Calnexin is a chaperone, characterized by assisting protein folding and quality control, ensuring that only properly folded and assembled proteins proceed further along the secretory pathway. …

Calnexin is a type I integral endoplasmic reticulum (ER) membrane protein with an N-terminal domain that resides in the lumen of the ER and a C-terminal domain that extends into the …

In this chapter we present the evidence that calnexin (CNX) and calreticulin (CRT) function as molecular chaperones to assist in the folding and subunit assembly of the majority of Asn …

2023年1月24日 · Calnexin is a type I integral endoplasmic reticulum (ER) membrane protein with an N-terminal domain that resides in the lumen of the ER and a C-terminal domain that …

2024年12月24日 · This gene encodes a member of the calnexin family of molecular chaperones. The encoded protein is a calcium-binding, endoplasmic reticulum (ER)-associated protein that …

Calreticulin and calnexin are Ca2+-binding proteins with chaperone activity in the endoplasmic reticulum. These proteins have been eliminated by gene replacement in Dictyostelium, the …

Calnexin is a new type of molecular chaperone that interacts with many nascent membrane and soluble proteins of the secretory pathway. Calnexin is unrelated to molecular chaperones of …

2006年1月19日 · Here, we investigate whether calnexin functions as a chaperone for Rh1 and whether mutations in calnexin lead to neurodegeneration. In addition to its role as a molecular …

Calnexin, a single-pass membrane protein, and calreticulin, a soluble protein, are lectins (sugar-binding proteins) that bind to N-linked oligosaccharides containing a single glucose residue. …

Gutiérrez et al. investigated the role of calnexin, an ER chaperone that interacts with SERCA, the ATPase that pumps Ca 2+ into the ER, in mitochondrial bioenergetics. The authors found that …