At first glance, archaea and bacteria look alike; however, the composition of the archaeal
cell envelope is fundamentally different from the bacterial cell envelope. With just one …

Investigations into bacterial protein glycosylation continue to progress rapidly. It is now
established that bacteria possess both N-linked and O-linked glycosylation pathways that …

Asparagine-linked glycosylation is a post-translational modification of proteins containing
the conserved sequence motif Asn-X-Ser/Thr. The attachment of oligosaccharides is …

Dilysine motifs in cytoplasmic domains of transmembrane proteins are signals for their
continuous retrieval from the Golgi back to the endoplasmic reticulum (El?). We describe a …

Background Although the origin of the eukaryotic cell has long been recognized as the
single most profound change in cellular organization during the evolution of life on earth …

Aims This review is intended to update our previous discussion on the chemoenzymatic
synthesis of carbohydrates and glycoconjugates,(1) with new emphasis placed on …

SUMMARY N-glycosylation of proteins is one of the most prevalent posttranslational
modifications in nature. Accordingly, a pathway with shared commonalities is found in all …

Protein families with functionally diverse members can illuminate the structural determinants
of protein function and the process by which protein structure and function evolve. To identify …

Asparagine-linked glycosylation involves the sequential assembly of an oligosaccharide
onto a polyisoprenyl donor, followed by the en bloc transfer of the glycan to particular …

Protein glycosylation is widespread throughout all three domains of life. Bacterial protein N-
glycosylation and its application to engineering recombinant glycoproteins continue to be …