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1.
Adv Sci (Weinh) ; 10(17): e2301002, 2023 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-37083256

RESUMEN

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.

2.
Adv Mater ; 34(1): e2104598, 2022 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-34618384

RESUMEN

Modern artificial neural network technology using a deterministic computing framework is faced with a critical challenge in dealing with massive data that are largely unstructured and ambiguous. This challenge demands the advances of an elementary physical device for tackling these uncertainties. Here, we designed and fabricated a SiOx nanorod memristive device by employing the glancing angle deposition (GLAD) technique, suggesting a controllable stochastic artificial neuron that can mimic the fundamental integrate-and-fire signaling and stochastic dynamics of a biological neuron. The nanorod structure provides the random distribution of multiple nanopores all across the active area, capable of forming a multitude of Si filaments at many SiOx nanorod edges after the electromigration process, leading to a stochastic switching event with very high dynamic range (≈5.15 × 1010 ) and low energy (≈4.06 pJ). Different probabilistic activation (ProbAct) functions in a sigmoid form are implemented, showing its controllability with low variation by manufacturing and electrical programming schemes. Furthermore, as an application prospect, based on the suggested memristive neuron, we demonstrated the self-resting neural operation with the local circuit configuration and revealed probabilistic Bayesian inferences for genetic regulatory networks with low normalized mean squared errors (≈2.41 × 10-2 ) and its robustness to the ProbAct variation.

3.
Sensors (Basel) ; 21(5)2021 Mar 09.
Artículo en Inglés | MEDLINE | ID: mdl-33803466

RESUMEN

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.


Asunto(s)
Gases , Nanotubos , Biomarcadores , Pruebas Respiratorias , Óxidos
4.
Small ; 15(40): e1902065, 2019 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-31379070

RESUMEN

The development of high performance gas sensors that operate at room temperature has attracted considerable attention. Unfortunately, the conventional mechanism of chemiresistive sensors is restricted at room temperature by insufficient reaction energy with target molecules. Herein, novel strategy for room temperature gas sensors is reported using an ionic-activated sensing mechanism. The investigation reveals that a hydroxide layer is developed by the applied voltages on the SnO2 surface in the presence of humidity, leading to increased electrical conductivity. Surprisingly, the experimental results indicate ideal sensing behavior at room temperature for NO2 detection with sub-parts-per-trillion (132.3 ppt) detection and fast recovery (25.7 s) to 5 ppm NO2 under humid conditions. The ionic-activated sensing mechanism is proposed as a cascade process involving the formation of ionic conduction, reaction with a target gas, and demonstrates the novelty of the approach. It is believed that the results presented will open new pathways as a promising method for room temperature gas sensors.

5.
ACS Appl Mater Interfaces ; 11(7): 7529-7538, 2019 Feb 20.
Artículo en Inglés | MEDLINE | ID: mdl-30672291

RESUMEN

Morphological evolution accompanying a surface roughening and preferred orientation is an effective way to realize a high-performance gas sensor because of its significant potential as a chemical catalyst through chemical potentials and atomic energy states. In this work, we investigated a heterojunction of double-side-W-decorated NiO nanoigloos fabricated through radio frequency sputtering and a soft-template method. Interestingly, a morphological evolution characterized by a pyramidal rough surface and the preferred orientation of the (111) plane was observed upon decorating the bare NiO nanoigloos with W. The underlying mechanism of the morphological evolution was precisely demonstrated based on the van der Drift competitive growth model originating from the oxygen transport and chemical strain in the lattice. The gas sensing properties of W-decorated NiO show an excellent NO2 response and selectivity when compared to other gases. In addition, high response stability was evaluated under interference gas and humidity conditions. The synergistic effects on the sensing performance were interpreted on the basis of the morphological evolution of W-decorated NiO nanoigloos.

6.
Mol Cells ; 40(12): 925-934, 2017 Dec 31.
Artículo en Inglés | MEDLINE | ID: mdl-29237113

RESUMEN

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.


Asunto(s)
Adenosina Trifosfatasas/metabolismo , Proteínas de Ciclo Celular/metabolismo , Centrosoma/fisiología , Replicación del ADN/fisiología , Proteínas Nucleares/metabolismo , Puntos de Control del Ciclo Celular , Proteínas de Ciclo Celular/deficiencia , Línea Celular Tumoral , Centriolos/metabolismo , Centrosoma/enzimología , Centrosoma/metabolismo , Humanos , Proteínas Nucleares/deficiencia , Transfección
7.
J Biol Chem ; 292(39): 16267-16276, 2017 09 29.
Artículo en Inglés | MEDLINE | ID: mdl-28827311

RESUMEN

The centrosome serves as a major microtubule-organizing center (MTOC). The Cdc6 protein is a component of the pre-replicative 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 MTOC activity 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.


Asunto(s)
Proteínas de Ciclo Celular/metabolismo , Centrosoma/metabolismo , Centro Organizador de los Microtúbulos/metabolismo , Proteínas Nucleares/metabolismo , Sustitución de Aminoácidos , Antígenos/metabolismo , Biomarcadores/metabolismo , Proteínas de Ciclo Celular/antagonistas & inhibidores , Proteínas de Ciclo Celular/química , Proteínas de Ciclo Celular/genética , Línea Celular Tumoral , Centrosoma/química , Proteínas Cromosómicas no Histona/metabolismo , Eliminación de Gen , Humanos , Péptidos y Proteínas de Señalización Intracelular/metabolismo , Microscopía Fluorescente , Centro Organizador de los Microtúbulos/química , Mutagénesis Sitio-Dirigida , Mutación , Proteínas del Tejido Nervioso/metabolismo , Proteínas Nucleares/antagonistas & inhibidores , Proteínas Nucleares/química , Proteínas Nucleares/genética , Fragmentos de Péptidos/química , Fragmentos de Péptidos/genética , Fragmentos de Péptidos/metabolismo , Transporte de Proteínas , Interferencia de ARN , Proteínas Recombinantes de Fusión/química , Proteínas Recombinantes de Fusión/metabolismo , Imagen de Lapso de Tiempo , Tubulina (Proteína)/metabolismo
8.
Biochem Biophys Res Commun ; 456(3): 763-7, 2015 Jan 16.
Artículo en Inglés | MEDLINE | ID: mdl-25498505

RESUMEN

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.


Asunto(s)
Proteínas de Ciclo Celular/metabolismo , Centrosoma/metabolismo , Fase G2 , Proteínas Nucleares/metabolismo , Fase S , Secuencia de Aminoácidos , Animales , Línea Celular Tumoral , Humanos , Datos de Secuencia Molecular , Señales de Clasificación de Proteína , Eliminación de Secuencia
9.
Biochem Biophys Res Commun ; 447(3): 437-40, 2014 May 09.
Artículo en Inglés | MEDLINE | ID: mdl-24732362

RESUMEN

Phosphorylation of Thr(116) and Thr(226) on Orc2, one of the six subunits of the origin recognition complex (ORC), by cyclin A/CDK2 during S phase leads to the dissociation of Orc2, Orc3, Orc4, and Orc5 subunits (Orc2-5) from human chromatin and replication origins. The phosphorylated Orc2 becomes dephosphorylated in the late M phase of the cell cycle. Here we show that protein phosphatase 1 (PP1) dephosphorylates Orc2. Dephosphorylation of Orc2 was accompanied by associating the dissociated Orc subunits with chromatin. Inhibitors of PP1 preferentially inhibited the dephosphorylation of Orc2. The overexpression of the α, ß and γ PP1 isoforms decreased the amount of phosphorylated Orc2, and the depletion of these isoforms by RNA interference increased the amount of phosphorylated Orc2. These results suggest that PP1 dephosphorylates Orc2 to promote the binding of ORC to chromatin.


Asunto(s)
Cromatina/metabolismo , Complejo de Reconocimiento del Origen/metabolismo , Proteína Fosfatasa 1/metabolismo , Células HeLa , Humanos , Isoenzimas/metabolismo , Complejo de Reconocimiento del Origen/genética , Fosforilación , Unión Proteica , Proteína Fosfatasa 1/antagonistas & inhibidores , Proteína Fosfatasa 1/genética , Treonina/genética , Treonina/metabolismo
10.
Biochem Biophys Res Commun ; 436(1): 31-4, 2013 Jun 21.
Artículo en Inglés | MEDLINE | ID: mdl-23685152

RESUMEN

Human TopBP1 is involved in the DNA damage checkpoint response, chromosome replication, and other functions of cell cycle control. The C-terminal region of TopBP1 (TbpCtr: amino acid residues 1222-1522) is involved in the localization of TopBP1 to the centrosomes during mitosis. Here, we showed that the amino acid residues 741-885 of TopBP1, in addition to TbpCtr, are necessary for the centrosomal localization of TopBP1. Whereas oligomeric tags fused to TbpCtr localized to mitotic centrosomes, monomeric tags fused to TbpCtr did not. Insertion of the amino acid residues 741-885 into the monomeric tag fused to TbpCtr allowed the protein to localize to the mitotic centrosome. These results suggest that the amino acid residues 741-885 are necessary for oligomerization of TopBP1 for centrosomal localization.


Asunto(s)
Proteínas Portadoras/metabolismo , Cromosomas/ultraestructura , Proteínas de Unión al ADN/metabolismo , Regulación de la Expresión Génica , Mitosis , Proteínas Nucleares/metabolismo , Ciclo Celular , Centrosoma/ultraestructura , Daño del ADN , Proteínas Fluorescentes Verdes/metabolismo , Células HeLa , Humanos , Fosforilación , Combinación Trimetoprim y Sulfametoxazol/química
11.
Exp Cell Res ; 317(7): 994-1004, 2011 Apr 15.
Artículo en Inglés | MEDLINE | ID: mdl-21291884

RESUMEN

TopBP1 contains repeats of the BRCA1 C-terminal (BRCT) domain and plays important roles in DNA damage response, DNA replication, and other cellular regulatory functions during the interphase. In prometaphase, metaphase, and anaphase, TopBP1 localizes to the mitotic centrosomes, which function as spindle-poles for the bipolar separation of sister chromatids. The localization of TopBP1 to the mitotic centrosomes is mediated by amino acid residues 1259 to 1420 in the TopBP1 C-terminal region (TbpCtr). GST and DsRed2 tags fused to TbpCtr were localized in the mitotic centrosomes, thereby suggesting that TbpCtr functions as a mitosis-specific centrosome localization signal (CLS). Mutations of Ser 1273 and/or Lys 1317, which were predicted to interact with a putative phosphoprotein, inhibited CLS function. Ectopic expression of TbpCtr specifically eliminated endogenous TopBP1 from the mitotic centrosomes, whereas mutant TbpCtr derivatives, containing substitutions at Ser 1273 and/or Lys 1317, did not. The specific elimination of TopBP1 from the mitotic centrosomes prolonged the durations of prometaphase and metaphase and shortened the inter-kinetochore distances of metaphase sister chromatids while maintaining the spindle assembly checkpoint. These results suggest that the localization of TopBP1 to the mitotic centrosomes is necessary for proper mitotic progression.


Asunto(s)
Proteínas Portadoras/metabolismo , Centrosoma/metabolismo , Proteínas de Unión al ADN/metabolismo , Mitosis/fisiología , Proteínas Nucleares/metabolismo , Huso Acromático/metabolismo , Secuencia de Aminoácidos , Animales , Proteínas Portadoras/química , Proteínas Portadoras/genética , Cromátides/metabolismo , Proteínas de Unión al ADN/química , Proteínas de Unión al ADN/genética , Eliminación de Gen , Células HeLa , Humanos , Modelos Moleculares , Datos de Secuencia Molecular , Proteínas Nucleares/química , Proteínas Nucleares/genética , Estructura Terciaria de Proteína , Proteínas Recombinantes de Fusión/genética , Proteínas Recombinantes de Fusión/metabolismo , Alineación de Secuencia
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