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In humans, studies of monozygotic twin pairs have demonstrated modification of epigenetic profile across the life course in response to environmental exposure (reviewed in [ 5]).
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A few authors have demonstrated modifications of plasma biochemical parameters, notably urea and creatinine, despite the absence of molecular or histological effects.
Recently, we have demonstrated a novel modification approach, plasma treatment, to modify the polystyrene microspheres surface with hydroxyl groups [10].
We have demonstrated direct surface modification of nanocolumn relative humidity sensors with conformal coatings deposited by atomic layer deposition (ALD).
Although lysine acetylation was initially reported to regulate nuclear proteins such as histones and transcription factors (Allfrey et al., 1964; Gershey et al., 1968; Gu and Roeder, 1997), large-scale proteomic surveys have demonstrated that this modification is also prevalent outside the nucleus.
Previous studies have demonstrated that this modification results in dramatically increased CDK5 activity.
Previously, we have demonstrated that H2Bub1 modification is one of the events that precede entering the differentiation program (Karpiuk et al., 2012).
Previous reports have demonstrated that ECM modification generates a panoply of signalling pathways implicated in various physiological and pathophysiological events [ 29].
In addition to the rare genetic mutations seen in the genes encoding mitochondrial fission and fusion proteins, recent studies have demonstrated that posttranslational modification of these molecules can contribute to altered mitochondria dynamics.
Several clinical trials have demonstrated that lifestyle modification with weight loss and moderate physical exercise can reduce the incidence of type 2 diabetes by up to 58% for people at high risk [ 1].
More specifically, we have demonstrated the selective modification of a free cysteine residue in a protein and also that dibromopyridazinedione 8 can be used to successfully bridge the disulfide bond of the peptide hormone somatostatin.
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