protein disulfide-isomerase-like protein of the testis isoform X1 [Hom - Protein

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Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity. [J Biol Chem. 2018]
Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity.
Li H, Yang K, Wang W, Niu Y, Li J, Dong Y, Liu Y, Wang CC, Wang L, Liang H. J Biol Chem. 2018 Jan 26; 293(4):1192-1202. Epub 2017 Dec 4.
Structure of the substrate-binding b' domain of the Protein Disulfide Isomerase-Like protein of the Testis. [Sci Rep. 2014]
Structure of the substrate-binding b' domain of the Protein Disulfide Isomerase-Like protein of the Testis.
Bastos-Aristizabal S, Kozlov G, Gehring K. Sci Rep. 2014 Mar 25; 4:4464. Epub 2014 Mar 25.
PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum. [J Biol Chem. 2005]
PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.
van Lith M, Hartigan N, Hatch J, Benham AM. J Biol Chem. 2005 Jan 14; 280(2):1376-83. Epub 2004 Oct 8.

RefSeq mRNA
See reference mRNA sequence for the PDILT gene (XM_011545765.2).
RefSeq protein isoforms
See 7 reference sequence protein isoforms for the PDILT gene.

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Protein