Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1203449#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B585210.
- aggregation creator B585211.
- aggregation creator B585212.
- aggregation creator B585213.
- aggregation creator B585214.
- aggregation creator B585215.
- aggregation creator B585216.
- aggregation creator person.
- aggregation date "2006".
- aggregation format "application/pdf".
- aggregation hasFormat 1203449.bibtex.
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- aggregation isPartOf urn:issn:0036-8075.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase".
- aggregation abstract "N-linked protein glycosylation is found in all domains of life. In eukaryotes, it is the most abundant protein modification of secretory and membrane proteins, and the process is coupled to protein translocation and folding. We found that in bacteria, N-glycosylation can occur independently of the protein translocation machinery. In an in vitro assay, bacterial oligosaccharyltransferase glycosylated a folded endogenous substrate protein with high efficiency and folded bovine ribonuclease A with low efficiency. Unfolding the eukaryotic substrate greatly increased glycosylation. We propose that in the bacterial system, glycosylation sites are located in flexible parts of folded proteins, whereas the eukaryotic cotranslational glycosylation evolved to a mechanism presenting the substrate in a flexible form before folding.".
- aggregation authorList BK938797.
- aggregation endPage "1150".
- aggregation issue "5802".
- aggregation startPage "1148".
- aggregation volume "314".
- aggregation aggregates 1203459.
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