Dietary reference intake for military operations: a scoping review.

Background: Reports that collect and organize dietary reference intake (DRI) data for military operations in different countries and regions worldwide are limited.This scoping review aimed to collect and organize information on the status of formulating a DRI for military operations in each country.

Methodology: For the information search, we queried PubMed and Google for literature and reports on the DRI for military operations and summarized the content of the adopted literature and reports.

Long-term changes in corneal endothelial cell density after repeat penetrating keratoplasty in eyes with endothelial decompensation.

Purpose: To compare the longitudinal changes in corneal endothelial cell density (ECD) and the incidence of postoperative complications between eyes with endothelial decompensation after repeat penetrating keratoplasty (RPK) and those after primary penetrating keratoplasty (PPK).

Methods: Fifty-seven eyes with endothelial decompensation scheduled for RPK (RPK group) and 57 eyes with endothelial decompensation scheduled for PPK (PPK group) were enrolled. Corneal ECD was evaluated using a specular microscope at 1, 3, 6, 9, and 12 months, and every 6 months until 60 months postoperatively.

Redox-dependent domain rearrangement of protein disulfide isomerase from a thermophilic fungus.

Protein disulfide isomerase (PDI) acts as folding catalyst and molecular chaperone for disulfide-containing proteins through the formation, breakage, and rearrangement of disulfide bonds. PDI has a modular structure comprising four thioredoxin domains, a, b, b', and a', followed by a short segment, c. The a and a' domains have an active site cysteine pair for the thiol-disulfide exchange reaction, which alters PDI between the reduced and oxidized forms, and the b' domain provides a primary binding site for substrate proteins.

Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface.

Protein disulfide isomerase (PDI) is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges. This enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides.