modification
- Proteasomal degradation
- Tandem ubiquitin-binding entities
- UbiCRest
- Ubiquitination
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)