4 research outputs found

    A Novel Mechanism for Gridification of Compiled Java Applications

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    Exploiting Grids intuitively requires developers to alter their applications, which calls for expertise on Grid programming. Gridification tools address this problem by semi-automatically making user applications to be Grid-aware. However, most of these tools produce monolithic Grid applications in which common tuning mechanisms (e.g. parallelism) are not applicable, and do not reuse existing Grid middleware services. We propose BYG (BYtecode Gridifier), a gridification tool that relies on novel bytecode rewriting techniques to parallelize and easily execute existing applications via Grid middlewares. Experiments performed by using several computing intensive applications on a cluster and a simulated wide-area Grid suggest that our techniques are effective while staying competitive compared to programmatically using such services for gridifying applications

    BYG: An Approach to Just-in-Time Gridification of Conventional Java Applications

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    Grid technologies allow developers to run applications with enormous demands for resources such as processing power, data and network bandwidth. However, exploiting Grid resources demands developers to alter their applications to explicitly access the services of specific Grid middlewares. This involves more development effort and requires expertise on Grid programming. A number of recent research efforts among the so-called gridification methods aim to avoid these problems by semi-automatically deriving the Grid-enabled version of an application from its binary code. However, most of these approaches produce coarse-grained Grid applications that prevent programmers from employing tuning mechanisms such as parallelism and distribution, and are rather inflexible, since they were not designed to reuse existing Grid middleware services. To solve these issues, we propose BYG (BYtecode Gridifier), a new gridification method to easily gridify binary Java applications. The chapter describes the prototype implementation of BYG and some experiments showing the feasibility of the approach. Results show that BYG can be used to conveniently gridify and efficiently execute a broad range of computing intensive applications.Fil: Mateos Diaz, Cristian Maximiliano. Consejo Nacional de Investigaciones CientĂ­ficas y TĂ©cnicas. Centro CientĂ­fico TecnolĂłgico Conicet - Tandil. Instituto Superior de IngenierĂ­a del Software. Universidad Nacional del Centro de la Provincia de Buenos Aires. Instituto Superior de IngenierĂ­a del Software; ArgentinaFil: Zunino Suarez, Alejandro Octavio. Consejo Nacional de Investigaciones CientĂ­ficas y TĂ©cnicas. Centro CientĂ­fico TecnolĂłgico Conicet - Tandil. Instituto Superior de IngenierĂ­a del Software. Universidad Nacional del Centro de la Provincia de Buenos Aires. Instituto Superior de IngenierĂ­a del Software; ArgentinaFil: Campo, Marcelo Ricardo. Consejo Nacional de Investigaciones CientĂ­ficas y TĂ©cnicas. Centro CientĂ­fico TecnolĂłgico Conicet - Tandil. Instituto Superior de IngenierĂ­a del Software. Universidad Nacional del Centro de la Provincia de Buenos Aires. Instituto Superior de IngenierĂ­a del Software; ArgentinaFil: Trachsel, Ramiro. Consejo Nacional de Investigaciones CientĂ­ficas y TĂ©cnicas; Argentin

    Consecutive interactions with HSP90 and eEF1A underlie a functional maturation and storage pathway of AID in the cytoplasm

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    International audienceActivation-induced deaminase (AID) initiates mutagenic pathways to diversify the antibody genes during immune responses. The access of AID to the nucleus is limited by CRM1-mediated nuclear export and by an uncharacterized mechanism of cytoplasmic retention. Here, we define a conformational motif in AID that dictates its cytoplasmic retention and demonstrate that the translation elongation factor eukaryotic elongation factor 1 α (eEF1A) is necessary for AID cytoplasmic sequestering. The mechanism is independent of protein synthesis but dependent on a tRNA-free form of eEF1A. Inhibiting eEF1A prevents the interaction with AID, which accumulates in the nucleus and increases class switch recombination as well as chromosomal translocation byproducts. Most AID is associated to unspecified cytoplasmic complexes. We find that the interactions of AID with eEF1A and heat-shock protein 90 kD (HSP90) are inversely correlated. Despite both interactions stabilizing AID, the nature of the AID fractions associated with HSP90 or eEF1A are different, defining two complexes that sequentially produce and store functional AID in the cytoplasm. In addition, nuclear export and cytoplasmic retention cooperate to exclude AID from the nucleus but might not be functionally equivalent. Our results elucidate the molecular basis of AID cytoplasmic retention, define its functional relevance and distinguish it from other mechanisms regulating AID
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