Membrane-bound and soluble proteins of the secretory pathway are commonly glycosylated
in the endoplasmic reticulum. These adducts have many biological functions, including …

Complex processes are involved in the protection of cells and organisms by heat shock
proteins (hsps). Aberrant protein production due to high temperatures is prevented by the …

N-linked oligosaccharides arise when blocks of 14 sugars are added cotranslationally to
newly synthesized polypeptides in the endoplasmic reticulum (ER). These glycans are then …

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 …

The endoplasmic reticulum (ER) has a quality-control system for'proof-reading'newly
synthesized proteins, so that only native conformers reach their final destinations. Non …

Neurodegenerative disorders are characterized by a collapse in proteostasis, as shown by
the accumulation of insoluble protein aggregates in the brain. Proteostasis involves a …

Protein folding is a complex, error-prone process that often results in an irreparable protein
by-product. These by-products can be recognized by cellular quality control machineries …

The folding of most newly synthesized proteins in the cell requires the interaction of a variety
of protein cofactors known as molecular chaperones. These molecules recognize and bind …

Using a pulse-chase approach combined with immunoprecipitation, we showed that newly
synthesized influenza virus hemagglutinin (HA) and vesicular stomatitis virus G protein …