Sep15, a Thioredoxin-like Selenoprotein, Is Involved in the Unfolded Protein Response and Differentially Regulated by Adaptive and Acute ER Stresses-Reference-Cited by-同舟云学术

Sep15, a Thioredoxin-like Selenoprotein, Is Involved in the Unfolded Protein Response and Differentially Regulated by Adaptive and Acute ER Stresses

Published:2009-08-14 Issue:35 Volume:48 Page:8458-8465
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Labunskyy Vyacheslav M.¹,Yoo Min-Hyuk²,Hatfield Dolph L.²,Gladyshev Vadim N.¹

Affiliation:

1. Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588

2. Molecular Biology of Selenium Section, Laboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi900717p

Reference37 articles.

1. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.

2. Roles of N-Linked Glycans in the Endoplasmic Reticulum

3. Getting In and Out from Calnexin/Calreticulin Cycles

4. Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57

5. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain

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