Influenza viruses replicate within the nucleus of the host cell. This uncommon RNA virus trait
provides influenza with the advantage of access to the nuclear machinery during replication …

ER-phagy (reticulophagy) defines the degradation of portions of the endoplasmic reticulum
(ER) within lysosomes or vacuoles. It is part of the self-digestion (ie, autophagic) programs …

The endoplasmic reticulum (ER) is the major folding compartment for secreted and
membrane proteins and is the site of a specific chaperone system, the calnexin cycle, for …

▪ Abstract 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 …

Protein folding in the endoplasmic reticulum (ER) is monitored by ER quality control (ERQC)
mechanisms. Proteins that pass ERQC criteria traffic to their final destinations through the …

In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum
(ER), including the role of three types of covalent modifications: signal peptide removal, N …

The endoplasmic reticulum (ER) plays a critical role in the synthesis and chaperoning of
membrane-associated and secreted proteins. The membrane is also an important site of …

A substantial fraction of eukaryotic gene products are synthesized by ribosomes attached at
the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter …

Asparagine-linked glycans (N-glycans) are displayed on the majority of proteins synthesized
in the endoplasmic reticulum (ER). Removal of the outermost glucose residue recruits the …

In 1997, 18 confirmed cases of human influenza arising from multiple independent
transmissions of H5N1 viruses from infected chickens were reported from Hong Kong. To …