Literature DB >> 17705707

Functional proteomics in histone research and epigenetics.

Morten Beck Trelle1, Ole Nørregaard Jensen.   

Abstract

Post-translational modifications of histones comprise an important part of epigenetic gene regulation. Mass spectrometry and immunochemical techniques are currently the methods of choice for identification and quantitation of known and novel histone modifications. While peptide-centric mass spectrometry is a well-established tool for identification and quantification of histone modifications, recent technological advances have allowed discrete modification patterns to be assessed on intact histones. Chromatin immunoprecipitation assays (ChIP and ChIP-on-chip) are currently gaining tremendous popularity and are used to explore gene-specific patterns of histone modifications on a genomic scale. In this review, we introduce the basic concepts and recent developments of mass spectrometry, as well as immunochemical techniques and their applications in the analysis of histone modifications.

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Year:  2007        PMID: 17705707     DOI: 10.1586/14789450.4.4.491

Source DB:  PubMed          Journal:  Expert Rev Proteomics        ISSN: 1478-9450            Impact factor:   3.940


  14 in total

Review 1.  Proteomic investigation of epigenetics in neuropsychiatric disorders: a missing link between genetics and behavior?

Authors:  Mariana D Plazas-Mayorca; Kent E Vrana
Journal:  J Proteome Res       Date:  2010-09-09       Impact factor: 4.466

Review 2.  An overview of epigenetic assays.

Authors:  J Tyson DeAngelis; Woodrow J Farrington; Trygve O Tollefsbol
Journal:  Mol Biotechnol       Date:  2007-10-18       Impact factor: 2.695

3.  Large scale analysis of co-existing post-translational modifications in histone tails reveals global fine structure of cross-talk.

Authors:  Veit Schwämmle; Claudia-Maria Aspalter; Simone Sidoli; Ole N Jensen
Journal:  Mol Cell Proteomics       Date:  2014-04-16       Impact factor: 5.911

4.  Quantitative mass spectrometry of histones H3.2 and H3.3 in Suz12-deficient mouse embryonic stem cells reveals distinct, dynamic post-translational modifications at Lys-27 and Lys-36.

Authors:  Hye Ryung Jung; Diego Pasini; Kristian Helin; Ole N Jensen
Journal:  Mol Cell Proteomics       Date:  2010-02-11       Impact factor: 5.911

Review 5.  Breaking the histone code with quantitative mass spectrometry.

Authors:  Laura-Mae P Britton; Michelle Gonzales-Cope; Barry M Zee; Benjamin A Garcia
Journal:  Expert Rev Proteomics       Date:  2011-10       Impact factor: 3.940

6.  Small-molecule-based inhibition of histone demethylation in cells assessed by quantitative mass spectrometry.

Authors:  Mukram M Mackeen; Holger B Kramer; Kai-Hsuan Chang; Matthew L Coleman; Richard J Hopkinson; Christopher J Schofield; Benedikt M Kessler
Journal:  J Proteome Res       Date:  2010-08-06       Impact factor: 4.466

7.  One-pot shotgun quantitative mass spectrometry characterization of histones.

Authors:  Mariana D Plazas-Mayorca; Barry M Zee; Nicolas L Young; Ian M Fingerman; Gary LeRoy; Scott D Briggs; Benjamin A Garcia
Journal:  J Proteome Res       Date:  2009-11       Impact factor: 4.466

8.  Chromosome-wide analysis of protein binding and modifications.

Authors:  Kevin D Sarge; Hongyan Xing; Ok-Kyong Park-Sarge
Journal:  Methods Mol Biol       Date:  2009

Review 9.  Deciphering post-translational modification codes.

Authors:  Adam P Lothrop; Matthew P Torres; Stephen M Fuchs
Journal:  FEBS Lett       Date:  2013-02-10       Impact factor: 4.124

10.  Mass spectrometry-based proteomics for the analysis of chromatin structure and dynamics.

Authors:  Monica Soldi; Alessandro Cuomo; Michael Bremang; Tiziana Bonaldi
Journal:  Int J Mol Sci       Date:  2013-03-06       Impact factor: 5.923

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