Dynamic Structural Equation Models with Missing Data: Data Requirements on <i>N</i> and <i>T</i>

Dynamic structural equation modeling (DSEM) is a useful technique for analyzing intensive longitudinal data. A challenge of applying DSEM is the missing data problem. The impact of missing data on DSEM, especially on widely applied DSEM such as the two-level vector autoregressive (VAR) cross-lagged models, however, is understudied. To fill the research gap, we evaluated how well the fixed effects and variance parameters in two-level bivariate VAR models are recovered under different missingness percentages, sample sizes, the number of time points, and heterogeneity in missingness distributions through two simulation studies. To facilitate the use of DSEM under customized data and model scenarios (different from those in our simulations), we provided illustrative examples of how to conduct Monte Carlo simulations in Mplus to determine whether a data configuration is sufficient to obtain accurate and precise results from a specific DSEM.</p

Complexing Cations by Poly(ethylene oxide): Binding Site and Binding Mode

The binding of K⁺ and Ba²⁺ cations to short poly­(ethylene oxide) (PEO) chains with ca. 4–25 monomeric units in methanol was studied by determining the effective charge of the polymer through a combination of electrophoretic NMR and diffusion NMR experiments. These cations were previously found to bind to long PEO chains in a similar strong manner. In addition, ¹H chemical shift and longitudinal spin relaxation rate changes upon binding were quantified. For both systems, binding was stronger for the short chains than that for the longer chains, which is attributed mainly to interactions between bound ions. For K⁺ ions, the equilibrium binding constant of a cation to a binding site was measured. For both cations, the binding site was estimated to consist of ca. six monomeric units that coordinated with the respective ions. For the systems with barium, a significant fraction of the bound ions are (BaAnion)⁺ ion pairs. This leads to a strong anion effect in the effective charge of the oligomers acquired upon barium ion binding. For K⁺, the coordinating oligomer segment remains rather mobile and individual oligomers exchange rapidly (≪s) between their free and ion-complexing states. In contrast, segmental dynamics slows significantly for the oligomer section that coordinates with the barium species, and for individual oligomers, binding and nonbinding sections do not exchange on the time scale of seconds. Hence, oligomers also exchange slowly (>s) between their free and barium complexing states

Oleosin phylogeny in land plants inferred by maximum likelihood analysis of nucleotide sequences.

<p>The topology is rooted by <i>Marchantia polymorpha</i> representing the most basally diverging lineage of land plants, liverworts. The three oleosin isoforms are framed separately. The information followed the second underscore in each terminal node shows the position of intron in oleosin nucleotide sequences. Abbreviations used in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0103806#pone-0103806-g004" target="_blank">Figures 4</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0103806#pone-0103806-g005" target="_blank">5</a> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0103806#pone-0103806-g007" target="_blank">7</a> are as follows: OLE, published or submitted oleosin genes in GenBank (For more information, see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0103806#pone.0103806.s001" target="_blank">Table S1</a> online); ole (lower case), predicted oleosin genes from sequenced species in Joint Genome Institute database in this study; 0 (the number behind the second underscore in terminal node), no intron insertion in encoding region; 1(P), the site of intron insertion before the central domain coding region; (P)1, the site of intron insertion after the central domain coding region.</p

Additional file 6: Figure S4. of Molecular phylogeny of Anopheles hyrcanus group members based on ITS2 rDNA

Partial results of the sensitivity test of the Multiplex PCR for the five Hyrcanus Group members. (PDF 475 kb

Additional file 1: Table S1. of Molecular phylogeny of Anopheles hyrcanus group members based on ITS2 rDNA

List of the Anopheles hyrcanus group ITS2 sequences deposited in GenBank and obtained from this study, with GenBank accession numbers, geographical location, and corresponding authors. (XLSX 50 kb

Complete amino acid sequence comparison of three oleosin isoforms from diverse species.

<p>The alignments were generated with the clustalW2 program and then adjusted manually to optimize the alignment. Residues with the highest conservation are in black, while similar residues are shaded in gray. Oleosin isoforms are indicated on the right side. Dots above the sequences display the central hydrophobic region (72 amino acids). The four invariable residues of the proline knot sequence (-PX₅SPX₃P-) are highlighted with brackets. The 18-amino acid insertions present in the C-terminus domain both in M-oleosins and H-oleosins are boxed. Unaligned residues are shown as dashes within the sequence. Abbreviations: M_pol: <i>Marchantia polymorpha</i>; P_pat: <i>Physcomitrella patens</i>; S_moe: <i>Selaginella moellendorffii</i>; P_tae: <i>Pinus taeda</i>; A_tha: <i>Arabidopsis thaliana</i>.</p

Evolution of Oleosin in Land Plants

<div><p>Oleosins form a steric barrier surface on lipid droplets in cytoplasm, preventing them from contacting and coalescing with adjacent droplets. Oleosin genes have been detected in numerous plant species. However, the presence of oleosin genes in the most basally diverging lineage of land plants, liverworts, has not been reported previously. Thus we explored whether liverworts have an oleosin gene. In <i>Marchantia polymorpha</i> L., a thalloid liverwort, one predicted sequence was found that could encode oleosin, possessing the hallmark of oleosin, a proline knot (-PX₅SPX₃P-) motif. The phylogeny of the oleosin gene family in land plants was reconstructed based on both nucleotide and amino acid sequences of oleosins, from 31 representative species covering almost all the main lineages of land plants. Based on our phylogenetic trees, oleosin genes were classified into three groups: M-oleosins (defined here as a novel group distinct from the two previously known groups), low molecular weight isoform (L-oleosin), and high molecular weight isoform (H-oleosin), according to their amino-acid organization, phylogenetic relationships, expression tissues, and immunological characteristics. In liverworts, mosses, lycophytes, and gymnosperms, only M-oleosins have been described. In angiosperms, however, while this isoform remains and is highly expressed in the gametophyte pollen tube, two other isoforms also occur, L-oleosins and H-oleosins. Phylogenetic analyses suggest that the M-oleosin isoform is the precursor to the ancestor of L-oleosins and H-oleosins. The later two isoforms evolved by successive gene duplications in ancestral angiosperms. At the genomic level, most oleosins possess no introns. If introns are present, in both the L-isoform and the M-isoform a single intron inserts behind the central region, while in the H-isoform, a single intron is located at the 5′-terminus. This study fills a major gap in understanding functional gene evolution of oleosin in land plants, shedding new light on evolutionary transitions of lipid storage strategies.</p></div

The model transition of the three oleosin isoform distributions (percentage) in genomes of land plants throughout evolution.

<p>The model transition of the three oleosin isoform distributions (percentage) in genomes of land plants throughout evolution.</p

The intron position in each of the three oleosin isoforms.

<p>At the nucleotide level, Joint Genome Institute database predict that most of oleosins possess no introns, whereas oleosin genes with intron insertion sites a single intron preceding or following the sequence encoding the central domain. The intron insertion sites are variable in oleosins, but nearly conserved within each isoform. The region of the central domain is labeled in the ‘consensus’ row. The intron positions are in between of the two encoding regions: exon1 and exon2. (A) M-oleosins; (B) L-oleosins; (C) H-oleosins.</p

Data_Sheet_3_Meta-analysis and systematic review of physical activity on neurodevelopment disorders, depression, and obesity among children and adolescents.PDF

BackgroundNo consensus on whether physical activity (PA) is related to physical and mental health among pediatric population remains has been reached to date. To further explore their association, our study assessed the effect of PA on physical and mental health of children and adolescents through a systematic review and meta-analysis of randomized controlled studies (RCTs).MethodsSeveral databases(Web of science, PubMed, Embase, Cochrane Central register of controlled trials, CINAHL) were searched from inception to 1st, December 2020 without language restrictions.Results38,236 records were identified primitively and 31 included studies with 1,255 participants eventually met our inclusion criteria, all of which exhibited a relatively low-moderate risk of bias of overall quality. In regard to mental health, the administration of PA, compared with the control group, led to moderate improvements in Autism Spectrum Disorder(ASD)[Standard mean difference (SMD) = −0.50, Confidence interval(CI): −0.87, −0.14)] and depression(SMD = −0.68, CI: −0.98, −0.38) among children and adolescents. Similarly, significant result was observed in obesity (SMD = −0.58, CI: −0.80, −0.36). No significant differences were observed in Attention deficit hyperactivity disorder (ADHD) (SMD = −0.29, CI: −0.59, 0.01).ConclusionAltogether, PA may have a beneficial effect on children and adolescents with ASD, depression and obesity; nevertheless, there is insufficient evidence to confirm its efficacy in ADHD. More large-scale population based randomized controlled trials are needed to explore more reliable evidence between them.</p