The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.

Protein disulfide isomerase (PDI) is a multifunctional polypeptide that acts as a subunit in the animal prolyl 4-hydroxylases and the microsomal triglyceride transfer protein, and as a chaperone that binds various peptides and assists their folding. We report here that deletion of PDI sequences corr...

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Autores principales: Koivunen, P, Pirneskoski, A, Karvonen, P, Ljung, J, Helaakoski, T, Notbohm, H, Kivirikko, K I
Formato: Artigo
Lenguaje:Inglês
Publicado: 1999
Materias:
Research Article
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1171103/
https://ncbi.nlm.nih.gov/pubmed/9878051
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/18.1.65
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