Three Approaches to One Problem: Protein Folding in the Periplasm, the Endoplasmic Reticulum, and the Intermembrane Space-Reference-Cited by-同舟云学术

Three Approaches to One Problem: Protein Folding in the Periplasm, the Endoplasmic Reticulum, and the Intermembrane Space

Published:2014-07-20 Issue:3 Volume:21 Page:438-456
ISSN:1523-0864
Container-title:Antioxidants & Redox Signaling
language:en
Short-container-title:Antioxidants & Redox Signaling

Author:

Herrmann Johannes M.¹,Riemer Jan²

Affiliation:

1. Department of Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.

2. Department of Cellular Biochemistry, University of Kaiserslautern, Kaiserslautern, Germany.

Publisher

Mary Ann Liebert Inc

Subject

Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry,Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry

Link

http://www.liebertpub.com/doi/pdf/10.1089/ars.2014.5841

Reference171 articles.

1. Conserved substrate binding by chaperones in the bacterial periplasm and the mitochondrial intermembrane space

2. Erv1 Mediates the Mia40-dependent Protein Import Pathway and Provides a Functional Link to the Respiratory Chain by Shuttling Electrons to Cytochrome c

3. Protein quality control in the early secretory pathway

4. Deciphering Structural and Functional Roles of Individual Disulfide Bonds of the Mitochondrial Sulfhydryl Oxidase Erv1p

5. A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells

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