Articolele autorului Stefana Maria Petrescu
Link la profilul stiintific al lui Stefana Maria Petrescu

The solution NMR structure of Glc3Man9 unit in Glc3Man7GlcNAc2
Conformation – independent binding of monoglucosylated ribonuclease B to calnexin
Tyrosinase folding and copper loading in vivo: a crucial role for calnexin and alpha-glucosidase II
Tyrosinase and glycoprotein folding: roles of chaperones that recognize glycans
Glycosylation and glycoprotein folding
The inhibition of early N-glycan processing targets TRP-2 to degradation in B16 melanoma cell
The Glycosylation of Tyrosinase in melanoma cells and the effect on antigen presentation
Soluble tyrosinase is an ER- associated degradation substrate retained in the ER by calreticulin and BIP and not calnexin
Productive folding of tyrosinase ectodomain is controlled by the transmembrane anchor

Transmembrane domains (TMDs) are known as structural elements required for the insertion into the membrane of integral membrane proteins. We have provided here an example showing that the presence of the TMD is compulsory for the productive folding pathway of a membrane-anchored glycoprotein. Tyrosinase, a type I transmembrane protein whose insertion into the melanosomal membrane initiates melanin synthesis, is misfolded and degraded when expressed

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