Heterogeneous integration approach based on flip-chip bonding and misalignment self-correction elements for electronics-optics integration applications

This paper presents a high precision bonding approach, capable of submicron alignment accuracy, based on the thermosonic flip-chip bonding technique and misalignment self-correction elements. The precision of the bonding technique is guaranteed by using of misalignment self-correction bump (convex) and hollow (concave) elements. Metal cone bump and conductive sloped hollow bonding pad elements are created using micro-machining techniques, on a chip specimen and substrate, respectively. The chip and substrate are bonded face-to-face using of an ultrasonic-enhanced flip-chip bonder. By introducing of misalignment self-correction elements, repeatable bonding accuracies of less than 500 nm were confirmed through experimental investigation. Bond properties, including electrical and mechanical properties, are also characterized to confirm the success of the bonding approach. With the obtained results, the proposed bonding approach is capable of being use in electronics-optics heterogeneous integration applications

Graphene-oxide-semiconductor planar-type electron emission device

Graphene was used as the topmost electrode for a metal-oxide-semiconductor planar-type electron emission device. With several various layers, graphene as a gate electrode on the thin oxide layer was directly deposited by gallium vapor-assisted chemical vapor deposition. The maximum efficiency of the electron emission, defined as the ratio of anode current to cathode current, showed no dependency on electrode thickness in the range from 1.8 nm to 7.0 nm, indicating that electron scattering on the inside of the grapheneelectrode is practically suppressed. In addition, a high emission current density of 1–100 mA/cm2 was obtained while maintaining a relatively high electron emission efficiency of 0.1%–1.0%. The graphene-oxide-semiconductor planar-type electron emission device has great potential to achieve both high electron emission efficiency and high electron emissioncurrent density in practical applications

Protection of front-line nurses from life-threatening infection by suctioning robots : a systematic review

29th International Council of Nurses Congress from 1-5 July 2023 in Montreal, Canad

Minoxidil-induced lung disease, masquerading as hypersensitivity pneumonitis

We report the case of a 71-year-old male with essential thrombosis who presented with ground-glass lung opacity with a mosaic pattern on computed tomography, which resolved spontaneously with hospitalization. This was confused with a case of hypersensitivity pneumonitis (HP), which later turned out to be a drug-induced lung disease caused by surreptitiously administered minoxidil. This case emphasizes the importance of obtaining a correct medication history to make an accurate diagnosis, and this is the first report of minoxidil causing HP-like pulmonary illness

AGIA Tag System Based on a High Affinity Rabbit Monoclonal Antibody against Human Dopamine Receptor D1 for Protein Analysis.

Polypeptide tag technology is widely used for protein detection and affinity purification. It consists of two fundamental elements: a peptide sequence and a binder which specifically binds to the peptide tag. In many tag systems, antibodies have been used as binder due to their high affinity and specificity. Recently, we obtained clone Ra48, a high-affinity rabbit monoclonal antibody (mAb) against dopamine receptor D1 (DRD1). Here, we report a novel tag system composed of Ra48 antibody and its epitope sequence. Using a deletion assay, we identified EEAAGIARP in the C-terminal region of DRD1 as the minimal epitope of Ra48 mAb, and we named this sequence the "AGIA" tag, based on its central sequence. The tag sequence does not include the four amino acids, Ser, Thr, Tyr, or Lys, which are susceptible to post-translational modification. We demonstrated performance of this new tag system in biochemical and cell biology applications. SPR analysis demonstrated that the affinity of the Ra48 mAb to the AGIA tag was 4.90 × 10-9 M. AGIA tag showed remarkably high sensitivity and specificity in immunoblotting. A number of AGIA-fused proteins overexpressed in animal and plant cells were detected by anti-AGIA antibody in immunoblotting and immunostaining with low background, and were immunoprecipitated efficiently. Furthermore, a single amino acid substitution of the second Glu to Asp (AGIA/E2D) enabled competitive dissociation of AGIA/E2D-tagged protein by adding wild-type AGIA peptide. It enabled one-step purification of AGIA/E2D-tagged recombinant proteins by peptide competition under physiological conditions. The sensitivity and specificity of the AGIA system makes it suitable for use in multiple methods for protein analysis

Development of AGIA/E2D tag.

<p>(A) Amino acid substitution of AGIA tag sequence. Red characters indicate substituted residues. (B) Immunoblot of proteins fused with AGIA mutants. FLAG-GST-AGIA / AGIA mutants were subjected to western blotting. (C) Amino acid substitution in the AGIA tag enabled competitive dissociation. Anti-AGIA antibody was captured on a protein G-immobilized Biacore sensorchip at 100 RU. FLAG-GST-AGIA/AGIA mutant was injected for 300 sec, and dissociation was observed for 1,800 sec. Then, 150 μM AGIA peptide was injected for 300 sec. Blue, wild-type AGIA: red, AGIA/E1D; green, AGIA/E2D; purple, AGIA/P9V. (D) Competitive elution of AGIA mutants by AGIA peptide. Six hundred μL of cell-free synthesized FLAG-GST-AGIA/mutant was mixed with 20 μL anti-AGIA sepharose. After washing with 200 μL HBS three times, proteins were eluted 3 times by 200 μL of 150 μM AGIA peptide (Elution). After elution, the resin was boiled in SDS-PAGE sample buffer for 10 min (Resin). Fractions were applied to SDS-PAGE and CBB staining. (E) Kinetics assay of AGIA/E2D tag. Anti-AGIA antibody was captured on a protein G-immobilized Biacore sensorchip at 100 RU. Purified FLAG-GST-AGIA/E2D protein was injected for 180 sec as analyte. Black lines represent a global fit of a 1:1 interaction model to each kinetic data set. (F) Elution condition of AGIA/E2D tag. Anti-AGIA antibody was captured on a protein G immobilized Biacore sensorchip at 800 RU, and FLAG-GST-AGIA/E2D was injected for 60 sec. The sensorchip was then treated by following elution solutions; gray, HBS-EP+ buffer; yellow, 2M MgCl₂; blue, 100 mM sodium acetate buffer pH4.0, red, 150 μM AGIA peptide; green, 100 mM sodium acetate buffer pH4.0 and 2M MgCl₂; orange, 2M MgCl₂ and 150 μM AGIA peptide; purple, 100 mM sodium acetate buffer pH4.0 and 150 μM AGIA peptide.</p