Literature DB >> 28137562

Retrieving Quantitative Information of Histone PTMs by Mass Spectrometry.

C Zhang1, Y Liu2.   

Abstract

Posttranslational modifications (PTMs) of histones are one of the main research interests in the rapidly growing field of epigenetics. Accurate and precise quantification of these highly complex histone PTMs is critical for understanding the histone code and the biological significance behind it. It nonetheless remains a major analytical challenge. Mass spectrometry (MS) has been proven as a robust tool in retrieving quantitative information of histone PTMs, and a variety of MS-based quantitative strategies have been successfully developed and employed in basic research as well as clinical studies. In this chapter, we provide an overview for quantitative analysis of histone PTMs, often highly flexible and case dependent, as a primer for future experimental designs.
© 2017 Elsevier Inc. All rights reserved.

Keywords:  Histone PTM; Label-free quantification; Mass spectrometry; PTM quantification; Stable isotope labeling

Mesh:

Substances:

Year:  2016        PMID: 28137562     DOI: 10.1016/bs.mie.2016.10.017

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN: 0076-6879            Impact factor:   1.600


  2 in total

Review 1.  Targeting Farnesoid X receptor (FXR) for developing novel therapeutics against cancer.

Authors:  Sosmitha Girisa; Sahu Henamayee; Dey Parama; Varsha Rana; Uma Dutta; Ajaikumar B Kunnumakkara
Journal:  Mol Biomed       Date:  2021-07-10

2.  Precursor Intensity-Based Label-Free Quantification Software Tools for Proteomic and Multi-Omic Analysis within the Galaxy Platform.

Authors:  Subina Mehta; Caleb W Easterly; Ray Sajulga; Robert J Millikin; Andrea Argentini; Ignacio Eguinoa; Lennart Martens; Michael R Shortreed; Lloyd M Smith; Thomas McGowan; Praveen Kumar; James E Johnson; Timothy J Griffin; Pratik D Jagtap
Journal:  Proteomes       Date:  2020-07-08
  2 in total

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