29 research outputs found

    Redox Flow Battery for Continuous and Energy-Effective Lithium Recovery from Aqueous Solution

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    Lithium-ion batteries are the primary power source for electric vehicles and portable electronic devices, creating a massive demand to mine and extract lithium. So far, lithium extraction has focused on brine and geological deposits. Yet, access to the enormous amount of lithium (at low concentration) in the earth’s oceans and other aqueous media remains challenging. Electrodialysis with Li-selective ceramic membranes could effectively separate lithium from seawater but at a high energy cost. Reversible electrochemical processes, like redox flow batteries, can overcome the limitation of electrodialysis-based systems. Herein we propose a system combining Li-selective ceramic membranes and a simple redox flow electrolyte to accomplish continuous lithium recovery from seawater. The lithium-extraction redox flow battery (LE-RFB) extracts dissolved lithium with a purity of 93.5% from simulated seawater, corresponding to a high Li/Mg selectivity factor of about 500.000:1. Benefiting from a low operating voltage, 1 g of lithium is extracted with only 2.5 Wh of energy consumption

    Citric Acid-Assisted Two-Step Enrichment with TiO<sub>2</sub> Enhances the Separation of Multi- and Monophosphorylated Peptides and Increases Phosphoprotein Profiling

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    Phosphopeptide enrichment is essential for large-scale phosphoprotein profiling. Titanium dioxide (TiO<sub>2</sub>) is widely used in phosphopeptide enrichment, but it is limited in the isolation of multiphosphorylated peptides due to their strong binding. In this study, we found that citric acid greatly affects the binding of mono- and multiphosphopeptides with TiO<sub>2</sub>, which can be used for stepwise phosphopeptide separation coupled with mass spectrum (MS) identification. We first loaded approximately 1 mg of peptide mixture of HeLa cell digests onto TiO<sub>2</sub> beads in highly concentrated citric acid (1 M). Then the flow-through fraction was diluted to ensure low concentration of citric acid (50 mM) and followed by loading onto another aliquot of TiO<sub>2</sub> beads. The two eluted fractions were subjected to nanoLC–MS/MS analysis. We identified 1,500 phosphorylated peptides, of which 69% were multiphosphorylated after the first enrichment. After the second enrichment, 2,167 phosphopeptides, of which 92% were monophosphorylated, were identified. In total, we successfully identified 3,136 unique phosphopeptides containing 3,973 phosphosites utilizing this strategy. Finally, more than 37% of the total phosphopeptides and 2.6-fold more of the multiphosphorylated peptides were identified as compared to the frequently used DHB/TiO<sub>2</sub> enrichment strategy. Combining SCX with CATSET, we identified 14,783 phosphopeptides and 15,713 phosphosites, of which 3,678 were unrecorded in PhosphoSitePlus database. This two-step separation procedure for sequentially enriching multi- and monophosphorylated peptides by using citric acid is advantageous in multiphosphorylated peptide separation, as well as for more comprehensive phosphoprotein profiling

    Visualization 1: Pump-probe imaging of the fs-ps-ns dynamics during femtosecond laser Bessel beam drilling in PMMA

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    An animation showing the evolution process during fs laser Bessel beam drilling in PMMA Originally published in Optics Express on 14 December 2015 (oe-23-25-32728

    Citric Acid-Assisted Two-Step Enrichment with TiO<sub>2</sub> Enhances the Separation of Multi- and Monophosphorylated Peptides and Increases Phosphoprotein Profiling

    No full text
    Phosphopeptide enrichment is essential for large-scale phosphoprotein profiling. Titanium dioxide (TiO<sub>2</sub>) is widely used in phosphopeptide enrichment, but it is limited in the isolation of multiphosphorylated peptides due to their strong binding. In this study, we found that citric acid greatly affects the binding of mono- and multiphosphopeptides with TiO<sub>2</sub>, which can be used for stepwise phosphopeptide separation coupled with mass spectrum (MS) identification. We first loaded approximately 1 mg of peptide mixture of HeLa cell digests onto TiO<sub>2</sub> beads in highly concentrated citric acid (1 M). Then the flow-through fraction was diluted to ensure low concentration of citric acid (50 mM) and followed by loading onto another aliquot of TiO<sub>2</sub> beads. The two eluted fractions were subjected to nanoLC–MS/MS analysis. We identified 1,500 phosphorylated peptides, of which 69% were multiphosphorylated after the first enrichment. After the second enrichment, 2,167 phosphopeptides, of which 92% were monophosphorylated, were identified. In total, we successfully identified 3,136 unique phosphopeptides containing 3,973 phosphosites utilizing this strategy. Finally, more than 37% of the total phosphopeptides and 2.6-fold more of the multiphosphorylated peptides were identified as compared to the frequently used DHB/TiO<sub>2</sub> enrichment strategy. Combining SCX with CATSET, we identified 14,783 phosphopeptides and 15,713 phosphosites, of which 3,678 were unrecorded in PhosphoSitePlus database. This two-step separation procedure for sequentially enriching multi- and monophosphorylated peptides by using citric acid is advantageous in multiphosphorylated peptide separation, as well as for more comprehensive phosphoprotein profiling

    Citric Acid-Assisted Two-Step Enrichment with TiO<sub>2</sub> Enhances the Separation of Multi- and Monophosphorylated Peptides and Increases Phosphoprotein Profiling

    No full text
    Phosphopeptide enrichment is essential for large-scale phosphoprotein profiling. Titanium dioxide (TiO<sub>2</sub>) is widely used in phosphopeptide enrichment, but it is limited in the isolation of multiphosphorylated peptides due to their strong binding. In this study, we found that citric acid greatly affects the binding of mono- and multiphosphopeptides with TiO<sub>2</sub>, which can be used for stepwise phosphopeptide separation coupled with mass spectrum (MS) identification. We first loaded approximately 1 mg of peptide mixture of HeLa cell digests onto TiO<sub>2</sub> beads in highly concentrated citric acid (1 M). Then the flow-through fraction was diluted to ensure low concentration of citric acid (50 mM) and followed by loading onto another aliquot of TiO<sub>2</sub> beads. The two eluted fractions were subjected to nanoLC–MS/MS analysis. We identified 1,500 phosphorylated peptides, of which 69% were multiphosphorylated after the first enrichment. After the second enrichment, 2,167 phosphopeptides, of which 92% were monophosphorylated, were identified. In total, we successfully identified 3,136 unique phosphopeptides containing 3,973 phosphosites utilizing this strategy. Finally, more than 37% of the total phosphopeptides and 2.6-fold more of the multiphosphorylated peptides were identified as compared to the frequently used DHB/TiO<sub>2</sub> enrichment strategy. Combining SCX with CATSET, we identified 14,783 phosphopeptides and 15,713 phosphosites, of which 3,678 were unrecorded in PhosphoSitePlus database. This two-step separation procedure for sequentially enriching multi- and monophosphorylated peptides by using citric acid is advantageous in multiphosphorylated peptide separation, as well as for more comprehensive phosphoprotein profiling

    Carbon Disulfide Cosolvent Electrolytes for High-Performance Lithium Sulfur Batteries

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    Development of lithium sulfur (Li–S) batteries with high Coulombic efficiency and long cycle stability remains challenging due to the dissolution and shuttle of polysulfides in electrolyte. Here, a novel additive, carbon disulfide (CS<sub>2</sub>), to the organic electrolyte is reported to improve the cycling performance of Li–S batteries. The cells with the CS<sub>2</sub>-additive electrolyte exhibit high Coulombic efficiency and long cycle stability, showing average Coulombic efficiency >99% and a capacity retention of 88% over the entire 300 cycles. The function of the CS<sub>2</sub> additive is 2-fold: (1) it inhibits the migration of long-chain polysulfides to the anode by forming complexes with polysulfides and (2) it passivates electrode surfaces by inducing the protective coatings on both the anode and the cathode

    The Short- and Long-Term Risk of Stroke after Herpes Zoster: A Meta-Analysis

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    <div><p>Background</p><p>Accumulating evidence indicates that stroke risk may be increased following herpes zoster. The aim of this study is to perform a meta-analysis of current literature to systematically analyze and quantitatively estimate the short and long-term effects of herpes zoster on the risk of stroke.</p><p>Methods</p><p>Embase, PubMed and Cochrane library databases were searched for relevant studies up to March 2016. Studies were selected for analysis based on certain inclusion and exclusion criteria. Relative risks with 95% confidence interval (CI) were extracted to assess the association between herpes zoster and stroke.</p><p>Results</p><p>A total of 8 articles were included in our analysis. The present meta-analysis showed that the risks of stroke after herpes zoster were 2.36 (95% CI: 2.17–2.56) for first 2 weeks, 1.56 (95% CI: 1.46–1.66) for first month, 1.17 (95% CI: 1.13–1.22) for first year, and 1.09 (95% CI: 1.02–1.16) for more than 1 year, respectively.</p><p>Conclusion</p><p>The results of our study demonstrated that herpes zoster was associated with a higher risk of stroke, but the risks decreased along with the time after herpes zoster.</p></div

    Flow diagram of the search result for the meta-analysis.

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    <p>The figure shows detailed information in the process of search, review, exclusion and inclusion of the potential articles.</p

    Secretome Analyses of Aβ<sub>1–42</sub> Stimulated Hippocampal Astrocytes Reveal that CXCL10 is Involved in Astrocyte Migration

    No full text
    Amyloid-beta (Aβ) aggregation plays an important role in the development of Alzheimer’s disease (AD). In the AD brain, amyloid plaques are surrounded by reactive astrocytes, and many essential functions of astrocytes have been reported to be mediated by protein secretion. However, the roles of activated astrocytes in AD progression are under intense debate. To provide an in-depth view of the secretomes of activated astrocytes, we present in this study a quantitative profile of rat hippocampal astrocyte secretomes at multiple time points after both brief and sustained Aβ<sub>1–42</sub> stimulation. Using SILAC labeling and LC–MS/MS analyses, we identified 19 up-regulated secreted proteins after Aβ<sub>1–42</sub> treatment. These differentially expressed proteins have been suggested to be involved in key aspects of biological processes, such as cell recruitment, Aβ clearance, and regulation of neurogenesis. Particularly, we validated the role played by CXCL10 in promoting astrocyte aggregation around amyloid plagues through <i>in vitro</i> cell migration analysis. This research provides global, quantitative profiling of astrocyte secretomes produced on Aβ stimulation and hence provides a detailed molecular basis for the relationship between amyloid plaques and astrocyte aggregation; the findings thus have important implications for further investigations into AD development and therapy

    Secretome Analyses of Aβ<sub>1–42</sub> Stimulated Hippocampal Astrocytes Reveal that CXCL10 is Involved in Astrocyte Migration

    No full text
    Amyloid-beta (Aβ) aggregation plays an important role in the development of Alzheimer’s disease (AD). In the AD brain, amyloid plaques are surrounded by reactive astrocytes, and many essential functions of astrocytes have been reported to be mediated by protein secretion. However, the roles of activated astrocytes in AD progression are under intense debate. To provide an in-depth view of the secretomes of activated astrocytes, we present in this study a quantitative profile of rat hippocampal astrocyte secretomes at multiple time points after both brief and sustained Aβ<sub>1–42</sub> stimulation. Using SILAC labeling and LC–MS/MS analyses, we identified 19 up-regulated secreted proteins after Aβ<sub>1–42</sub> treatment. These differentially expressed proteins have been suggested to be involved in key aspects of biological processes, such as cell recruitment, Aβ clearance, and regulation of neurogenesis. Particularly, we validated the role played by CXCL10 in promoting astrocyte aggregation around amyloid plagues through <i>in vitro</i> cell migration analysis. This research provides global, quantitative profiling of astrocyte secretomes produced on Aβ stimulation and hence provides a detailed molecular basis for the relationship between amyloid plaques and astrocyte aggregation; the findings thus have important implications for further investigations into AD development and therapy
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