TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain

The lectin chaperone calreticulin (CRT) assists the folding and quality control of newly synthesized glycoproteins in the endoplasmic reticulum (ER). It interacts with ERp57, a thiol-disulfide oxidoreductase that promotes the formation of disulfide bonds in glycoproteins bound by CRT. Here, we inves...

Täydet tiedot

Bibliografiset tiedot

Julkaisussa:	Proc Natl Acad Sci U S A
Päätekijät:	Frickel, Eva-Maria, Riek, Roland, Jelesarov, Ilian, Helenius, Ari, Wüthrich, Kurt, Ellgaard, Lars
Aineistotyyppi:	Artigo
Kieli:	Inglês
Julkaistu:	National Academy of Sciences 2002
Aiheet:	Biological Sciences
Linkit:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC122301/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11842220/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.042699099
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