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Here we demonstrate that EGFP and EGFP fusion proteins inhibit polyubiquitination, a posttranslational modification that controls a wide variety of cellular processes, like activation of kinase signalling or protein degradation by the proteasome.
ADP-ribosylation is a posttranslational modification that controls both intra- and extracellular processes [ 2].
Ubiquitylation is an essential posttranslational modification that controls many aspects of cellular behavior.
Protein phosphorylation is a particularly important post-translational modification that controls many essential cellular signaling pathways.
SUMOylation was initially identified as a reversible post-translational modification that controls a variety of cellular processes including replication, chromosome segregation, and DNA repair [ 1– 3].
Protein phosphorylation and dephosphorylation represent a major form of reversible post-translational modification that controls many regulatory circuits in eukaryotes by modulating the conformation, activity, localization and stability of substrate proteins [ 68].
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Mutant forms of the gene disrupt chemical modifications that control access to genes necessary for normal brain cell function.
5-methylcytosine is considered to be the fifth base of DNA as – through its non-random distribution along the genome – it constitutes part of the epigenetic chromatin modifications that control gene expression patterns.
Inactivation of the cubilin allele might occur through epigenetic modifications that control the transition of chromatin from transcriptionally active to inactive state.
Thus, p53 from mESCs and from differentiated cells may possess post-translational modifications that control their function under normal culture conditions and these modifications may be different from those after genotoxic stress.
Furthermore, Myc is regulated by multiple signals that control promoter activity, transcriptional elongation and translation, as well as by post-translational modifications that control Myc's transcriptional targets as well as protein stability.
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