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 …

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 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 …

Calcium signaling underlies much of physiology. Almost all the Ca2+ in the cytoplasm is
bound to buffers, with typically only∼ 1% being freely ionized at resting levels in most cells …

Generation, Control, and Processing of Cellular Calcium Signals Page 1 107 1040-9238/01/$.50
© 2001 by CRC Press LLC Critical Reviews in Biochemistry and Molecular Biology, 36(2):107–260 …

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 ubiquitous Ca2+ binding protein, located in the endoplasmic reticulum
lumen, which has been implicated in many diverse functions including: regulation of …

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 …

Four genes expressed in the olfactory system of Drosophila melanogaster have been
identified by subtractive hybridization. Two of these genes, OS-E and OS-F, are related to …