AbstractThe N-glycans found on eukaryotic glycoproteins occur in a vast range of different structures. A universal N-glycan core is attached to proteins during synthesis in the endoplasmic reticulum, and then diversity is generated as the proteins pass through the Golgi apparatus. Many of the Golgi-localised glycosyltransferases have now been identified in both yeast and mammalian cells, but it is still unclear how these enzymes are integrated into the Golgi and the rest of the cell so as to ensure efficient and specific processing of passing substrates. This review discusses the potential of the yeast system to address these issues
AbstractThe Golgi apparatus is known to modify and sort newly synthesized secretory proteins. Howeve...
<p>A: Standard N-glycosylation pathway in the ER. The early steps in N-glycosylation start with the ...
Secretory trafficking in eukaryotic cells occurs via membrane-enclosed organelles and vesicular inte...
AbstractThe N-glycans found on eukaryotic glycoproteins occur in a vast range of different structure...
N-linked glycosylation is an essential modification of secretory and membrane proteins in all eukary...
AbstractThe study of glycosylation and glycosylation enzymes has been instrumental for the advanceme...
N-glycosylation is an important feature of therapeutic and other industrially relevant proteins, and...
N-glycosylation is an important feature of therapeutic and other industrially relevant proteins, and...
N-glycosylation is an important feature of therapeutic and other industrially relevant proteins, and...
N-glycosylation is an important feature of therapeutic and other industrially relevant proteins, and...
N-glycosylation is an important feature of therapeutic and other industrially relevant proteins, and...
D ow nloaded from 2Abstract The yeast Saccharomyces cerevisiae is widely regarded as being only capa...
Outer-chain addition of mannose residues to yeast glycoproteins occurs in the Golgi compartment of ...
Glycosylation of proteins is important for protein stability, secretion, and localization. In this s...
N-linked protein glycosylation is a highly conserved and an essential protein modification found thr...
AbstractThe Golgi apparatus is known to modify and sort newly synthesized secretory proteins. Howeve...
<p>A: Standard N-glycosylation pathway in the ER. The early steps in N-glycosylation start with the ...
Secretory trafficking in eukaryotic cells occurs via membrane-enclosed organelles and vesicular inte...
AbstractThe N-glycans found on eukaryotic glycoproteins occur in a vast range of different structure...
N-linked glycosylation is an essential modification of secretory and membrane proteins in all eukary...
AbstractThe study of glycosylation and glycosylation enzymes has been instrumental for the advanceme...
N-glycosylation is an important feature of therapeutic and other industrially relevant proteins, and...
N-glycosylation is an important feature of therapeutic and other industrially relevant proteins, and...
N-glycosylation is an important feature of therapeutic and other industrially relevant proteins, and...
N-glycosylation is an important feature of therapeutic and other industrially relevant proteins, and...
N-glycosylation is an important feature of therapeutic and other industrially relevant proteins, and...
D ow nloaded from 2Abstract The yeast Saccharomyces cerevisiae is widely regarded as being only capa...
Outer-chain addition of mannose residues to yeast glycoproteins occurs in the Golgi compartment of ...
Glycosylation of proteins is important for protein stability, secretion, and localization. In this s...
N-linked protein glycosylation is a highly conserved and an essential protein modification found thr...
AbstractThe Golgi apparatus is known to modify and sort newly synthesized secretory proteins. Howeve...
<p>A: Standard N-glycosylation pathway in the ER. The early steps in N-glycosylation start with the ...
Secretory trafficking in eukaryotic cells occurs via membrane-enclosed organelles and vesicular inte...