Inhibition of asparagine-linked glycosylation by incorporation of a threonine analog into nascent peptide chains.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Primary structural requirements for the enzymatic formation of the N-glycosidic bond in glycoproteins. Studies with natural and synthetic peptides.
2. Enzymatic conversion of proteins to glycoproteins.
3. Studies on the acceptor specificity of asparagine-N -glycosyl-transferase from rat liver
4. Primary structural requirements for the enzymatic formation of the N-glycosidic bond in glycoproteins. Studies with alpha-lactalbumin
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3. The Ost1p Subunit of Yeast Oligosaccharyl Transferase Recognizes the Peptide Glycosylation Site Sequence, -Asn-X-Ser/Thr-;Journal of Biological Chemistry;1999-02
4. Asparagine-linked glycosylation: Specificity and function of oligosaccharyl transferase;Bioorganic & Medicinal Chemistry;1995-12
5. Chapter 5 Biosynthesis 7. How Can N-Linked Glycosylation and Processing Inhibitors be Used to Study Carbohydrate Synthesis and Function;New Comprehensive Biochemistry;1995
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