Asparagine-linked glycosylation: specificity and function of oligosaccharyl transferase.
Imperiali
B
B
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.
Hendrickson
T L
TL
D000595:Amino Acid Sequence; D000818:Animals; D001216:Asparagine / Q000737:chemistry / Q000378:metabolism*; D002240:Carbohydrate Sequence; D006023:Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006031:Glycosylation; D006602:Hexosyltransferases; D066298:In Vitro Techniques; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D013379:Substrate Specificity; D014166:Transferases / Q000737:chemistry / Q000378:metabolism*
D006023:Glycoproteins; D008565:Membrane Proteins; D009842:Oligopeptides; D009844:Oligosaccharides; D001216:Asparagine; D014166:Transferases; D006602:Hexosyltransferases; C025620:dolichyl-diphosphooligosaccharide - protein glycotransferase