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Quantitative proteomics for understanding modified proteins and proteomes
Author(s) -
Garcia Benjamin A.
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.474.1
Subject(s) - computational biology , proteomics , proteome , epigenetics , quantitative proteomics , histone , reprogramming , biology , posttranslational modification , systems biology , chemistry , bioinformatics , cell , gene , biochemistry , enzyme
Mass spectrometry has become a powerful tool for characterization of thousands of proteins from any cellular source. Here in this presentation, I will highlight advances in mass spectrometry based methodology to detect post‐translational modifications on histone proteins involved in epigenetic regulation of gene expression, dynamics of global protein modifications and to also identify RNA‐protein interaction domains. We will specifically describe high‐throughput comparison of proteins from multiple cellular states (ii) mass spectrometry methods for quantitative tracking of combinatorial modifications (iii) monitoring in vivo post‐translational modification dynamics, and (iv) instrumental methods to improve data acquisition. These studies in combination with biological experiments will help provide a systems biology outlook on gene expression that will lay down the basic scientific foundation to advance several applications, such as stem cell reprogramming and cancer progression. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .