Proteins following the secretory pathway acquire their proper tertiary and in certain cases also quaternary structures in the endoplasmic reticulum (ER). Incompletely folded species are retained in the ER and eventually ...

Folding of glycoproteins entering the secretory pathway is strictly surveyed in the endoplasmic reticulum by a quality control system. Folding intermediates and proteins irreparably misfolded are marked via glucosylation ...

I read with great interest a recent study by Poterico and Mestanza who described mutations in 30 SARS‐CoV‐2 genomes from South American countries (Argentina, Brazil, Chile, Colombia, Ecuador, and Peru). Next‐generation ...

N-glycosylation is the most drastic and frequent modification of secretory pathway proteins. N-glycans fulfill several biological and structural roles. In the early secretory pathway, these moieties are exploited as an ...

The N-glycan-dependent quality control of glycoprotein folding occurring in the endoplasmic reticulum prevents exit to Golgi of folding intermediates, irreparably misfolded glycoproteins, and incompletely assembled multimeric ...

Circulating immune complexes (CIC) have been described in the hemolytic uremic syndrome (HUS) in children. They may represent an epiphenomenon or could be related to the platelet activation and endothelial damage observed ...

The present study aimed to determine P-glycoprotein expression according to TVT cell morphology in 42 dogs with confirmed TVT, classified into lymphocytoid, plasmocytoid, and mixed. The chemotherapy efficiency was investigated ...

The experiments reported here were designed to characterize the intrinsic vitreous glycoproteins and to understand the process of their sulfation. Rabbits were injected intravitreally with S-35-sodium sulfate and killed ...