Dimerization of ER-resident molecular chaperones mediated by ERp29
Author:
Funder
JSPS
Sasakawa Scientific Research
Japan Science Society
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference29 articles.
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2. Protein quality control in the endoplasmic reticulum;Adams;Protein J.,2019
3. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57;Zapun;J. Biol. Chem.,1998
4. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain;Frickel;Proc. Natl. Acad. Sci. U.S.A.,2002
5. Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin;Jessop;J. Biol. Chem.,2009
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1. Intramembrane client recognition potentiates the chaperone functions of calnexin;The EMBO Journal;2022-10-31
2. ER Endogenous Protein Complexed with Lectin Chaperones Calnexin/Calreticulin;Trends in Glycoscience and Glycotechnology;2022-07-25
3. Intra-membrane client recognition potentiates the chaperone functions of Calnexin;2022-03-08
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