Identification, quantification, and site localization of protein posttranslational modifications via mass spectrometry-based proteomics

55Citations
Citations of this article
79Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Posttranslational modifications (PTMs) are important biochemical processes for regulating various signaling pathways and determining specific cell fate. Mass spectrometry (MS)-based proteomics has been developed extensively in the past decade and is becoming the standard approach for systematic characterization of different PTMs on a global scale. In this chapter, we will explain the biological importance of various PTMs, summarize key innovations in PTMs enrichment strategies, highperformance liquid chromatography (HPLC)-based fractionation approaches, mass spectrometry detection methods, and lastly bioinformatic tools for PTMs related data analysis. With great effort in recent years by the proteomics community, highly efficient enriching methods and comprehensive resources have been developed. This chapter will specifically focus on five major types of PTMs; phosphorylation, glycosylation, ubiquitination/sumosylation, acetylation, and methylation.

Cite

CITATION STYLE

APA

Ke, M., Shen, H., Wang, L., Luo, S., Lin, L., Yang, J., & Tian, R. (2016). Identification, quantification, and site localization of protein posttranslational modifications via mass spectrometry-based proteomics. In Advances in Experimental Medicine and Biology (Vol. 919, pp. 345–382). Springer New York LLC. https://doi.org/10.1007/978-3-319-41448-5_17

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free