3,379 research outputs found

    THE FARM LEVEL EFFECTS OF BETTER ACCESS TO INFORMATION: THE CASE OF DART

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    In this study, two methods of entering and accessing dairy herd records are compared: the traditional mail-in Dairy Herd Improvement (DHI) system and the Direct Access to Records by Telephone (DART) system, which provides more timely and convenient access to records. An evaluation of DART was carried out using mail survey responses from 117 DART users and telephone surveys of 40 randomly selected users. Results indicate that DART users are generally satisfied with the system and feel that it improves their herd management. Variations in use of the DART system by DART users are explained by herd, cost, and management variables. DART users and comparable non-DART, DHI users are compared with respect to gains in herd production efficiency. Results indicate that DART users made somewhat better gains in most efficiency measures but that the differences were generally not statistically significant.Farm Management,

    Extension Educators Collecting Industry-specific Stakeholder Input

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    Extension educators have explored different methods for collecting stakeholder input, but a suitable methodology has not been agreed on. The Michigan State University Extension dairy team works with an advisory board and also collected formal stakeholder input through ten regional partner group surveys in 1997. In 2007, the team decided to seek another round of broad-based and inclusive stakeholder input. The research team decided to employ issue identification groups at different locations throughout the state and a mail survey. This paper reports on the procedure developed for this purpose and its results.focus group discussion, formative evaluation, issue identification, issue prioritization, multi-disciplinary teams, nominal group technique, Agribusiness, Research Methods/ Statistical Methods, Teaching/Communication/Extension/Profession,

    The Master\u27s Teachings Are Not Far: \u3cem\u3eThe Analects\u3c/em\u3e of Confucius and Its Modern Relevance

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    About the Authors Katherine E. Brigman is a Chemistry major at Armstrong and has earned the distinction of Dean’s List numerous times. She is a member of the National Society of Leadership and Success. During her studies, Katie found that she enjoyed learning about other cultures and various aspects of history, so she decided to obtain a minor in History, which she finds to be an exciting compliment to the scientific world. Brian Lee is a junior History major at Armstrong. He enjoys studying Mediterranean empires of Antiquity and mid-20th Century America. He has plans to enter the graduate program after completing his undergraduate degree. Juan Rojelio is a history major and will graduate in 2019

    FAST: FAST Analysis of Sequences Toolbox.

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    FAST (FAST Analysis of Sequences Toolbox) provides simple, powerful open source command-line tools to filter, transform, annotate and analyze biological sequence data. Modeled after the GNU (GNU's Not Unix) Textutils such as grep, cut, and tr, FAST tools such as fasgrep, fascut, and fastr make it easy to rapidly prototype expressive bioinformatic workflows in a compact and generic command vocabulary. Compact combinatorial encoding of data workflows with FAST commands can simplify the documentation and reproducibility of bioinformatic protocols, supporting better transparency in biological data science. Interface self-consistency and conformity with conventions of GNU, Matlab, Perl, BioPerl, R, and GenBank help make FAST easy and rewarding to learn. FAST automates numerical, taxonomic, and text-based sorting, selection and transformation of sequence records and alignment sites based on content, index ranges, descriptive tags, annotated features, and in-line calculated analytics, including composition and codon usage. Automated content- and feature-based extraction of sites and support for molecular population genetic statistics make FAST useful for molecular evolutionary analysis. FAST is portable, easy to install and secure thanks to the relative maturity of its Perl and BioPerl foundations, with stable releases posted to CPAN. Development as well as a publicly accessible Cookbook and Wiki are available on the FAST GitHub repository at https://github.com/tlawrence3/FAST. The default data exchange format in FAST is Multi-FastA (specifically, a restriction of BioPerl FastA format). Sanger and Illumina 1.8+ FastQ formatted files are also supported. FAST makes it easier for non-programmer biologists to interactively investigate and control biological data at the speed of thought

    Dynamical Decoupling in Optical Fibers: Preserving Polarization Qubits from Birefringent Dephasing

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    One of the major challenges in quantum computation has been to preserve the coherence of a quantum system against dephasing effects of the environment. The information stored in photon polarization, for example, is quickly lost due to such dephasing, and it is crucial to preserve the input states when one tries to transmit quantum information encoded in the photons through a communication channel. We propose a dynamical decoupling sequence to protect photonic qubits from dephasing by integrating wave plates into optical fiber at prescribed locations. We simulate random birefringent noise along realistic lengths of optical fiber and study preservation of polarization qubits through such fibers enhanced with Carr-Purcell-Meiboom-Gill (CPMG) dynamical decoupling. This technique can maintain photonic qubit coherence at high fidelity, making a step towards achieving scalable and useful quantum communication with photonic qubits.Comment: 8 pages, 5 figure

    The ectodomain of Toll-like receptor 9 is cleaved to generate a functional receptor.

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    Mammalian Toll-like receptors (TLRs) 3, 7, 8 and 9 initiate immune responses to infection by recognizing microbial nucleic acids; however, these responses come at the cost of potential autoimmunity owing to inappropriate recognition of self nucleic acids. The localization of TLR9 and TLR7 to intracellular compartments seems to have a role in facilitating responses to viral nucleic acids while maintaining tolerance to self nucleic acids, yet the cell biology regulating the transport and localization of these receptors remains poorly understood. Here we define the route by which TLR9 and TLR7 exit the endoplasmic reticulum and travel to endolysosomes in mouse macrophages and dendritic cells. The ectodomains of TLR9 and TLR7 are cleaved in the endolysosome, such that no full-length protein is detectable in the compartment where ligand is recognized. Notably, although both the full-length and cleaved forms of TLR9 are capable of binding ligand, only the processed form recruits MyD88 on activation, indicating that this truncated receptor, rather than the full-length form, is functional. Furthermore, conditions that prevent receptor proteolysis, including forced TLR9 surface localization, render the receptor non-functional. We propose that ectodomain cleavage represents a strategy to restrict receptor activation to endolysosomal compartments and prevent TLRs from responding to self nucleic acids

    Phosphatases Generate Signal Specificity Downstream of Ssp1 Kinase in Fission Yeast

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    AMPK-related protein kinases (ARKs) coordinate cell growth, proliferation, and migration with environmental status. It is unclear how specific ARKs are activated at specific times. In the fission yeast Schizosaccharomyces pombe, the CaMKK-like protein kinase Ssp1 promotes cell cycle progression by activating the ARK Cdr2 according to cell growth signals. Here, we demonstrate that Ssp1 activates a second ARK, Ssp2/AMPKα, for cell proliferation in low environmental glucose. Ssp1 activates these two related targets by the same biochemical mechanism: direct phosphorylation of a conserved residue in the activation loop (Cdr2-T166 and Ssp2-T189). Despite a shared upstream kinase and similar phosphorylation sites, Cdr2 and Ssp2 have distinct regulatory input cues and distinct functional outputs. We investigated this specificity and found that distinct protein phosphatases counteract Ssp1 activity toward its different substrates. We identified the PP6 family phosphatase Ppe1 as the primary phosphatase for Ssp2-T189 dephosphorylation. The phosphatase inhibitor Sds23 acts upstream of PP6 to regulate Ssp2-T189 phosphorylation in a manner that depends on energy but not on the intact AMPK heterotrimer. In contrast, Cdr2-T166 phosphorylation is regulated by protein phosphatase 2A but not by the Sds23-PP6 pathway. Thus, our study provides a phosphatase-driven mechanism to induce specific physiological responses downstream of a master protein kinase
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