2,921 research outputs found

    Low level commutation using mos fet transistors

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    Metal oxide silicon field effect transistors /MOS FET/ as switching elements for low level commutato

    Spiral FFAG lattice design tools - Application to 6-D tracking

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    Ray-tracing based methods for 3-D modeling of magnetic field and particle motion in spiral scaling FFAG accelerators have been developed. They allow efficient simulation of particle motion in presence of the strong field non-linearities proper to FFAG magnets, and of possible field overlapping in configurations of neighboring magnets, thus yielding a performing tool for spiral FFAG lattice design and optimizations, and for 6-D tracking studies. It is applied for illustration to a principle design of a 200 MeV medical class proton FFAG now under study in the frame of the RACCAM hadrontherapy project

    Federal-State Relations in Labor Exchange Policy

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    Maldi-tof Ms In The Clinical Microbiology Laboratory

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    Traditional methods for microbial identification are often very laborious and time consuming. A new mass spectrometry based technique, matrix-assisted laser desorption ionization-time of flight (MALDI-TOF), has been described as a rapid, practical and low-cost method for this purpose. In this article, primary and possible future applications of this tool are briefly discussed © agosto 2013.494256259Anhalt, J.P., Fenselau, C., Identification of bacteria using mass spectrometry (1975) Anal Chem, 47, pp. 219-225Bittar, F., MALDI-TOF-MS for rapid detection of staphylococcal Panton-Valentine leukocidin (2009) Int J Antimicrob Agents, 34, pp. 467-470Bizzini, A., Greub, G., Matrix-assisted laser desorption ionization time-of-flight mass spectrometry, a revolution in clinical microbial identification (2010) Clin Microbiol Infect, 16, pp. 1614-1619Bizzini, A., Performance of matrix-assisted laser desorption ionization-time of flight mass spectrometry for identification of bacterial strains routinely isolated in a clinical microbiology laboratory (2010) J Clin Microbiol, 48, pp. 1549-1554Buchan, B.W., Riebe, K.M., Ledeboer, N.A., Comparison of the MALDI biotyper system using sepsityper specimen processing to routine microbiological methods for identification of bacteria from positive blood culture bottles (2012) J Clin Microbiol, 50, pp. 346-352Carbonnelle, E., Rapid identification of Staphylococci isolated in clinical microbiology laboratories by matrix-assisted laser desorption ionization-time of flight mass spectrometry (2007) J Clin Microbiol, 45, pp. 2156-2161Cherkaoui, A., Comparison of two matrix-assisted laser desorption ionization-time of flight mass spectrometry methods with conventional phenotypic identification for routine identification of bacteria to the species level (2010) J Clin Microbiol, 48, pp. 1169-1175Christner, M., Rapid identification of bacteria from positive blood culture bottles by use of matrix-assisted laser desorption-ionization time of flight mass spectrometry fingerprinting (2010) J Clin Microbiol, 48, pp. 1584-1591Croxatto, A., Prodhom, G., Greub, G., Applications of MALDI-TOF mass spectrometry in clinical diagnostic microbiology (2012) FEMS Microbiol Rev, 36, pp. 380-407Degand, N., Matrix-assisted laser desorption ionization-time of flight mass spectrometry for identification of nonfermenting gramnegative bacilli isolated from cystic fibrosis patients (2008) J Clin Microbiol, 46, pp. 3361-3367Drancourt, M., Detection of microorganisms in blood specimens using matrix-assisted laser desorption ionization time-of-flight mass spectrometry: A review (2010) Clin Microbiol Infect, 16, pp. 1620-1625Edwards-Jones, V., Rapid discrimination between methicillinsensitive and methicillin-resistant Staphylococcus aureus by intact cell mass spectrometry (2000) J Med Microbiol, 49, pp. 295-300Eigner, U., Performance of a matrix-assisted laser desorption ionization-time-of- flight mass spectrometry system for the identification of bacterial isolates in the clinical routine laboratory (2009) Clin Lab, 55, pp. 289-296Emonet, S., Application and use of various mass spectrometry methods in clinical microbiology (2010) Clin Microbiol Infect, 16, pp. 1604-1613Erhard, M., Identification of dermatophyte species causing onychomycosis and tinea pedis by MALDI-TOF mass spectrometry (2008) Exp Dermatol, 17, pp. 356-361Ferroni, A., Real-time identification of bacteria and Candida species in positive blood culture broths by matrix-assisted laser desorption ionization-time of flight mass spectrometry (2010) J Clin Microbiol, 48, pp. 1542-1548Grosse-Herrenthey, A., Challenging the problem of clostridial identification with matrix-assisted laser desorption and ionization-timeof- flight mass spectrometry (MALDI-TOF MS) (2008) Anaerobe, 14, pp. 242-249Hettick, J.M., Discrimination of Penicillium isolates by matrixassisted laser desorption/ionization time-of-flight mass spectrometry fingerprinting (2008) Rapid Commun Mass Spectrom, 22, pp. 2555-2560Hettick, J.M., Discrimination of Aspergillus isolates at the species and strain level by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry fingerprinting (2008) Anal Biochem, 380, pp. 276-281Kaleta, E.J., Comparative analysis of PCR-electrospray ionization/mass spectrometry (MS) and MALDI-TOF/MS for the identification of bacteria and yeast from positive blood culture bottles (2011) Clin Chem, 57, pp. 1057-1067Karas, M., Bachmann, D., Hillenkamp, F., Influence of the wavelength in high-irradiance ultraviolet laser desorption mass spectrometry of organic molecules (1985) Anal Chem, 57, pp. 2935-2939Scola, B.L.A., Raoult, D., Direct identification of bacteria in positive blood culture bottles by matrix-assisted laser desorption ionization timeof- flight mass spectrometry (2009) PLoS One, 4, pp. e8041Majcherczyk, P.A., The discriminatory power of MALDITOF mass spectrometry to differentiate between isogenic teicoplanin susceptible and teicoplanin-resistant strains of methicillin-resistant Staphylococcus aureus (2006) FEMS Microbiol Lett, 255, pp. 233-239Marinach-Patrice, C., Use of mass spectrometry to identify clinical Fusarium isolates (2009) Clin Microbiol Infect, 15, pp. 634-642Marinach, C., MALDI-TOF MS-based drug susceptibility testing of pathogens: The example of Candida albicans and fluconazole (2009) Proteomics, 9, pp. 4627-4631Marklein, G., Matrix-assisted laser desorption ionization-time of flight mass spectrometry for fast and reliable identification of clinical yeast isolates (2009) J Clin Microbiol, 47, pp. 2912-2917Martiny, D., Comparison of Microflex LT and Vitek MS systems for routine identification of bacteria by matrix-assisted laser desorption ionization-time of flight mass spectrometry (2012) J Clin Microbiol, 50, pp. 1313-1325Murray, P.R., Matrix-assisted laser desorption ionization time-offlight mass spectrometry: Usefulness for taxonomy and epidemiology (2010) Clin Microbiol Infect, 16, pp. 1626-1630Neville, S.A., Utility of matrix-assisted laser desorption ionization-time of flight mass spectrometry following introduction for routine laboratory bacterial identification (2011) J Clin Microbiol, 49, pp. 2980-2984Pignone, M., Identification of mycobacteria by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (2006) J Clin Microbiol, 44, pp. 1963-1970Prodhom, G., Matrix-assisted laser desorption ionization-time of flight mass spectrometry for direct bacterial identification from positive blood culture pellets (2010) J Clin Microbiol, 48, pp. 1481-1483Seng, P., Ongoing revolution in bacteriology: Routine identification of bacteria by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (2009) Clin Infect Dis, 49, pp. 543-551Seyfarth, F., Identification of yeast isolated from dermatological patients by MALDI-TOF mass spectrometry (2012) Mycoses, 55, pp. 276-280Stevenson, L.G., Drake, S.K., Murray, P.R., Rapid identification of bacteria in positive blood culture broths by matrix-assisted laser desorption ionization-time of flight mass spectrometry (2010) J Clin Microbiol, 48, pp. 444-447Van Belkum, A., Biomedical mass spectrometry in todays and tomorrows clinical microbiology laboratories (2012) J Clin Microbiol, 50, pp. 1513-1517Van Veen, Q.S., Claas, E.C., Kuijper, E.J., High-throughput identification of bacteria and yeast by matrix-assisted laser desorption ionization-time of flight mass spectrometry in conventional medical microbiology laboratories (2010) J Clin Microbiol, 48, pp. 900-90

    LEIR lattice

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    The Low Energy Ion Ring (LEIR) is a low energy ion cooling and accumulation ring and serves to compress long ion pulses from Linac3 into high density bunches suitable for LHC ion operation. Issues of the LEIR lattice are to fulfil all constraints with a small number of quadrupoles and compensations of perturbations due to an electron cooler and gradients seen by the beam in the bending magnets during the ramp. Furthermore, experimental investigations via orbit response measurements will be reported

    Improved RE31 Analogues Containing Modified Nucleic Acid Monomers: Thermodynamic, Structural, and Biological Effects.

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    This is the author accepted manuscript. The final version is available from the American Chemical Society via the DOI in this record.RE31 is a 31-nt DNA aptamer, consisting of the G-quadruplex and a duplex domain, which is able to effectively prolong thrombin time. This article reports on the influence of certain modified nucleotide residues on thermodynamic and biological properties as well as the folding topology of RE31. Particularly, the effect of the presence of nucleosides in unlocked nucleic acid (UNA), locked nucleic acid (LNA), or β-l-RNA series was evaluated. The studies presented herein show that all modified residues can influence thermal and biological stabilities of G-quadruplex in a position-dependent manner. The aptamers modified simultaneously with UNA at the T15 position and LNAs in the duplex part possess the highest value of melting temperature and a 2-fold higher anticoagulant effect. Importantly, RE31 variants modified with nucleosides in UNA, LNA, or β-l-RNA series exhibit unchanged G-quadruplex folding topology. Crucially, introduction of any of the modified residues into RE31 causes prolongation of aptamer stability in human serum.National Science CenterPolish Ministry of Science and Higher Educatio
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