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This article examines the contributions of mass spectrometry-based proteomics in the identification and quantification of histone post-translational modifications.
Amidst the fast-growing science of epigenetics, Creative Proteomics, a leading provider of proteomics and bioinformatics services, has dramatically extended its workbench with the launch of an ...
Antibody-Based Proteomics Core About the Core The Antibody-based Proteomics Core provides cutting edge antibody-based proteomic platforms for both validation and protein biomarker discovery, ...
Creative Proteomics, a leading provider of advanced proteomics services globally, has recently extended its services portfolio with protein post-translational modification (PTM) analysis. This new ...
Dr. Parthun and colleagues performed a quantitative proteomics analysis of newly replicated chromatin in cell lines from wild type and histone acetyltranferase 1 (Hat1) deletion-mutant mouse embryos.
The histone amino terminus has a 'tail' region that is highly conserved between species and consists of protein modules that are responsible for post-translational modification of histones.
Making a mark: reading histone modifications using top-down As with many new techniques, early applications of top-down proteomics were primarily concerned with demonstrating that the platform could ...
Modification of histone tails, by acetylation, methylation or phosphorylation, affects the local chromatin structure and the transcriptional regulation of adjacent genes. Pericentric heterochromatin ...
The Emory researchers wanted to test the theory that removal of a particular histone protein modification involved in the packaging of DNA – dimethylation of histone H3 on lysine 4 – is involved in ...
Scientists at Tokyo Institute of Technology (Tokyo Tech) observed changes to the gene-regulating factors during zebrafish development and discovered that modifications to 'histone H3', one of the ...
Histone H4 is arguably the easiest histone to work with, possessing the best ionization, separation and fragmentation properties of any histone at both the polypeptide and intact protein level.