Sentence examples for majority of secretory from inspiring English sources

(196 words) Since the majority of secretory proteins, such as antibodies, digestive enzymes, and hormones, are synthesized in the cytoplasm and are cotranslationally translocated into the lumen of the endoplasmic reticulum (ER) through a narrow channel called translocon on the ER membrane, they are initially located in the ER as unfolded and unmodified nascent polypeptides.

The majority of secretory and cell surface glycoproteins are N-glycosylated by the co-, or post-translational addition of the oligosaccharide, Glc3Man9GlcNAc2, that is transferred from the mature dolichol-linked oligosaccharide (DLO), Glc3Man9GlcNAc2-PP-dolichol, onto nascent polypeptides in the lumen of the endoplasmic reticulum (ER) by oligosaccharyltransferase (OST, see Fig. 1).

The Sec23A mutation is not lethal as presumably the majority of secretory cargoes can still become exported from the ER.

Upon weaning, a process of involution destroys the majority of secretory epithelium, leaving the ductal tree extant for repeated cycles of growth and differentiation.

The vast majority of secretory and integral membrane proteins acquire asparagine (N -linked glycaN -linked biosynthesis to ensure proper foldinglycansmbly, anduringficking out of the endoplasmic reticulum (ER).

The majority of secretory proteins are targeted to the endoplasmic reticulum (ER) via an N-terminal signal peptide, which helps to initiate translocation of nascent chains into the ER.

This involution period is characterized by proteolytic degradation of the extracellular matrix and elimination of the majority of the secretory epithelial cells by apoptosis [ 13, 14].

The majority of mammalian secretory and membrane proteins are modified through glycosylation: the covalent linkage of polysaccharide moieties (i.e., glycans) to either serine/threonine (O-linked) or asparagine (N-linked) residues [ 1].

Interestingly, the majority of the secretory salivary gland-expressed transcripts displayed a lower abundance after blood-feeding, suggesting that their products may have been employed for protein synthesis during feeding and eventually degraded, or their transcription had been shut down.

ER expansion and autophagy occurred in both the pancreatic endocrine cells and the zymogen-rich acinar cells by 6 dpf, suggesting that the ER-stress-induced pathology is subsequently propagated in the majority of the secretory cells of the digestive system (supplementary material Fig. S5D,E).

Thus the mechanism of acinar salivary hypofunction is reversible and the majority of loss of secretory function following 24 h of ligation was not due to cell death caused by either apoptosis or necrosis as both are irreversible.