カルネキシン
Proceedings of the National Academy of Sciences of the United States of America 93 (18): 9606–11. (Sep 1996). Bibcode: 1996PNAS...93.9606L. doi:10.1073/pnas.93.18.9606. PMC 38475. PMID 8790377. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC38475/.
“Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit”. The Journal of Biological Chemistry 271 (44): 27509–16. (Nov 1996). doi:10.1074/jbc.271.44.27509. PMID 8910335.
“Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum”. The Journal of Cell Biology 136 (3): 555–65.
(Apr 1994). doi:10.1016/S0021-9258(17)32710-2. PMID 8163531.
“Retention of unassembled components of integral membrane proteins by calnexin”. Science 263 (5145): 387–90. (Jan 1994). Bibcode: 1994Sci...263..387R. doi:10.1126/science.8278814. PMID 8278814.
“Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin)”. The Journal of Biological Chemistry 268 (13): 9585–92. (May 1993). doi:10.1016/S0021-9258(18)98391-2. PMID 8486646.
“Retinol binding protein and transthyretin are secreted as a complex formed in the endoplasmic reticulum in HepG2 human hepatocarcinoma cells”.