Protein traffic is of critical importance for normal cellular physiology. In eukaryotes, spherical
transport vesicles move proteins and lipids from one internal membrane-bound …

Analysis of the human genome reveals that approximately a third of all open reading frames
code for proteins that enter the endoplasmic reticulum (ER), demonstrating the importance of …

The unfolded protein response (UPR) controls the levels of molecular chaperones and
enzymes involved in protein folding in the endoplasmic reticulum (ER). We recently isolated …

Obesity and insulin resistance are associated with deposition of triglycerides in tissues other
than adipose tissue. Previously, we showed that a missense mutation (I148M) in PNPLA3 …

Calreticulin is an ER (endoplasmic reticulum) luminal Ca2+-buffering chaperone. The
protein is involved in regulation of intracellular Ca2+ homoeostasis and ER Ca2+ capacity …

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

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 …

Nearly all resident proteins of the organelles along the secretory pathway, as well as
proteins that are expressed at the cell surface or secreted from the cell, are first co …

Calnexin and calreticulin are related proteins that comprise an ER chaperone system that
ensures the proper folding and quality control of newly synthesized glycoproteins. The …

The endoplasmic reticulum is a centrally located organelle which affects virtually every
cellular function. Its unique luminal environment consists of Ca2+ binding chaperones …