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Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins.
Calreticulin (CRT) is thought to be a molecular chaperone that interacts with glycoproteins exclusively through a lectin site specific for monoglucosylated oligosaccharides. However, this chaperone function has never been directly demonstrated nor is it clear how lectin-oligosaccharide interactions...
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| Main Authors: | , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
1999
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1171734/ https://ncbi.nlm.nih.gov/pubmed/10581245 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/18.23.6718 |
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