Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1203342#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B444358.
- aggregation creator B444359.
- aggregation creator B444360.
- aggregation creator B444361.
- aggregation creator B444362.
- aggregation creator B444363.
- aggregation creator B444364.
- aggregation creator person.
- aggregation date "2006".
- aggregation format "application/pdf".
- aggregation hasFormat 1203342.bibtex.
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- aggregation isPartOf urn:issn:0261-4189.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides".
- aggregation abstract "Translocation of lipid-linked oligosaccharide (LLO) intermediates across membranes is an essential but poorly understood process in eukaryotic and bacterial glycosylation pathways. Membrane proteins defined as translocases or flippases are implicated to mediate the translocation reaction. The membrane protein Wzx has been proposed to mediate the translocation across the plasma membrane of lipopolysaccharide (LPS) O antigen subunits, which are assembled on an undecaprenyl pyrophosphate lipid carrier. Similarly, PglK (formerly WlaB) is a Campylobacter jejuni-encoded ABC-type transporter proposed to mediate the translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate involved in the recently identified bacterial N-linked protein glycosylation pathway. A combination of genetic and carbohydrate structural analyses defined and characterized flippase activities in the C. jejuni N-linked protein glycosylation and the Escherichia coli LPS O antigen biosynthesis. PglK displayed relaxed substrate specificity with respect to the oligosaccharide structure of the LLO intermediate and complemented a wzx deficiency in E. coli O-antigen biosynthesis. Our experiments provide strong genetic evidence that LLO translocation across membranes can be catalyzed by two distinct proteins that do not share any sequence similarity.".
- aggregation authorList BK775640.
- aggregation endPage "976".
- aggregation issue "5".
- aggregation startPage "967".
- aggregation volume "25".
- aggregation aggregates 1203363.
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