Oligosaccharyltransferase (OST) is a membrane-integral enzyme that catalyzes the transfer
of glycans from lipid-linked oligosaccharides (LLOs) onto asparagine side chains, the first …

Glycosylation of asparagine residues is a ubiquitous protein modification. This N-
glycosylation is essential in Eukaryotes, but principally nonessential in Prokaryotes …

Olefinic staples enhance α-helical content and conformational stability in peptides,
maintaining a structural scaffold that allows the emulation of specific regions of protein …

Staurosporine and its analogs (STA-analogs) are indolocarbazoles (ICZs) compounds able
to inhibit kinase proteins in a non-specific way, while present antimicrobial and cytostatic …

N-linked glycosylation is an enzymatic reaction in which an oligosaccharide is transferred en
bloc onto an asparagine residue of an acceptor polypeptide, catalyzed by …

Lipid-linked oligosaccharides (LLOs) play an important role in the N-glycosylation pathway
as the donor substrate of oligosaccharyltransferases (OSTs), which are responsible for the …

Cancer is an unsolved clinical problem and a challenge for the current medical science
given the limitations of conventional therapies. Systemic therapy presents serious …

The oligosaccharyltransferase of Campylobacter lari (PglB) catalyzes the glycosylation of
asparagine in the consensus sequence NXS/T, where X is any residue except proline …

The outer membrane factor CmeC of the efflux machinery CmeABC plays an important role
in conferring antibiotic and bile resistance to Campylobacter jejuni. Curiously, the proteins in …

Lipid-linked oligosaccharides (LLOs) are the substrates of oligosaccharyltransferases
(OSTs), enzymes that catalyze the en bloc transfer of a glycan chain during the process of N …