La poblaci??n y movimientos migratorios : B2.2

Monogr??fico con el t??tulo: "Unidades did??cticas de lengua y cultura espa??olas ( I)"

Cartilla de comprensi??n lectora para nivel B2 (seg??n el Marco Com??n de Referencia) para aprendientes de E/LE en Colombia

Trabajo fin de m??ster (Universidad de Ja??n-FUNIBER, 2013)

Materiales para la clase de espa??ol como lengua extranjera 2013 : nivel B2

Resumen basado en el de la publicaci??n

Una historia de piratas : la transitividad verbal y el uso de los pronombres objeto : propuesta d??d??ctica comunicativa para la ense??anza en el nivel B2 de la clase de ELE

Resumen basado en el de la publicaci??n

Ellas tienen la palabra : poemas de escritoras para la interacci??n oral en la clase de ELE : material complementario para los niveles B2, C1 y C2 del MCER

Resumen basado en el de la publicaci??n

Propuesta curricular de la lengua de signos espa??ola : nivel usuario independiente : B2

Esta publicaci??n de la serie de propuestas curriculares para la ense??anza y el aprendizaje de la lengua de signos espa??ola recoge las especificaciones (objetivos, contenidos y orientaciones metodol??gicas) para el Nivel B2, que se corresponde con el hom??nimo de la escala del MCER. Con ella se describe, en l??nea de continuidad con las entregas anteriores (Niveles A1 y A2; y Nivel B1), lo que supone que los alumnos alcancen un nuevo estadio en la estructura del curr??culo de la lengua de signos espa??ola.

Euskararen B2 maila : Derrigorrezko irakaskuntzaren amaieran (DBH-4) : ISEI-IVEI 2005

Existe una versi??n en espa??ol, con el t??tulo "Nivel B2 de euskera : al finalizar la ense??anza obligatoria (4?? ESO) : ISEI-IVEI 2005"

Nivel B2 de euskera : al finalizar la ense??anza obligatoria (4?? ESO) : ISEI-IVEI 2005

Existe una versi??n en euskera, con el t??tulo "Euskararen B2 maila : Derrigorrezko irakaskuntzaren amaieran (DBH-4) : ISEI-IVEI 2005"

Tumour necrosis factor alpha induces rapid reduction in AMPA receptor-mediated calcium entry in motor neurones by increasing cell surface expression of the GluR2 subunit: relevance to neurodegeneration

The AMPA receptor (AMPAR) subunit GluR2, which regulates excitotoxicity and the inflammatory cytokine tumour necrosis factor alpha (TNF alpha) have both been implicated in motor neurone vulnerability in Amyotrophic Lateral Sclerosis/Motor Neurone Disease. TNF alpha has been reported to increase cell surface expression of AMPAR subunits to increase synaptic strength and enhance excitotoxicity, but whether this mechanism occurs in motor neurones is unknown. We used primary cultures of mouse motor neurones and cortical neurones to examine the interaction between TNF alpha receptor activation, GluR2 availability, AMPAR-mediated calcium entry and susceptibility to excitotoxicity. Short exposure to a physiologically relevant concentration of TNFalpha (10 ng/ml, 15 min) caused a marked redistribution of both GluR1 and GluR2 to the cell surface as determined by cell surface biotinylation and immunofluorescence. Using Fura-2 AM microfluorimetry we showed that exposure to TNFalpha caused a rapid reduction in the peak amplitude of AMPA-mediated calcium entry in a PI3-kinase and p38 kinase-dependent manner, consistent with increased insertion of GluR2-containing AMPAR into the plasma membrane. This resulted in a protection of motor neurones against kainate-induced cell death. Our data therefore, suggests that TNF alpha acts primarily as a physiological regulator of synaptic activity in motor neurones rather than a pathological drive in ALS

Characterisation of an s-type low molecular weight glutenin subunit of wheat and its proline and glutamine-rich repetitive domain

The low molecular weight glutenin subunits (LMW-GS) are major components of the glutenin polymers which determine the elastomeric properties of wheat (Triticum aestivum L.) gluten and dough. They comprise a complex mixture of components and have proved to be difficult to purify for detailed characterisation. The mature LMW subunit proteins comprise two structural domains, with one domain consisting of repeated sequences based on short peptide motifs. DNA sequences encoding this domain and a whole subunit were expressed in Escherichia coli and the recombinant proteins purified. Detailed comparisons by spectroscopy (CD, FT-IR) and dynamic light scattering indicated that the repetitive and non-repetitive domains of the proteins formed different structures with the former having an extended conformation with an equilibrium between poly-L-proline II-like structure and type II’ b-turns, and the latter a more compact globular structure rich in a-helix. Although the structures of these two domains appear to form independently, dynamic light scattering of the whole subunit dissolved in trifluoroethanol(TFE) suggested that they interact, leading to a more compact conformation. These observations may have relevance to the role of the LMW-GS in gluten structure and functionality.

Caf1A usher possesses a Caf1 subunit-like domain that is crucial for Caf1 fibre secretion

The chaperone/usher pathway controls assembly of fibres of adhesive organelles of Gram-negative bacteria. The final steps of fibre assembly and fibre translocation to the cell surface are co-ordinated by the outer membrane proteins, ushers. Ushers consist of several soluble periplasmic domains and a single transmembrane beta-barrel. Here we report isolation and structural/functional characterization of a novel middle domain of the Caf1A usher from Yersinia pestis. The isolated UMD (usher middle domain) is a highly soluble monomeric protein capable of autonomous folding. A 2.8 angstrom (1 angstrom = 0.1 nm) resolution crystal structure of UMD revealed that this domain has an immunoglobulin-like fold similar to that of donor-strand-complemented Caf1 fibre subunit. Moreover, these proteins displayed significant structural similarity. Although UMD is in the middle of the predicted amphipathic beta-barrel of Caf1A, the usher still assembled in the membrane in the absence of this domain. UMD did not bind Caf1M-Caf1 complexes, but its presence was shown to be essential for Caf1 fibre secretion. The study suggests that UMD may play the role of a subunit-substituting protein (dummy subunit), plugging or priming secretion through the channel in the Caf1A usher. Comparison of isolated UMD with the recent strcture of the corresponding domain of PapC usher revealed high similarity of the core structures, suggesting a universal structural adaptation of FGL (F(1)G(1) long) and FGS (F(1)G(1) short) chaperone/usher pathways for the secretion of different types of fibres. The functional role of two topologically different states of this plug domain suggested by structural and biochemical results is discussed.