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Sökning: (WFRF:(Tang W)) srt2:(2000-2004) > (2004)

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  • Tang, Ou, et al. (författare)
  • Economic evaluation of disassembly processes in remanufacturing systems
  • 2004
  • Ingår i: International Journal of Production Research. - : Informa UK Limited. - 0020-7543 .- 1366-588X. ; 42:17, s. 3603-3617
  • Tidskriftsartikel (refereegranskat)abstract
    • A model to deal with the disassembly processes in remanufacturing systems is presented with focus being on evaluating their economic consequences. More specifically, the model assists decisions such as to which degree and for the sake of which components should the returned items be disassembled. Consequently, using the economic values of recoverable items, the inventory holding costs of these items are obtained. This information is further used to determine the inventory control policy. To access such economic values, the above average cost approach is compared with the net present value method. The latter is often considered a more 'correct' way in remanufacturing systems from the viewpoint of inventory control. The results from the economic evaluation model are intended to aid companies in systematically evaluating current as well as projected remanufacturing systems.
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  • Tang, W. H., et al. (författare)
  • LeSTIG1, an extracellular binding partner for the pollen receptor kinases LePRK1 and LePRK2, promotes pollen tube growth in vitro
  • 2004
  • Ingår i: The Plant Journal. - 0960-7412 .- 1365-313X. ; 39:3, s. 343-353
  • Tidskriftsartikel (refereegranskat)abstract
    • As pollen tubes grow through the pistil they are thought to perceive and respond to diverse signals. The tomato pollen-specific receptor kinases LePRK1 and LePRK2 might participate in signaling during pollen tube growth. We previously showed that the extracellular domain of LePRK2 interacts with a pollen protein, LAT52, before but not after pollen germination. To determine whether LePRK2 might have different binding partner(s) after pollen germination, we characterized two more proteins that, like LAT52, were identified in yeast two-hybrid screens using the extracellular domains of LePRK1 and LePRK2 as baits. We show that LeSHY, a leucine-rich repeat protein from pollen, and LeSTIG1, a small cysteine-rich protein from pistil, can bind the extracellular domains of both LePRK1 and LePRK2 in vitro. In vitro binding assays with the extracellular domain of LePRK2 suggested that LeSTIG1 could displace binding of LAT52, consistent with the idea that LePRK1 and LePRK2 might interact with different ligands at different stages of pollen tube growth. Exogenous LeSTIG1 promotes pollen tube growth in vitro. The interaction of these pollen kinases with LeSTIG1 supports the notion that LePRK1 and LePRK2 are involved in mediating pollen-pistil interactions.
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