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P. E. Koehler,J. A. Harvey,F. Becvar,M. Krticka,K. H. Guber 한국물리학회 2011 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.59 No.23
We describe new techniques for determining spins and parities of neutron resonances which have resulted in large improvements over previous methods. These advances have made it possible, for the first time, to obtain reduced-neutron- and total-radiation-width distributions separately for resonances of different spin and parity in odd-A target nuclides. Using these new as well as previous data, we show that neutron distributions sometimes are significantly different from the Porter-Thomas distribution assumed by the nuclear statistical model. Furthermore, we show that the radiation-width distributions often are substantially different than predicted by the nuclear statistical model using standard level densities and photon strength functions. These differences could have significant impact on astrophysical reaction rates calculated using the statistical model.
Neutron Cross-Section Measurements on Structural Materials at ORELA
K. H. Guber,P. E. Koehler,D. Wiarda,J. A. Harvey 한국물리학회 2011 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.59 No.23
Neutron capture experiments, using isotopically enriched and natural samples of chromium and titanium, were performed on flight paths 6 and 7 at the 40 m flight station of ORELA. The experimental data were acquired using a pair of deuterated benzene detectors employing the now well-established pulse-height-weighting technique. These data were complemented by new total cross-section measurements where no useful previous data were available.
Sadaghiani, A.,Lee, S.,Odegaard, Justin I.,Leveson-Gower, Dennis B.,McPherson, Olivia M.,Novick, P.,Kim, M.,Koehler, Angela N.,Negrin, R.,Dolmetsch, Ricardo E.,Park, C. Current Biology Ltd ; Elsevier Science Ltd 2014 Chemistry & biology Vol.21 No.10
Store-operated calcium (SOC) channels are vital for activation of the immune cells, and mutations in the channel result in severe combined immunodeficiency in human patients. In lymphocytes, SOC entry is mediated by the Orai1 channel, which is activated by direct binding of STIM1. Here we describe an alternative approach for identifying inhibitors of SOC entry using minimal functional domains of STIM1 and Orai1 to screen a small-molecule microarray. This screen identified AnCoA4, which inhibits SOC entry at submicromolar concentrations and blocks T cell activation in vitro and in vivo. Biophysical studies revealed that AnCoA4 binds to the C terminus of Orai1, directly inhibiting calcium influx through the channel and also reducing binding of STIM1. AnCoA4, unlike other reported SOC inhibitors, is a molecule with a known binding site and mechanism of action. These studies also provide proof of principle for an approach to ion channel drug discovery.