Additional file 1: of The gut microbiota in young and middle-aged rats showed different responses to chicken protein in their diet

Table S1. Richness and diversity indexes relative to each sample. Table S2. The differentially fecal bacterial communities between Young-0d and Middle aged-0d using LEfSe at the OTU level. Table S3. The differentially fecal bacterial communities between Young-14d and Middle aged-14d using LEfSe at the OTU level. Table S4. The differentially fecal bacterial communities between Young-0d and Young-14d using LEfSe at the OTU level. Table S5. The differentially fecal bacterial communities between Middle aged-0d and Middle aged-14d using LEfSe at the OTU level. (DOC 254 kb

High-Level Production of l‑Fucose by Plasmid-Free or Antibiotic-Independent Metabolically Engineered Escherichia coli Strains

l-Fucose is an important monosaccharide unit that exists in various biomasses, especially in microalgae. Microbial l-fucose using metabolically engineered strains has attracted attention due to its high yield and industrial feasibility. Previously, we engineered Escherichia coli MG1655 to efficiently produce 2′-fucosyllactose by genomic integration. Herein, this plasmid-free strain was further engineered to produce l-fucose by integrating a specific α-l-fucosidase gene and deleting the l-fucose degradation pathway. Its effectiveness of l-fucose biosynthesis by plasmid-free and inducer-free fermentation was demonstrated by both shake-flask and fed-batch cultivation with titers of 2.74 and 21.15 g/L, respectively. The precursor GDP-l-fucose supply was strengthened to obviously enhance l-fucose biosynthesis by introducing a single plasmid expressing four pathway genes. The hok/sok system was introduced to promote the plasmid stabilization without antibiotic. The final engineered strain efficiently could produce l-fucose without antibiotics, with titers of 6.83 and 35.68 g/L by shake-flask and fed-cultivation cultivation, respectively

Improving the Catalytic Behavior of DFA I‑Forming Inulin Fructotransferase from Streptomyces davawensis with Site-Directed Mutagenesis

Previously, a α-d-fructofuranose-β-d-fructofuranose 1,2′:2,1′-dianhydride (DFA I)-forming inulin fructotransferase (IFTase), namely, <i>Sd</i>IFTase, was identified. The enzyme does not show high performances. In this work, to improve catalytic behavior including activity and thermostability, the enzyme was modified using site-directed mutagenesis on the basis of structure. The mutated residues were divided into three groups. Those in group I are located at central tunnel including G236, A257, G281, T313, and A314S. The group II contains residues at the inner edge of substrate binding pocket including I80, while group III at the outer edge includes G121 and T122. The thermostability was reflected by the melting temperature (<i>T</i>_m) determined by Nano DSC. Finally, the <i>T</i>_m values of G236S/G281S/A257S/T313S/A314S in group I and G121A/T122L in group III were enhanced by 3.2 and 4.5 °C, and the relative activities were enhanced to 140.5% and 148.7%, respectively. The method in this work may be applicable to other DFA I-forming IFTases

Comparison of ventricular premature beats and KCNQ1 expression between groups.

<p>(<b>A</b>) Comparison of the total premature ventricular beats (PVBs) between the groups within 10 min after bolus injection of epinephrine. <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0031545#s2" target="_blank">Results</a> are presented in a box plot format (n = 6–8) where boxes indicate the 25–75% interval along with the median of the data. * P<0.05 vs. the other groups. (<b>B</b>) Reverse transcription-polymerase chain reaction (RT-PCR) of KCNQ1 mRNA levels. Top: Examples of KCNQ1 mRNA with samples harvested from the peri-infarct zone and remote zone of the Healing (2-d; n = 6), Infarct (2-d; n = 8), Sham (2-d; n = 7), Healing (5-d; n = 7), Infarct (5-d; n = 7), and Sham (5-d; n = 8) groups of rabbit hearts. Bottom: mean KCNQ1 mRNA band intensities. (<b>C</b>) Western blot analysis of membrane-associated KCNQ1 protein levels. Top: Representative immunoblot results showing membrane KCNQ1 protein (∼75 kDa) with samples harvested from the peri-infarct zone and remote zone of the six groups of rabbit hearts. Bottom: mean membrane KCNQ1 protein band intensities. * P<0.05 vs. Sham (2-d) and Sham (5-d) respectively; # P<0.05 vs. Healing (2-d) and Healing (5-d) respectively; $ P<0.05 vs. Infarct (5-d).</p

Comparison of waveforms between the Sham (2-d) and Infarct (2-d) groups after bolus injection of epinephrine.

<p>The only morphological differences in peri-infarct MAP were identified in the Infarct (2-d) group. (<b>A</b>) ECG Lead II waveforms showing that both groups had a comparable degree of heart rate increase. (<b>B</b>) MAP recorded at the peri-infarct epicardial zone showing that after the adrenergic challenge, the MAP of the Infarct (2-d) group had a dramatic shortening of MAPD30, whereas the MAPD90 was only minimally changed. (<b>C</b>) Direct overlapping of MAP showing that the MAP of the Infarct (2-d) group demonstrates more prominent triangulation.</p

Divergent molecular mechanisms for potassium channel remodeling in animal models of heart disease.

<p>AV, atrioventricular; ICM, ischemic cardiomyopathy; ND, not determined; -, no change.</p><p>*Weak bands limited the reliability of the measurement.</p>‡<p>KCNQ1.2, a truncated isoform of canine KCNQ1, was increased and may suppress I_Ks in a dominant-negative fashion.</p

Table S1.docx

Table S1: The primers used in this study

Details of PCR.

<p>Details of PCR.</p

Table S6

<p>Functional annotation analysis of has-miR-4640-5p</p

Table S2

The differentially expressed circRNAs in laryngeal squamous cell carcinoma tissues and normal laryngeal tissues. FC: Fold changes. abs: absolute value