Sharon S. Krag

TL;DR: The characterization of the dolichol pyrophosphate biosynthetic pathway and the recent identification of potential rate limiting enzymes in yeast and mammalian cells has made it possible to investigate their role in site occupancy, and insights into the location and residues in and around the acceptor tripeptide sequon suggest an influence on N-glycan site occupancy.

TL;DR: This first large-scale proteomic analysis of Chinese hamster ovary (CHO) cells will enhance the knowledge base about CHO capabilities for recombinant expression and provide information useful in cell engineering efforts aimed at modifying CHO cellular functions.

TL;DR: The glycosylation defect may alter adversely the function of several glycoproteins in the mutant, including that of the mannose 6-phosphate receptor, but it appears to have no effect on the formation or function of theMannoses 6- phosphate recognition marker on acid hydrolases of B4-2-1.

TL;DR: How organisms in each basic domain of life synthesize the polyisoprenoids that they utilize for N-linked glycosylation is elucidated and the subsequent modifications of the lipid to generate a lipid-linked oligosaccharide is discussed.

TL;DR: Changes in dolichyl phosphate levels were not detected under a variety of conditions where the levels of enzyme activity utilizing this substrate were varied, and all three enzymes appear to have access to the same pool of dolicyl phosphate, and further, to have similar Km values for dolICHyl phosphate.