990 resultados para Mons, Jean-Baptiste van, 1765-1842.
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Sign.: []4, B1, A2-A4, B-Z4-, 2A-2Z4, 3A-3N4
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Estampado en la misma hoja con: "Detalles geometrales del Arco de Cabanes"
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Datos de publicación tomados de la obra a la que pertenece
Plaza del mercado de Valencia [Material gráfico] =Place du marché à Valence=Market-Place at Valencia
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Estampado en la misma hoja con: "Plano de la Lonja de Valencia"
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Contiene: Fig. 3 Retrato de soldado de frente y cuerpo entero; con mano izquierda sujeta un rifle. Fig. 4 Retrato de mujer de cuerpo entero y mirando hacia la derecha, viste atuendo militar y sustenta un racimo de uvas y otra frutas
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Contiene : "Tons de chasse et fanfares" (p. 433-446) con partituras musicales
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Tit. en antep.: "Supplementum systematis plantarum Europae"
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Tit. en antep.: "Supplementum systematis plantarum Europae"
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Estampado junto a: "Vista de la Ciudadela"
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Resumen: Descripción: vista general del Teatro de Sagunto desde el exterior, se observan las gradas
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Datos de publicación tomados de la obra a la que pertenece
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3
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Staphylococcus aureus produces a virulence factor, protein A (SpA), that contains five homologous Ig-binding domains. The interactions of SpA with the Fab region of membrane-anchored Igs can stimulate a large fraction of B cells, contributing to lymphocyte clonal selection. To understand the molecular basis for this activity, we have solved the crystal structure of the complex between domain D of SpA and the Fab fragment of a human IgM antibody to 2.7-Å resolution. In the complex, helices II and III of domain D interact with the variable region of the Fab heavy chain (VH) through framework residues, without the involvement of the hypervariable regions implicated in antigen recognition. The contact residues are highly conserved in human VH3 antibodies but not in other families. The contact residues from domain D also are conserved among all SpA Ig-binding domains, suggesting that each could bind in a similar manner. Features of this interaction parallel those reported for staphylococcal enterotoxins that are superantigens for many T cells. The structural homology between Ig VH regions and the T-cell receptor Vβ regions facilitates their comparison, and both types of interactions involve lymphocyte receptor surface remote from the antigen binding site. However, T-cell superantigens reportedly interact through hydrogen bonds with T-cell receptor Vβ backbone atoms in a primary sequence-independent manner, whereas SpA relies on a sequence-restricted conformational binding with residue side chains, suggesting that this common bacterial pathogen has adopted distinct molecular recognition strategies for affecting large sets of B and T lymphocytes.