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  • 1
    Call number: AWI A1-00-0196-3
    In: 33rd COSPAR Scientific Assembly
    Type of Medium: Monograph available for loan
    Pages: iv, 271 S. : Ill., graph. Darst., Kt.
    ISBN: 066229047X
    Location: AWI Reading room
    Branch Library: AWI Library
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  • 2
    Publication Date: 2011-12-06
    Description: Author(s): Carl Ekdahl, E. O. Abeyta, R. Archuleta, H. Bender, W. Broste, C. Carlson, G. Cook, D. Frayer, J. Harrison, T. Hughes, J. Johnson, E. Jacquez, B. Trent McCuistian, N. Montoya, S. Nath, K. Nielsen, C. Rose, M. Schulze, H. V. Smith, C. Thoma, and C. Y. Tom [Phys. Rev. ST Accel. Beams 14, 120401] Published Mon Dec 05, 2011
    Keywords: Pulsed-Power Accelerators, Technology, and Dynamics
    Electronic ISSN: 1098-4402
    Topics: Physics
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  • 3
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    Joshua B. Benoit; Zach N. Adelman; Klaus Reinhardt; Amanda Dolan; Monica Poelchau; Emily C. Jennings; Elise M. Szuter; Richard W. Hagan; Hemant Gujar; Jayendra Nath Shukla; Fang Zhu; M. Mohan; David R. Nelson; Andrew J. Rosendale; Christian Derst; Valentina Resnik; Sebastian Wernig; Pamela Menegazzi; Christian Wegener; Nicolai Peschel; Jacob M. Hendershot; Wolfgang Blenau; Reinhard Predel; Paul R. Johnston; Panagiotis Ioannidis; Robert M. Waterhouse; Ralf Nauen; Corinna Schorn; Mark-Christoph Ott; Frank Maiwald; J. Spencer Johnston; Ameya D. Gondhalekar; Michael E. Scharf; Brittany F. Peterson; Kapil R. Raje; Benjamin A. Hottel; David Armisén; Antonin Jean Johan Crumière; Peter Nagui Refki; Maria Emilia Santos; Essia Sghaier; Sèverine Viala; Abderrahman Khila; Seung-Joon Ahn; Christopher Childers; Chien-Yueh Lee; Han Lin; Daniel S. T. Hughes; Elizabeth J. Duncan; Shwetha C. Murali; Jiaxin Qu; Shannon Dugan; Sandra L. Lee; Hsu Chao; Huyen Dinh; Yi Han; Harshavardhan Doddapaneni; Kim C. Worley; Donna M. Muzny; David Wheeler; Kristen A. Panfilio; Iris M. Vargas Jentzsch; Edward L. Vargo; Warren Booth; Markus Friedrich; Matthew T. Weirauch; Michelle A. E. Anderson; Jeffery W. Jones; Omprakash Mittapalli; Chaoyang Zhao; Jing-Jiang Zhou; Jay D. Evans; Geoffrey M. Attardo; Hugh M. Robertson; Evgeny M. Zdobnov; Jose M. C. Ribeiro; Richard A. Gibbs; John H. Werren; Subba R. Palli; Coby Schal; Stephen Richards
    Springer Nature
    Publication Date: 2016-02-04
    Description: Article The bed bug, Cimex lectularius , is a ubiquitous human ectoparasite with global distribution. Here, the authors sequence the genome of the bed bug and identify reductions in chemosensory genes, expansion of genes associated with blood digestion and genes linked to pesticide resistance. Nature Communications doi: 10.1038/ncomms10165 Authors: Joshua B. Benoit, Zach N. Adelman, Klaus Reinhardt, Amanda Dolan, Monica Poelchau, Emily C. Jennings, Elise M. Szuter, Richard W. Hagan, Hemant Gujar, Jayendra Nath Shukla, Fang Zhu, M. Mohan, David R. Nelson, Andrew J. Rosendale, Christian Derst, Valentina Resnik, Sebastian Wernig, Pamela Menegazzi, Christian Wegener, Nicolai Peschel, Jacob M. Hendershot, Wolfgang Blenau, Reinhard Predel, Paul R. Johnston, Panagiotis Ioannidis, Robert M. Waterhouse, Ralf Nauen, Corinna Schorn, Mark-Christoph Ott, Frank Maiwald, J. Spencer Johnston, Ameya D. Gondhalekar, Michael E. Scharf, Brittany F. Peterson, Kapil R. Raje, Benjamin A. Hottel, David Armisén, Antonin Jean Johan Crumière, Peter Nagui Refki, Maria Emilia Santos, Essia Sghaier, Sèverine Viala, Abderrahman Khila, Seung-Joon Ahn, Christopher Childers, Chien-Yueh Lee, Han Lin, Daniel S. T. Hughes, Elizabeth J. Duncan, Shwetha C. Murali, Jiaxin Qu, Shannon Dugan, Sandra L. Lee, Hsu Chao, Huyen Dinh, Yi Han, Harshavardhan Doddapaneni, Kim C. Worley, Donna M. Muzny, David Wheeler, Kristen A. Panfilio, Iris M. Vargas Jentzsch, Edward L. Vargo, Warren Booth, Markus Friedrich, Matthew T. Weirauch, Michelle A. E. Anderson, Jeffery W. Jones, Omprakash Mittapalli, Chaoyang Zhao, Jing-Jiang Zhou, Jay D. Evans, Geoffrey M. Attardo, Hugh M. Robertson, Evgeny M. Zdobnov, Jose M. C. Ribeiro, Richard A. Gibbs, John H. Werren, Subba R. Palli, Coby Schal, Stephen Richards
    Electronic ISSN: 2041-1723
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 4
    Publication Date: 2016-03-02
    Description: An antibiotic resistance (AR) Dashboard application is being developed regarding the occurrence of antibiotic resistance genes (ARG) and bacteria (ARB) in environmental and clinical settings. The application gathers and geospatially maps AR studies, reported occurrence and antibiograms, which can be downloaded for offline analysis. With the integration of multiple data sets, the database can be used on a regional or global scale to identify hot spots for ARGs and ARB; track and link spread and transmission, quantify environmental or human factors influencing presence and persistence of ARG harboring organisms; differentiate natural ARGs from those distributed via human or animal activity; cluster and compare ARGs connections in different environments and hosts; and identify genes that can be used as proxies to routinely monitor anthropogenic pollution. To initially populate and develop the AR Dashboard, a qPCR ARG array was tested with 30 surface waters, primary influent from three waste water treatment facilities, ten clinical isolates from a regional hospital and data from previously published studies including river, park soil and swine farm samples. Interested users are invited to download a beta version (available on iOS or Android), submit AR information using the application, and provide feedback on current and prospective functionalities.
    Print ISSN: 0168-6496
    Electronic ISSN: 1574-6941
    Topics: Biology
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  • 5
    Publication Date: 2013-11-29
    Description: Bacterial pathogens use an injectisome to deliver virulence proteins into eukaryotic host cells. The bacterial flagellum and injectisome export their component proteins for self-assembly. These two systems show high structural similarities and are classified as the type III secretion system, but it remains elusive how similar they are in situ because the structures of these complexes isolated from cells and visualized by electron cryomicroscopy have shown only the export channel and housing for the export apparatus. Here we report in situ structures of Salmonella injectisome and flagellum by electron cryotomography. The injectisome lacks the flagellar basal body C-ring, but a wing-like disc and a globular density corresponding to the export gate platform and ATPase hexamer ring, respectively, are stably attached through thin connectors, revealing yet unidentified common architectures of the two systems. The ATPase ring is far from the disc, suggesting that both apparatuses are observed in an export-off state. Scientific Reports 3 doi: 10.1038/srep03369
    Electronic ISSN: 2045-2322
    Topics: Natural Sciences in General
    Published by Springer Nature
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  • 6
    Publication Date: 2008-01-25
    Description: Bacterial flagella contain a specialized secretion apparatus that functions to deliver the protein subunits that form the filament and other structures to outside the membrane. This apparatus is related to the injectisome used by many gram-negative pathogens and symbionts to transfer effector proteins into host cells; in both systems this export mechanism is termed 'type III' secretion. The flagellar secretion apparatus comprises a membrane-embedded complex of about five proteins, and soluble factors, which include export-dedicated chaperones and an ATPase, FliI, that was thought to provide the energy for export. Here we show that flagellar secretion in Salmonella enterica requires the proton motive force (PMF) and does not require ATP hydrolysis by FliI. The export of several flagellar export substrates was prevented by treatment with the protonophore CCCP, with no accompanying decrease in cellular ATP levels. Weak swarming motility and rare flagella were observed in a mutant deleted for FliI and for the non-flagellar type-III secretion ATPases InvJ and SsaN. These findings show that the flagellar secretion apparatus functions as a proton-driven protein exporter and that ATP hydrolysis is not essential for type III secretion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paul, Koushik -- Erhardt, Marc -- Hirano, Takanori -- Blair, David F -- Hughes, Kelly T -- England -- Nature. 2008 Jan 24;451(7177):489-92. doi: 10.1038/nature06497.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Utah, 257 South 1400 East, Salt Lake City, Utah 84112, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18216859" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Antigens, Bacterial/genetics/metabolism ; Bacterial Proteins/genetics/metabolism/secretion ; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology ; *Energy Metabolism/drug effects ; Flagella/chemistry/metabolism/*secretion ; Hydrogen-Ion Concentration ; Mutation/genetics ; Protein Transport/drug effects/genetics ; Proton-Motive Force/drug effects/*physiology ; Proton-Translocating ATPases/metabolism ; Salmonella enterica/enzymology/genetics/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 2009-09-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rockstrom, Johan -- Steffen, Will -- Noone, Kevin -- Persson, Asa -- Chapin, F Stuart 3rd -- Lambin, Eric F -- Lenton, Timothy M -- Scheffer, Marten -- Folke, Carl -- Schellnhuber, Hans Joachim -- Nykvist, Bjorn -- de Wit, Cynthia A -- Hughes, Terry -- van der Leeuw, Sander -- Rodhe, Henning -- Sorlin, Sverker -- Snyder, Peter K -- Costanza, Robert -- Svedin, Uno -- Falkenmark, Malin -- Karlberg, Louise -- Corell, Robert W -- Fabry, Victoria J -- Hansen, James -- Walker, Brian -- Liverman, Diana -- Richardson, Katherine -- Crutzen, Paul -- Foley, Jonathan A -- England -- Nature. 2009 Sep 24;461(7263):472-5. doi: 10.1038/461472a.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stockholm Resilience Centre, Stockholm University, Kraftriket 2B, 10691 Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19779433" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; Civilization ; Conservation of Natural Resources/*methods/trends ; *Earth (Planet) ; Ecology/*methods/*trends ; *Ecosystem ; Extinction, Biological ; Fossils ; Green Chemistry Technology/*methods/trends ; Greenhouse Effect ; History, 20th Century ; History, 21st Century ; History, Ancient ; *Human Activities/history ; Humans ; Nitrogen/metabolism ; Phosphorus/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 2012-03-31
    Description: Synchronizing rhythms of behaviour and metabolic processes is important for cardiovascular health and preventing metabolic diseases. The nuclear receptors REV-ERB-alpha and REV-ERB-beta have an integral role in regulating the expression of core clock proteins driving rhythms in activity and metabolism. Here we describe the identification of potent synthetic REV-ERB agonists with in vivo activity. Administration of synthetic REV-ERB ligands alters circadian behaviour and the circadian pattern of core clock gene expression in the hypothalami of mice. The circadian pattern of expression of an array of metabolic genes in the liver, skeletal muscle and adipose tissue was also altered, resulting in increased energy expenditure. Treatment of diet-induced obese mice with a REV-ERB agonist decreased obesity by reducing fat mass and markedly improving dyslipidaemia and hyperglycaemia. These results indicate that synthetic REV-ERB ligands that pharmacologically target the circadian rhythm may be beneficial in the treatment of sleep disorders as well as metabolic diseases.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3343186/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3343186/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Solt, Laura A -- Wang, Yongjun -- Banerjee, Subhashis -- Hughes, Travis -- Kojetin, Douglas J -- Lundasen, Thomas -- Shin, Youseung -- Liu, Jin -- Cameron, Michael D -- Noel, Romain -- Yoo, Seung-Hee -- Takahashi, Joseph S -- Butler, Andrew A -- Kamenecka, Theodore M -- Burris, Thomas P -- DK080201/DK/NIDDK NIH HHS/ -- DK088499/DK/NIDDK NIH HHS/ -- DK089984/DK/NIDDK NIH HHS/ -- MH092769/MH/NIMH NIH HHS/ -- R01 DK073189/DK/NIDDK NIH HHS/ -- R01 DK080201/DK/NIDDK NIH HHS/ -- R01 DK080201-05/DK/NIDDK NIH HHS/ -- R01 MH092769/MH/NIMH NIH HHS/ -- R01 MH092769-02/MH/NIMH NIH HHS/ -- R01 MH093429/MH/NIMH NIH HHS/ -- R01 MH093429-01A1/MH/NIMH NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2012 Mar 29;485(7396):62-8. doi: 10.1038/nature11030.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Therapeutics, The Scripps Research Institute, Jupiter, Florida 33458, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22460951" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/drug effects/metabolism ; Animals ; Biological Clocks/drug effects/genetics/physiology ; Circadian Rhythm/*drug effects/genetics/*physiology ; Disease Models, Animal ; Energy Metabolism/*drug effects ; HEK293 Cells ; Humans ; Hypothalamus/drug effects/metabolism ; Liver/drug effects/metabolism ; Metabolome/drug effects ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Muscle, Skeletal/drug effects/metabolism ; Nuclear Receptor Subfamily 1, Group D, Member 1/*antagonists & ; inhibitors/metabolism ; Obesity/chemically induced/drug therapy/metabolism ; Pyrrolidines/*pharmacology ; Receptors, Cytoplasmic and Nuclear/*antagonists & inhibitors/metabolism ; Repressor Proteins/*antagonists & inhibitors/metabolism ; Thiophenes/*pharmacology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 1993-11-19
    Description: The ability of a regulatory protein to sense the integrity of the bacterial flagellar structure was investigated. In response to a defective hook-basal body complex, the anti-sigma 28 FlgM protein inhibits flagellin transcription. In cells with a functional hook-basal body complex, the flagellin genes are transcribed normally and the FlgM protein is expelled into the growth medium. In strains with a defective hook-basal body structure, FlgM is absent from the media. The presence of flagellin protein in the media is substantially reduced in strains carrying a FlgM-LacZ protein fusion, suggesting that the fusion is blocking the flagellar export apparatus. These results suggest that the FlgM protein assesses the integrity of the flagellar hook-basal body complex by itself being a substrate for export by the flagellar-specific export apparatus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hughes, K T -- Gillen, K L -- Semon, M J -- Karlinsey, J E -- GM43149/GM/NIGMS NIH HHS/ -- T32-GM07270/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 19;262(5137):1277-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235660" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/*metabolism ; Flagella/metabolism/*ultrastructure ; Flagellin/*genetics ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Genes, Regulator ; Models, Biological ; Morphogenesis ; Recombinant Fusion Proteins/metabolism ; Salmonella typhimurium/genetics/growth & development/metabolism/*ultrastructure ; Sigma Factor/genetics/metabolism ; *Transcription, Genetic
    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: 2008-08-23
    Description: Many bacterial pathogens rely on a conserved membrane histidine sensor kinase, QseC, to respond to host adrenergic signaling molecules and bacterial signals in order to promote the expression of virulence factors. Using a high-throughput screen, we identified a small molecule, LED209, that inhibits the binding of signals to QseC, preventing its autophosphorylation and consequently inhibiting QseC-mediated activation of virulence gene expression. LED209 is not toxic and does not inhibit pathogen growth; however, this compound markedly inhibits the virulence of several pathogens in vitro and in vivo in animals. Inhibition of signaling offers a strategy for the development of broad-spectrum antimicrobial drugs.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2605406/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2605406/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rasko, David A -- Moreira, Cristiano G -- Li, De Run -- Reading, Nicola C -- Ritchie, Jennifer M -- Waldor, Matthew K -- Williams, Noelle -- Taussig, Ron -- Wei, Shuguang -- Roth, Michael -- Hughes, David T -- Huntley, Jason F -- Fina, Maggy W -- Falck, John R -- Sperandio, Vanessa -- P01 AI055637/AI/NIAID NIH HHS/ -- P01 AI055637-010005/AI/NIAID NIH HHS/ -- P01-AI055637-03/AI/NIAID NIH HHS/ -- R01 AI053067/AI/NIAID NIH HHS/ -- R01 AI053067-06/AI/NIAID NIH HHS/ -- R01 GM31278/GM/NIGMS NIH HHS/ -- R03 NS053582/NS/NINDS NIH HHS/ -- R03 NS053582-01/NS/NINDS NIH HHS/ -- R21 AI067827/AI/NIAID NIH HHS/ -- U01 AI077853/AI/NIAID NIH HHS/ -- U01 AI077853-01/AI/NIAID NIH HHS/ -- UO1-AI77853/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 Aug 22;321(5892):1078-80. doi: 10.1126/science.1160354.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Texas (UT) Southwestern Medical Center, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18719281" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Bacterial Agents/administration & dosage/*pharmacology/therapeutic use ; Enterohemorrhagic Escherichia coli/drug ; effects/genetics/metabolism/*pathogenicity ; Escherichia coli Infections/drug therapy ; Escherichia coli Proteins/antagonists & inhibitors/genetics/*metabolism ; Francisella tularensis/drug effects/genetics/metabolism/*pathogenicity ; Gene Expression Regulation, Bacterial/drug effects ; Gram-Negative Bacterial Infections/*drug therapy ; Mice ; Norepinephrine/metabolism ; Phosphorylation ; Protein Kinases/genetics/*metabolism ; Rabbits ; Salmonella Infections, Animal/drug therapy ; Salmonella typhimurium/drug effects/genetics/metabolism/*pathogenicity ; Signal Transduction/drug effects ; Small Molecule Libraries ; Sulfonamides/administration & dosage/chemistry/*pharmacology/therapeutic use ; Tularemia/drug therapy ; Virulence Factors/genetics
    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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