Understanding the crucial role of local crystal order in the electrocatalytic activity of crystalline manganese oxide

2018 ◽  
Vol 6 (26) ◽  
pp. 12565-12573 ◽  
Author(s):  
Jang Mee Lee ◽  
Sharad B. Patil ◽  
Bohyun Kang ◽  
Seul Lee ◽  
Min Gyu Kim ◽  
...  
Keyword(s):  
Manganese Oxide ◽  
Spectroscopic Investigation ◽  
Electrocatalytic Activity ◽  
Crucial Role ◽  
Structural Order

In situ spectroscopic investigation elucidates the crucial role of local structural order in the excellent electrocatalytic activity of crystalline MnO2.

scholarly journals The Role of Al3+-Based Aqueous Electrolytes in the Charge Storage Mechanism of MnOx Cathodes

2020 ◽  
Author(s):  
Véronique Balland ◽  
Mickaël Mateos ◽  
Kenneth D. Harris ◽  
Benoit Limoges
Keyword(s):  
Manganese Oxide ◽  
Critical Analysis ◽  
Charge Storage ◽  
Aqueous Electrolytes ◽  
Storage Mechanism ◽  
Main Charge ◽  
Charge Storage Mechanism ◽  
The Subject

<p>Rechargeable aqueous aluminium batteries are the subject of growing interest, but the charge storage mechanisms at manganese oxide-based cathodes remain poorly understood with as many mechanisms as studies. Here, we use an original <i>in situ</i> spectroelectrochemical methodology to unambiguously demonstrate that the reversible proton-coupled MnO<sub>2</sub>-to-Mn<sup>2+</sup> conversion is the main charge storage mechanism occurring at MnO<sub>2</sub> cathodes over a range of slightly acidic Al<sup>3+</sup>-based aqueous electrolytes. In Zn/MnO<sub>2</sub> assemblies, this mechanism is associated with high gravimetric capacity and discharge potentials, up to 560 mAh·g<sup>-1</sup> and 1.76 V respectively, attractive efficiencies (<i>CE</i> > 98.5 % and <i>EE</i> > 80%) and excellent cyclability (> 750 cycles at 10 A·g<sup>-1</sup>). Finally, we conducted a critical analysis of the data previously published on MnO<sub>x</sub> cathodes in Al<sup>3+</sup>-based aqueous electrolytes to conclude on a universal charge storage mechanism, <i>i.e.</i>, the reversible electrodissolution/electrodeposition of MnO<sub>2</sub>.<i></i></p>

scholarly journals Different roles for two enhancer domains in the organ- and age-specific pattern of polyomavirus replication in the mouse.

1992 ◽  
Vol 12 (8) ◽  
pp. 3628-3635 ◽  
Author(s):  
A Amalfitano ◽  
L G Martin ◽  
M M Fluck
Keyword(s):  
Transcription Factors ◽  
In Situ Hybridization ◽  
Mammary Gland ◽  
Crucial Role ◽  
Specific Pattern ◽  
Neonatal Stage ◽  
Murine Polyomavirus ◽  
A Domains

Viral replication in mice infected with murine polyomavirus strains with novel enhancer rearrangements was analyzed by direct in situ hybridization of whole mouse sections and by hybridization of nucleic acids extracted from a specific set of organs. The enhancer rearrangements included a deletion of the B domain as well as duplications within the A domain. Comparisons between enhancer variants demonstrate that the B domain plays an important role in replication in most organs, in particular in the kidney, at the neonatal stage (days 0 to 7 postbirth). In contrast, the B domain is not required in those organs which can sustain replication in the adult, i.e. mammary gland, skin, and bone (class I organs [J. J. Wirth, A. Amalfitano, R. Gross, M. B. A. Oldstone, and M. M. Fluck, J. Virol. 66:3278-3286, 1992]). Altogether, the results suggest that the B and A domains mediate very different functions in infection of mice, controlling the acute and persistent phases of infection, respectively. A model of mouse infection based on the crucial role of differentially expressed host transcription factors is presented.

Cobalt-catalyzed direct transformation of aldehydes to esters: the crucial role of an enone as a mediator

2019 ◽  
Vol 6 (6) ◽  
pp. 801-807 ◽  
Author(s):  
Biao-Lin Jiang ◽  
Yang Lin ◽  
Meng-Liang Wang ◽  
Dian-Sheng Liu ◽  
Bao-Hua Xu ◽  
...  
Keyword(s):  
Crucial Role ◽  
Direct Transformation ◽  
Oxidative Esterification ◽  
Low Valent

An oxidative esterification of aldehydes with alkanols catalyzed by an in situ generated low-valent cobalt system has been developed using an enone as a mild oxidant.

Role of Satellite Technology in Oceanic Study

2018 ◽  
pp. 80-103
Author(s):  
Thomas Mathew
Keyword(s):  
Remote Sensing ◽  
Electromagnetic Radiation ◽  
Crucial Role ◽  
Near Infrared ◽  
Thermal Infrared ◽  
Microwave Region ◽  
Satellite Technology ◽  
The Earth

The three-fourth surface of the earth is covered with ocean. The study of the ocean is important for sustainable overall development of a nation and world at large in view of it being rich in resources and playing a crucial role in the climate of the region and changes associated with it. The space-based observations assume significance, as it provides synoptic and repetitive coverage of the ocean in contrast to the sparse and isolated in-situ buoy or ship observations. The remote sensing of the ocean with the help of satellite or satellite oceanography has many other applications also. The electromagnetic radiation in the visible, near infrared, thermal infrared, and microwave regions are used by the sensors on-board space platforms to measure the diverse physical, biological, and geological parameters of the ocean. Amongst the various electromagnetic regions, the microwave region plays an important role in the study of the ocean.

Crucial role of interdiffusion on magnetic properties of in situ formed MgO∕Fe3−δO4 heterostructured nanowires

2008 ◽  
Vol 92 (17) ◽  
pp. 173119 ◽  
Author(s):  
Aurelian Marcu ◽  
Takeshi Yanagida ◽  
Kazuki Nagashima ◽  
Keisuke Oka ◽  
Hidekazu Tanaka ◽  
...  
Keyword(s):  
Magnetic Properties ◽  
Crucial Role

scholarly journals The Role of Al3+-Based Aqueous Electrolytes in the Charge Storage Mechanism of MnOx Cathodes

2020 ◽  
Author(s):  
Véronique Balland ◽  
Mickaël Mateos ◽  
Kenneth D. Harris ◽  
Benoit Limoges
Keyword(s):  
Manganese Oxide ◽  
Critical Analysis ◽  
Charge Storage ◽  
Aqueous Electrolytes ◽  
Storage Mechanism ◽  
Main Charge ◽  
Charge Storage Mechanism ◽  
The Subject

<p>Rechargeable aqueous aluminium batteries are the subject of growing interest, but the charge storage mechanisms at manganese oxide-based cathodes remain poorly understood with as many mechanisms as studies. Here, we use an original <i>in situ</i> spectroelectrochemical methodology to unambiguously demonstrate that the reversible proton-coupled MnO<sub>2</sub>-to-Mn<sup>2+</sup> conversion is the main charge storage mechanism occurring at MnO<sub>2</sub> cathodes over a range of slightly acidic Al<sup>3+</sup>-based aqueous electrolytes. In Zn/MnO<sub>2</sub> assemblies, this mechanism is associated with high gravimetric capacity and discharge potentials, up to 560 mAh·g<sup>-1</sup> and 1.76 V respectively, attractive efficiencies (<i>CE</i> > 98.5 % and <i>EE</i> > 80%) and excellent cyclability (> 750 cycles at 10 A·g<sup>-1</sup>). Finally, we conducted a critical analysis of the data previously published on MnO<sub>x</sub> cathodes in Al<sup>3+</sup>-based aqueous electrolytes to conclude on a universal charge storage mechanism, <i>i.e.</i>, the reversible electrodissolution/electrodeposition of MnO<sub>2</sub>.<i></i></p>

Different roles for two enhancer domains in the organ- and age-specific pattern of polyomavirus replication in the mouse

1992 ◽  
Vol 12 (8) ◽  
pp. 3628-3635
Author(s):  
A Amalfitano ◽  
L G Martin ◽  
M M Fluck
Keyword(s):  
Transcription Factors ◽  
In Situ Hybridization ◽  
Mammary Gland ◽  
Crucial Role ◽  
Specific Pattern ◽  
Neonatal Stage ◽  
Murine Polyomavirus ◽  
A Domains

Viral replication in mice infected with murine polyomavirus strains with novel enhancer rearrangements was analyzed by direct in situ hybridization of whole mouse sections and by hybridization of nucleic acids extracted from a specific set of organs. The enhancer rearrangements included a deletion of the B domain as well as duplications within the A domain. Comparisons between enhancer variants demonstrate that the B domain plays an important role in replication in most organs, in particular in the kidney, at the neonatal stage (days 0 to 7 postbirth). In contrast, the B domain is not required in those organs which can sustain replication in the adult, i.e. mammary gland, skin, and bone (class I organs [J. J. Wirth, A. Amalfitano, R. Gross, M. B. A. Oldstone, and M. M. Fluck, J. Virol. 66:3278-3286, 1992]). Altogether, the results suggest that the B and A domains mediate very different functions in infection of mice, controlling the acute and persistent phases of infection, respectively. A model of mouse infection based on the crucial role of differentially expressed host transcription factors is presented.

scholarly journals The Involvement of the Androgen Receptor in the Secretion of the Epididymalcorpusin the LizardPodarcis sicula

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Mariailaria Verderame
Keyword(s):  
Androgen Receptor ◽  
Estrogen Receptors ◽  
Expression Pattern ◽  
Crucial Role ◽  
Secretory Activity ◽  
Seasonal Breeding ◽  
Podarcis Sicula ◽  
Mating Period

A crucial role in the maintenance of male reproductive functions is carried out by the androgen through its receptor in balance with the estrogen receptors (ERs). The distribution of the androgen receptor (AR) is well documented in the testis and in the reproductive tissues of mammals but the findings about the AR in nonmammalian vertebrates and in particular in reptiles are very scarce. Here by means ofin situhybridization (ISH) we investigated the AR expression along the epididymal channel (efferent ductules,corpus, andcauda) ofPodarcis siculaduring the mating and nonmating period. The results show that in this seasonal breeding species the AR expression pattern is always constant throughout the epididymis. The administration of estradiol-17βin the mating period does not affect the AR expression but inhibits the secretory activity of the epididymalcorpus. To verify the expression pattern of ERs, we also conducted ISH investigations on adjacent sections with ERs probes. The findings suggest that AR induces the secretory activity in the epithelial cells of the epididymalcorpusand confirm our previous results that showed the role of ERalpha (ERα) as switch off for the secretion of this compartment.

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