For organic thin‐film transistors (OTFTs) made of solution processed stacks of organic semiconductor and dielectric materials, it is a grand challenge to eliminate the leakage current paths. With a top‐gate bottom‐contact structure, this work introduces a strong dipole interfacial layer made of self‐assembled monolayer (SAM) molecules at metal‐semiconductor contacts to suppress minority carrier injection for low leakage and stable operation, while not affecting majority carrier injection. Both gate insulator (GI) leakage and parasitic leakage in the device architecture are also effectively suppressed with a sputtering‐resistant polymer GI layer and photolith patterned OSC islands, respectively. The devices present a decent mobility with a typical value of 1.98 cm2 V–1 s–1, record‐low leakage current at 10–18 A µm−1 and large ON/OFF ratio (>1010) in a wide gate voltage range (100 V), reaching the theoretical limit and also the best level of inorganic counterparts despite much lower processing temperature (120 °C). Manufacturability of the material stack is verified on a 200 mm × 200 mm substrate and the fabricated 4.7 in. active‐matrix organic light‐emitting diode display, integrating more than 150 000 OTFTs, can be operated at ultra‐low frame‐rate (0.1 Hz) for power saving.

Evidence before this studyAs a classic mitochondrial protease, Mitochondrial ATPdependent Lon protease 1 (LONP1) has been well demonstrated to regulate metabolism and perform mitochondrial quality control in vitro. A growing number of studies have indicated that LONP1 is involved in regulating the unfolded protein response and mitochondrial dynamics in vitro and mouse heart development. The ovarian reserve and oocyte quality determine the reproductive life of mammals. Oocytes contain the largest number of mitochondria among all cell types, and the mitochondrial quality and quantity determine the oocyte quality and survival. However, far less is known about the function of LONP1 in oocyte development.

Background and objectiveThis study aimed to identify crosstalk genes between periodontitis (PD) and osteoporosis (OP) and potential relationships between crosstalk and pyroptosis-related genes.MethodsPD and OP datasets were downloaded from the GEO database and were performed differential expression analysis to obtain DEGs. Overlapping DEGs got crosstalk genes linking PD and OP. Pyroptosis-related genes were obtained from literature reviews. Pearson coefficients were used to calculate crosstalk and pyroptosis-related gene correlations in the PD and OP datasets. Paired genes were obtained from the intersection of correlated genes in PD and OP. PINA and STRING databases were used to conduct the crosstalk-bridge-pyroptosis genes PPI network. The clusters in which crosstalk and pyroptosis-related genes were mainly concentrated were defined as key clusters. The key clusters’ hub genes and the included paired genes were identified as key crosstalk-pyroptosis genes. Using ROC curve analysis and XGBoost screened key genes. PPI subnetwork, gene–biological process and gene-pathway networks were constructed based on key genes. In addition, immune infiltration was analyzed on the PD dataset using the CIBERSORT algorithm.ResultsA total of 69 crosstalk genes were obtained. 13 paired genes and hub genes TNF and EGFR in the key clusters (cluster2, cluster8) were identified as key crosstalk-pyroptosis genes. ROC and XGBoost showed that PRKCB, GSDMD, ARMCX3, and CASP3 were more accurate in predicting disease than other key crosstalk-pyroptosis genes while better classifying properties as a whole. KEGG analysis showed that PRKCB, GSDMD, ARMCX3, and CASP3 were involved in neutrophil extracellular trap formation and MAPK signaling pathway pathways. Immune infiltration results showed that all four key genes positively correlated with plasma cells and negatively correlated with T cells follicular helper, macrophages M2, and DCs.ConclusionThis study shows a joint mechanism between PD and OP through crosstalk and pyroptosis-related genes. The key genes PRKCB, GSDMD, ARMCX3, and CASP3 are involved in the neutrophil extracellular trap formation and MAPK signaling pathway, affecting both diseases. These findings may point the way to future research.

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