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Year | Number of Results |
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2012 | 1 |
2013 | 2 |
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PubMed (GeneRIF) for id: 121506
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High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility.
Biochem J. 2013 Mar 1;450(2):321-32. doi: 10.1042/BJ20121635.
Biochem J. 2013.
PMID: 23234573
Free PMC article.
The crystal structure of the protein-disulfide isomerase family member ERp27 provides insights into its substrate binding capabilities.
Kober FX, Koelmel W, Kuper J, Drechsler J, Mais C, Hermanns HM, Schindelin H.
Kober FX, et al.
J Biol Chem. 2013 Jan 18;288(3):2029-39. doi: 10.1074/jbc.M112.410522. Epub 2012 Nov 28.
J Biol Chem. 2013.
PMID: 23192347
Free PMC article.
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ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57.
Alanen HI, Williamson RA, Howard MJ, Hatahet FS, Salo KE, Kauppila A, Kellokumpu S, Ruddock LW.
Alanen HI, et al.
J Biol Chem. 2006 Nov 3;281(44):33727-38. doi: 10.1074/jbc.M604314200. Epub 2006 Aug 28.
J Biol Chem. 2006.
PMID: 16940051
Free article.
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