Variation in the Subcellular Localization and Protein Folding Activity among Arabidopsis thaliana Homologs of Protein Disulfide Isomerase

Variation in the Subcellular Localization and Protein Folding Activity among Arabidopsis thaliana Homologs of Protein Disulfide Isomerase

Protein disulfide isomerases (PDIs) catalyze the formation, breakage, and rearrangement of disulfide bonds to properly fold nascent polypeptides within the endoplasmic reticulum (ER). Classical animal and yeast PDIs possess two catalytic thioredoxin-like domains (a, a′) and two non-catalytic domains...

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Bibliographic Details
Main Authors: Christen Y. L. Yuen, David A. Christopher, Kristie O. Matsumoto
Format: Article
Language:English
Published: MDPI AG 2013-10-01
Series:Biomolecules
Subjects:
chaperone
endoplasmic reticulum
foldase
protein body
protein disulfide isomerase
protein folding
Online Access:http://www.mdpi.com/2218-273X/3/4/848

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http://www.mdpi.com/2218-273X/3/4/848

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