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N-linked glycosylation is an essential modification of secretory and membrane proteins in all eukaryotic cells.
In eukaryotes, N-linked protein glycosylation is the most common modification of secretory proteins and is coupled to protein translocation and folding.
It is the site of synthesis, folding and modification of secretory and cell-surface proteins and serves many essential functions, including the production of the components of cellular membranes, proteins, lipids and sterols (Hebert and Molinari 2007).
Although our present investigation cannot distinguish between these possibilities, it demonstrates the existence of complex rhythms in the cellular activities associated with the formation and modification of secretory granules.
Mannose is one of the core sugar building blocks to form the mature LLO, which is used as the oligosaccharide donor for modification of secretory proteins on asparagine residues (i.e. N-linked glycosylation).
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The endoplasmic reticulum (ER) is not only a home for folding and posttranslational modifications of secretory proteins but also a reservoir for intracellular Ca2+.
A variety of Ca2+-dependent functions occur within the Golgi, which include post-translational modifications of secretory proteins [ 40], formation of COPI (coatamer protein I) coats on Golgi ER transport vesicles [ 41] and both anterograde and retrograde vesicular transport through and to the Golgi complex [ 42, 43].
It can be generally assumed that it is either involved in post-translational protein modification, transport of secretory proteins, cell signalling regulation or simply maintenance of Golgi apparatus function.
So it can be hypothesized that GH excess may affect PTH secretory dynamics in patients with acromegaly, but potentially negative bone effects of the modifications of PTH secretory pattern in acromegaly still remain to be investigated.
The Golgi complex is the site of the modification, completion, and export of secretory proteins and glycoproteins.
These profiling results indicated that HTorAΔE in the ER involved defects in the synthesis, modification, folding, assembly and trafficking of secretory and membrane proteins that translocate to the cell surface or to intracellular organelles.
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