4,252 research outputs found

    Lepton flavor violation in low-scale seesaw models: SUSY and non-SUSY contributions

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    Taking the supersymmetric inverse seesaw mechanism as the explanation for neutrino oscillation data, we investigate charged lepton flavor violation in radiative and 3-body lepton decays as well as in neutrinoless μ−e\mu-e conversion in muonic atoms. In contrast to former studies, we take into account all possible contributions: supersymmetric as well as non-supersymmetric. We take CMSSM-like boundary conditions for the soft supersymmetry breaking parameters. We find several regions where cancellations between various contributions exist, reducing the lepton flavor violating rates by an order of magnitude compared to the case where only the dominant contribution is taken into account. This is in particular important for the correct interpretation of existing data as well as for estimating the reach of near future experiments where the sensitivity will be improved by one to two orders of magnitude. Moreover, we demonstrate that ratios like BR(τ→3μ\tau\to 3 \mu)/BR(τ→μe+e−\tau\to \mu e^+ e^-) can be used to determine whether the supersymmetric contributions dominate over the W±W^\pm and H±H^\pm contributions or vice versa.Comment: 75 pages, 7 figures. v3: references and comments added. Matches published versio

    Vitamin A potency of market milk

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    Nerve degeneration associated with avitaminosis A in the white rat

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    PHYCOBILISOMES AND ISOLATED PHYCOBILIPROTEINS. EFFECT OF GLUTARDIALDEHYDE AND BENZOQUINONE ON FLUORESCENCE

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    The fluorescence of the biliproteins C-phycocyanin from Spirulina platensis, B-phycoerythrin from Porphyridium cruentum and of isolated whole P. cruentum phycobilisomes is quenched in the presence of glutardialdehyde (GA) or benzoquinone (BQ). The kinetics of fluorescence decrease thus induced is biphasic. If GA is used as a quencher, the fluorescence can be recovered at 77 K. Contrary to the GA-effect, only a minor recovery takes place with BQ at 77K, thus demonstrating a different mechanism of action of GA and BQ on biliprotein
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