Advancements in the analysis of protein post-translational modifications

Sandip Mukherjee, Ritesh Kumar, Arianne L. Theiss, K. Venuprasad

Research output: Chapter in Book/Report/Conference proceedingChapter


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 languageEnglish (US)
Title of host publicationAdvances in Protein Molecular and Structural Biology Methods
Number of pages6
ISBN (Electronic)9780323902649
ISBN (Print)9780323902656
StatePublished - Jan 1 2022


  • 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)


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