Anastomotic aneurysm can occur anytime after operations for Takayasu's arteritis. The development of anastomotic aneurysm is not influenced by any factor specific to this disease except the presence of an aneurysmal lesion.

An automated patient recognition method for correcting "wrong" chest radiographs being stored in a picture archiving and communication system (PACS) environment has been developed. The method is based on an image-matching technique that uses previous chest radiographs. For identification of a "wrong" patient, the correlation value was determined for a previous image of a patient and a new, current image of the presumed corresponding patient. The current image was shifted horizontally and vertically and rotated, so that we could determine the best match between the two images. The results indicated that the correlation values between the current and previous images for the same, "correct" patients were generally greater than those for different, "wrong" patients. Although the two histograms for the same patient and for different patients overlapped at correlation values greater than 0.80, most parts of the histograms were separated. The correlation value was compared with a threshold value that was determined based on an analysis of the histograms of correlation values obtained for the same patient and for different patients. If the current image is considered potentially to belong to a "wrong" patient, then a warning sign with the probability for a "wrong" patient is provided to alert radiology personnel. Our results indicate that at least half of the "wrong" images in our database can be identified correctly with the method described in this study. The overall performance in terms of a receiver operating characteristic curve showed a high performance of the system. The results also indicate that some readings of "wrong" images for a given patient in the PACS environment can be prevented by use of the method we developed. Therefore an automated warning system for patient recognition would be useful in correcting "wrong" images being stored in the PACS environment.

This paper reports the nanoscale texture and microstructure of a high-performance NdFeAs(O,F) superconducting thin film grown by molecular beam epitaxy on a textured MgO/Y 2 O 3 /Hastelloy substrate. The NdFeAs(O,F) film forms a highly textured columnar grain structure by epitaxial growth on the MgO template. Although the film contains stacking faults along the abplane as well as grain boundaries perpendicular to the ab-plane, good superconducting properties are measured: a critical temperature, T c , of 46 K and a self-field critical current density, J c , of 2 × 10 6 A/cm 2 at 4.2 K. Automated crystal orientation mapping by scanning precession electron diffraction in transmission electron microscope is employed to analyze the misorientation angles between adjacent grains in a large ensemble (247 grains), and 99% of the grain boundaries show in-plane misorientation angles (Δγ) less than the critical angle θ c , which satisfies one of the necessary conditions for the high J c . Comparing the columnar grain size distribution with the mean distance of the flux line lattice, the triple junctions of low-angle grain boundaries are found to be effective pinning centers, even at high temperatures (≥35 K) and/or low magnetic fields.

We report on the growth of NdFeAs(O,H) epitaxial thin films on MgO (001) substrates and their electrical transport properties. The maximum carrier density of the NdFeAs(O,H) films was more than twice as large as that of our NdFeAs(O,F) films. This enabled us to investigate the physical properties of heavily electron doped NdFeAsO, which could not be achieved with NdFeAs(O,F). The irreversibility field H irr of NdFeAs(O,H) was larger than that of NdFeAs(O,F) for H || c due to the decrease in the anisotropy of the upper critical field. A very high critical current density of 17 MA cm −2 was recorded at 4 K, which corresponds to about 13% of the depairing current density of NdFeAs(O,F).

We developed a novel method for capturing proteins that interact with a target protein. This method utilizes a protein containing a site-specifically incorporated 3-azidotyrosine (N3-Y) and FG beads for immobilization of the protein via an azido group. Using calmodulin (CaM) as the target protein, we introduced N3-Y at position 72 and conjugated it to FG beads by copper-free click chemistry. From the Ca(2+)/CaM-binding proteins captured from mouse brain cell lysate and analysis by mass spectrometry, we identified six proteins: alpha-enolase (ENOA), glucose-6-phosphate isomerase (GPI), annexin A5 (ANXA5), malate dehydrogenase 1 (MDH1), glyceraldehyde-3-phosphate dehydrogenase and the well-known CaM-binding protein phosphoglycerate kinase 1 (PGK1). The presence of photo-crosslinking products via N3-Y for all the captured proteins except GPI indicated that they bound directly to CaM. In this study, ENOA, ANXA5 and MDH1 were identified as novel CaM-binding proteins, and PGK1 was bound to Ca(2+)/CaM and also Ca(2+)-free CaM. This method should prove useful for capturing novel interacting proteins and serve as a useful tool for proteomic analyses.