Table_1_Identification of marker genes for spinal cord injury.DOCX

IntroductionSpinal cord injury (SCI) is a profoundly disabling and devastating neurological condition, significantly impacting patients’ quality of life. It imposes unbearable psychological and economic pressure on both patients and their families, as well as placing a heavy burden on society.MethodsIn this study, we integrated datasets GSE5296 and GSE47681 as training groups, analyzed gene variances between sham group and SCI group mice, and conducted Gene Ontology (GO) enrichment analysis and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analysis based on the differentially expressed genes. Subsequently, we performed Weighted Gene Correlation Network Analysis (WGCNA) and Lasso regression analyses.ResultsWe identified four characteristic disease genes: Icam1, Ch25h, Plaur and Tm4sf1. We examined the relationship between SCI and immune cells, and validated the expression of the identified disease-related genes in SCI rats using PCR and immunohistochemistry experiments.DiscussionIn conclusion, we have identified and verified four genes related to SCI: Icam1, Ch25h, Plaur and Tm4sf1, which could offer insights for SCI treatment.</p

Table_2_Identification of marker genes for spinal cord injury.xlsx

IntroductionSpinal cord injury (SCI) is a profoundly disabling and devastating neurological condition, significantly impacting patients’ quality of life. It imposes unbearable psychological and economic pressure on both patients and their families, as well as placing a heavy burden on society.MethodsIn this study, we integrated datasets GSE5296 and GSE47681 as training groups, analyzed gene variances between sham group and SCI group mice, and conducted Gene Ontology (GO) enrichment analysis and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analysis based on the differentially expressed genes. Subsequently, we performed Weighted Gene Correlation Network Analysis (WGCNA) and Lasso regression analyses.ResultsWe identified four characteristic disease genes: Icam1, Ch25h, Plaur and Tm4sf1. We examined the relationship between SCI and immune cells, and validated the expression of the identified disease-related genes in SCI rats using PCR and immunohistochemistry experiments.DiscussionIn conclusion, we have identified and verified four genes related to SCI: Icam1, Ch25h, Plaur and Tm4sf1, which could offer insights for SCI treatment.</p

Luminescent and Magnetic Properties in Semiconductor Nanocrystals with Radial-Position-Controlled Mn²⁺ Doping

Colloidal nanocrystals (NCs) with radial-position-controlled doping were synthesized to study the effect of the binding symmetry around Mn²⁺ dopant. For the four samples ZnSe:Mn/ZnSe, ZnSe/ZnS­(2 ML):Mn/ZnS­(2 ML), ZnSe/ZnS­(1 ML):Mn/ZnS­(2 ML), and ZnSe:Mn/ZnS­(2 ML), which were in sequence of binding asymmetry around Mn²⁺ dopant, their photoluminescent (PL) peak showed gradual red-shift (579 to 599 nm) and the PL lifetime became monotonously shorter (0.57 to 0.31 ms), while, as indicated in the electronic paramagnetic resonance spectra, the hyperfine splitting constant became larger (67.9 to 68.4 G) and the <i>g</i> factor became smaller (2.0076 to 2.005). The relation between the luminescent and magnetic properties of the Mn-doped NCs was discussed

Additional file 1 of Down-regulated TAB1 suppresses the replication of Coxsackievirus B5 via activating the NF-κB pathways through interaction with viral 3D polymerase

Additional file 1. Figure S1: pcDNA3.1-3D-2Flag was transfected into RD cells and harvested at 24hours post-transfection (pcDNA3.1 as the control). The expression of 3D-2Flag was analyzed by Western blotting

Effects of Core Size and Shell Thickness on Luminescence Dynamics of Wurtzite CdSe/CdS Core/Shell Nanocrystals

Colloidal CdSe nanocrystals (NCs), whose size is 2.8, 3.8, and 4.9 nm, respectively, were successively overcoated with CdS monolayers (MLs). The X-ray diffraction patterns indicated that the stress in the wurtzite CdSe core was increased with the epitaxial growth of CdS shell, and the CdSe lattice contraction, which was sensitive to core size, did not release with the CdS shell toward 5 MLs. The effects of the CdSe core size and the CdS shell thickness on the temperature-dependent photoluminescence (PL) lifetime were investigated. The PL lifetime undulation with temperature is indicative of the spatial distribution of trap states, and the strong interplay between intrinsic excitons and surface traps can be activated even in the case of the NCs with 5 ML CdS shell

Comprehensive characterization of the <i>in vitro</i> and <i>in vivo</i> metabolites of geniposide in rats using ultra-high-performance liquid chromatography coupled with linear ion trap–Orbitrap mass spectrometer

<p>1. Geniposide (genipin 1-<i>O-</i>glucose), one of the major bioactive constituents isolated from Fructus Gardeniae, possesses many biological activities. In this study, an efficient strategy was developed using ultra-high-performance liquid chromatography coupled with linear ion trap–Orbitrap mass spectrometer (UPLC–LTQ–Orbitrap) to profile the <i>in vitro</i> and <i>in vivo</i> metabolic patterns of geniposide in rat liver microsomes (RLMs), plasma, urine, and various tissues. And post-acquisition data-mining methods including extracted ion chromatogram (EIC), multiple mass defect filters (MMDF), fragment ion searching (FISh), and isotope pattern filtering (IPF) were adopted to characterize the known and unknown metabolites.</p> <p>2. A total of 33 metabolites were detected and interpreted according to accurate mass measurement, diagnostic fragment ions, relevant drug biotransformation knowledge, and bibliography data. Among them, 17 metabolites were detected in the plasma, 31 metabolites were identified in the urine, six metabolites could be found in rat heart, 12 in liver, three in spleen, six in lung, 12 in kidney, six in brain, and four in RLMs.</p> <p>3. A series of corresponding reactions such as hydrolysis, hydroxylation, taurine conjugation, hydrogenation, decarboxylation, demethylation, sulfate conjugation, cysteine S-conjugation, glucosylation, and their composite reactions were all discovered.</p> <p>4. The results could provide comprehensive insights and guidance for elucidation of side effect mechanism and safety monitoring as well as for rational formulation design in drug delivery system. The newly discovered geniposide metabolites could be targets for future metabolism studies on the important chemical constituents from herbal medicines.</p

Association rate, dissociation rate, and equilibrium dissociation constants of Trn1 and wild-type and mutant FUS-NLS.

<p>The 12 ALS mutations are organized in the order of decreasing affinity.</p>a<p>The relative affinity is defined as <i>K</i>_D of WT (M) divided by <i>K</i>_D of the FUS-NLS mutants <i>(</i>M<i>).</i></p><p>The correlation coefficient χ² value is a statistical measure of how closely the fitted curve fits the experimental data <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0047056#pone.0047056-Imasaki1" target="_blank">[15]</a> (see Methods).</p

The interactions between the Trn1 and the FUS-NLS.

<p>(A) Summary of the polar/electrostatic interactions between FUS-NLS (yellow) and Trn1 (cyan). FUS-NLS is divided into region I (E523–Y526), region II (D512–R522), and region III (P508–M511). (B) Schematic illustration of the hydrophobic contacts between the region I of FUS-NLS (E523–R524–P525–Y526) and Trn1. (C) Schematic illustration of the hydrophobic contacts between the region III of FUS-NLS (P508–G509–K510–M511) and Trn1. (D). The interaction between R524 and Q519, D520 and R522 within FUS-NLS. The figure is prepared with LIGPLOT <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0047056#pone.0047056-Wallace1" target="_blank">[38]</a>.</p

Correlation between the disease duration of familial ALS patients carrying R518K, R521G, R524S and P525L mutations and the relative binding affinity of the mutant proteins to Trn1.

<p>The coefficient of determination R² is 0.88, suggesting strong correlation. The number of patients for the R518K, R521G, R524S and P525L mutations are 12, 4, 2, and 8, respectively.</p

Sequence analysis of FUS-NLS.

<p>(A). Domain structure of FUS with the C-terminal NLS. The ALS mutations are clustered in the NLS and the mutations studied here are shown in red. (B) Amino acid sequence alignments of FUS-NLS with other PY NLS’s from hnRNP A1, hnRNP D, hnRNP M and TAP. (C). Sequence alignment of FUS-NLS from different organisms.</p