Calreticulin (CALR) is an endoplasmic reticulum (ER)-resident protein involved in a
spectrum of cellular processes. In healthy cells, CALR operates as a chaperone and Ca2+ …

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 …

Dendritic spines, the postsynaptic compartments of excitatory neurotransmission, have
different shapes classified from 'stubby'to 'mushroom-like'. Whereas mushroom spines are …

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

The field of endoplasmic reticulum (ER) stress in mammalian cells has expanded rapidly
during the past decade, contributing to understanding of the molecular pathways that allow …

Mitochondria-endoplasmic reticulum (ER) contact sites (MERCS) are morpho-functional
units, formed at the loci of close apposition of the ER-forming endomembrane and outer …

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 …

Calreticulin is a calcium-binding chaperone that has several functions in the immune
response. In the endoplasmic reticulum (ER), calreticulin facilitates the folding of major …