2004
DOI: 10.1016/j.sbi.2004.09.001
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Biosynthesis of human-type N-glycans in heterologous systems

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Cited by 62 publications
(45 citation statements)
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“…In general secretory glycoproteins, the high-mannosetype glycans are extensively trimmed by Golgi mannosidases a n d t h e n s u b j e c t e d t o N -a c e t y l g l u c o s a m i n y l a t i o n , galactosylation, sialylation, and/or sulfation in the Golgi apparatus (1,2). In marked contrast, the high-mannosetype glycans of lysosomal enzymes undergo specific modifications of M6P residues in the cis-Golgi.…”
Section: B Role Of P-type Lectins and Mrh Domain-containing Proteinsmentioning
confidence: 99%
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“…In general secretory glycoproteins, the high-mannosetype glycans are extensively trimmed by Golgi mannosidases a n d t h e n s u b j e c t e d t o N -a c e t y l g l u c o s a m i n y l a t i o n , galactosylation, sialylation, and/or sulfation in the Golgi apparatus (1,2). In marked contrast, the high-mannosetype glycans of lysosomal enzymes undergo specific modifications of M6P residues in the cis-Golgi.…”
Section: B Role Of P-type Lectins and Mrh Domain-containing Proteinsmentioning
confidence: 99%
“…In eukaryotic cells, N-linked glycoproteins are subjected to diverse modifications and transported through the endoplasmic reticulum (ER) via the Golgi apparatus to their final destinations inside or outside the cell (1,2). The sugar chain is initially introduced by oligosaccharyltransferase as a high-mannose-type tetradecasaccharide (Glc 3 Man 9 GlcNAc 2 ) ( Fig.…”
Section: A Introductionmentioning
confidence: 99%
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“…Therefore, using a human DNA sequence does not guarantee that the molecule will be glycosylated as it is when synthesized by the human bodies. The peptide sequence may determine where glycosylation is added to the protein but the mix of glycosyltransferases, within the cell the protein is expressed in and even the conditions under which those cells are cultured will determine what oligosaccharide structures are added to the molecule (Raju et al, 2003;Betenbaugh et al, 2004). Covalent binding between the sugars and the peptide chain is a central part of the structure of glycoproteins.…”
Section: Gene Constructions For Expression In Mammary Glandmentioning
confidence: 99%
“…An approach for improving the pharmacological properties of higher molecular weight drug candidates, analogous to Lipinski's guidelines for the modification of small molecule drugs, has been applied for protein therapeutics such as recombinant antibodies and protein toxins used in cancer treatment. In these cases, the amino acid sequences of recombinant proteins have been ''humanized'' by genetic engineering to avoid immunogenicity [61,62] and their glycosylation patterns have been modified to increase serum half-life [63,64]. These efforts, undertaken with actual proteins, illuminate design features that can benefit the development of protein mimics, dendrimers.…”
Section: 5mentioning
confidence: 99%