318 research outputs found

    Apparently third in a series of ten books

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    Here is the Japanese version of a book I have liked in its 1990 Korean incarnation. Part of the fun is that the books are mirror opposites: one opens to the left and the other to the right. GA is pictured on the cover. Where that Korean book was #5 in its series, this Japanese version is #3 in its series. As I mention there, I like this book, principally for its vivid color reproductions. Four stories: TMCM, GA (maybe the best art), The Bat and the Birds and the Animals, and LM (the poorest art). It is still true that the back cover presents 15, but now it is not reversed. Originally purchased in BookTown2008 for 150 Yen. Like its original, the book begins with Page 2, which is the inside front cover.This is a hardbound book (hard cover)Language note: JapaneseIriart

    Acceptance conditions in automated negotiation

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    In every negotiation with a deadline, one of the negotiating parties has to accept an offer to avoid a break off. A break off is usually an undesirable outcome for both parties, therefore it is important that a negotiator employs a proficient mechanism to decide under which conditions to accept. When designing such conditions one is faced with the acceptance dilemma: accepting the current offer may be suboptimal, as better offers may still be presented. On the other hand, accepting too late may prevent an agreement from being reached, resulting in a break off with no gain for either party. Motivated by the challenges of bilateral negotiations between automated agents and by the results and insights of the automated negotiating agents competition (ANAC), we classify and compare state-of-the-art generic acceptance conditions. We focus on decoupled acceptance conditions, i.e. conditions that do not depend on the bidding strategy that is used. We performed extensive experiments to compare the performance of acceptance conditions in combination with a broad range of bidding strategies and negotiation domains. Furthermore we propose new acceptance conditions and we demonstrate that they outperform the other conditions that we study. In particular, it is shown that they outperform the standard acceptance condition of comparing the current offer with the offer the agent is ready to send out. We also provide insight in to why some conditions work better than others and investigate correlations between the properties of the negotiation environment and the efficacy of acceptance conditions.MediamaticsElectrical Engineering, Mathematics and Computer Scienc

    2 in 1 Tales

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    Here is the first printing of a pamphlet whose republication I have listed under 1995 from the same publisher. Books in this edition and this year cost 2.50.Whenreprintedayearlater,theycost2.50. When reprinted a year later, they cost 2.95. See my comments there

    Asymmetric Diels-Alder Reaction of 5,5,5-Trichloro-3-penten-2-one and Its Related Compound

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    Diels-Alder reactions of 5,5,5-trichloro-3-penten-2-one and ethyl 4,4,4-trichloro-2-butenoate with cyclopentadiene in the presence of a chiral Lewis acid gave exo-2-acetyl-endo-3-trichloromethyl-bicyclo[2.2.1]hept-5-ene and exo-2-ethoxycarbonyl-endo-3-trichloromethylbicyclo[2.2.1]hept-5-ene with 40% and 7% e.e., respectively

    Asymmetric Diels-Alder Reaction of 5,5,5-Trichloro-3-penten-2-one and Its Related Compound

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    Diels-Alder reactions of 5,5,5-trichloro-3-penten-2-one and ethyl 4,4,4-trichloro-2-butenoate with cyclopentadiene in the presence of a chiral Lewis acid gave exo-2-acetyl-endo-3-trichloromethyl-bicyclo[2.2.1]hept-5-ene and exo-2-ethoxycarbonyl-endo-3-trichloromethylbicyclo[2.2.1]hept-5-ene with 40% and 7% e.e., respectively

    G-substrate

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    A 55-kDa endonuclease of mammalian mitochondria: comparison of its subcellular localization and endonucleolytic properties with those of endonuclease G

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    A novel endonuclease of 55-kDa was found in rat liver mitochondria by a zymographic assay, in addition to the 29 kDa enzyme that is well-known as endonuclease G (Endo G). Subcellular localization of these enzymes in rat liver cells was examined by biochemical fractionation. Endo G was located in both nuclei and mitochondria as has been previously reported, while the 55-kDa enzyme was only detected in the mitochondrial fraction. The levels of the endonucleases in the mitochondria varied greatly among the rat organs, and the activity in the heart was about 30 times higher than that in the liver. The 55-kDa enzyme and Endo G were extracted from bovine heart mitochondria with 0.4 M NaCl. During purification the 55-kDa enzyme and Endo G were copurified because of their similar chromatographic behavior, so they were separated by gel filtration or electrophoresis in the presence of SDS and the proteins were then renatured. The nucleolytic properties of the 55-kDa enzyme resembled those of Endo G and other known mitochondrial nucleases. The enzyme degraded single-stranded DNA more rapidly than duplex DNA at a weak alkaline pH, requiring Mg2+ or Mn2+ but not Ca2+ or Zn2+. Nicks generated by the enzyme had 5&#8242;-P and 3&#8242;-OH ends. The 55-kDa enzyme, like Endo G, displayed an unusually strong preference to nick within a (dG)n · (dC)n tract.</p
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