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1.
Small ; : e2310239, 2024 Feb 01.
Artigo em Inglês | MEDLINE | ID: mdl-38299473

RESUMO

Solid-state hydrogen storage materials are safe and lightweight hydrogen carriers. Among the various solid-state hydrogen carriers, hydrogen boride (HB) sheets possess a high gravimetric hydrogen capacity (8.5 wt%). However, heating at high temperatures and/or strong ultraviolet illumination is required to release hydrogen (H2 ) from HB sheets. In this study, the electrochemical H2 release from HB sheets using a dispersion system in an organic solvent without other proton sources is investigated. H2 molecules are released from the HB sheets under the application of a cathodic potential. The Faradaic efficiency for H2 release from HB sheets reached >90%, and the onset potential for H2 release is -0.445 V versus Ag/Ag+ , which is more positive than those from other proton sources, such as water or formic acid, under the same electrochemical conditions. The total electrochemically released H2 in a long-time experiment reached ≈100% of the hydrogen capacity of HB sheets. The H2 release from HB sheets is driven by a small bias; thus, they can be applied as safe and lightweight hydrogen carriers with economical hydrogen release properties.

2.
Sci Rep ; 13(1): 19540, 2023 Nov 09.
Artigo em Inglês | MEDLINE | ID: mdl-37945635

RESUMO

Most of previous photocatalysts contain metal species, thus exploring a metal-free photocatalyst is still challenging. A metal-free photocatalyst has an advantage for the development of economical and non-toxic artificial photosynthesis system and/or environmental purification applications. In this study, rhombohedral boron monosulfide (r-BS) was synthesized by a high-pressure solid-state reaction, and its photocatalytic properties were investigated. r-BS absorbed visible light, and its photocurrent action spectrum also exhibited visible light responsivity. The r-BS evolved hydrogen (H2) from water under ultraviolet (UV) as well as under visible light irradiation, and its internal quantum efficiency reached 1.8% under UV light irradiation. In addition to the H2 evolution reaction, the r-BS photocatalyst drove carbon dioxide (CO2) reduction and dye oxidation reactions under UV irradiation. Although bare r-BS was not so stable under strong light irradiation in water, cocatalyst modification improved its stability. These results indicate that r-BS is a new class of non-metal photocatalyst applicable for H2 production, CO2 reduction, and environmental purification reactions.

3.
Molecules ; 28(4)2023 Feb 16.
Artigo em Inglês | MEDLINE | ID: mdl-36838883

RESUMO

Two-dimensional materials have wide ranging applications in electronic devices and catalysts owing to their unique properties. Boron-based compounds, which exhibit a polymorphic nature, are an attractive choice for developing boron-based two-dimensional materials. Among them, rhombohedral boron monosulfide (r-BS) has recently attracted considerable attention owing to its unique layered structure similar to that of transition metal dichalcogenides and a layer-dependent bandgap. However, experimental evidence that clarifies the charge carrier type in the r-BS semiconductor is lacking. In this study, we synthesized r-BS and evaluated its performance as a semiconductor by measuring the Seebeck coefficient and photo-electrochemical responses. The properties unique to p-type semiconductors were observed in both measurements, indicating that the synthesized r-BS is a p-type semiconductor. Moreover, a distinct Fano resonance was observed in Fourier transform infrared absorption spectroscopy, which was ascribed to the Fano resonance between the E(2) (TO) phonon mode and electrons in the band structures of r-BS, indicating that the p-type carrier was intrinsically doped in the synthesized r-BS. These results demonstrate the potential future application prospects of r-BS.


Assuntos
Boro , Eletrônica , Elétrons , Excipientes , Semicondutores
4.
Genes Cells ; 10(7): 665-78, 2005 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-15966898

RESUMO

Fhos1 is a mammalian formin-family protein, and functions as an organizer of the actin microfilament. Here we have cloned human and mouse cDNAs for a novel Fhos homolog, designated Fhos2. The messages for Fhos2 are expressed in the heart, kidney, and brain, where the Fhos1 mRNAs are not abundant. Two splice variants of Fhos2 exist in a tissue-specific manner; the longer variant Fhos2L is the major form in the heart, whereas the kidney and brain predominantly express Fhos2S that encodes a shorter protein. Over-expression of an active form of the two Fhos2 variants, as well as that of Fhos1, induces the formation of actin stress fibers in HeLa cells, suggesting that Fhos2 acts as an actin-organizing protein. Biochemical analysis using rat cardiomyoblastic H9c2 (2-1) cells reveals that endogenous Fhos2 is enriched in the intermediate filament fraction. Consistent with this, Fhos2 localizes to the nestin intermediate filament but not to other cytoskeletons, as demonstrated by staining of H9c2 (2-1) cells with anti-Fhos2 antibodies. Furthermore, Fhos2 is present in nestin-expressing neuroepithelial cells of the fetal rat brain. Thus, Fhos2 not only has the actin-organizing activity but also associates with nestin, which may imply a Fhos2-mediated link between the nestin intermediate filament and actin microfilament.


Assuntos
Actinas/metabolismo , Proteínas de Filamentos Intermediários/metabolismo , Proteínas dos Microfilamentos/metabolismo , Miócitos Cardíacos/metabolismo , Proteínas do Tecido Nervoso/metabolismo , Sequência de Aminoácidos , Animais , Citoesqueleto/metabolismo , Proteínas Fetais , Forminas , Células HeLa , Humanos , Filamentos Intermediários , Camundongos , Proteínas dos Microfilamentos/genética , Dados de Sequência Molecular , Miócitos Cardíacos/citologia , Nestina , Células Neuroepiteliais/citologia , Células Neuroepiteliais/metabolismo , Proteínas Nucleares , RNA Mensageiro/genética , RNA Mensageiro/metabolismo , Ratos , Homologia de Sequência de Aminoácidos , Distribuição Tecidual
5.
Nucleic Acids Res ; 30(13): 2906-10, 2002 Jul 01.
Artigo em Inglês | MEDLINE | ID: mdl-12087176

RESUMO

Overlapping of genes, especially in an anti-parallel fashion, is quite rare in eukaryotic genomes. We have found a rare instance of exon overlapping involving CHRNE and MINK gene loci on chromosome 17 in humans. CHRNE codes for the epsilon subunit of the nicotinic acetylcholine receptor (AChRepsilon) whereas MINK encodes a serine/threonine kinase belonging to the GCK family. To elucidate the evolutionary trail of this gene overlapping event, we examined the genomes of a number of primates and found that mutations in the polyadenylation signal of the CHRNE gene in early hominoids led to the overlap. Upon extending this analysis to genomes of other orders of placental mammals, we observed that the overlapping occurred at least three times independently during the course of mammalian evolution. Because CHRNE and MINK are differentially expressed, the potentially hazardous mutations responsible for the exon overlap seem to have escaped evolutionary pressures by differential temporo-spatial expression of the two genes.


Assuntos
Evolução Molecular , Homologia de Genes/genética , Proteínas Serina-Treonina Quinases/genética , Receptores Nicotínicos/genética , Animais , Sequência de Bases , Bovinos , Cromossomos Humanos Par 17/genética , DNA/química , DNA/genética , Cães , Genoma , Genoma Humano , Cavalos , Humanos , Camundongos , Camundongos Endogâmicos C57BL , Repetições de Microssatélites , Dados de Sequência Molecular , Filogenia , Poli A/genética , Primatas , Coelhos , Alinhamento de Sequência , Análise de Sequência de DNA , Homologia de Sequência do Ácido Nucleico , Suínos , Baleias
6.
Oncogene ; 21(24): 3939-48, 2002 May 30.
Artigo em Inglês | MEDLINE | ID: mdl-12032833

RESUMO

The p21-activated kinase (PAK) family of protein kinases has recently attracted considerable attention as an effector of Rho family of small G proteins and as an upstream regulator of MAPK signalling pathways during cellular events such as re-arrangement of the cytoskeleton and apoptosis. We have cloned a novel human PAK family kinase that has been designated as PAK5. PAK5 contains a CDC42/Rac1 interactive binding (CRIB) motif at the N-terminus and a Ste20-like kinase domain at the C-terminus. PAK5 is structurally most related to PAK4 and PAK6 to make up the PAK-II subfamily. We have shown that PAK5 preferentially binds to CDC42 in the presence of GTP and that CRIB motif is essential for this interaction. PAK5 is a functional protein kinase but unlike PAK-I family kinases (PAK1, 2, and 3), the kinase activity of PAK5 does not seem to require the binding of CDC42. Overexpression of PAK5 activates the JNK kinase pathway but not p38 or ERK pathways. PAK5 transcript is predominantly expressed in brain as revealed by Northern blot and in situ hybridization. The expression pattern of PAK5 is distinct from that of PAK4 and PAK6, suggesting a functional division among PAK-II subfamily kinases based on differential tissue distribution.


Assuntos
Encéfalo/enzimologia , Ciclinas/química , Proteínas Serina-Treonina Quinases/química , Proteínas Serina-Treonina Quinases/genética , Motivos de Aminoácidos , Sequência de Aminoácidos , Northern Blotting , Mapeamento Cromossômico , Cromossomos Humanos Par 20 , Clonagem Molecular , Inibidor de Quinase Dependente de Ciclina p21 , DNA Complementar/metabolismo , GTP Fosfo-Hidrolases/metabolismo , Humanos , Hibridização In Situ , Proteína Quinase 8 Ativada por Mitógeno , Proteínas Quinases Ativadas por Mitógeno/metabolismo , Modelos Genéticos , Dados de Sequência Molecular , Fosforilação , Testes de Precipitina , Ligação Proteica , Proteínas Serina-Treonina Quinases/metabolismo , Estrutura Terciária de Proteína , RNA Mensageiro/metabolismo , Distribuição Tecidual , Transfecção , Proteína cdc42 de Ligação ao GTP/metabolismo , Quinases Ativadas por p21 , Proteínas Quinases p38 Ativadas por Mitógeno
7.
J Biol Chem ; 277(8): 5929-39, 2002 Feb 22.
Artigo em Inglês | MEDLINE | ID: mdl-11741893

RESUMO

We have cloned a novel human GCK family kinase that has been designated as MASK (Mst3 and SOK1-related kinase). MASK is widely expressed and encodes a protein of 416 amino acid residues, with an N-terminal kinase domain and a unique C-terminal region. Like other GCK-III subfamily kinases, MASK does not activate any mitogen-activated protein kinase pathways. Wild type MASK, but not a form lacking the C terminus, exhibits homophilic binding in the yeast two-hybrid system and in coimmunoprecipitation experiments. Additionally, deletion of this C-terminal region of MASK leads to an increased kinase activity toward itself as well as toward an exogenous substrate, myelin basic protein. A potential caspase 3 cleavage site (DESDS) is present in the C-terminal region of MASK, and we show that MASK is cleaved in vitro by caspase 3. Finally, wild type and C-terminally truncated forms of MASK can both induce apoptosis upon overexpression in mammalian cells that is abrogated by CrmA, suggesting involvement of MASK in the apoptotic machinery in mammalian cells.


Assuntos
Apoptose/fisiologia , Proteínas Quinases/genética , Proteínas Serina-Treonina Quinases/genética , Motivos de Aminoácidos , Sequência de Aminoácidos , Animais , Sequência de Bases , Clonagem Molecular , Fragmentação do DNA , Primers do DNA , Éxons , Centro Germinativo/enzimologia , Quinases do Centro Germinativo , Humanos , Íntrons , Mamíferos , Dados de Sequência Molecular , Fragmentos de Peptídeos/química , Proteínas Quinases/química , Proteínas Quinases/metabolismo , Proteínas Serina-Treonina Quinases/química , Proteínas Serina-Treonina Quinases/metabolismo , Saccharomyces cerevisiae/enzimologia
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