Kyoto University

About: Kyoto University is a education organization based out in Kyoto, Japan. It is known for research contribution in the topics: Catalysis & Population. The organization has 85837 authors who have published 217215 publications receiving 6526826 citations. The organization is also known as: Kyōto University & Kyōto daigaku.

Diffusion in polymer-diluent systems

Abstract: Introduction The diffusion of small molecules in polymeric solids has been a subject in which relatively little interest has been shown by the polymer chemist, in contrast to its counterpart, i.e., the diffusion of macromolecules in dilute solutions. However, during the past ten years there has been a great accumulation of important data on this subject, both experimental and theoretical, and it has become apparent that in many cases diffusion in polymers exhibits features which cannot be expected from classical theories and that such departures are related to the molecular structure characteristic of polymeric solids and gels. Also there have been a number of important contributions to the procedures by which diffusion coefficients of given systems can be determined accurately from experiment. I t is impossible, and apparently beyond the author's ability, to t reat all these recent investigations in the limited space allowed. So, in this article, the author wishes to discuss some selected topics with which he has a relatively greater acquaintance but which he feels are of fundamental importance for understanding the current situation in this field of polymer research. Thus the present paper is a kind of personal note, rather than a balanced review of diverse aspects of recent diffusion studies.

Calcium channel characteristics conferred on the sodium channel by single mutations.

Abstract: THE sodium channel, one of the family of structurally homologous voltage-gated ion channels1, differs from other members, such as the calcium and the potassium channels, in its high selectivity for Na+. This selectivity presumably reflects a distinct structure of its ion-conducting pore. We have recently identified two clusters of predominantly negatively charged amino-acid residues, located at equivalent positions in the four internal repeats of the sodium channel as the main determinants of sensitivity to the blockers tetrodotoxin and saxitoxin2. All site-directed mutations reducing net negative charge at these positions also caused a marked decrease in single-channel conductance2. Thus these two amino-acid clusters probably form part of the extracellular mouth and/or the pore wall of the sodium channel. We report here the effects on ion selectivity of replacing lysine at position 1,422 in repeat III and/or alanine at position 1,714 in repeat IV of rat sodium channel II (ref. 3), each located in one of the two clusters, by glutamic acid, which ccurs at the equivalent positions in calcium channels. These amino-acid substitutions, unlike other substitutions in the adjacent regions, alter ion-selection properties of the sodium channel to resemble those of calcium channels. This result indicates that lysine 1,422 and alanine 1,714 are critical in deter mining the ion selectivity of the sodium channel, suggesting that these residues constitute part of the selectivity filter of the channel.

Material science and device physics in SiC technology for high-voltage power devices

Abstract: Power semiconductor devices are key components in power conversion systems. Silicon carbide (SiC) has received increasing attention as a wide-bandgap semiconductor suitable for high-voltage and low-loss power devices. Through recent progress in the crystal growth and process technology of SiC, the production of medium-voltage (600?1700 V) SiC Schottky barrier diodes (SBDs) and power metal?oxide?semiconductor field-effect transistors (MOSFETs) has started. However, basic understanding of the material properties, defect electronics, and the reliability of SiC devices is still poor. In this review paper, the features and present status of SiC power devices are briefly described. Then, several important aspects of the material science and device physics of SiC, such as impurity doping, extended and point defects, and the impact of such defects on device performance and reliability, are reviewed. Fundamental issues regarding SiC SBDs and power MOSFETs are also discussed.

Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA

Abstract: E-cadherin is a cell surface glycoprotein responsible for Ca2+-dependent intercellular adhesion between epithelial cells1; it is also called uvomorulin2, L-CAM (ref. 3), cell-CAM 120/80 (ref. 4) or Arc-1 (ref. 5). Because blocking the action of E-cadherin by monoclonal antibodies causes dispersion of compact cell colonies1, this molecule is thought to be an important factor for maintenance of multicellular systems. To demonstrate directly that E-cadherin is involved in cell–cell adhesion, we cloned full-length cDNA encoding E-cadherin from F9 cells and introduced it into L fibroblasts deficient in E-cadherin. These L cells acquire strong Ca2+-dependent aggregating activity by expressing the E-cadherin derived from the introduced cDNA, and were morphologically transformed so as to form colonies in which cells were tightly connected to each other.

The receptor tyrosine kinase Ror2 is involved in non‐canonical Wnt5a/JNK signalling pathway

Abstract: Background: Ror2 is an orphan receptor, belonging to the Ror family of receptor tyrosine kinases. Although Ror2 has been shown to play crucial roles in developmental morphogenesis, the precise signalling events that Ror2 mediates remain elusive. Since Ror2 possesses an extracellular cysteine-rich domain (CRD) that resembles the Wnt-binding sites of the Frizzled (Fz) proteins, it is conceivable that Ror2 interacts with members of the Wnt family. Results: Both Ror2−/− and Wnt5a−/− mice exhibit dwarfism, facial abnormalities, short limbs and tails, dysplasia of lungs and genitals, and ventricular septal defects. In vitro binding assay revealed that Wnt5a binds to the CRD of Ror2. Furthermore, Ror2 associates via its CRD with rFz2, a putative receptor for Wnt5a. Interestingly, Wnt5a and Ror2 activate the non-canonical Wnt pathway, as assessed by activation of JNK in cultured cells and inhibition of convergent extension movements in Xenopus. Conclusions: Our findings indicate that Wnt5a and Ror2 interact physically and functionally. Ror2 may thus act as a receptor for Wnt5a to activate non-canonical Wnt signalling.