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Due to the influence of many factors, distribution cables are often densely placed at the bottom of the cable trench. As a result, it is easy for distribution cables to become the thermal bottleneck of the whole transmission line. To address this dilemma, this paper establishes a finite element simulation model of a cable trench to analyze the hot spots of cables with different arrangements in the cable trench. Then, the model’s accuracy is verified based on real temperature rise experiments. For an arrangement with overheating risk, the ampacity improvement method of filling the cable trench with high-thermal-conductivity material was proposed, and the ampacity improvement effect under different filling ratios was assessed. Finally, combined with the analysis of economic benefit and cost, the method of determining the optimal filling ratio was used, and the impact resistance of the cables under the impact of new energy load was analyzed. The results indicate that, for the case of the optimal filling ratio, the cables in the dense cable trench showed superior impact resistance. The investigations in this paper make significant contributions to the promotion of the maximum utilization of cables.

Protein folding in the cell is regulated by several quality-control mechanisms. Correct folding of glycoproteins in the endoplasmic reticulum (ER) is tightly monitored by the recognition of glycan signals by lectins in the ER-associated degradation (ERAD) pathway. In mammals, mannose trimming from N-glycans is crucial for disposal of misfolded glycoproteins. The mannosidases responsible for this process are ER mannosidase I and ER degradation-enhancing α-mannosidase-like proteins (EDEMs). However, the molecular mechanism of mannose removal by EDEMs remains unclear, partly owing to the difficulty of reconstituting mannosidase activity in vitro. Here, our analysis of EDEM3-mediated mannose-trimming activity on a misfolded glycoprotein revealed that ERp46, an ER-resident oxidoreductase, associates stably withEDEM3.This interaction, which depended on the redox activity of ERp46, involved formation of a disulfide bond between the cysteine residues of the ERp46 redox-active sites and the EDEM3 α-mannosidase domain. In a defined in vitro system consisting of recombinant proteins purified from HEK293 cells, the mannose-trimming activity of EDEM3 toward the model misfolded substrate, the glycoprotein T-cell receptor α locus (TCRα), was reconstituted only when ERp46 had established a covalent interaction with EDEM3. On the basis of these findings, we propose that disposal of misfolded glycoproteins through mannose trimming is tightly connected to redox-mediated regulation in the ER. [ABSTRACT FROM AUTHOR]