280 resultados para Radakovic, Nikola
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Social software tools have become an integral part of students? personal lives and their primary communication medium. Likewise, these tools are increasingly entering the enterprise world (within the recent trend known as Enterprise 2.0) and becoming a part of everyday work routines. Aiming to keep the pace with the job requirements and also to position learning as an integral part of students? life, the field of education is challenged to embrace social software. Personal Learning Environments (PLEs) emerged as a concept that makes use of social software to facilitate collaboration, knowledge sharing, group formation around common interests, active participation and reflective thinking in online learning settings. Furthermore, social software allows for establishing and maintaining one?s presence in the online world. By being aware of a student's online presence, a PLE is better able to personalize the learning settings, e.g., through recommendation of content to use or people to collaborate with. Aiming to explore the potentials of online presence for the provision of recommendations in PLEs, in the scope of the OP4L project, we have develop a software solution that is based on a synergy of Semantic Web technologies, online presence and socially-oriented learning theories. In this paper we present the current results of this research work.
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This paper presents results of the benchmarking of COBAYA3 pin-by-pin for VVER-1000 obtained in the frame of the EU NURISP project. The 3D lattice solver in COBAYA3 uses transport corrected multi-group diffusion approximation with side-dependent interface discontinuity factors of GET or Selengut Black Box type. The objective of this study is to test the few-group calculation scheme when using structur ed and unstructured spatial meshes. Unstructured mesh is necessary to model the water gaps between the hexagonal assemblies. The benchmark problems include pin-by-pin calculations of 2D subsets of the core and comparison with APOLLO2 and TR IPOLI4 transport reference solutions. COBAYA3 solutions in 2, 4 and 8 energy groups have been tested. The results show excellent agreement with the reference on es when using side-dependent interface discontinuity factors.
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This paper presents solutions of the NURISP VVER lattice benchmark using APOLLO2, TRIPOLI4 and COBAYA3 pin-by-pin. The main objective is to validate MOC based calculation schemes for pin-by-pin cross-section generation with APOLLO2 against TRIPOLI4 reference results. A specific objective is to test the APOLLO2 generated cross-sections and interface discontinuity factors in COBAYA3 pin-by-pin calculations with unstructured mesh. The VVER-1000 core consists of large hexagonal assemblies with 2mm inter-assembly water gaps which require the use of unstructured meshes in the pin-by-pin core simulators. The considered 2D benchmark problems include 19-pin clusters, fuel assemblies and 7-assembly clusters. APOLLO2 calculation schemes with the step characteristic method (MOC) and the higher-order Linear Surface MOC have been tested. The comparison of APOLLO2 vs.TRIPOLI4 results shows a very close agreement. The 3D lattice solver in COBAYA3 uses transport corrected multi-group diffusion approximation with interface discontinuity factors of GET or Black Box Homogenization type. The COBAYA3 pin-by-pin results in 2, 4 and 8 energy groups are close to the reference solutions when using side-dependent interface discontinuity factors.
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Cell cycle progression is controlled by the sequential functions of cyclin-dependent kinases (cdks). Cdk activation requires phosphorylation of a key residue (on sites equivalent to Thr-160 in human cdk2) carried out by the cdk-activating kinase (CAK). Human CAK has been identified as a p40MO15/cyclin H/MAT1 complex that also functions as part of transcription factor IIH (TFIIH) where it phosphorylates multiple transcriptional components including the C-terminal domain (CTD) of the large subunit of RNA polymerase II. In contrast, CAK from budding yeast consists of a single polypeptide (Cak1p), is not a component of TFIIH, and lacks CTD kinase activity. Here we report that Cak1p and p40MO15 have strikingly different substrate specificities. Cak1p preferentially phosphorylated monomeric cdks, whereas p40MO15 preferentially phosphorylated cdk/cyclin complexes. Furthermore, p40MO15 only phosphorylated cdk6 bound to cyclin D3, whereas Cak1p recognized monomeric cdk6 and cdk6 bound to cyclin D1, D2, or D3. We also found that cdk inhibitors, including p21CIP1, p27KIP1, p57KIP2, p16INK4a, and p18INK4c, could block phosphorylation by p40MO15 but not phosphorylation by Cak1p. Our results demonstrate that although both Cak1p and p40MO15 activate cdks by phosphorylating the same residue, the structural mechanisms underlying the enzyme-substrate recognition differ greatly. Structural and physiological implications of these findings will be discussed.
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The F-box protein Skp2 (S-phase kinase-associated protein 2) positively regulates the G1-S transition by controlling the stability of several G1 regulators, such as the cell cycle inhibitor p27. We show here that Skp2 expression correlates directly with grade of malignancy and inversely with p27 levels in human lymphomas. To directly evaluate the potential of Skp2 to deregulate growth in vivo, we generated transgenic mice expressing Skp2 targeted to the T-lymphoid lineage as well as double transgenic mice coexpressing Skp2 and activated N-Ras. A strong cooperative effect between these two transgenes induced T cell lymphomas with shorter latency and higher penetrance, leading to significantly decreased survival when compared with control and single transgenic animals. Furthermore, lymphomas of Nras single transgenic animals often expressed higher levels of endogenous Skp2 than tumors of double transgenic mice. This study provides evidence of a role for an F-box protein in oncogenesis and establishes SKP2 as a protooncogene causally involved in the pathogenesis of lymphomas.
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Mullā Mūsá ibn Mullā ʻĪsá Sayrāmī nīng taʼlīfī.
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Translation of Nezabyvaemoe.
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London edition (Hutchinson & co., ltd.) has title: The Russian glory.
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Pl. no. 1008.
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Mode of access: Internet.
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"Iz Uchenykh zapisok istoriko-filologicheskago fakulʹteta Imperatorskago Kazanskago universiteta 1888 g."
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Includes bibliographical references.
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Mode of access: Internet.