Insights into the cause of the Oroville dam spillway failure, 2017, California.

Earth internal seepage erosion in weathered bedrock under infrequently used hydraulic structures is often overlooked, which causes some solid particles to break away from the solid skeleton, degrading the earth's strength, and even causing unanticipated hydraulic engineering failures. The flood on the Oroville dam spillway in California in 2017 was caused by disturbed water flow due to a crack in the spillway chute caused by internal erosion in poorly weathered bedrock. The abnormal water flow of the spillway in the early stage and subsequent investigation revealed that the main reason for the accident was the insufficient weathered bedrock under the spillway chute. In this study, we formulated a coupled hydro-mechanical mechanism for internal erosion in weathered bedrock during the early stages. Using this model, we conducted an internal erosion numerical simulation at early stage, and the results showed that the physical characteristics of the weathered bedrock were degraded. Our results show the coupling analysis of quantitative computation during the early stage of internal erosion in weathered bedrock, which can provide an early warning method for the occurrence of internal erosion to avoid hydraulic disasters.

A triphenylamine-benzofuran-derived fluorescent probe for monitoring sulfite in Chinese medicinal materials and bioimaging.

In this work, a triphenylamine-benzofuran-derived fluorescent probe TBSF was developed for monitoring the sulfite level in Chinese medicinal materials and imaging in living cells. In the testing system, under 445 nm excitation, TBSF responded to sulfite steadily with a 540 nm fluorescence reporting signal. The testing system showed advantages including high sensitivity, rapid response, and high selectivity. In particular, TBSF achieved the sulfite detection in the water decoction of Chinese medicinal materials from both addition and excessive fumigation. It also realized the intracellular imaging of both exogenous and endogenous sulfite in living HepG2 cells. The imaging in water decoction-treated cells inferred the potential for the interdisciplinary detection.

Protein disulfide isomerase PDI8 is indispensable for parasite growth and associated with secretory protein processing in Toxoplasma gondii.

Protein disulfide isomerase, containing thioredoxin (Trx) domains, serves as a vital enzyme responsible for oxidative protein folding (the formation, reduction, and isomerization of disulfide bonds in newly synthesized proteins) in the endoplasmic reticulum (ER). However, the role of ER-localized PDI proteins in parasite growth and their interaction with secretory proteins remain poorly understood. In this study, we identified two ER-localized PDI proteins, TgPDI8 and TgPDI6, in Toxoplasma gondii. Conditional knockdown of TgPDI8 resulted in a significant reduction in intracellular proliferation and invasion abilities, leading to a complete block in plaque formation on human foreskin fibroblast monolayers, whereas parasites lacking TgPDI6 did not exhibit any apparent fitness defects. The complementation of TgPDI8 with mutant variants highlighted the critical role of the CXXC active site cysteines within its Trx domains for its enzymatic activity. By utilizing TurboID-based proximity labeling, we uncovered a close association between PDI proteins and canonical secretory proteins. Furthermore, parasites lacking TgPDI8 showed a significant reduction in the expression of secretory proteins, especially those from micronemes and dense granules. In summary, our study elucidates the roles of TgPDI8 and sets the stage for future drug discovery studies. IMPORTANCE: Apicomplexans, a phylum of intracellular parasites, encompass various zoonotic pathogens, including Plasmodium, Cryptosporidium, Toxoplasma, and Babesia, causing a significant economic burden on human populations. These parasites exhibit hypersensitivity to disruptions in endoplasmic reticulum (ER) redox homeostasis, necessitating the presence of ER-localized thioredoxin (Trx) superfamily proteins, particularly protein disulfide isomerase (PDI), for proper oxidative folding. However, the functional characteristics of ER-localized PDI proteins in Toxoplasma gondii remain largely unexplored. In this study, we identified two ER-localized proteins, namely, TgPDI8 and TgPDI6, and demonstrated the indispensable role of TgPDI8 in parasite survival. Through a comprehensive multi-omics analysis, we elucidated the crucial role of TgPDI8 in the processing of secretory proteins in T. gondii. Additionally, we introduced a novel ER-anchored TurboID method to label and identify canonical secretory proteins in T. gondii. This research opens up new avenues for understanding oxidative folding and the secretory pathway in apicomplexan parasites, laying the groundwork for future advancements in antiparasitic drug development.

Textural Restoration of Broiler Breast Fillets with Spaghetti Meat Myopathy, Using Two Alginate Gels Systems.

The effects of salt-sensitive alginate ("A") and a two-component salt-tolerant alginate system ("B") used at a 0.5% or 1.0% level were evaluated in normal breast (NB) chicken fillets and in spaghetti meat (SM) fillets. Minced raw and cooked SM samples showed higher cooking loss (p < 0.05) and lower penetration force compared to NB meat. Both alginate systems significantly raised the penetration force in raw samples and decreased cooking loss (p < 0.05). Adding 1% of "A" or 0.5% "B" to SM, without salt, resulted in a similar penetration force as the cooked NB meat, while 1% "B" with salt resulted in a higher penetration force. Excluding salt from SM samples while adding alginate "A" or "B" improved texture profiles, but not to the same level as using NB without additives. Overall, salt, together with alginate "B", improved the texture of SM to that of normal meat without myopathy.