2014
DOI: 10.1021/cr500350x
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Post-Translational Modifications of Histones That Influence Nucleosome Dynamics

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Cited by 433 publications
(371 citation statements)
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References 362 publications
(831 reference statements)
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“…Post translational modifications (PTMs) of the histone proteins have been the subject of interest since the very discovery of their role in chromatin [10,79,80]. Among the large number of post translational modifications, glyoxidation of histone proteins has been widely reported and both in vitro and in vivo studies on histone glyoxidation have revealed histone proteins as easy targets to non-enzymatic glycation reactions [12,13,26].…”
Section: Resultsmentioning
confidence: 99%
“…Post translational modifications (PTMs) of the histone proteins have been the subject of interest since the very discovery of their role in chromatin [10,79,80]. Among the large number of post translational modifications, glyoxidation of histone proteins has been widely reported and both in vitro and in vivo studies on histone glyoxidation have revealed histone proteins as easy targets to non-enzymatic glycation reactions [12,13,26].…”
Section: Resultsmentioning
confidence: 99%
“…Nucleosomes spontaneously partially unwrap due to thermal fluctuations, providing DNA binding complexes transient access to sites within the nucleosome (12,13). This occurs most frequently near the DNA entry-exit region of the nucleosome and can be influenced by histone PTMs (14).…”
mentioning
confidence: 99%
“…Genomic compartments and chromatin-related activities are tightly correlated with histone modifications (1,4,6). These modifications either directly organize chromatin structure or recruit effectors that impact genome organization (1,4,6,7). However, cellular molecular details about how epigenetic complexes assemble on and spread along chromatin are incompletely understood.…”
mentioning
confidence: 99%