SuperNova, a monomeric photosensitizing fluorescent protein for chromophore-assisted light inactivation

Takemoto, K., Matsuda, T., Sakai, N. et al. SuperNova, a monomeric photosensitizing fluorescent protein for chromophore-assisted light inactivation. Sci Rep 3, 2629 (2013). https://doi.org/10.1038/srep02629

Antitumor effects on primary tumor and metastatic lymph nodes by superselective intra-arterial concurrent chemoradiotherapy for oral cancer.

OBJECTIVE: Superselective intra-arterial infusion of anticancer agents with concurrent delivery of external beam radiotherapy was applied to 13 previously untreated cases of oral cancer for the purpose of avoiding surgical resection of the primary tumor. STUDY DESIGN: The catheter tips were placed in the tumor feeder arteries via the superficial temporal artery and/or occipital artery. The catheters were retained for 6 weeks to infuse anticancer agents daily with concurrent radiotherapy for 6 weeks. The total radiation doses to the primary tumor and neck were 60.0 Gy and 40.0 Gy, respectively. RESULTS: Complete response of the primary tumor was achieved in all 13 patients; complete response of neck node metastasis was achieved in 5 out of 6 patients. CONCLUSION: This strategy is quite effective for oral cancer at both the primary site and metastatic lymph nodes, and it has the potential to be curative in advanced cases that are inoperable

A low-cost affinity purification system using β-1,3-glucan recognition protein and curdlan beads

Silkworm β-1,3-glucan recognition protein (βGRP) tightly and specifically associates with β-1,3-glucan. We report here an affinity purification system named the 'GRP system', which uses the association between the β-1,3-glucan recognition domain of βGRP (GRP-tag), as an affinity tag, and curdlan beads. Curdlan is a water-insoluble β-1,3-glucan reagent, the low cost of which (about 100 JPY/g) allows the economical preparation of beads. Curdlan beads can be readily prepared by solubilization in an alkaline solution, followed by neutralization, sonication and centrifugation. We applied the GRP system to preparation of several proteins and revealed that the expression levels of the GRP-tagged proteins in soluble fractions were two or three times higher than those of the glutathione S-transferase (GST)-tagged proteins. The purity of the GRP-tagged proteins on the curdlan beads was comparable to that of the GST-tagged proteins on glutathione beads. The chemical stability of the GRP system was more robust than conventional affinity systems under various conditions, including low pH (4-6). Biochemical and structural analyses revealed that proteins produced using the GRP system were structurally and functionally active. Thus, the GRP system is suitable for both the large- and small-scale preparation of recombinant proteins for functional and structural analyses

Self-limiting oxidation of SiGe alloy on silicon-on-insulator wafers

Takayoshi Shimura, Michihiro Shimizu, Shinichiro Horiuchi, Heiji Watanabe, Kiyoshi Yasutake, Masataka Umeno, "Self-limiting oxidation of SiGe alloy on silicon-on-insulator wafers", Appl. Phys. Lett. 89, 111923 (2006) https://doi.org/10.1063/1.2353812

Solution Structures of Cytosolic RNA Sensor MDA5 and LGP2 C-terminal Domains : Identification of the RNA Recognition Loop in RIG-I-LIKE Receptors

The RIG-I like receptor (RLR) comprises three homologues: RIG-I (retinoic acid-inducible gene I), MDA5(melanoma differentiation-associated gene 5), and LGP2 (laboratory of genetics and physiology 2). Each RLR senses different viral infections by recognizing replicating viral RNA in the cytoplasm. The RLR contains a conserved C-terminal domain (CTD), which is responsible for the binding specificity to the viral RNAs, including double-stranded RNA (dsRNA) and 5'-triphosphated single-stranded RNA (5'ppp-ssRNA). Here, the solution structures of the MDA5 and LGP2 CTD domains were solved by NMR and compared with those of RIG-I CTD. The CTD domains each have a similar fold and a similar basic surface but there is the distinct structural feature of a RNA binding loop; The LGP2 and RIG-I CTD domains have a large basic surface, one bank of which is formed by the RNA binding loop. MDA5 also has a large basic surface that is extensively flat due to open conformation of the RNA binding loop. The NMR chemical shift perturbation study showed that dsRNA and 5'ppp-ssRNA are bound to the basic surface of LGP2 CTD, whereas dsRNA is bound to the basic surface of MDA5 CTD but much more weakly, indicating that the conformation of the RNA binding loop is responsible for the sensitivity to dsRNA and 5'ppp-ssRNA. Mutation study of the basic surface and the RNA binding loop supports the conclusion from the structure studies. Thus, the CTD is responsible for the binding affinity to the viral RNAs

Novel recognition mode between Vav and Grb2 SH3 domains

Vav is a guanine nucleotide exchange factor for the Rho/Rac family that is expressed exclusively in hematopoietic cells. Growth factor receptor-bound protein 2 (Grb2) has been proposed to play important roles in the membrane localization and activation of Vav through dimerization of its C-terminal Src-homology 3 (SH3) domain (GrbS) and the N-terminal SH3 domain of Vav (VavS). The crystal structure of VavS complexed with GrbS has been solved. VavS is distinct from other SH3 domain proteins in that its binding site for proline-rich peptides is blocked by its own RT loop. One of the ends of the VavS β-barrel forms a concave hydrophobic surface. The GrbS components make a contiguous complementary interface with the VavS surface. The binding site of GrbS for VavS partially overlaps with the canonical binding site for proline-rich peptides, but is definitely different. Mutations at the interface caused a decrease in the binding affinity of VavS for GrbS by 4- to 40-fold. The structure reveals how GrbS discriminates VavS specifically from other signaling molecules without binding to the proline-rich motif