974 resultados para Açaí solitário
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The paper presents a consistent set of results showing the ability of Laser Shock Processing (LSP) in modifying the overall properties of the Friction Stir Welded (FSW) joints made of AA 2024-T351. Based on laser beam intensities above 109 W/cm2 with pulse energies of several Joules and pulses durations of nanoseconds, LSP is able of inducing a compression residual stress field, improving the wear and fatigue resistance by slowing crack propagation and stress corrosion cracking, but also improving the overall behaviour of the structure. After the FSW and LSP procedures are briefly presented, the results of micro-hardness measurements and of transverse tensile tests, together with the corrosion resistance of the native joints vs. LSP treated are discussed. The ability of LSP to generate compressive residual stresses and to improve the behaviour of the FSW joints is underscored.
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Segun Palau V, 91265, la fecha de impresión es 1802
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Autor tomado del final del texto
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De otros textos de la época se deduce la fecha, 1802
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otras obras (arm. 65)
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Hay un ejemplar encuadernado con: Individual noticia de todos los altares, arcos pinturas, adornos y lo mas exquisito y notable que havia en la carrera de la procession, y de las iluminaciones en general ... : (XVIII/1705).
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The crystal structure of the RNA dodecamer 5′-GGCC(GAAA)GGCC-3′ has been determined from x-ray diffraction data to 2.3-Å resolution. In the crystal, these oligomers form double helices around twofold symmetry axes. Four consecutive non-Watson–Crick base pairs make up an internal loop in the middle of the duplex, including sheared G·A pairs and novel asymmetric A·A pairs. This internal loop sequence produces a significant curvature and narrowing of the double helix. The helix is curved by 34° from end to end and the diameter is narrowed by 24% in the internal loop. A Mn2+ ion is bound directly to the N7 of the first guanine in the Watson–Crick region following the internal loop and the phosphate of the preceding residue. This Mn2+ location corresponds to a metal binding site observed in the hammerhead catalytic RNA.
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An extensive repertoire of protein 4.1R isoforms is predominantly generated by alternative pre-mRNA splicing and differential usage of two translation initiation sites. The usage of the most upstream ATG (ATG-1) generates isoforms containing N-terminal extensions of up to 209 aa compared with those translated from the downstream ATG (ATG-2). To characterize nonerythroid 4.1R proteins translated from ATG-1 and analyze their intracellular localization, we cloned 4.1R cDNAs containing this translation initiation site. Six different clones were isolated from the nucleated human MOLT-4 T-cell line by reverse transcriptase–PCR techniques. Transient expression of the six ATG-1-translated 4.1R isoforms tagged with a c-Myc epitope revealed that all of them predominantly distributed to the plasma membrane and the endoplasmic reticulum. Staining of MOLT-4 cell plasma membranes but not nuclei was also observed by immunofluorescence microscopy by using an antibody specific to the N-terminal extension. Consistent with this, the antibody reacted with a major endogenous protein of ≈145 kDa present in nonnuclear but absent from nuclear fractions prepared from MOLT-4 cells. Because these data suggested that ATG-1-translated 4.1R isoforms were predominantly excluded from the nucleus, we fused the 209-aa domain to nuclear 4.1R isoforms encoded from ATG-2 and observed that this domain inhibited their nuclear targeting. All these results indicate that the N-terminal domain of ATG-1-translated 4.1R isoforms plays a pivotal role in differential targeting of proteins 4.1R.