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Neuronal activity triggers the dispersal of the Golgi into dendritic Golgi satellites, leading to reshaping of the neuronal surface glycoproteome through processing of glycans to mature, sialic acid-containing forms.

Imaging, quantitative immunoblotting and mass spectrometry reveal that hundreds of surface-expressed neuronal membrane proteins exhibit atypical glycosylation profiles, resulting in changes in protein half-life and synaptic responses.

Molecular dynamics simulation assisted engineering of recombinant soluble human ACE2 N-glycosylation by site-directed mutagenesis or glycosidase treatment yields a superior SARS-CoV-2 decoy receptor.

Multiple lines of evidence demonstrate that a single N-glycan on one receptor influences the strength of a cytotoxic response elicited by natural killer cells following stimulation with an antibody-coated target.

An in silico analysis of gap junction proteins supports the hypothesis that connexins replaced the primordial innexins in chordate gap junctions due to an evolutionary bottleneck.

N-glycanase 1 is required for a BMP autoregulatory loop in the visceral mesoderm and for intestinal development in Drosophila.

A critical role for glycosylation on viral entry and methods to use this knowledge to reduce SARS-CoV-2 infectivity has been demonstrated.

Structurally dissimilar N-glycans can be functionally equivalent, and are produced via a self-correcting feature of the Golgi.

Natural substrates of the central endoplasmic reticulum quality control glycoprotein sensors UDP-glucose:glycoproteinglucosyltransferase (UGGT)1 and UGGT2 were identified using a glycoproteomics approach and the role for their modification was explored.

An ion transporter is hyperglycosylated and 50% less functional in NGLY1-deficient cells, potentially explaining several symptoms of NGLY1 deficiency such as lack of sweat and tears.