カルネキシン
関連文献

Protein quality control, retention, and degradation at the endoplasmic reticulum. International Review of Cell and Molecular Biology. 292. (2011). pp. 197–280. doi:10.1016/B978-0-12-386033-0.00005-0. ISBN 9780123860330. PMID 22078962
“The evolutionary history of calreticulin and calnexin genes in green plants”. Genetica 139 (2):  225–9. (Feb 2011). doi:10.1007/s10709-010-9544-y. PMID 21222018.
“Protein folding and quality control in the endoplasmic reticulum”. Current Opinion in Cell Biology 16 (4):  343–9. (Aug 2004). doi:10.1016/j.ceb.2004.06.012. hdl:1874/5106. PMID 15261665.
“Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes”. Electrophoresis 13 (12):  960–9. (Dec 1992). doi:10.1002/elps.11501301199. PMID 1286667.
“The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene”. Proceedings of the National Academy of Sciences of the United States of America 89 (18):  8452–6. (Sep 1992). Bibcode: 1992PNAS...89.8452G. doi:10.1073/pnas.89.18.8452. PMC 49938. PMID 1326756. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC49938/.
“Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator”. The Journal of Biological Chemistry 269 (17):  12784–8. (Apr 1994). doi:10.1016/S0021-9258(18)99944-8. PMID 7513695.
“The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit strikingly different levels in quiescent keratinocytes as compared to their proliferating normal and transformed counterparts: cDNA cloning and expression of calnexin”. Electrophoresis 15 (3–4):  482–90. (1992). doi:10.1002/elps.1150150166. PMID 8055875.
“Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5”. Biochemistry 33 (11):  3229–36. (Mar 1994). doi:10.1021/bi00177a013. PMID 8136357.
“The integrin chains beta 1 and alpha 6 associate with the chaperone calnexin prior to integrin assembly”. The Journal of Biological Chemistry 269 (16):  12263–8. (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”. Experimental Cell Research 222 (1):  77–83. (Jan 1996). doi:10.1006/excr.1996.0010. PMID 8549676.
“Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin”. The Journal of Biological Chemistry 271 (1):  97–103. (Jan 1996). doi:10.1074/jbc.271.1.97. PMID 8550632.
“A novel interleukin-12 p40-related protein induced by latent Epstein-Barr virus infection in B lymphocytes”. Journal of Virology 70 (2):  1143–53. (Feb 1996). doi:10.1128/JVI.70.2.1143-1153.1996. PMC 189923. PMID 8551575. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC189923/.
“A "double adaptor" method for improved shotgun library construction”. Analytical Biochemistry 236 (1):  107–13. (Apr 1996). doi:10.1006/abio.1996.0138. PMID 8619474.
“Calnexin associates exclusively with individual CD3 delta and T cell antigen receptor (TCR) alpha proteins containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexes”. The Journal of Biological Chemistry 271 (16):  9660–5. (Apr 1996). doi:10.1074/jbc.271.16.9660. PMID 8621641.
“The glut 1 glucose transporter interacts with calnexin and calreticulin”. The Journal of Biological Chemistry 271 (23):  13691–6. (Jun 1996). doi:10.1074/jbc.271.23.13691. PMID 8662691.
“Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport”. 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. (Feb 1997). doi:10.1083/jcb.136.3.555. PMC 2134297. PMID 9024687. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2134297/.
“Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular chaperones”. Proceedings of the National Academy of Sciences of the United States of America 94 (5):  1884–9. (Mar 1997). Bibcode: 1997PNAS...94.1884W. doi:10.1073/pnas.94.5.1884. PMC 20012. PMID 9050874. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC20012/.
“Large-scale concatenation cDNA sequencing”. Genome Research 7 (4):  353–8. (Apr 1997). doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139146/.