29 research outputs found
Redox Flow Battery for Continuous and Energy-Effective Lithium Recovery from Aqueous Solution
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
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
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
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
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
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
<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.
<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
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
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