About: Shizuoka University is a education organization based out in Shizuoka, Japan. It is known for research contribution in the topics: Thin film & Laser. The organization has 11711 authors who have published 19885 publications receiving 319861 citations. The organization is also known as: Shizuoka Daigaku & Shizudai.
Papers published on a yearly basis
TL;DR: It is shown that a large bowel microbial fermentation product, butyrate, induces the differentiation of colonic Treg cells in mice and ameliorated the development of colitis induced by adoptive transfer of CD4+ CD45RBhi T cells in Rag1−/− mice.
Abstract: Gut commensal microbes shape the mucosal immune system by regulating the differentiation and expansion of several types of T cell. Clostridia, a dominant class of commensal microbe, can induce colonic regulatory T (Treg) cells, which have a central role in the suppression of inflammatory and allergic responses. However, the molecular mechanisms by which commensal microbes induce colonic Treg cells have been unclear. Here we show that a large bowel microbial fermentation product, butyrate, induces the differentiation of colonic Treg cells in mice. A comparative NMR-based metabolome analysis suggests that the luminal concentrations of short-chain fatty acids positively correlates with the number of Treg cells in the colon. Among short-chain fatty acids, butyrate induced the differentiation of Treg cells in vitro and in vivo, and ameliorated the development of colitis induced by adoptive transfer of CD4(+) CD45RB(hi) T cells in Rag1(-/-) mice. Treatment of naive T cells under the Treg-cell-polarizing conditions with butyrate enhanced histone H3 acetylation in the promoter and conserved non-coding sequence regions of the Foxp3 locus, suggesting a possible mechanism for how microbial-derived butyrate regulates the differentiation of Treg cells. Our findings provide new insight into the mechanisms by which host-microbe interactions establish immunological homeostasis in the gut.
TL;DR: In this paper, the authors used a new technique to fabricate p-type ZnO reproducibly, and showed high-quality undoped films with electron mobility exceeding that in the bulk.
Abstract: Since the successful demonstration of a blue light-emitting diode (LED)1, potential materials for making short-wavelength LEDs and diode lasers have been attracting increasing interest as the demands for display, illumination and information storage grow2,3,4. Zinc oxide has substantial advantages including large exciton binding energy, as demonstrated by efficient excitonic lasing on optical excitation5,6. Several groups have postulated the use of p-type ZnO doped with nitrogen, arsenic or phosphorus7,8,9,10, and even p–n junctions11,12,13. However, the choice of dopant and growth technique remains controversial and the reliability of p-type ZnO is still under debate14. If ZnO is ever to produce long-lasting and robust devices, the quality of epitaxial layers has to be improved as has been the protocol in other compound semiconductors15. Here we report high-quality undoped films with electron mobility exceeding that in the bulk. We have used a new technique to fabricate p-type ZnO reproducibly. Violet electroluminescence from homostructural p–i–n junctions is demonstrated at room-temperature.
01 Apr 1985-Graphical Models \/graphical Models and Image Processing \/computer Vision, Graphics, and Image Processing
TL;DR: Two border following algorithms are proposed for the topological analysis of digitized binary images, which determine the surroundness relations among the borders of a binary image and follow only the outermost borders.
Abstract: Two border following algorithms are proposed for the topological analysis of digitized binary images. The first one determines the surroundness relations among the borders of a binary image. Since the outer borders and the hole borders have a one-to-one correspondence to the connected components of 1-pixels and to the holes, respectively, the proposed algorithm yields a representation of a binary image, from which one can extract some sort of features without reconstructing the image. The second algorithm, which is a modified version of the first, follows only the outermost borders (i.e., the outer borders which are not surrounded by holes). These algorithms can be effectively used in component counting, shrinking, and topological structural analysis of binary images, when a sequential digital computer is used.
TL;DR: The results show that PINK1-dependent phosphorylation of both parkin and ubiquitin is sufficient for full activation of parkin E3 activity, and demonstrate that phosphorylated ubiquit in is a parkin activator.
Abstract: Ubiquitin, known for its role in post-translational modification of other proteins, undergoes post-translational modification itself; after a decrease in mitochondrial membrane potential, the kinase enzyme PINK1 phosphorylates ubiquitin at Ser 65, and the phosphorylated ubiquitin then interacts with ubiquitin ligase (E3) enzyme parkin, which is also phosphorylated by PINK1, and this process is sufficient for full activation of parkin enzymatic activity. The small protein ubiquitin, familiar for its role in post-translational modification of other proteins by binding to them and regulating their activity or stability, is shown here to be the substrate of the kinase PINK1, which together with the ubiquitin ligase parkin is a causal gene for hereditary recessive Parkinsonism. Noriyuki Matsuda and colleagues show that following a decrease in mitochondrial membrane potential, PINK1 phosphorylates ubiquitin at serine residue 65; the phosphorylated ubiquitin then interacts with parkin, which is also phosphorylated by PINK1. This interaction allows full activation of parkin enzymatic activity, which involves tagging mitochondrial substrates with ubiquitin. PINK1 (PTEN induced putative kinase 1) and PARKIN (also known as PARK2) have been identified as the causal genes responsible for hereditary recessive early-onset Parkinsonism1,2. PINK1 is a Ser/Thr kinase that specifically accumulates on depolarized mitochondria, whereas parkin is an E3 ubiquitin ligase that catalyses ubiquitin transfer to mitochondrial substrates3,4,5. PINK1 acts as an upstream factor for parkin6,7 and is essential both for the activation of latent E3 parkin activity8 and for recruiting parkin onto depolarized mitochondria8,9,10,11,12. Recently, mechanistic insights into mitochondrial quality control mediated by PINK1 and parkin have been revealed3,4,5, and PINK1-dependent phosphorylation of parkin has been reported13,14,15. However, the requirement of PINK1 for parkin activation was not bypassed by phosphomimetic parkin mutation15, and how PINK1 accelerates the E3 activity of parkin on damaged mitochondria is still obscure. Here we report that ubiquitin is the genuine substrate of PINK1. PINK1 phosphorylated ubiquitin at Ser 65 both in vitro and in cells, and a Ser 65 phosphopeptide derived from endogenous ubiquitin was only detected in cells in the presence of PINK1 and following a decrease in mitochondrial membrane potential. Unexpectedly, phosphomimetic ubiquitin bypassed PINK1-dependent activation of a phosphomimetic parkin mutant in cells. Furthermore, phosphomimetic ubiquitin accelerates discharge of the thioester conjugate formed by UBCH7 (also known as UBE2L3) and ubiquitin (UBCH7∼ubiquitin) in the presence of parkin in vitro, indicating that it acts allosterically. The phosphorylation-dependent interaction between ubiquitin and parkin suggests that phosphorylated ubiquitin unlocks autoinhibition of the catalytic cysteine. Our results show that PINK1-dependent phosphorylation of both parkin and ubiquitin is sufficient for full activation of parkin E3 activity. These findings demonstrate that phosphorylated ubiquitin is a parkin activator.
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|Carlos F. Barbas||115||518||53545|
|William I. Milne||80||663||27167|
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