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  • 1
    Publication Date: 2018-01-26
    Description: Structure changes of a multiwall carbon nanotube (MWNT) during Joule heating were studied with simultaneous measurement of light emission spectra. The outer shells of the MWNT peeled off one by one because of excessive heating. All the peeled outer shells finally disappeared and inner shells whose tips were closed emerged, i.e., a new MWNT was formed. Each diameter of the shells comprising the MWNT decreased compared with those before the fracture. Light emission spectra during Joule heating of an MWNT were composed of both the blackbody radiation and characteristic peaks. The peaks in the light emission spectra shifted to higher energies in accordance with shrinkage of the inner shells. The energies of the peaks in the spectra corresponded to energy gaps between van Hove singularities calculated from the diameters of the shells, indicating that the peaks in the spectra are attributed to the interband electron transition in the MWNT.
    Print ISSN: 1757-8981
    Electronic ISSN: 1757-899X
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
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  • 2
    Publication Date: 2012-07-04
    Description: To understand complex biological systems, such as the development of multicellular organisms, it is important to characterize the gene expression dynamics. However, there is currently no universal technique for targeted insertion of reporter genes and quantitative imaging in multicellular model systems. Recently, genome editing using zinc-finger nucleases (ZFNs) has been reported in several models. ZFNs consist of a zinc-finger DNA-binding array with the nuclease domain of the restriction enzyme FokI and facilitate targeted transgene insertion. In this study, we successfully inserted a GFP reporter cassette into the HpEts1 gene locus of the sea urchin, Hemicentrotus pulcherrimus. We achieved this insertion by injecting eggs with a pair of ZFNs for HpEts1 with a targeting donor construct that contained ∼1-kb homology arms and a 2A-histone H2B–GFP cassette. We increased the efficiency of the ZFN-mediated targeted transgene insertion by in situ linearization of the targeting donor construct and cointroduction of an mRNA for a dominant-negative form of HpLig4, which encodes the H. pulcherrimus homolog of DNA ligase IV required for error-prone nonhomologous end joining. We measured the fluorescence intensity of GFP at the single-cell level in living embryos during development and found that there was variation in HpEts1 expression among the primary mesenchyme cells. These findings demonstrate the feasibility of ZFN-mediated targeted transgene insertion to enable quantification of the expression levels of endogenous genes during development in living sea urchin embryos.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 3
    Publication Date: 2014-01-22
    Description: E-cadherin is an important adhesion molecule whose loss is associated with progression and poor prognosis of liver cancer. However, it is unclear whether the loss of E-cadherin is a real culprit or a bystander in liver cancer progression. In addition, the precise role of E-cadherin in maintaining liver homeostasis is...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 4
    Publication Date: 2012-02-22
    Description: Glioblastoma, the most common primary malignant cancer of the brain, is characterized by rapid tumor growth and infiltration of tumor cells throughout the brain. These traits cause glioblastomas to be highly resistant to current therapies with a resultant poor prognosis. Although aberrant oncogenic signaling driven by signature genetic alterations, such as EGF receptor (EGFR) gene amplification and mutation, plays a major role in glioblastoma pathogenesis, the responsible downstream mechanisms remain less clear. Here, we report that EGFRvIII (also known as ΔEGFR and de2-7EGFR), a constitutively active EGFR mutant that is frequently co-overexpressed with EGFR in human glioblastoma, promotes tumorigenesis through Src family kinase (SFK)-dependent phosphorylation of Dock180, a guanine nucleotide exchange factor for Rac1. EGFRvIII induces phosphorylation of Dock180 at tyrosine residue 722 (Dock180Y722) and stimulates Rac1-signaling, glioblastoma cell survival and migration. Consistent with this being causal, siRNA knockdown of Dock180 or expression of a Dock180Y722F mutant inhibits each of these EGFRvIII-stimulated activities. The SFKs, Src, Fyn, and Lyn, induce phosphorylation of Dock180Y722 and inhibition of these SFKs by pharmacological inhibitors or shRNA depletion markedly attenuates EGFRvIII-induced phosphorylation of Dock180Y722, Rac1 activity, and glioblastoma cell migration. Finally, phosphorylated Dock180Y722 is coexpressed with EGFRvIII and phosphorylated SrcY418 in clinical specimens, and such coexpression correlates with an extremely poor survival in glioblastoma patients. These results suggest that targeting the SFK-p-Dock180Y722-Rac1 signaling pathway may offer a novel therapeutic strategy for glioblastomas with EGFRvIII overexpression.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 5
    Publication Date: 2014-11-02
    Description: Emerging infectious diseases are reducing biodiversity on a global scale. Recently, the emergence of the chytrid fungus Batrachochytrium salamandrivorans resulted in rapid declines in populations of European fire salamanders. Here, we screened more than 5000 amphibians from across four continents and combined experimental assessment of pathogenicity with phylogenetic methods to estimate the threat that this infection poses to amphibian diversity. Results show that B. salamandrivorans is restricted to, but highly pathogenic for, salamanders and newts (Urodela). The pathogen likely originated and remained in coexistence with a clade of salamander hosts for millions of years in Asia. As a result of globalization and lack of biosecurity, it has recently been introduced into naive European amphibian populations, where it is currently causing biodiversity loss.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martel, A -- Blooi, M -- Adriaensen, C -- Van Rooij, P -- Beukema, W -- Fisher, M C -- Farrer, R A -- Schmidt, B R -- Tobler, U -- Goka, K -- Lips, K R -- Muletz, C -- Zamudio, K R -- Bosch, J -- Lotters, S -- Wombwell, E -- Garner, T W J -- Cunningham, A A -- Spitzen-van der Sluijs, A -- Salvidio, S -- Ducatelle, R -- Nishikawa, K -- Nguyen, T T -- Kolby, J E -- Van Bocxlaer, I -- Bossuyt, F -- Pasmans, F -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2014 Oct 31;346(6209):630-1. doi: 10.1126/science.1258268.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Bacteriology and Avian Diseases, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, B-9820 Merelbeke, Belgium. an.martel@ugent.be. ; Department of Pathology, Bacteriology and Avian Diseases, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, B-9820 Merelbeke, Belgium. Centre for Research and Conservation, Royal Zoological Society of Antwerp, Koningin Astridplein 26, Antwerp, Belgium. ; Department of Pathology, Bacteriology and Avian Diseases, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, B-9820 Merelbeke, Belgium. ; CIBIO/InBIO, Centro de Investigacao em Biodiversidade e Recursos Geneticos da Universidade do Porto, Instituto de Ciencias Agrarias de Vairao, Rua Padre Armando Quintas, Vairao, Portugal. ; Department of Infectious Disease Epidemiology, Imperial College London, Norfolk Place, London W2 1PG, UK. ; Genome Sequencing and Analysis Program, The Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA. ; Koordinationsstelle fur amphibien- und reptilienschutz in der Schweiz (KARCH), Passage Maximilien-de-Meuron 6, 2000 Neuchatel, Switzerland. Institut fur Evolutionsbiologie und Umweltwissenschaften, Universitat Zurich. Winterthurerstrasse 190, 8057 Zurich, Switzerland. ; Invasive Alien Species Research Team, National Institute for Environment Studies, 16-2 Onogawa, Tsukuba, Ibaraki 305-8506, Japan. ; Department of Biology, University of Maryland, College Park, MD 20742, USA. ; Department of Ecology and Evolutionary Biology, Cornell University, Ithaca, NY 14853, USA. ; Museo Nacional de Ciencias Naturales, Consejo Superior de Investigaciones cientificas (CSIC), Jose Gutierrez Abascal 2, 28006 Madrid, Spain. ; Biogeography Department, Trier University, 54286 Trier, Germany. ; Durrell Institute of Conservation and Ecology, University of Kent, Kent CT2 7NR, UK. Institute of Zoology, Zoological Society of London, London NW1 4RY, UK. ; Institute of Zoology, Zoological Society of London, London NW1 4RY, UK. ; Reptile, Amphibian and Fish Conservation the Netherlands (RAVON), Post Office Box 1413, 6501 BK Nijmegen, Netherlands. ; Department of Earth Science, Environmental and Life (Di.S.T.A.V.), University of Genova, Corso Europa 26, I-16132 Genova, Italy. ; Graduate School of Human and Environmental Studies, Kyoto University, Yoshida Nihonmatsu-cho, Sakyo-ku, Kyoto 606-8501, Japan. ; Vietnam National Museum of Nature, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Hanoi, Vietnam. ; James Cook University, One Health Research Group, School of Public Health, Tropical Medicine and Rehabilitation Sciences, Townsville, Queensland, Australia. ; Amphibian Evolution Lab, Biology Department, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25359973" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; *Chytridiomycota ; Communicable Diseases, Emerging/microbiology/*veterinary ; *Endangered Species ; Mycoses/microbiology/*veterinary ; Phylogeny ; Urodela/classification/*microbiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2018
    Description: 〈p〉Topological defects have been explored in different fields ranging from condensed matter physics and particle physics to cosmology. In condensed matter, strong coupling between charge, spin, and lattice degrees of freedom brings about emergent excitations with topological characteristics at low energies. One-dimensional (1D) systems with degenerate dimerization patterns are typical stages for the generation of topological defects, dubbed "solitons"; for instance, charged solitons are responsible for high electrical conductivity in doped 〈i〉trans〈/i〉-polyacetylene. Here, we provide evidence based on a nuclear magnetic resonance (NMR) study for mobile spin solitons deconfined from a strongly charge-lattice–coupled spin-singlet ferroelectric order in a quasi-1D organic charge-transfer complex. The NMR spectral shift and relaxation rate associated with static and dynamic spin susceptibilities indicate that the ferroelectric order is violated by dilute solitonic spin excitations, which were further demonstrated to move diffusively by the frequency dependence of the relaxation rate. The traveling solitons revealed here may promise the emergence of anomalous electrical and thermal transport.〈/p〉
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
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  • 7
    Publication Date: 2018-12-01
    Description: Topological defects have been explored in different fields ranging from condensed matter physics and particle physics to cosmology. In condensed matter, strong coupling between charge, spin, and lattice degrees of freedom brings about emergent excitations with topological characteristics at low energies. One-dimensional (1D) systems with degenerate dimerization patterns are typical stages for the generation of topological defects, dubbed "solitons"; for instance, charged solitons are responsible for high electrical conductivity in doped trans -polyacetylene. Here, we provide evidence based on a nuclear magnetic resonance (NMR) study for mobile spin solitons deconfined from a strongly charge-lattice–coupled spin-singlet ferroelectric order in a quasi-1D organic charge-transfer complex. The NMR spectral shift and relaxation rate associated with static and dynamic spin susceptibilities indicate that the ferroelectric order is violated by dilute solitonic spin excitations, which were further demonstrated to move diffusively by the frequency dependence of the relaxation rate. The traveling solitons revealed here may promise the emergence of anomalous electrical and thermal transport.
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
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  • 8
    Publication Date: 2008-02-02
    Description: Cathepsin K was originally identified as an osteoclast-specific lysosomal protease, the inhibitor of which has been considered might have therapeutic potential. We show that inhibition of cathepsin K could potently suppress autoimmune inflammation of the joints as well as osteoclastic bone resorption in autoimmune arthritis. Furthermore, cathepsin K-/- mice were resistant to experimental autoimmune encephalomyelitis. Pharmacological inhibition or targeted disruption of cathepsin K resulted in defective Toll-like receptor 9 signaling in dendritic cells in response to unmethylated CpG DNA, which in turn led to attenuated induction of T helper 17 cells, without affecting the antigen-presenting ability of dendritic cells. These results suggest that cathepsin K plays an important role in the immune system and may serve as a valid therapeutic target in autoimmune diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Asagiri, Masataka -- Hirai, Toshitake -- Kunigami, Toshihiro -- Kamano, Shunya -- Gober, Hans-Jurgen -- Okamoto, Kazuo -- Nishikawa, Keizo -- Latz, Eicke -- Golenbock, Douglas T -- Aoki, Kazuhiro -- Ohya, Keiichi -- Imai, Yuuki -- Morishita, Yasuyuki -- Miyazono, Kohei -- Kato, Shigeaki -- Saftig, Paul -- Takayanagi, Hiroshi -- New York, N.Y. -- Science. 2008 Feb 1;319(5863):624-7. doi: 10.1126/science.1150110.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Signaling, Graduate School, Tokyo Medical and Dental University, Tokyo 113-8549, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18239127" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/metabolism ; Arthritis, Experimental/drug therapy/*immunology/*metabolism ; Autoimmune Diseases/drug therapy/immunology/*metabolism ; Bone Resorption ; Cathepsin K ; Cathepsins/antagonists & inhibitors/deficiency/*metabolism ; Cytokines/metabolism ; DNA/immunology/metabolism ; Dendritic Cells/drug effects/immunology ; Dinucleoside Phosphates/immunology/metabolism ; Encephalomyelitis, Autoimmune, Experimental/immunology/metabolism ; Endosomes/metabolism ; Freund's Adjuvant/immunology ; Lymphocyte Activation/drug effects ; Male ; Mice ; Osteoporosis/drug therapy ; Protease Inhibitors/pharmacology ; Rats ; *Signal Transduction ; T-Lymphocytes/drug effects/enzymology/immunology ; Toll-Like Receptor 9/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2015-02-14
    Description: The C-terminal region of Clostridium perfringens enterotoxin (C-CPE) can bind to specific claudins, resulting in the disintegration of tight junctions (TJs) and an increase in the paracellular permeability across epithelial cell sheets. Here we present the structure of mammalian claudin-19 in complex with C-CPE at 3.7 A resolution. The structure shows that C-CPE forms extensive hydrophobic and hydrophilic interactions with the two extracellular segments of claudin-19. The claudin-19/C-CPE complex shows no density of a short extracellular helix that is critical for claudins to assemble into TJ strands. The helix displacement may thus underlie C-CPE-mediated disassembly of TJs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saitoh, Yasunori -- Suzuki, Hiroshi -- Tani, Kazutoshi -- Nishikawa, Kouki -- Irie, Katsumasa -- Ogura, Yuki -- Tamura, Atsushi -- Tsukita, Sachiko -- Fujiyoshi, Yoshinori -- New York, N.Y. -- Science. 2015 Feb 13;347(6223):775-8. doi: 10.1126/science.1261833.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular and Structural Physiology Institute, Nagoya University, Chikusa, Nagoya 464-8601, Japan. Department of Basic Medical Science, Graduate School of Pharmaceutical Science, Nagoya University, Chikusa, Nagoya 464-8601, Japan. ; Cellular and Structural Physiology Institute, Nagoya University, Chikusa, Nagoya 464-8601, Japan. ; Laboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University, Suita, Osaka 565-0871, Japan. ; Cellular and Structural Physiology Institute, Nagoya University, Chikusa, Nagoya 464-8601, Japan. Department of Basic Medical Science, Graduate School of Pharmaceutical Science, Nagoya University, Chikusa, Nagoya 464-8601, Japan. yoshi@cespi.nagoya-u.ac.jp.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25678664" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Claudins/*chemistry ; Enterotoxins/*chemistry ; Hydrophobic and Hydrophilic Interactions ; Mice ; Protein Structure, Secondary ; Tight Junctions/chemistry/*ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 2015-01-28
    Description: The enzyme hydrogenase reversibly converts dihydrogen to protons and electrons at a metal catalyst. The location of the abundant hydrogens is of key importance for understanding structure and function of the protein. However, in protein X-ray crystallography the detection of hydrogen atoms is one of the major problems, since they display only weak contributions to diffraction and the quality of the single crystals is often insufficient to obtain sub-angstrom resolution. Here we report the crystal structure of a standard [NiFe] hydrogenase ( approximately 91.3 kDa molecular mass) at 0.89 A resolution. The strictly anoxically isolated hydrogenase has been obtained in a specific spectroscopic state, the active reduced Ni-R (subform Ni-R1) state. The high resolution, proper refinement strategy and careful modelling allow the positioning of a large part of the hydrogen atoms in the structure. This has led to the direct detection of the products of the heterolytic splitting of dihydrogen into a hydride (H(-)) bridging the Ni and Fe and a proton (H(+)) attached to the sulphur of a cysteine ligand. The Ni-H(-) and Fe-H(-) bond lengths are 1.58 A and 1.78A, respectively. Furthermore, we can assign the Fe-CO and Fe-CN(-) ligands at the active site, and can obtain the hydrogen-bond networks and the preferred proton transfer pathway in the hydrogenase. Our results demonstrate the precise comprehensive information available from ultra-high-resolution structures of proteins as an alternative to neutron diffraction and other methods such as NMR structural analysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ogata, Hideaki -- Nishikawa, Koji -- Lubitz, Wolfgang -- England -- Nature. 2015 Apr 23;520(7548):571-4. doi: 10.1038/nature14110. Epub 2015 Jan 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, D-45470 Mulheim an der Ruhr, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25624102" target="_blank"〉PubMed〈/a〉
    Keywords: Biocatalysis ; Carbon Monoxide/metabolism ; Catalytic Domain ; Crystallography, X-Ray ; Cysteine/chemistry/metabolism ; Desulfovibrio vulgaris/*enzymology ; Hydrogen/*analysis/*chemistry ; Hydrogen Bonding ; Hydrogenase/*chemistry/metabolism ; Iron/chemistry/metabolism ; Ligands ; Models, Molecular ; Molecular Weight ; Nickel/chemistry/metabolism ; Protons ; Sulfur/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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