Ubiquitin binding of OspG is required for inhibiting host NF-κB signaling during <i>Shigella</i> infection.

<p>(<b>A</b>) The role of OspG in recruitment of ubiquitin to intracellular <i>Shigella</i>. HeLa cells were infected with wild type (WT) or Δ<i>ospG</i> mutant <i>S. flexneri</i> strain. Polyubiquitinated proteins stained by the FK1 antibody (green), intracellular bacteria stained by anti-<i>Shigella</i> antibody (red) and DAPI-stained nuclei (blue) were visualized by fluorescence microscopy. (<b>B</b>) The role of OspG ubiquitin binding activity in inhibiting NF-κB activation in <i>Shigella</i>-infected cells. HeLa cells were infected with indicated <i>S. flexneri</i> strains. Infected cells were treated with TNFα to stimulate NF-κB pathway activation. Lysates of infected cell collected at indicated time points after the stimulation were subjected to anti-IκBα and anti-tubulin immunoblotting analyses.</p

Multipole Dirichlet-to-Neumann map method for photonic crystals with complex unit cells

The periodicity of photonic crystals can be utilized to develop efficient numerical methods for analyzing light waves propagating in these structures. The Dirichlet-to-Neumann (DtN) operator of a unit cell maps the wave field on the boundary of the unit cell to its normal derivative, and it can be used to reduce the computation to the edges of the unit cells. For two-dimensional photonic crystals with complex unit cells each containing a number of possibly different circular cylinders, we develop an efficient multipole method for constructing the DtN maps. The DtN maps are used to calculate the transmission and reflection spectra for finite photonic crystals with complex unit cells.

IEEE Access special section editorial: Biologically inspired image processing challenges and future directions

No description supplie

Secondary structure-based sequence alignment of OspG with human JNK3.

<p>The protein names are indicated at the left of the alignment. The key residues in the kinase domain are colored in red. Predicted secondary structures of OspG are shown on top of the OspG sequence. Secondary structures determined from crystal structure of JNK3 are shown underneath the sequence of JNK3 in the alignment. Green ovals are α helices and blue arrows are β strands. The sub-domains are labeled with Roman numerals.</p

High-affinity binding between OspG and ubiquitin conjugates, poly-ubiquitin chains and free ubiquitin.

<p>(<b>A</b>) Pulldown of ubiquitin-conjugated proteins by purified GST-OspG. Glutathione-Sepharose beads coated with GST-OspG or GST alone were incubated with lysates of intact 293T cells or MG132- treated 293T cells. Proteins retained on the beads were eluted with SDS loading buffer and separated onto12% SDS-PAGE gels. Shown on the left are anti-ubiquitin immunoblots and on the right are Coomassie blue staining of GST or GST-OspG proteins present on the beads. (<b>B</b> and <b>C</b>) Pulldown of OpsG by K48- or K63-linked poly-ubiquitin chains. Ni-NTA Sepharose beads coated with His6-ubiquitin chains with indicated linkages were incubated with GST or GST-OspG. Proteins retained on the beads were subjected to SDS-PAGE and anti-GST immunoblotting analysis. (<b>D</b>) Pulldown of free ubiquitin by GST-OspG. GST or GST-OspG proteins were immobilized onto Glutathione Sepharose beads and the beads were then incubated with lysates of 293T cells. The interacting proteins eluted from the beads were resolved by 4–20% gradient SDS-PAGE gel and analyzed by anti-ubiquitin immunoblotting.</p

Biocompatible and Highly Luminescent Near-Infrared CuInS₂/ZnS Quantum Dots Embedded Silica Beads for Cancer Cell Imaging

Bright and stable CuInS₂/ZnS@SiO₂ nanoparticles with near-infrared (NIR) emission were competently prepared by incorporating the as-prepared hydrophobic CuInS₂/ZnS quantum dots (QDs) directly into lipophilic silane micelles and subsequently an exterior silica shell was formed. The obtained CuInS₂/ZnS@SiO₂ nanoparticles homogeneously comprised both single-core and multicore remarkable CuInS₂/ZnS QDs, while the silica shell thickness could be controlled to within 5–10 nm and their overall size was 17–25 nm. Also, the functionalized CuInS₂/ZnS QDs encapsulated in the silica spheres, expedited their bioconjugation with holo-Transferrin (Tf) for further cancer cell imaging. The CuInS₂/ZnS@SiO₂ nanoparticles not only showed a dominant NIR band-edge luminescence at 650–720 nm with a quantum yield (QY) between 30 and 50%, without a recognized photoluminescence (PL) red shift, but also exhibited excellent PL and colloidal stability in aqueous media. Impressively, the cytotoxicity studies revealed minor suppression on cell viability under both CuInS₂/ZnS@SiO₂ and CuInS₂/ZnS@SiO₂@Tf concentrations up to 1 mg/mL. The application in live-cell imaging revealed that the potential of CuInS₂/ZnS QDs as biocompatible, robust, cadmium-free, and brilliant NIR emitters is considered promising for fluorescent labels

Parameter determinations in the proposed VQA method.

<p>(a) Tuning Performance of <i>ω</i>₁. (b) Tuning Performance of <i>a</i>⁺ and <i>a</i>^-.</p

PLCC comparison for each module of the proposed VQA method.

<p>PLCC comparison for each module of the proposed VQA method.</p

Training set from randomly selected temporal LPCs

<p>Training set from randomly selected temporal LPCs</p

Performance comparison on the LIVE VQA database.

<p>Performance comparison on the LIVE VQA database.</p