Hard scattering and jets--from p-p collisions in the 1970's to Au+Au collisions at RHIC

Hard scattering in p-p collisions, discovered at the CERN ISR in 1972 by the method of leading particles, proved that the partons of Deeply Inelastic Scattering strongly interacted with each other. Further ISR measurements utilizing inclusive single or pairs of hadrons established that high pT particles are produced from states with two roughly back-to-back jets which are the result of scattering of constituents of the nucleons as described by Quantum Chromodynamics (QCD), which was developed during the course of these measurements. These techniques, which are the only practical method to study hard-scattering and jet phenomena in Au+Au central collisions, are reviewed, with application to measurements at RHIC.Comment: 4 pages, 5 figures, Proceedings of Hard Probes 2004, International Conference on Hard and Electromagnetic Probes of High Energy Nuclear Collisions, Nov 4-10, 2004, to appear in EPJ

The ALICE Transition Radiation Detector: Construction, operation, and performance

The Transition Radiation Detector (TRD) was designed and built to enhance the capabilities of the ALICE detector at the Large Hadron Collider (LHC). While aimed at providing electron identification and triggering, the TRD also contributes significantly to the track reconstruction and calibration in the central barrel of ALICE. In this paper the design, construction, operation, and performance of this detector are discussed. A pion rejection factor of up to 410 is achieved at a momentum of 1 GeV/c in p-Pb collisions and the resolution at high transverse momentum improves by about 40% when including the TRD information in track reconstruction. The triggering capability is demonstrated both for jet, light nuclei, and electron selection. (c) 2017 CERN for the benefit of the Authors. Published by Elsevier B.V

Japan Perspectives Recent Articles from the Tokyo Foundation Website No.10

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WHO global research priorities for antimicrobial resistance in human health

The WHO research agenda for antimicrobial resistance (AMR) in human health has identified 40 research priorities to be addressed by the year 2030. These priorities focus on bacterial and fungal pathogens of crucial importance in addressing AMR, including drug-resistant pathogens causing tuberculosis. These research priorities encompass the entire people-centred journey, covering prevention, diagnosis, and treatment of antimicrobial-resistant infections, in addition to addressing the overarching knowledge gaps in AMR epidemiology, burden and drivers, policies and regulations, and awareness and education. The research priorities were identified through a multistage process, starting with a comprehensive scoping review of knowledge gaps, with expert inputs gathered through a survey and open call. The priority setting involved a rigorous modified Child Health and Nutrition Research Initiative approach, ensuring global representation and applicability of the findings. The ultimate goal of this research agenda is to encourage research and investment in the generation of evidence to better understand AMR dynamics and facilitate policy translation for reducing the burden and consequences of AMR

boreale

Galium boreale Linnaeusnorthern bedstraw;boreal bedstraw;crosswortgaillet boréalNorth of Fort McMurray Cutline 1km south of Poplar Ck. Bridgethrough moist black spruce forestBlack spruc

rhombifolia

Thermopsis rhombifolia (Nuttall ex Pursh) Richardsonprairie golden bean;false lupine;yellow buffalo bean;prairie buck bean;golden bean;prairie bean;round-leaved thermopsis;prairie golden banner;prairie thermopsis;yellow peathermopsis rhombifoliéThermopsis rhombifolia� mile W of Spring Point Hutterite Cattle Camp, N side of road, S facing slopeS facing slope, lower part of slope on grasslan

nuttallii

Arabis nuttallii (Kuntze) B.L.Rob.arabette de NuttallNuttall's rockcressBehind Mt. BackusT. ChisholmN.E. facing flat, exposed meadow; across from Lrg. Shell Station; summit of Carbondale and Castle River watersheds1544 mPinus contorta, Delphinium bicolor, Rosa sp., Lupinus lepidus, Comandra umbellata, Sedum lanceolatum, Anemone patens, Amelanchier alnifolia, Oxytropis sp., Cerastium arvense, Achillea millefolium, Galium boreal

nuttallii

Arabis nuttallii (Kuntze) B.L.Rob.Nuttall's rockcressarabette de NuttallBehind Mt. BackusT. ChisholmN.E. facing flat, exposed meadow; across from Lrg. Shell Station; summit of Carbondale and Castle River watersheds1544 mPinus contorta, Delphinium bicolor, Rosa sp., Lupinus lepidus, Comandra umbellata, Sedum lanceolatum, Anemone patens, Amelanchier alnifolia, Oxytropis sp., Cerastium arvense, Achillea millefolium, Galium boreal

Workflow for Large Scale Detection and Validation of Peptide Modifications by RPLC-LTQ-Orbitrap: Application to the <i>Arabidopsis thaliana</i> Leaf Proteome and an Online Modified Peptide Library

Post-translational modifications (PTMs) of proteins add to the complexity of proteomes, thereby complicating the task of proteome characterization. An efficient strategy to identify this peptide heterogeneity is important for determination of protein function, as well as for mass spectrometry-based protein quantification. Furthermore, studies of allelic variation or single nucleotide polymorphisms (SNPs) at the proteome level, as well as mRNA editing, are increasingly relevant, but validation and determination of false positive rates are challenging. Here we describe an effective workflow for large scale PTM and amino acid substitution identification based on high resolution and high mass accuracy RPLC-MS data sets. A systematic validation strategy of PTMs using RPLC retention time shifts was implemented, and a decision tree for validation is presented. This workflow was applied to Arabidopsis proteome preparations; 1.5 million MS/MS spectra were processed resulting in 20% sequence assignments, with 5% from modified sequences and matching to 2904 proteins; this high assignment rate is in part due to the high quality spectral data. A searchable modified peptide library for Arabidopsis is available online at http://ppdb.tc.cornell.edu/. We discuss confidence in peptide and PTM assignment based on the acquired data set, as well as implications for quantitative analysis of physiologically induced and preparation-related modifications