19 research outputs found
Effects of the consumption of RE on body weight (g) and food utility index (FUI) in Zucker female rats.
No full text<p>Lean (Le) and obese (Ob) rats were fed the control diet (CT) or the diet supplemented with 0.05% of RE (RE) for 64 days. Data are presented as the mean value ± SD (n = 7 for lean animals and n = 5 for obese animals). * <i>P</i><0.05, ** <i>P</i><0.01 compared to their respective CT values.</p
Alveol kemiğinin yapısı, rezorbsiyon mekanizmaları ve alloplastik kemik greftlerine yaklaşım.
No full textMemòria, història i identitat: el debat teòric
No full textUna societat desmemoriada, o amb la seva memòria manipulada, és una societat sense identitat. La pèrdua de la memòria afecta directament a la pèrdua de la identitat. A partir d’aquestes premisses, l’autor ressegueix els diferents enfocaments teòrics que han nodrit el debat sobre les relaciones entre memòria, història i identitat al llarg del segle xx i principis del xxi
Conference Report – 1st Japanese Studies Conference “Text and Film in Interaction” on 25–26 February, 2016, in Berlin
No full textConference Repor
MOESM3 of Characterization of resistance to a potent d-peptide HIV entry inhibitor
No full textAdditional file 3. Effect of Q577R on C-peptide Inhibitors. Single-cycle viral infectivity assays in which HIV-1 HXB2 Env (WT and Q577R) pseudotyped HIV-1 with a luciferase reporter was used to infect HOS-LES cells in the absence or presence of six fivefold dilutions of the indicated C-peptide (in quadruplicate). The data are the average of two experiments with the standard deviation in parentheses
MOESM1 of Characterization of resistance to a potent d-peptide HIV entry inhibitor
No full textAdditional file 1. Mutations observed in PIE12-trimer resistant viral pools. Env gene position (pNL4-3 numbering), reference base, and all base calls for control and PIE12-trimer resistance viral populations with a mutation > 10% of the population (with percentage of the base calls for each position colored on a spectrum from low (light pink) to high (red)) are indicated. Additionally, the positions are annotated by their location in Env according to the following categories: known or putative glycosylation site (green), gp120 variable loops (gray), chemokine receptor (co-receptor) binding site (blue), rev-response element (dark gray), gp41 N-trimer (orange), gp41 C-peptide region (light blue), or the Rev coding region included within the env gene (yellow). Eighty-one positions were identified. Of these, 74 conform to our analysis criteria (found in the resistant pool(s) and > 10% different frequency than in the control pool)
MOESM4 of Characterization of resistance to a potent d-peptide HIV entry inhibitor
No full textAdditional file 4. Prevalence of PIE12-trimer resistant candidate compensatory amino acid mutations in Group M primary isolates containing Q577R
MOESM2 of Characterization of resistance to a potent d-peptide HIV entry inhibitor
No full textAdditional file 2. SPR sensorgrams for PIE12 monomer binding to IZN36 WT (left panel) or Q577R (right panel), processed in Scrubber2 (BioLogic Software) and used for the equilibrium fit shown in Fig. 2. Six threefold dilutions of PIE12 monomer (617 nM to 2.54 nM) were flowed over the WT surface, and ten threefold dilutions (50 µM to 2.54 nM) were flowed over the Q577R surface. The calculated KD’s are 0.031 µM for WT and 2.0 µM for Q577R
2D-SDS-PAGE of BGP coat proteins (cyclohexane-soluble) stained with Sypro Ruby and IgE-immunoblotting.
No full text<p>Pollen coat proteins were separated first by isoelectric point and then by molecular weight. Labeled spots were excised, destained, and digested with trypsin for peptide mass fingerprinting. (<b>A</b>) The identities of spots E1, E2, and C1 were verified by mass-spectrum peptide identification as two endoxylanases and a cysteine protease. Two-dimensional IgE-immunoblotting of BGP coat proteins (<b>B</b>). Approximately 50 µg of pollen coat proteins were loaded into an IPG strip (pH 3–10). Following 2D-SDS-PAGE, Western blotting was performed, and the membranes were probed with human pooled allergic sera and detected with anti-human IgE antibodies as shown in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0053337#pone-0053337-g002" target="_blank">Figure 2</a>. The IgE-reactive spots corresponded to E1, E2, and C1 spots on 2D-SDS-PAGE in Figure A. IgE in the pooled sera also reacted with the 14.4 kDa mass marker, lysozyme from chicken egg white. 2D-SDS-PAGE and 2D-Western blot were repeated three times and generally found to be reproducible.</p
