Exact(1)
For example, is the facultative heterochromatin aggregating inside the nucleus in foci, and is this colocalisation lost upon activation of the genes during meiosis and does this then have an influence on the expression of nearby genes?
Similar(59)
When the housekeeper fails, proteins seem to aggregate inside nerve cells, which may be contributing to their destruction.
If cells are under stress or the formation of damaged or misfolded proteins exceeds the capacity of protein degradation, the misfolded proteins aggregate inside the cells, which could eventually choke the cell to death.
For instance, around a H × f factor of 7 × 109 A/m × s, non-interacting monodispersed cubic IOMNPs of 19 and 35 nm exhibit SAR values of 1000 and 1391 W/gFe, respectively [22, 26], whereas 23 nm cubic IOMNPs aggregated inside 200-nm magnetic nano-beads display a SAR values of 194 W/gFe [57].
Biological response of the cell culture, expressed as dark and photocytotoxicity as well as fluorescence of drug molecules loaded in the multilayer vehicles, analyzed by the FACS and CLSM techniques, have indicated that the delivered IR-786 did not aggregate inside the cells and could, therefore, act as an effective third-generation photosensitizing agent.
In-situ hybridization for BFF showed amplified expressions within signet-ring cells, aggregated inside interacting ampullae, supporting its relevancy to Botryllus rejection process.
These results demonstrate that the formation of multiple protein layers is localized in specific nanometric structures; in fact, part of the surface pores is filled by proteins that aggregate inside the pores.
Number and brightness analysis suggests that BaP does not aggregate inside Chlorella sp. (average brightness = 5.330), while it aggregates in the supernatant.
This attenuation was dependent on the PrP signal peptide and, when bypassed, led to its increased propensity to aggregate inside the ER.
The prolamins (which are related to the wheat gluten proteins) aggregate inside the ER lumen aided by the chaperone BiP and form type-I protein bodies (PB-Is) (Li et al., 1993) while the glutelins are translated on separate sub-domains of the ER and transported via the Golgi apparatus and vesicles into type-II protein bodies (PB-IIs) of vacuolar origin.
In some cells, huge vacuoles with aggregates inside were observed.
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