Ambient air pollution and COVID-19 in Delhi, India: a time-series evidence

This study aimed to explore the short-term health effects of ambient air pollutants PM2.5, PM10, SO2, NO2, O3, and CO on COVID-19 daily new cases and COVID-19 daily new deaths. A time-series design used in this study. Data were obtained from 1 April 2020 to 31 December 2020 in the National Capital Territory (NCT) of Delhi, India. The generalized additive models (GAMs) were applied to explore the associations of six air pollutants with COVID-19 daily new cases and COVID-19 daily new deaths. The GAMs revealed statistically significant associations of ambient air pollutants with COVID-19 daily new cases and COVID-19 daily new deaths. These findings suggest that governments need to give greater considerations to regions with higher concentrations of PM2.5, PM10, SO2, NO2, O3, and CO, since these areas may experience a more serious COVID-19 pandemic or, in general, any respiratory disease.</p

Additional file 1: Table S1 of Mesenchymal stem cells in cardiac regeneration: a detailed progress report of the last 6 years (2010–2015)

Clinical trials executed during 2010–2015 which used MSCs to treat heart diseases. (DOCX 36 kb

The actin affinity and T_M from the ellipticity at 222 nm and DSC melts.

a<p>The values for <i>K_app</i>, shown with standard errors. The data were fit to the Hill equation, and the <i>K_app</i> and α^H, Hill coefficient, are those reported by SigmaPlot (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-g006" target="_blank">Figure 6</a>).</p>b<p>T_M1 and T_M2 represent the tropomyosin transitions obtained in the absence of F-actin. T_M3 is the transition corresponding to tropomyosin dissociation from F-actin (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-g003" target="_blank">Figure 3</a>). The ΔΔH value was obtained by subtracting the total ΔH values of the endotherms in the presence and absence of F-actin. The difference is proportional to the amount of energy required for dissociation of tropomyosin bound F-actin.</p>c<p>T_M is the point at which 50% of tropomyosin is unfolded (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-g002" target="_blank">Figure 2</a>). The experimental conditions differ for the three analyses and are described in the <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#s4" target="_blank">Materials and Methods</a> as well as the figure legends. The values can be compared on a relative rather than absolute basis.</p

Tropomyosin period 2 and period 3 cluster and period shift mutants.^*

*<p>Residues in capitals are in proposed consensus actin binding positions <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone.0006336-Phillips2" target="_blank">[13]</a>. Residues in capitals and italics are consensus acting binding residues. Residues in lower case and italics are at the interface at the Ala cluster positions <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone.0006336-Brown1" target="_blank">[8]</a>. See <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-g001" target="_blank">Figure 1</a> to correlate with the structure.</p

Excimer fluorescence of PIA-labeled and light scattering of unlabeled P2 and P3 mutants.

<p>A. P2 control (C190S/L71C) B. P2Shift C190S/L71C C. P3 control (C190S/L113C). D. P3Shift C190S/L113C. Light scattering (red solid line and left axis with red label) was conducted with unlabeled tropomyosin due to interference from excimer peak in light scattering experiments with labeled tropomyosin. Excimer fluorescence (right axis) in the presence of actin (black solid line) and absence of actin (black dotted lines). Buffer conditions and the experimental procedure are as described for <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-g004" target="_blank">Figure 4</a>. The P2Shift and P3Shift mutations locally stabilize the interaction with actin.</p

The T_Ms of the light scattering, PIA excimer fluorescence, and unfolding.

a<p>T_M is the value for half maximal dissociation of tropomyosin from F-actin or the 50% decrease in light scattering (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-g004" target="_blank">Figures 4</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-g005" target="_blank">5</a>).</p>b<p>The value is the absolute maximum of the excimer peak in the presence of F-actin (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-g004" target="_blank">Figures 4</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-g005" target="_blank">5</a>).</p>c<p>T_M is the point at which 50% of tropomyosin is unfolded (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-g002" target="_blank">Figure 2</a>). Values in parentheses are unlabeled tropomyosins, except in the case of the Excimer Peak column in which values in ( ) are in the absence of F-actin.</p

Supplemental Material - Viloxazine for Attention-Deficit Hyperactivity Disorder: A Systematic Review and Meta-analysis of Randomized Clinical Trials

Supplemental Material for Viloxazine for Attention-Deficit Hyperactivity Disorder: A Systematic Review and Meta-analysis of Randomized Clinical Trials by Alok Singh, Mahesh K B, and Abhishek Singh in Journal of Central Nervous System Disease</p

Excimer fluorescence of PIA-labeled (at Cys190) and light scattering of unlabeled wildtype, P2Shift, and P3Shift mutants.

<p>A. PIA wt; B. PIA P2Shift; C. PIA P3Shift. Excimer fluorescence and light scattering experiments: Tropomyosin (6 µM) and TnT_70–170 (9 µM) were mixed with phalloidin (27 µM) stabilized F-actin (18 µM). Light scattering (red solid line and left axis with red label) was conducted with unlabeled tropomyosin due to interference from excimer peak in light scattering experiments with labeled tropomyosin. Excimer fluorescence (right axis) in the presence of actin (black solid line) and absence of actin (black dotted lines). Buffer conditions for all of the experiments: 100 mM NaCl, 10 mM sodium phosphate pH 7.5, 2 mM MgCl₂, 1 mM DTT. Experimental Procedure: The excimer temperature scans were repeated three times at a 1°C/min scan rate <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone.0006336-Levitsky1" target="_blank">[24]</a>. First, the sample was heated from 0–70°C and then cooled again. Second, the sample was heated to 90°C to denature the F-actin and subsequently cooled. In the third scan, post F-actin denaturation, the sample was heated to 70°C and the excimer peak is detected in the absence of actin. The first two scans, in the presence of actin, were marked with appearance of the excimer peak at higher temperatures, indicating actin-induced stabilization.</p

Models illustrating the P2 and P3 regions in wildtype and mutant tropomyosins.

<p>The side chains of the alanine clusters (magenta) and consensus actin binding sites (cyan) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone.0006336-Phillips2" target="_blank">[13]</a> are illustrated on a ribbon model of the 7 Å structure (pdb ID: 1C1G; <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone.0006336-Whitby1" target="_blank">[60]</a>). Period 2, residues 46–69, and period 3, residues 88–111, are enlarged with the side chains of interface Ala residues (in magenta, space filling), canonical interface residues (green) and consensus residues (cyan, C_β in spacefill). The colors used are the same as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-t001" target="_blank">Table 1</a>.</p

The effect on the thermal stability of the cluster and period replacement mutants.

<p>Fraction folded as measured by relative ellipticity at 222 nm as a function of temperature in 500 mM NaCl, 10 mM sodium phosphate pH 7.5, 1 mM EDTA, 0.5 mM DTT. The tropomyosin concentration was 0.01 mg/ml (1.6 µM). The T_Ms are reported in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-t002" target="_blank">Tables 2</a> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0006336#pone-0006336-t003" target="_blank">3</a>. The fraction folded is relative to the mean residue ellipticity at 0°C where the proteins were fully folded. A. Symbols: •, wildtype; ○, P3Shift, ▾, P2Shift. B. Symbols: •, wildtype; ○, P2P3Shift. C. Symbols: •, wildtype; ○, P5→P3.</p