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BACKGROUND: Rapid on-site triage is critical after mass-casualty incidents (MCIs) and other mass injury events. Unmanned aerial vehicles (UAVs) have been used in MCIs to search and rescue wounded individuals, but they mainly depend on the UAV operator's experience. We used UAVs and artificial intelligence (AI) to provide a new technique for the triage of MCIs and more efficient solutions for emergency rescue. METHODS: This was a preliminary experimental study. We developed an intelligent triage system based on two AI algorithms, namely OpenPose and YOLO. Volunteers were recruited to simulate the MCI scene and triage, combined with UAV and Fifth Generation (5G) Mobile Communication Technology real-time transmission technique, to achieve triage in the simulated MCI scene. RESULTS: Seven postures were designed and recognized to achieve brief but meaningful triage in MCIs. Eight volunteers participated in the MCI simulation scenario. The results of simulation scenarios showed that the proposed method was feasible in tasks of triage for MCIs. CONCLUSION: The proposed technique may provide an alternative technique for the triage of MCIs and is an innovative method in emergency rescue. [ABSTRACT FROM AUTHOR]

Hepatitis C virus (HCV) nonstructural protein 5A (NS5A) is thought to regulate the replication of viral RNA and the assembly of virus particles in a serine/threonine phosphorylation-dependent manner. However, the host kinases that phosphorylate NS5A have not been fully identified. Here, we show that HCV particle assembly involves the phosphorylation of NS5A by the c-Abl tyrosine kinase. Pharmacological inhibition or knockdown of c-Abl reduces the production of infectious HCV (J6/ JFH1) particles in Huh-7.5 cells without markedly affecting viral RNA translation and replication. NS5A is tyrosine-phosphorylated in HCV-infected cells, and this phosphorylation is also reduced by the knockdown of c-Abl. Mutational analysis reveals that NS5A tyrosine phosphorylation is dependent, at least in part, on Tyr330 (Tyr2306 in polyprotein numbering). Mutation of this residue to phenylalanine reduces the production of infectious HCV particles but does not affect the replication of the JFH1 subgenomic replicon. These findings suggest that c-Abl promotes HCV particle assembly by phosphorylating NS5A at Tyr330. [ABSTRACT FROM AUTHOR]

We study the place scheduling problem which has many application backgrounds in realities. For the block manufacturing project with special manufacturing platform requirements, we propose a place resource schedule problem. First, the mathematical model for the place resource schedule problem is given. On the basis of resource-constrained project scheduling problem and packing problem, we develop a hybrid heuristic method which combines priority rules and three-dimensional best fit algorithm, in which the priority rules determine the scheduling order and the three-dimensional best fit algorithm solves the placement. After this method is used to get an initial solution, the iterated local search is employed to get an improvement. Finally, we use a set of simulation data to demonstrate the steps of the proposed method and verify its feasibility. [ABSTRACT FROM AUTHOR]

Hepatitis C virus (HCV) infects B lymphocytes and induces mixed cryoglobulinemia and B cell non-Hodgkin's lymphoma. The molecular mechanism for the pathogenesis of HCV infection-mediated B cell disorders remains obscure. To identify the possible role for HCV nonstructural 5A (NS5A) protein in B cells, we generated the stable B cell lines expressing Myc-His tagged NS5A. Immunoprecipitation study in the presence or absence of pervanadate (PV) implied that NS5A was tyrosine phosphorylated by pervanadate (PV) treatment of the cells. Therefore we examined pull-down assay by using glutathione S-transferase (GST)-fusion proteins of various Src homology 2 (SH2) domains, which associates with phosphotyrosine within a specific amino acid sequence. The results showed that NS5A specifically bound to SH2 domain of Fyn from PV-treated B cells in addition to Src homology 3 (SH3) domain. Substitution of Arg176 to Lys in the SH2 domain of Fyn abrogated this interaction. Deletion mutational analysis demonstrated that N-terminal region of NS5A was not required for the interaction with the SH2 domain of Fyn. Tyr334 was identified as a tyrosine phosphorylation site in NS5A. Far-western analysis revealed that SH2 domain of Fyn directly bound to NS5A. Fyn and NS5A were colocalized in the lipid raft. These results suggest that NS5A directly binds to the SH2 domain of Fyn in a tyrosine phosphorylation-dependent manner. Lastly, we showed that the expression of NS5A in B cells increased phosphorylation of activation loop tyrosine in the kinase domain of Fyn. NS5A containing ligand for both SH2 and SH3 domains enhances an aberrant autophosphorylation and kinase activity of Fyn in B cells. [ABSTRACT FROM AUTHOR]