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Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex

We previously showed that the major histocompatibility complex (MHC) class I chaperone tapasin can be detected as a mixed disulfide with the thiol-oxidoreductase ERp57. Here we show that tapasin is a unique and preferred substrate, a substantial majority of which is disulfide-linked to ERp57 within...

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Detaylı Bibliyografya
Asıl Yazarlar: Peaper, David R, Wearsch, Pamela A, Cresswell, Peter
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 2005
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC1276702/
https://ncbi.nlm.nih.gov/pubmed/16193070
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/sj.emboj.7600814
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