999 resultados para État Shan


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Heinrich York-Steiner

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Jakob Loewenberg

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Israel Reichert

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publ. sous la dir. de Liebrechts. Par les soins du Th. Masui

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par Gustave Moynier

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par H. Droogmans

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Signatur des Originals: S 36/F12056

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El Shan shui como la línea principal de investigación de Wang Shu, todavía está estimulando la exploración de la arquitectura de Wang shu. La filosofía y la visión universal del Shan shui se basan en la naturaleza, que es una manifestación específica de los valores culturales tradicionales chinos. Wang Shu sigue esta visión de valor observando el mundo y pensando la arquitectura china ideal. Vuelvo a analizar la presentación y la teoría del Shan shui para buscar más posibilidades de la aplicación de la estética tradicional a la arquitectura contemporánea. ABSTRACT. The Shan shui, as the main line of Wang Shu's research, is constantly stimulating his exploration of the architecture. The philosophy and the universal vision of Shan shui are based on nature, which is a specific manifestation of the traditional Chinese cultural values. And Wang Shu still values the world and thinks about the ideal Chinese architecture through this vision. This text aims at returning to the presentation and Shan shui theory in order to search for more possibilities of applying traditional aesthetics to contemporary architecture.

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Hay un ejemplar encuadernado con: Poesías colocadas en el pórtico del Convento de San Francisco de Valencia (NP849.91/3086).

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The HIV-1 Tat protein is a potent chemoattractant for monocytes. We observed that Tat shows conserved amino acids corresponding to critical sequences of the chemokines, a family of molecules known for their potent ability to attract monocytes. Synthetic Tat and a peptide (CysL24–51) encompassing the “chemokine-like” region of Tat induced a rapid and transient Ca2+ influx in monocytes and macrophages, analogous to β-chemokines. Both monocyte migration and Ca2+ mobilization were pertussis toxin sensitive and cholera toxin insensitive. Cross-desensitization studies indicated that Tat shares receptors with MCP-1, MCP-3, and eotaxin. Tat was able to displace binding of β-chemokines from the β-chemokine receptors CCR2 and CCR3, but not CCR1, CCR4, and CCR5. Direct receptor binding experiments with the CysL24–51 peptide confirmed binding to cells transfected with CCR2 and CCR3. HIV-1 Tat appears to mimic β-chemokine features, which may serve to locally recruit chemokine receptor-expressing monocytes/macrophages toward HIV producing cells and facilitate activation and infection.

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In cells infected with HIV type 1 (HIV-1), the integrated viral promoter is present in a chromatin-bound conformation and is transcriptionally silent in the absence of stimulation. The HIV-1 Tat protein binds to a stem-loop structure at the 5′ end of viral mRNA and relieves this inhibition by inducing a remodeling of the nucleosome arrangement downstream of the transcription-initiation site. Here we show that Tat performs this activity by recruiting to the viral long terminal repeat (LTR) the transcriptional coactivator p300 and the closely related CREB-binding protein (CBP), having histone acetyltransferase (HAT) activity. Tat associates with HAT activity in human nuclear extracts and binds to p300 and CBP both in vitro and in vivo. Integrity of the basic domain of Tat is essential for this interaction. By a quantitative chromatin immunoprecipitation assay we show that the delivery of recombinant Tat induces the association of p300 and CBP with the chromosomally integrated LTR promoter. Expression of human p300 in both human and rodent cells increases the levels of Tat transactivation of the integrated LTR. These results reinforce the evidence that p300 and CBP have a pivotal function at both cellular and viral promoters and demonstrate that they also can be recruited by an RNA-targeted activator. Additionally, these findings have important implications for the understanding of the mechanisms of HIV-1 latency and reactivation.

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We have previously identified a cellular protein kinase activity termed TAK that specifically associates with the HIV types 1 and 2 Tat proteins. TAK hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II in vitro in a manner believed to activate transcription [Herrmann, C. H. & Rice, A. P. (1995) J. Virol. 69, 1612–1620]. We show here that the catalytic subunit of TAK is a known human kinase previously named PITALRE, which is a member of the cyclin-dependent family of proteins. We also show that TAK activity is elevated upon activation of peripheral blood mononuclear cells and peripheral blood lymphocytes and upon differentiation of U1 and U937 promonocytic cell lines to macrophages. Therefore, in HIV-infected individuals TAK may be induced in T cells following activation and in macrophages following differentiation, thus contributing to high levels of viral transcription and the escape from latency of transcriptionally silent proviruses.