"Calnexin" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A lectin found in ENDOPLASMIC RETICULUM membranes that binds to specific N-linked OLIGOSACCHARIDES found on newly synthesized proteins. It may play role in PROTEIN FOLDING or retention and degradation of misfolded proteins in the endoplasmic reticulum.
| Descriptor ID |
D037281
|
| MeSH Number(s) |
D12.644.360.372.311 D12.776.157.125.412.311 D12.776.476.387.311 D12.776.503.295 D12.776.543.162
|
| Concept/Terms |
Calnexin- Calnexin
- Phosphoprotein pp90
- pp90, Phosphoprotein
- IP90 Protein
- Integral Membrane Protein IP90
|
Below are MeSH descriptors whose meaning is more general than "Calnexin".
Below are MeSH descriptors whose meaning is more specific than "Calnexin".
This graph shows the total number of publications written about "Calnexin" by people in this website by year, and whether "Calnexin" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2005 | 1 | 0 | 1 |
| 2007 | 1 | 0 | 1 |
| 2009 | 0 | 1 | 1 |
| 2013 | 0 | 1 | 1 |
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Below are the most recent publications written about "Calnexin" by people in Profiles.
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Pathogenic brucellae replicate in human trophoblasts. J Infect Dis. 2013 Apr; 207(7):1075-83.
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Loss of specific chaperones involved in membrane glycoprotein biosynthesis during the maturation of human erythroid progenitor cells. J Biol Chem. 2009 May 22; 284(21):14547-57.
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Endoplasmic reticulum chaperones stabilize nicotinic receptor subunits and regulate receptor assembly. J Biol Chem. 2007 Oct 26; 282(43):31113-23.
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N-linked glycosylation is required for nicotinic receptor assembly but not for subunit associations with calnexin. J Biol Chem. 2005 Oct 07; 280(40):33800-10.
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Polypeptide substrate recognition by calnexin requires specific conformations of the calnexin protein. J Biol Chem. 2005 Sep 30; 280(39):33497-505.