5,780 research outputs found

    On the nonlinear statistics of range image patches

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    In [A. B. Lee, K. S. Pedersen, and D. Mumford, Int. J. Comput. Vis., 54 (2003), pp. 83–103], the authors study the distributions of 3 × 3 patches from optical images and from range images. In [G. Carlsson, T. Ishkanov, V. de Silva, and A. Zomorodian, Int. J. Comput. Vis., 76 (2008), pp. 1–12], the authors apply computational topological tools to the data set of optical patches studied by Lee, Pedersen, and Mumford and find geometric structures for high density subsets. One high density subset is called the primary circle and essentially consists of patches with a line separating a light and a dark region. In this paper, we apply the techniques of Carlsson et al. to range patches. By enlarging to 5×5 and 7×7 patches, we find core subsets that have the topology of the primary circle, suggesting a stronger connection between optical patches and range patches than was found by Lee, Pedersen, and Mumford

    Using superlattice potentials to probe long-range magnetic correlations in optical lattices

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    In Pedersen et al. (2011) we proposed a method to utilize a temporally dependent superlattice potential to mediate spin-selective transport, and thereby probe long and short range magnetic correlations in optical lattices. Specifically this can be used for detecting antiferromagnetic ordering in repulsive fermionic optical lattice systems, but more generally it can serve as a means of directly probing correlations among the atoms by measuring the mean value of an observable, the number of double occupied sites. Here, we provide a detailed investigation of the physical processes which limit the effectiveness of this "conveyer belt method". Furthermore we propose a simple ways to improve the procedure, resulting in an essentially perfect (error-free) probing of the magnetic correlations. These results shows that suitably constructed superlattices constitute a promising way of manipulating atoms of different spin species as well as probing their interactions.Comment: 12 pages, 9 figure

    Oncology trainee perceptions of the prior authorization process: A national survey

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    Purpose: The medical trainee perspective regarding the prior authorization process has not been previously assessed. Here we evaluate the perceptions of radiation and medical oncology trainees regarding the prior authorization process and its effect on their training and patient care. Methods and Materials: A 12-question, nonincentivized, electronic national survey of radiation and medical oncology trainees at all Accreditation Council for Graduate Medical Education accredited oncology programs was conducted. Participation, perspectives, and experiences with the prior authorization process were assessed by Likert scale, free response, and multiple response selection. Results: Between January and March of 2019, the survey was distributed to 1505 trainees at 76 institutions with responses from 174/616 radiation (28.2%) and 139/889 medical oncology trainees (15.6%). The majority (69.2%) reported participating in the prior authorization process (radiation: 78.2% vs medical: 57.6%; Conclusions: These data indicate that trainees in US oncology programs are active participants in the prior authorization process and report that prior authorization approvals negatively influence their medical training and the quality of patient care. Additional efforts to revise the insurance approval process are warranted

    Boundary Correct Real-Time Soft Shadows

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    Thermodynamics of Heat Shock Response

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    Production of heat shock proteins are induced when a living cell is exposed to a rise in temperature. The heat shock response of protein DnaK synthesis in E.coli for temperature shifts from temperature T to T plus 7 degrees, respectively to T minus 7 degrees is measured as function of the initial temperature T. We observe a reversed heat shock at low T. The magnitude of the shock increases when one increase the distance to the temperature T023oT_0 \approx 23^o, thereby mimicking the non monotous stability of proteins at low temperature. Further we found that the variation of the heat shock with T quantitatively follows the thermodynamic stability of proteins with temperature. This suggest that stability related to hot as well as cold unfolding of proteins is directly implemented in the biological control of protein folding. We demonstrate that such an implementation is possible in a minimalistic chemical network.Comment: To be published in Physical Review Letter
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