N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

By M. Wacker, D. Linton, P. Hitchen, M. Nita-Lazar, S. Haslam, S. North, M. Panico, H. Morris, A. Dell, B. Wren and 1 more. Science, 2002

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How researchers see this paper

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Biological roles of glycans (2016, positive): “To cite just a few examples, the following glycans were mostly unknown when the previous version of this review was being written: functional sialylation in the fly nervous system (181); O-fucose and O-glucose glycans on Notch (182-184), and O-fucose on thrombospondin repeats (185) ; mucin type O-gl”
Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems (2008, background): “A gene (pglK) encoding an IM-ABC transporter has also been discovered in a locus involved in the N-linked glycosylation pathway of Campylobacter jejuni (160, 512).”
Recombinant protein folding and misfolding in Escherichia coli (2004, background): “coli has allowed (non-eukaryotic) N-linked glycosylation of the model protein Acr”
Campylobacter jejuni: molecular biology and pathogenesis (2007, background): “The N -linked glycan that is assembled by the Pgl system consists of a heptasaccharide, unlike the tetradecasaccharide that is transferred by the eukaryotic N -linked-glycosylation machiner”
Posttranslational Protein Modification in Archaea (2005, background): “Analysis of the composition of the N-linked glycan moieties of archaeal S-layer glycoproteins has revealed the wide variety of saccharides available for protein glycosylation in Archaea, including galactofuranose, galactouronic acid, glucose, glucuronic acid, iduronic acid, mannose, N-acetylgalactos”