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Abstract 2D transition metal dichalcogenides (TMDs) have significant research interests in various novel applications due to their intriguing physicochemical properties. Notably, one of the 2D TMDs, SnS2, has superior chemiresistive sensing properties, including a planar crystal structure, a large surface‐to‐volume ratio, and a low electronic noise. However, the long‐term stability of SnS2 in humid conditions remains a critical shortcoming towards a significant degradation of sensitivity. Herein, it is demonstrated that the subsequent self‐assembly of zeolite imidazolate framework (ZIF‐8) can be achieved in situ growing on SnS2 nanoflakes as the homogeneous porous materials. ZIF‐8 layer on SnS2 allows the selective diffusion of target gas species, while effectively preventing the SnS2 from severe oxidative degradation. Molecular modeling such as molecular dynamic simulation and DFT calculation, further supports the mechanism of sensing stability and selectivity. From the results, the in situ grown ZIF‐8 porous membrane on 2D materials corroborates the generalizable strategy for durable and reliable high‐performance electronic applications of 2D materials.

The breath gas analysis through gas phase chemical analysis draws attention in terms of non-invasive and real time monitoring. The array-type sensors are one of the diagnostic methods with high sensitivity and selectivity towards the target gases. Herein, we presented a 2 × 4 sensor array with a micro-heater and ceramic chip. The device is designed in a small size for portability, including the internal eight-channel sensor array. In2O3 NRs and WO3 NRs manufactured through the E-beam evaporator’s glancing angle method were used as sensing materials. Pt, Pd, and Au metal catalysts were decorated for each channel to enhance functionality. The sensor array was measured for the exhaled gas biomarkers CH3COCH3, NO2, and H2S to confirm the respiratory diagnostic performance. Through this operation, the theoretical detection limit was calculated as 1.48 ppb for CH3COCH3, 1.9 ppt for NO2, and 2.47 ppb for H2S. This excellent detection performance indicates that our sensor array detected the CH3COCH3, NO2, and H2S as biomarkers, applying to the breath gas analysis. Our results showed the high potential of the gas sensor array as a non-invasive diagnostic tool that enables real-time monitoring.

The Cdc6 protein is essential for the initiation of chromosomal replication and functions as a licensing factor to maintain chromosome integrity. During the S and G2 phases of the cell cycle, Cdc6 has been found to inhibit the recruitment of pericentriolar material (PCM) proteins to the centrosome and to suppress centrosome over-duplication. In this report, we analyzed the correlation between these two functions of Cdc6 at the centrosome. Cdc6 depletion increased the population of cells showing centrosome over-duplication and premature centrosome separation; Cdc6 expression reversed these changes. Deletion and fusion experiments revealed that the 18 amino acid residues (197-214) of Cdc6, which were fused to the Cdc6-centrosomal localization signal, suppressed centrosome over-duplication and premature centrosome separation. Cdc6 mutant proteins that showed defective ATP binding or hydrolysis did not exhibit a significant difference in suppressing centrosome over-duplication, compared to the wild type protein. In contrast to the Cdc6-mediated inhibition of PCM protein recruitment to the centrosome, the independence of Cdc6 on its ATPase activity for suppressing centrosome over-duplication, along with the difference between the Cdc6 protein regions participating in the two functions, suggested that Cdc6 controls centrosome duplication in a manner independent of its recruitment of PCM proteins to the centrosome. [ABSTRACT FROM AUTHOR]

The centrosome serves as a major microtubule-organizing center (MTOC). The Cdc6 protein is a component of the prereplicative complex and a licensing factor for the initiation of chromosome replication and localizes to centrosomes during the S and G2 phases of the cfell cycle of human cells. This cell cycle-dependent localization of Cdc6 to the centrosome motivated us to investigate whether Cdc6 negatively regulates MTOCactivity and to determine the integral proteins that comprise the pericentriolar material (PCM). Time-lapse live-cell imaging of microtubule regrowth revealed that Cdc6 depletion increased microtubule nucleation at the centrosomes and that expression of Cdc6 in Cdc6-depleted cells reversed this effect. This increase and decrease in microtubule nucleation correlated with the centrosomal intensities of PCM proteins such as γ-tubulin, pericentrin, CDK5 regulatory subunit-associated protein 2 (CDK5RAP2), and centrosomal protein 192 (Cep192). The regulation of microtubule nucleation and the recruitment of PCM proteins to the centrosome required Cdc6 ATPase activity, as well as a centrosomal localization of Cdc6. These results suggest a novel function for Cdc6 in coordinating centrosome assembly and function. [ABSTRACT FROM AUTHOR]

The Cdc6 protein has been primarily investigated as a component of the pre-replicative complex for the initiation of chromosome replication, which contributes to maintenance of chromosomal integrity. Here, we show that Cdc6 localized to the centrosomes during S and G2 phases of the cell cycle. The centrosomal localization was mediated by Cdc6 amino acid residues 311-366, which are conserved within other Cdc6 homologues and contains a putative nuclear export signal. Deletions or substitutions of the amino acid residues did not allow the proteins to localize to centrosomes. In contrast, DsRed tag fused to the amino acid residues localized to centrosomes. These results indicated that a centrosome localization signal is contained within amino acid residues 311-366. The cell cycle-dependent centrosomal localization of Cdc6 in S and G2 phases suggest a novel function of Cdc6 in centrosomes. [ABSTRACT FROM AUTHOR]