Na/beta-alumina/NaAlCl4, Cl2/C circulating cell

A study was made of a high specific energy battery based on a sodium negative electrode and a chlorine positive electrode with molten AlCl3-NaCl electrolyte and a solid beta alumina separator. The basic performance of a Na beta-alumina NaAlCl4, Cl2/C circulating cell at 200 C was demonstrated. This cell can be started at 150 C. The use of melting sodium chloroaluminate electrolyte overcomes some of the material problems associated with the high working temperatures of present molten salt systems, such as Na/S and LiAl/FeS, and retains the advantages of high energy density and relatively efficient electrode processes. Preliminary investigations were conducted on a sodium-chlorine static cell, material compability, electrode design, wetting, and theoretical calculations to assure a better chance of success before assembling a Na/Cl2 circulating cell. Mathematical models provide a theoretical explanation for the performance of the NaCl2 battery. The results of mathematical models match the experimental results very well. According to the result of the mathematical modeling, an output at 180 mA/sq cm and 3.2 V can be obtained with optimized cell design

Proteomics Analysis of the Expression of Neurogranin in Murine Neuroblastoma (Neuro-2a) Cells Reveals Its Involvement for Cell Differentiation

Neurogranin (Ng) is a neural-specific, calmodulin (CaM)-binding protein that is phosphorylated by protein kinase C (PKC). Although its biochemical property has been well characterized, the physiological function of Ng needs to be elucidated. In the present study, we performed proteomics analysis of the induced compositional changes due to the expression of Ng in murine neuroblastoma (Neuro-2a) cells using isotope coded affinity tags (ICAT) combined with 2-dimensional liquid chromatography/tandem mass spectrometry (2D-LC/MS/MS). We found that 40% of identified proteins were down-regulated and most of these proteins are microtubule components and associated proteins that mediated neurite outgrowth. Western blot experiments confirmed the expression of α-tubulin and microtubule- associated protein 1B (MAP 1B) was dramatically reduced in Neuro-2a-Ng cells compared to control. Cell morphology of Neuro-2a-Ng showed far less neurites than the control. Serum deprivation induced the extension of only one or two long neurites per cell in Neuro-2a-Ng, contrasting to the extension of multiple neurites per control cell. Ng may be linked to neurite formation by affecting expression of several microtubule related proteins. Furthermore, the PKC activator (PMA) induced an enhanced ERK1/2 activity in the cells that expressed Ng. The mutation of Ng at S36A caused sustained increase of ERK1/2 activity, whereas the ERK1/2 activity in mutation at I33Q showed no difference compared to wild type Ng, suggesting the phosphorylation of Ng but not the CaM /Ng interaction plays an important role in ERK activation. Ng may be involved in neuronal growth and differentiation via PKC and ERK1/2 signaling pathways

Endocytic Pathways Downregulate the L1-type Cell Adhesion Molecule Neuroglian to Promote Dendrite Pruning in Drosophila

SummaryPruning of unnecessary axons and/or dendrites is crucial for maturation of the nervous system. However, little is known about cell adhesion molecules (CAMs) that control neuronal pruning. In Drosophila, dendritic arborization neurons, ddaCs, selectively prune their larval dendrites. Here, we report that Rab5/ESCRT-mediated endocytic pathways are critical for dendrite pruning. Loss of Rab5 or ESCRT function leads to robust accumulation of the L1-type CAM Neuroglian (Nrg) on enlarged endosomes in ddaC neurons. Nrg is localized on endosomes in wild-type ddaC neurons and downregulated prior to dendrite pruning. Overexpression of Nrg alone is sufficient to inhibit dendrite pruning, whereas removal of Nrg causes precocious dendrite pruning. Epistasis experiments indicate that Rab5 and ESCRT restrain the inhibitory role of Nrg during dendrite pruning. Thus, this study demonstrates the cell-surface molecule that controls dendrite pruning and defines an important mechanism whereby sensory neurons, via endolysosomal pathway, downregulate the cell-surface molecule to trigger dendrite pruning

Cytoskeletal protein expression was down- regulated in Neuro-2a-Ng cells

<p><b>Copyright information:</b></p><p>Taken from "Proteomics Analysis of the Expression of Neurogranin in Murine Neuroblastoma (Neuro-2a) Cells Reveals Its Involvement for Cell Differentiation"</p><p></p><p>International Journal of Biological Sciences 2007;3(5):263-273.</p><p>Published online 19 Apr 2007</p><p>PMCID:PMC1865092.</p><p>© Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.</p> , A typical μLC/MS spectrum of an ICAT-labeled sample. Proteins from Neuro-2a-Ng cells were labeled with heavy C reagent and those from Neuro-2a control were labeled with C reagent. The C/C ratio of this ICAT labeled molecular ion pair was 0.4, representing the relative abundance of one peptide derived from Neuro-2a-Ng and Neuro-2a. , Western blot validation of ICAT mass spectrometry results. The identities and corresponding C/C ratios for the protein in this figure are as follows: MAP1B (0.3), α-tubulin (0.5). GAPDH is loading control. GAPDH was used as the loading control (5 μg of protein/lane)

The expression of Ng induced sustained activation and up-regulation of ERK1/2 phosphorylation by PMA treatment in Neuro-2a-Ng cells

<p><b>Copyright information:</b></p><p>Taken from "Proteomics Analysis of the Expression of Neurogranin in Murine Neuroblastoma (Neuro-2a) Cells Reveals Its Involvement for Cell Differentiation"</p><p></p><p>International Journal of Biological Sciences 2007;3(5):263-273.</p><p>Published online 19 Apr 2007</p><p>PMCID:PMC1865092.</p><p>© Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.</p> The time points after the treatment of 300 nM PMA were shown above. The phosphorylation of ERK1/2, total ERK1/2 and Ng expression level were detected by Western blot analysis (10 μg of protein/lane) (A). The quantitation of Western blot images of the ratio between phospho-ERK1/2 and total-ERK was shown in B. *p < 0.05 and **p < 0.001, comparing Neuro-2a-Ng to Neuro-2a cells (n = 3)

Phosphorylation of ERK1/2 after 300 nM PMA treatment in HEK293 transiently transfected with EGFP or EGFP-Ng wild-type

<p><b>Copyright information:</b></p><p>Taken from "Proteomics Analysis of the Expression of Neurogranin in Murine Neuroblastoma (Neuro-2a) Cells Reveals Its Involvement for Cell Differentiation"</p><p></p><p>International Journal of Biological Sciences 2007;3(5):263-273.</p><p>Published online 19 Apr 2007</p><p>PMCID:PMC1865092.</p><p>© Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.</p> The time points after the treatment of 300 nM PMA were shown above. The phosphorylation of ERK1/2, total ERK1/2, Ng expression level and the phosphorylation of Ng were detected by Western blot analysis (10 μg of protein/lane) (A). The quantitation of Western blot images of the ratio between phospho-ERK1/2 and total-ERK was shown in B. *p < 0.05 and **p < 0.001, comparing wild type HEK293 to HEK293 cells transfected with Ng (n = 4)

Multi-Agent System Fault Protection with Topology Identification in Microgrids

Data acquisition and supervisory control are usually performed using client-server architecture and centralized control in conventional power systems. However, the message transmission and fault clearing are too slow for large-scale complex power systems. Microgrid systems have various types of distributed energy resources (DERs) which are quite different in characteristics and capacities, thus, the client-server architecture and centralized control are inadequate to control and operate in microgrids. Based on MATLAB/Simulink (ver.R2012a) simulation software and Java Agent Development Framework (JADE) (JADE 4.1.1-revision 6532), this paper proposes a novel fault protection technology that used multi-agent system (MAS) to perform fault detection, fault isolation and service restoration in microgrids. A new topology identification method using the YBus Matrix Algorithm is presented to successfully recognize the network configurations. The identification technology can respond to microgrid variations. Furthermore, the interactive communications among intelligent electronic devices (IEDs), circuit breakers (CBs), and agents are clarified during fault occurrence. The simulation results show that the proposed MAS-based microgrids can promptly isolate faults and protect the system against faults in real time

ALS motor neurons exhibit hallmark metabolic defects that are rescued by SIRT3 activation

10.1038/s41418-020-00664-0Cell Death and Differentiation2841379-139

Slimb forms a protein complex with Akt and promotes Akt ubiquitination.

<p>(A–C and E–F″) Confocal images show Akt stainings (in red) in various genotypes of ddaC neurons expressing <i>UAS-mCD8-GFP</i> driven by <i>ppk</i>-<i>Gal4</i> at WP. ddaC somas/dendrites/axons are marked by dashed lines. Endogenous Akt level was significantly upregulated in the somas of <i>cul1</i> RNAi ddaC neurons (B and D) compared to that in the control RNAi somas (A and D). Akt signals were abolished in <i>akt</i> RNAi ddaC neurons (C and D). Overexpressed Akt is upregulated in <i>cul1</i> RNAi ddaC somas, dendrites, and axons (F–F″ and G), compared to the control RNAi (E–E″ and G). Quantification of Akt immunostaining was performed as described in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1001657#s4" target="_blank">Materials and Methods</a> (D and G). The graph displays the normalized Akt immunostaining intensity and S.E.M.; <i>n</i> is shown on the bars ***<i>p</i><0.001. The scale bars are 5 µm. (H) Akt expression and activity were upregulated in the <i>cul1</i> RNAi brain extracts. (I) Slimb and Akt associated each other in S2 cells cotransfected with Flag-Slimb and Myc-Akt. (J) Akt associated with Myc-Slimb in brain extracts expressing Myc-Slimb and Akt. (K) The mutant F-box protein, Slimb^ΔWD40, lacking its substrate-recognition WD40 domains, did not associate with Akt in S2 cells co-transfected with Myc-Slimb^ΔWD40 and Flag-Akt. (L) In vivo ubiquitination assay, Slimb but not Slimb^ΔWD40 enhanced ubiquitination of Akt in S2 cells overexpressing HA-Ubiquitin, Myc-Akt, and Flag-Slimb or Flag-Slimb^ΔWD40. * indicates a nonspecific band. See genotypes in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1001657#pbio.1001657.s023" target="_blank">Text S1</a>.</p