The absence of N-response in G2 after HP1 overexpression suggests that N-responsiveness is modulated by modifications in the chromatin structure.
Existing data supporting the role of nanotopography suggest that critical steps in osseointegration can be modulated by nanoscale modification of the implant surface.
The stability of cell patterns could be modulated by simply modification of the surface chemistry of base substrate and PEM films with conjugation of bioactive macromolecules.
There is evidence that the protomap exists without the need for sensory input (e.g., Armentano et al. 2007; Cholfin and Rubenstein 2007), although the size and location of the architectonic areas can be modulated by the modification of afferent input (Goldman-Rakic 1980), perhaps contributing to the observed variability in the localization with respect to the surrounding folding patterns.
Moreover, GR-mediated transcriptional regulation can be modulated by posttranslational modifications or by concurrent expression of dominant negative splice variants and other isoforms.
The range of cognitive outcomes could be modulated by epigenetic modifications that occur in response to environmental influences and affect gene transcription in cognitively relevant brain regions.
Gene transcription may be modulated by epigenetic modifications which involved different reactions such as methylation of DNA and phosphorylation, sumoylation, ubiquitination, or acetylation of histone proteins (Huber et al. 2007a).
We also note that the regulatory effects of PRC2 can be modulated by histone modifications associated with active chromatin, such as H3K4me3 [ 31], raising the possibility that PRC2 effects might differ depending on levels of histone acetylation.
In addition the transfer of Ca2+ across the IMM appears to be modulated by posttranslational modifications, such as phosphorylation [12,13], small diffusible messengers such as nucleotides [14] or polyamines [15], the proton concentration within the matrix of mitochondria [16] and Ca2+ itself [17,18], which all are thought to affect the activity of mitochondrial Ca2+ channels in intact cells.
The disagreement observed between Mn-SOD protein content and its activity in the AO adults is intriguing and suggests that Mn-SOD activity may be modulated by post-translational modification [66].
