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J Coggins

Publications and source records attributed to J Coggins.

5 recordsLinked to original sources

Portable software tools for 3D radiation therapy planning.

PURPOSE: Produce a collection of software tools (computer programs) that support three-dimensional (3D) radiation therapy planning. The tools are not a complete 3D planning system. Instead, they work with any 3D planning system that meets certain minimal specifications. The tools assist in deriving anatomic data from images, generating target volume contours, evaluating treatment plans, and verifying accurate treatment delivery. The tools are portable: they can run without source code changes in any computing environment that provides a library of functions and data definitions called the Foundation. The Foundation couples the portable tools to the (usually nonportable) file system and dose calculation associated with a particular 3D planning system. METHODS AND MATERIALS: Tools were written at three different (geographically separated) institutions. Software developers from all three sites specified the Foundation. The programmers' interface to the Foundation is portable, but a Foundation implementation need not be portable. Each group implemented a Foundation adapted to the (different) 3D planning system used at their site. RESULTS: All tools run at all three sites without source code changes. Each Foundation was implemented in a few person-months of programming effort. The program text and documentation for the tools have been placed in the public domain. CONCLUSIONS: It is practical and economical to produce portable radiotherapy treatment planning tools. Providers of 3D planning programs should offer Foundations for their systems, so they can be used with tools. Researchers considering new computer programs should write them as tools, so they can work with any 3D planning system.

Costs and Cost Analysis↗

Plant protein phosphatases. Subcellular distribution, detection of protein phosphatase 2C and identification of protein phosphatase 2A as the major quinate dehydrogenase phosphatase.

Protein phosphatases 1 and 2A (PP1 and PP2A) were identified in a variety of plant cells and found to be particulate or soluble depending on the species. In extracts prepared from oilseed-rape seeds these enzymes were associated with microsomes and more rapidly sedimenting fractions, whereas in wheat leaf extracts they were largely microsomal, the remainder being present in the soluble fraction. In pea leaf and carrot cell extracts PP1 and PP2A were almost entirely soluble. No PP1 or PP2A activity was associated with the membranes or stroma of chloroplasts in oilseed-rape seeds, pea leaves and wheat leaves. An Mg2(+)-dependent okadaic acid-insensitive protein phosphatase that resembles protein phosphatase 2C (PP2C) was detected in carrot cells, pea leaves and wheat leaves, but not in oilseed-rape seeds. In wheat leaf extracts PP2C was mostly present in the soluble fraction, a different location from PP1 or PP2A. The rapid inactivation of the cytosolic enzyme quinate dehydrogenase (QDH) in a fraction prepared from light-grown carrot cells was completely blocked by either okadaic acid or microcystin (two potent and specific inhibitors of PP1 and PP2A), whereas inhibitor 2 (a specific inhibitor of PP1) inhibited inactivation by only about 10%. Addition of the purified PP2A catalytic subunit from mammalian skeletal muscle increased the rate of QDH inactivation, whereas addition of mammalian PP1 did not. It is concluded that PP2A is the major enzyme responsible for dephosphorylating (inactivating) QDH in carrot cells. These observations indicate that okadaic acid and microcystin may be useful for identifying other plant processes that are controlled by phosphorylation/dephosphorylation mechanisms. Okadaic acid did not prevent the rapid inactivation of phosphoribulokinase or activation of glucose-6-phosphate dehydrogenase in a fraction prepared from light-grown pea leaves, and addition of the purified catalytic subunits of PP1 and PP2A did not accelerate either process. These observations, in conjunction with the absence of PP1 and PP2A activity in chloroplasts, suggest that these phosphatases are not involved in the regulation of chloroplast metabolism.

Brassica↗

Survey for Ixodes spp. and Borrelia burgdorferi in southeastern Wisconsin and northeastern Illinois.

Forested areas adjacent to Milwaukee, Wis., and Chicago, Ill., were investigated for rodents and ticks infected with Borrelia burgdorferi, the causative agent of Lyme disease. White-footed mice (Peromyscus leucopus or Peromyscus maniculatus), meadow voles (Microtus pennsylvanicus), and eastern chipmunks (Tamias striatus) were captured; and specimens from these animals were cultured for B. burgdorferi to define whether the midwestern Lyme disease area currently encompasses these large metropolitan centers. During 1988, B. burgdorferi was successfully cultured from the tissues of two M. pennyslvanicus voles captured from the Chicago area. However, no Ixodes spp. ticks were captured. None of 274 animals captured from sites I3 and 12 additional sites in Wisconsin and Illinois during the summer of 1989 were infected with B. burgdorferi or Ixodes spp. In addition, no ticks were recovered when the underbrush in 11 contiguous areas was flagged. Apparently, B. burgdorferi is rarely found in these areas because of the absence of the appropriate tick vectors. Further studies are needed to monitor the dispersal of B. burgdorferi-infected Ixodes dammini into this heavily populated midwestern region.

Animals↗

Surface strain distribution in isolated single lumbar vertebrae.

The surface strains of isolated single lumbar vertebrae under compressive load were examined by the techniques of brittlecoat and photoelastic analysis. Directions of principal strain components have been determined. Areas of stress concentration were found around the vertebral rims, near the pedicles, and around the foramina of the basivertebral veins.

Adult↗