Prestack depth migration using straight ray technique(SRT)

Kirchhoff prestack depth migration requires an elaborate book-keeping effort and a massive IO process to construct Kirchhoff hyperbolas. In order to avoid the complexity of the programming code and the massive IO process, we propose a straight ray technique (SRT) for traveltimi calculations in Kirchhoff migration. Since all the rays are straight in. polar coordinates for the 2D velocity model,or in sphericalc oordinatesf or the 3D velocity model, traveltimesc an be simply computed along a straight ray for a given source-receiver configuration,without suffering from shadow zones and caustics, and used directly for building Kirchhoff hyperbolas. In this way, we clrcumvent the substantial IO process required for reading traveltimes on a disk and save computationals torage.N umerical examplesd emonstrateth at SRT computest raveltimesi ntermediate between first-arrival traveltimes and the most energetic arrival traveltimes, resulting in better images than the first arrival traveltimes for the 2D IFP Marmousi data. With the implementation of SRT for 2D Kirchhoff migration, we successfully extend our SRT to 3D Kirchhoff misration for the SECiEAGE salr dome data.This work was financially supported by the National Laboratory Project of the Ministry of Science and Technology, Brain Korea 21 Project of the Ministry of Education, grant No. R05-2000-00003 from the Basic Research Program of the Korea Science & Engineering Foundation, and grant No. PM10300 from the Korea Ocean Research & Development Institute

3-Hy­droxy-2-[(2E)-1-(2-hy­droxy-6-oxocyclo­hex-1-en-1-yl)-3-(2-meth­oxy­phen­yl)prop-2-en-1-yl]cyclo­hex-2-en-1-one

In the title compound, C22H24O5, each of the cyclo­hexenone rings adopts a half-chair conformation. The hy­droxy and carbonyl O atoms face each other and are orientated to allow for the formation of the two intra­molecular O—H⋯O hydrogen bonds which are typical of xanthene derivatives. In the crystal, weak inter­molecular C—H⋯O hydrogen bonds link mol­ecules into layers parallel to the ab plane

A role of DNA-dependent protein kinase for the activation of AMP-activated protein kinase in response to glucose deprivation

AbstractThe catalytic subunit of DNA-dependent protein kinase (DNA-PKcs) plays an essential role in double-strand break repair by initially recognizing and binding to DNA breaks. Here, we show that DNA-PKcs interacts with the regulatory γ1 subunit of AMP-activated protein kinase (AMPK), a heterotrimeric enzyme that has been proposed to function as a “fuel gauge” to monitor changes in the energy status of cells and is controlled by the upstream kinases LKB1 and Ca2+/calmodulin-dependent kinase kinase (CaMKK). In co-immunoprecipitation analyses, DNA-PKcs and AMPKγ1 interacted physically in DNA-PKcs-proficient M059K cells but not in DNA-PKcs-deficient M059J cells. Glucose deprivation-stimulated phosphorylation of AMPKα on Thr172 and of acetyl-CoA carboxylase (ACC), a downstream target of AMPK, is substantially reduced in M059J cells compared with M059K cells. The inhibition or down-regulation of DNA-PKcs by the DNA-PKcs inhibitors, wortmannin and Nu7441, or by DNA-PKcs siRNA caused a marked reduction in AMPK phosphorylation, AMPK activity, and ACC phosphorylation in response to glucose depletion in M059K, WI38, and IMR90 cells. In addition, DNA–DNA-PKcs−/− mouse embryonic fibroblasts (MEFs) exhibited decreased AMPK activation in response to glucose-free conditions. Furthermore, the knockdown of DNA-PKcs led to the suppression of AMPK (Thr172) phosphorylation in LKB1-deficient HeLa cells under glucose deprivation. Taken together, these findings support the positive regulation of AMPK activation by DNA-PKcs under glucose-deprived conditions in mammalian cells

Evaluation of the TEST 1 erythrocyte sedimentation rate system and intra- and inter-laboratory quality control using new latex control materials

Background: The erythrocyte sedimentation rate (ESR) test has been considered to be a simple procedure, not requiring quality control (QC). However, QC is essential for accuracy and precision. We evaluated the TEST 1 ESR system and performed QC procedures using newly developed latex control materials in three hospitals. Methods: Using tripotassium ethylenediaminetetraacetic acid blood samples (n=184), we compared TEST 1 ESR values with Westergren ESR data and evaluated intra-assay precision. Three levels of latex control materials were used to assess inter-assay precision. Reference range assessment was done using samples from 220 healthy individuals. Inter-laboratory QC with latex control materials in three hospitals was performed. Results: Correlation between TEST 1 ESR and Westergren ESR results was good (p<0.001). Intra-assay precision [coefficients of variation (CV) 6.6%-21.7%] with patient samples and inter-assay precision (CV 0.0%-6.8%) with latex control materials were satisfactory. The reference ranges of 2-10 mm/h for males and 2-19 mm/h for females were established. Inter-laboratory QC data with latex control materials in three hospitals demonstrated good accuracy and satisfactory precision (CV 0.0%-14.4%). Conclusions: Our results demonstrate that the TEST 1 QC is reliable and the latex control materials are valuable for inter-laboratory proficiency testing. Clin Chem Lab Med 2010; 48: 1043-8.Cha CH, 2009, AM J CLIN PATHOL, V131, P189, DOI 10.1309/AJCPOU1ASTLRANIJ*CLIN LAB STAND I, 2008, C28A3 CLSIPiva E, 2007, CLIN BIOCHEM, V40, P491, DOI 10.1016/j.clinbiochem.2006.12.002Padro-Miquel A, 2007, CLIN CHEM LAB MED, V45, P930, DOI 10.1515/CCLM.2007.150Romero A, 2003, CLIN CHEM LAB MED, V41, P232Plebani M, 2002, AM J CLIN PATHOL, V117, P621LEE BH, 2002, J CLIN PATHOL QUALIT, V24, P167GIAVARINA D, 2002, CLIN LAB, V48, P459Piva E, 2001, CLIN CHEM LAB MED, V39, P451*CLIN LAB STAND I, 2000, H2A4 CLSIPlebani M, 1998, AM J CLIN PATHOL, V110, P334BULL BS, 1993, J CLIN PATHOL, V46, P198BULL BS, 1991, PRACTICAL LAB HEMATOFABRY TL, 1987, BLOOD, V70, P1572WESTERGREN A, 1926, AM REV TUBERC, V14, P94

Reproducibility of Computer-Aided Detection Marks in Digital Mammography

OBJECTIVE: To evaluate the performance and reproducibility of a computeraided detection (CAD) system in mediolateral oblique (MLO) digital mammograms taken serially, without release of breast compression. MATERIALS AND METHODS: A CAD system was applied preoperatively to the fullfield digital mammograms of two MLO views taken without release of breast compression in 82 patients (age range: 33-83 years; mean age: 49 years) with previously diagnosed breast cancers. The total number of visible lesion components in 82 patients was 101: 66 masses and 35 microcalcifications. We analyzed the sensitivity and reproducibility of the CAD marks. RESULTS: The sensitivity of the CAD system for first MLO views was 71% (47/66) for masses and 80% (28/35) for microcalcifications. The sensitivity of the CAD system for second MLO views was 68% (45/66) for masses and 17% (6/35) for microcalcifications. In 84 ipsilateral serial MLO image sets (two patients had bilateral cancers), identical images, regardless of the existence of CAD marks, were obtained for 35% (29/84) and identical images with CAD marks were obtained for 29% (23/78). Identical images, regardless of the existence of CAD marks, for contralateral MLO images were 65% (52/80) and identical images with CAD marks were obtained for 28% (11/39). The reproducibility of CAD marks for the true positive masses in serial MLO views was 84% (42/50) and that for the true positive microcalcifications was 0% (0/34). CONCLUSION: The CAD system in digital mammograms showed a high sensitivity for detecting masses and microcalcifications. However, reproducibility of microcalcification marks was very low in MLO views taken serially without release of breast compression. Minute positional change and patient movement can alter the images and result in a significant effect on the algorithm utilized by the CAD for detecting microcalcifications