Calnexin acts as a molecular chaperone during the folding of glycoprotein B of human cytomegalovirus.

Eitemau Tebyg

• Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum
  Cyhoeddwyd: (1995)
• The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules.
  gan: Vassilakos, A, et al.
  Cyhoeddwyd: (1996)
• Rapid degradation of the heavy chain of class I major histocompatibility complex antigens in the endoplasmic reticulum of human cytomegalovirus-infected cells.
  gan: Yamashita, Y, et al.
  Cyhoeddwyd: (1994)
• Cotranslational folding and calnexin binding during glycoprotein synthesis.
  gan: Chen, W, et al.
  Cyhoeddwyd: (1995)
• Folding of Insulin Receptor Monomers Is Facilitated by the Molecular Chaperones Calnexin and Calreticulin and Impaired by Rapid Dimerization
  gan: Bass, Joseph, et al.
  Cyhoeddwyd: (1998)