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Lectin-deficient Calreticulin Retains Full Functionality as a Chaperone for Class I Histocompatibility Molecules

Calreticulin is a molecular chaperone of the endoplasmic reticulum that uses both a lectin site specific for Glc(1)Man(5-9)GlcNAc(2) oligosaccharides and a polypeptide binding site to interact with nascent glycoproteins. The latter mode of substrate recognition is controversial. To examine the relev...

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Hlavní autoři: Ireland, Breanna S., Brockmeier, Ulf, Howe, Christopher M., Elliott, Tim, Williams, David B.
Médium: Artigo
Jazyk:Inglês
Vydáno: The American Society for Cell Biology 2008
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2397311/
https://ncbi.nlm.nih.gov/pubmed/18337472
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1091/mbc.E07-10-1055
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