Functional Characterization of ERp18, a New Endoplasmic Reticulum-located Thioredoxin Superfamily Member-Reference-Cited by-同舟云学术

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Functional Characterization of ERp18, a New Endoplasmic Reticulum-located Thioredoxin Superfamily Member

Published:2003-08 Issue:31 Volume:278 Page:28912-28920
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Alanen Heli I.,Williamson Richard A.,Howard Mark J.,Lappi Anna-Kaisa,Jäntti Heli P.,Rautio Sini M.,Kellokumpu Sakari,Ruddock Lloyd W.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference45 articles.

1. The formation of protein disulphide bonds

2. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

3. Formation and transfer of disulphide bonds in living cells

4. Native and non-native intermediates in the BPTI folding pathway

5. Mechanisms and catalysts of disulphide bond formation in proteins

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1. Modulation of Protein Disulfide Isomerase Functions by Localization: The Example of the Anterior Gradient Family;Antioxidants & Redox Signaling;2024-04-03

2. Zn2+-dependent functional switching of ERp18, an ER-resident thioredoxin-like protein;Cell Reports;2024-02

3. ROS-induced translational regulation—through spatiotemporal differences in codon recognition—is a key driver of brown adipogenesis;2023-12-23

4. TXNDC12 inhibits lipid peroxidation and ferroptosis;iScience;2023-12

5. Deciphering the Role of Selenoprotein M;Antioxidants;2023-10-25

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