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Yingbo Niu on Muck Rack

Yingbo Niu

As seen in: The Journal of Biological Chemistry
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Articles

Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity

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By HuanHuan Li, Wenjia Wang, Yingbo Niu
| The Journal of Biological Chemistry Verified
Protein-disulfide isomerase-like protein of the testis (PDILT), a member of the protein-disulfide isomerase family, is a chaperone essential for the folding of spermatogenesis-specific proteins in male postmeiotic germ cells. However, the structural mechanisms that regulate the chaperone function of PDILTs are unknown. Here, we report the structures of human PDILT (hPDILT) determined by X-ray crystallography to 2.4 Å resolution and small-angle X-ray scattering (SAXS).
Open in Who Shared Issue with article?

Crystal and solution structures of human protein disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity

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By HuanHuan Li, Yingbo Niu, Jun Li, Wenjia Wang
| The Journal of Biological Chemistry Verified
Protein disulfide isomerase-like protein of the testis (PDILT), a member of the protein disulfide isomerase (PDI) family is a chaperone essential for the folding of spermatogenesis-specific proteins in male postmeiotic germ cells. However, the structural mechanisms that regulate the chaperone function of PDILT are unknown. Here, we report the structures of human PDILT (hPDILT) determined by X-ray crystallography to 2.4 angstrom resolution and small-angle X-ray scattering (SAXS).
Open in Who Shared Issue with article?

Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1

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By Yingbo Niu, Lihui Zhang, Jiaojiao Yu, Chih-chen Wang
| The Journal of Biological Chemistry Verified
The formation of disulfide bonds in the endoplasmic reticulum (ER) of eukaryotic cells is catalyzed by the sulfhydryl oxidase, ER oxidoreductin 1 (Ero1), and protein-disulfide isomerase (PDI). PDI is oxidized by Ero1 to continuously introduce disulfides into substrates, and feedback regulates Ero1 activity by manipulating the regulatory disulfides of Ero1.
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