平家物語におけるバ行マ行四段動詞の音便について

application/pdf女子大文学. 國文篇 : 大阪女子大學紀要. 2005, 56, p.A1-A11departmental bulletin pape

JIR-100型フーリエ変換赤外分光光度計(FT-IR)について

textapplication/pdfdepartmental bulletin pape

Studies of CP Violation in B→J/ψK* Decays

journal articl

経済のグローバリゼーションとEUのガバナンス（五） 欧州レベルの制度と政治過程

2008-06-25departmental bulletin pape

自己整合的カーボンナノチューブ成長とフィールドエミッタアレイ作製への応用

application/pdf三重大学電界放出ディスプレイなどの電界放出デバイスのための電子源として、カーボンナノチューブ(CNT)が密集して形成されるCNTピラーの電界放出電子源アレイの利用を検討した。CNTピラーからの電子放出特性向上のため、個々のCNTピラーの上部の形状を制御し、ピラー上部でのCNT分散状態を向上させた。その結果、ピラー上部の形状を従来のような平坦な形状から山形形状にすることにより,その電界放出特性が向上することが確認された。The influence of geometry of a carbon nanotube(CNT) pillar array on its field-emission properties was investigated for the purpose of designing a high-efficiency CNT field-emitter array. Here the dependence of the field-emission(FE) properties(turn-on voltage and emission site distribution) on the pillar pitch and the shape was examined. Our results showed that the change of the pillar shape from a square shape to a""mountain shape"", which was fabricated by the self-aligned CNT growth process, improved the FE properties. This improvement is due to the dispersed growth morphology, which reduces the field-screening effect at the top of the mountain-shaped pillars.平成21~23年度科学研究費補助金(基盤研究(C))研究成果報告書21560033research repor

Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7

Phagocytosis is a cellular process for internalization of micron-sized large particles including pathogens. The Bin-Amphiphysin-Rvs167 (BAR) domain proteins, including the FCH-BAR (F-BAR) domain proteins, impose specific morphologies on lipid membranes. Most BAR domain proteins are thought to form membrane invaginations or protrusions by assembling into helical submicron-diameter filaments, such as on clathrin-coated pits, caveolae, and filopodia. However, the mechanism by which BAR domain proteins assemble into micron-scale phagocytic cups was unclear. Here, we show that the two-dimensional sheet-like assembly of Growth Arrest-Specific 7 (GAS7) plays a critical role in phagocytic cup formation in macrophages. GAS7 has the F-BAR domain that possesses unique hydrophilic loops for two-dimensional sheet formation on flat membranes. Super-resolution microscopy reveals the similar assemblies of GAS7 on phagocytic cups and liposomes. The mutations of the loops abolishes both the membrane localization of GAS7 and phagocytosis. Thus, the sheet-like assembly of GAS7 plays a significant role in phagocytosis.journal articl