دورية أكاديمية

A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding.

التفاصيل البيبلوغرافية
العنوان: A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding.
المؤلفون: Li Zhu, Kai Yang, Xi'e Wang, Xi Wang, Chih-chen Wang
المصدر: PLoS ONE, Vol 9, Iss 8, p e105529 (2014)
بيانات النشر: Public Library of Science (PLoS), 2014.
سنة النشر: 2014
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: Peroxiredoxin 4 (Prx4) is the only endoplasmic reticulum localized peroxiredoxin. It functions not only to eliminate peroxide but also to promote oxidative protein folding via oxidizing protein disulfide isomerase (PDI). In Prx4-mediated oxidative protein folding we discovered a new reaction that the sulfenic acid form of Prx4 can directly react with thiols in folding substrates, resulting in non-native disulfide cross-linking and aggregation. We also found that PDI can inhibit this reaction by exerting its reductase and chaperone activities. This discovery discloses an off-pathway reaction in the Prx4-mediated oxidative protein folding and the quality control role of PDI.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
Relation: http://europepmc.org/articles/PMC4138195?pdf=render; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0105529
URL الوصول: https://doaj.org/article/f3896079877b4ab29a17910a3dc878be
رقم الأكسشن: edsdoj.f3896079877b4ab29a17910a3dc878be
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
DOI:10.1371/journal.pone.0105529