Matches in UGent Biblio for { <https://biblio.ugent.be/publication/4389955#aggregation> ?p ?o. }
Showing items 1 to 47 of
47
with 100 items per page.
- aggregation classification "A1".
- aggregation creator B799634.
- aggregation creator B799635.
- aggregation creator B799636.
- aggregation creator B799637.
- aggregation creator B799638.
- aggregation creator B799639.
- aggregation creator B799640.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2014".
- aggregation format "application/pdf".
- aggregation hasFormat 4389955.bibtex.
- aggregation hasFormat 4389955.csv.
- aggregation hasFormat 4389955.dc.
- aggregation hasFormat 4389955.didl.
- aggregation hasFormat 4389955.doc.
- aggregation hasFormat 4389955.json.
- aggregation hasFormat 4389955.mets.
- aggregation hasFormat 4389955.mods.
- aggregation hasFormat 4389955.rdf.
- aggregation hasFormat 4389955.ris.
- aggregation hasFormat 4389955.txt.
- aggregation hasFormat 4389955.xls.
- aggregation hasFormat 4389955.yaml.
- aggregation isPartOf urn:issn:1087-0156.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Medicine and Health Sciences".
- aggregation title "GlycoDelete engineering of mammalian cells simplifies N-glycosylation of recombinant proteins".
- aggregation abstract "Heterogeneity in the N-glycans on therapeutic proteins causes difficulties for protein purification and process reproducibility and can lead to variable therapeutic efficacy. This heterogeneity arises from the multistep process of mammalian complex-type N-glycan synthesis. Here we report a glycoengineering strategy—which we call GlycoDelete—that shortens the Golgi N-glycosylation pathway in mammalian cells. This shortening results in the expression of proteins with small, sialylated trisaccharide N-glycans and reduced complexity compared to native mammalian cell glycoproteins. GlycoDelete engineering does not interfere with the functioning of N-glycans in protein folding, and the physiology of cells modified by GlycoDelete is similar to that of wild-type cells. A therapeutic human IgG expressed in GlycoDelete cells had properties, such as reduced initial clearance, that might be beneficial when the therapeutic goal is antigen neutralization. This strategy for reducing N-glycan heterogeneity on mammalian protins could lead to more consistent performance of therapeutic proteins and modulation of biopharmaceutical functions.".
- aggregation authorList BK1171733.
- aggregation endPage "489".
- aggregation issue "5".
- aggregation startPage "485".
- aggregation volume "32".
- aggregation aggregates 4389960.
- aggregation isDescribedBy 4389955.
- aggregation similarTo nbt.2885.
- aggregation similarTo LU-4389955.