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Roles of N-linked glycans in the endoplasmic reticulum.
From a process involved in cell wall synthesis in archaea and some bacteria, N-linked glycosylation has evolved into the most common covalent protein modification in eukaryotic cells. The sugars areExpand
Intracellular functions of N-linked glycans.
TLDR
The division of synthesis and processing between the ER and the Golgi complex represents an evolutionary adaptation that allows efficient exploitation of the potential of oligosaccharides. Expand
The dolichol pathway of N-linked glycosylation.
  • P. Burda, M. Aebi
  • Biology, Medicine
  • Biochimica et biophysica acta
  • 6 January 1999
TLDR
It is suggested that N-linked glycosylation in eukaryotes and in archaea share a common evolutionary origin and the function of the lipid carrier dolichol in oligosaccharide assembly is discussed. Expand
X-ray structure of a bacterial oligosaccharyltransferase
TLDR
The X-ray structure of a bacterial OST, the PglB protein of Campylobacter lari, in complex with an acceptor peptide is reported, which defines the fold of STT3 proteins and provides insight into glycosylation sequon recognition and amide nitrogen activation, both of which are prerequisites for the formation of the N-glycosidic linkage. Expand
Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum
TLDR
The function of the Htm1 protein is defined as an α1,2-specific exomannosidase that generates the Man7GlcNAc2 oligosaccharide with a terminalα1,6-linked mannosyl residue on degradation substrates that triggers the ubiquitin-proteasome–dependent hydrolysis of these glycoproteins. Expand
N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.
TLDR
It is demonstrated that a functional N-linked glycosylation pathway could be transferred into Escherichia coli and opened up the possibility of engineering permutations of recombinant glycan structures for research and industrial applications. Expand
Degradation of Misfolded Endoplasmic Reticulum Glycoproteins in Saccharomyces cerevisiae Is Determined by a Specific Oligosaccharide Structure
TLDR
Results suggest the presence of a Man8GlcNAc2-binding lectin involved in targeting of misfolded glycoproteins to degradation in S. cerevisiae and suggest a role for the Man8glc NAc2 oligosaccharide in the degradation process. Expand
N-linked protein glycosylation in the ER.
  • M. Aebi
  • Biology, Medicine
  • Biochimica et biophysica acta
  • 1 November 2013
TLDR
This article summarizes the current knowledge of the N-glycosylation pathway in the ER that results in the covalent attachment of an oligosaccharide to asparagine residues of polypeptide chains and focuses on the model organism Saccharomyces cerevisiae. Expand
Htm1p, a mannosidase‐like protein, is involved in glycoprotein degradation in yeast
TLDR
The results indicate that although Htm1p is not involved in processing of N‐linked oligosaccharides, it is required for their proteolytic degradation, and it is proposed that this mannosidase homolog is a lectin that recognizes Man8GlcNAc2 oligosACcharides that serve as signals in the degradation pathway. Expand
Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli.
TLDR
E. coli cells are engineered in a way that two different pathways, protein N-glycosylation and lipopolysaccharide (LPS) biosynthesis, converge at the step in which PglB, the key enzyme of the C. jejuni N-gresylation system, transfers O polysaccharides from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein. Expand
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