Failure patterns after radiotherapy.

<p>LV-IMRT, large-target-volume intensity-modulated radiotherapy; RV-IMRT, reduced-target-volume intensity-modulated radiotherapy; Sig., significance</p><p>*, Statistical significance.</p><p>Failure patterns after radiotherapy.</p

Impact of the prognostic factors on the treatment results based on multivariate Cox regression analysis.

<p>LV-IMRT, large-target-volume intensity-modulated radiotherapy; RV-IMRT, reduced-target-volume intensity-modulated radiotherapy; OS, overall survival; PFS, progression-free survival; DMFS, distant metastasis-free survival; LRFFS, locoregional recurrence-free survival; RR, relative risk; CI, confidence interval;</p><p>*, Statistical significance.</p><p>Impact of the prognostic factors on the treatment results based on multivariate Cox regression analysis.</p

Patient clinical characteristics.

<p>LV-IMRT, large-target-volume intensity-modulated radiotherapy; RV-IMRT, reduced-target-volume intensity-modulated radiotherapy; SEM., standard error mean; *, Statistical significance.</p><p>Patient clinical characteristics.</p

Patient dosimetric characteristics.

<p>LV-IMRT, large-target-volume intensity-modulated radiotherapy; RV-IMRT, reduced-target-volume intensity-modulated radiotherapy; SEM., standard error mean</p><p>*, Statistical significance.</p><p>Patient dosimetric characteristics.</p

Kaplan-Meier curves illustrate the survival of two-group patients who underwent radiotherapy.

<p>Large-target-volume intensity-modulated radiotherapy [red line] and reduced-target-volume intensity-modulated radiotherapy [blue line]), including (A) overall survival, (B) progression-free survival, (C) distant metastasis-free survival, (D) locoregional recurrence-free survival, (E) local recurrence-free survival, (F) regional recurrence-free survival.</p

Radiation toxicity profiles.

<p>LV-IMRT, large-target-volume intensity-modulated radiotherapy; RV-IMRT, reduced-target-volume intensity-modulated radiotherapy; Sig., significance</p><p>*, Statistical significance.</p><p>Radiation toxicity profiles.</p

Quantum Dot Light-Emitting Diode Using Solution-Processable Graphene Oxide as the Anode Interfacial Layer

In this article, the solution processable graphene oxide (GO) thin film was utilized as the anode interfacial layer in quantum dot light emitting diodes (QD-LEDs). The QD-LED devices (ITO/GO/QDs/TPBi/LiF/Al) were fabricated by employing a layer-by-layer assembled deposition technique with the electrostatic interaction between GO and QDs. The thicknesses of GO thin films and the layer number of CdSe/ZnS QD emissive layers were carefully controlled by spin-casting processes. The GO thin films, which act as the electron blocking and hole transporting layer in the QD-LED devices, have demonstrated the advantage of being compatible with fully solution-processed fabrications of large-area printable optoelectronic devices

Additional file 1: of Green Synthesis of InP/ZnS Core/Shell Quantum Dots for Application in Heavy-Metal-Free Light-Emitting Diodes

Calculation of fluorescence quantum yield. Figure S1. Histogram of size distribution of InP/ZnS core/shell QDs and Gaussian fitting. Figure S2. EDX analysis of InP/ZnS core/shell QDs. Figure S3. a UV-Vis spectra and fluorescence of InP/ZnS core/shell QDs with red fluorescence. b UV-Vis spectra and fluorescence of InP/ZnS core/shell QDs with yellow fluorescence. c The red (right) and yellow (left) fluorescence of InP/ZnS core/shell QDs with the irradiation by hand-held long-wave UV lamp. (DOC 559 kb

FGD4, a Cdc42 GEF, is involved in LMP1-mediated Cdc42 activation.

<p>(A) Identification of FGD4 as a GEF candidate involved in LMP1-mediated Cdc42 activation in NPC cells. The potential GEF involved in the activation of Cdc42 by LMP1 was identified by co-transfecting NPC-TW04 cells with 1 µg of Flag-LMP1 expression plasmid or empty vector (control), and siRNAs (25 µM) directed against DOCK9 (siDock9), intersectin-1 (siITSN1), FGD4 (siFGD4), FGD1 (siFGD1), FGD3 (siFGD3) or non-targeting control (siCtrl). Following a 6-h serum starvation at 48 h post-transfection, cells lysates were harvested for GST-CBD pull-down assays. The knockdown efficiency for individual GEFs was analyzed by Western blotting with the respective antibody. The level of active Cdc42 was determined as described above. The constant amounts of GST-CBD for pull-down assays were shown by Ponceau S staining. The results shown are representative of five independent experiments. Quantitative data are shown in B. The relative fold-changes in active Cdc42 are presented as means ± SDs (*<i>P</i> = 0.0052; paired <i>t</i>-test). (C) Confirmation of FGD4 involvement in 293 Tet-On cells. 293 Tet-On cells that had been transfected with 25 µM control or FGD4 siRNA and incubated for 24 h were further treated with Dox (5 µg/ml) for 24 h to induce LMP1 expression. Cell extracts were then harvested for GST-CBD pull-down assays and the level of active Cdc42 was determined as described above. (D) Normalizing the reduced levels of active Cdc42 in FGD4-depleted cells by re-introduction of FGD4. NPC-TW04 cells were co-transfected with 25 µM control or FGD4 siRNA, together with 1 µg of Flag-LMP1 expression plasmid or empty vector (control), plus 2 µg of pMyc-FGD4 expression plasmids or Myc vector. Following a 6-h serum starvation at 48 h post-transfection, cells lysates were harvested for GST-CBD pull-down assays, and the level of active Cdc42 was analyzed as described above.</p

FGD4 modulates LMP1-mediated Cdc42 activation through protein-protein interaction.

<p>(A) Schematic illustrations of Myc-tagged FGD4 and its truncated derivatives. FL, full-length FGD4; ΔFAB, deletion of the F-actin-binding domain; ΔDH, deletion of the Dbl homology domain (catalytic domain); PH1 and PH2, pleckstrin homology domains 1 and 2; FYVE, a zinc finger domain named after Fab1, YOTB, Vac1, and EEA1. (B) Characterization of FGD4 function and its effect on LMP1-mediated Cdc42 activation. NPC-TW01 cells were co-transfected with 1.5 µg of Myc-FGD4 expression plasmids and 1 µg of Flag-LMP1 expression plasmid or empty vector (control). After 24-h incubation and a following 6-h serum starvation, cells were lysed for GST-CBD pull-down assays and the level of active Cdc42 was determined as described above. The constant amounts of GST-CBD for pull-down assays were shown by Ponceau S staining. The domain of FGD4 required for Cdc42 activation was determined by calculating the relative fold-change in active Cdc42 with expression of truncated FGD4 versus expression of full-length FGD4. The mean ± SD of five independent experiments is shown in C (*, <i>P</i><0.001; paired <i>t</i>-test). The effect of FGD4 on LMP1-mediated Cdc42 activation was demonstrated by calculating the relative fold-change in active Cdc42 with expression of both LMP1 and FGD4 versus expression of LMP1 alone (B; numbers in italics). The mean ± SD of five independent experiments is shown in D (*<i>P</i><0.05, **<i>P</i><0.01; paired <i>t</i>-test). (E) Co-immunoprecipitation of Flag-LMP1 with Myc-FGD4. NPC-TW01 cells that had been transfected with the indicated plasmids were lysed after incubation as described in B. The resulting cell lysates were applied to co-immunoprecipitation assays with an anti-Myc affinity matrix. The precipitated protein complexes were analyzed by Western blotting with anti-LMP1 (S12) and anti-Myc (9E10) antibodies. (F) NPC-TW01 cells that had been transfected with plasmids encoding Flag-LMP1 or Flag-CD40CT together with Myc-FGD4 were lysed after incubation as described in B. A portion of the resulting cell lysate was analyzed by co-immunoprecipitation assays using an ani-Myc affinity matrix and the remainder was analyzed by GST-CBD pull-down assays, as described above.</p