Actuación para el seguimiento de la adquisición de conocimientos por parte de los alumnos de la asignatura de Genética en el Grado de Biología

Memoria ID-032. Ayudas de la Universidad de Salamanca para la innovación docente, curso 2020-2021

Creación de recursos multimedia de autoaprendizaje para la docencia práctica de Genética. Valoración de su eficacia en la adquisición de habilidades y competencias

Memoria ID-0225. Ayudas de la Universidad de Salamanca para la innovación docente, curso 2016-2017

Empleo de la plataforma multimedia Kahoot! para fomentar el aprendizaje interactivo en las clases de teoría y seminarios de Genética

Memoria ID-0093. Ayudas de la Universidad de Salamanca para la innovación docente, curso 2017-2018

Empleo de la herramienta Perusall como estrategia docente para fomentar la participación y el pensamiento crítico de textos científicos en la asignatura de Genética

Memoria ID2022-... Ayudas de la Universidad de Salamanca para la innovación docente, curso 2022-2023

Precariedad, exclusión social y modelo de sociedad: lógicas y efectos subjetivos del sufrimiento social contemporáneo (IV). Innovación docente en Filosofía

El PIMCD “Precariedad, exclusión social y modelo de sociedad: lógicas y efectos subjetivos del sufrimiento social contemporáneo (IV). Innovación docente en Filosofía” constituye la cuarta edición de un PIMCD que ha recibido financiación en las últimas convocatorias de PIMCD UCM, de los que se han derivado actividades de formación para estudiantes de Grado, Máster y Doctorado y al menos 3 publicaciones colectivas publicadas por Ediciones Complutense, Siglo XXI y Palgrave McMillan

Characterizing Ligand-Microtubule binding by competition methods

16 páginas, 2 figuras, 1 tabla -- PAGS nros. 245-260The knowledge of the thermodynamics and kinetics of drug-microtubule interaction is essential to understand the structure/affinity relationship of a given ligand family. When a ligand does not show an appropriate signal change (absorbance or fluorescence) upon binding, the extensive direct characterization of its binding affinities and kinetic rate constants of association and dissociation becomes a complex task. In those cases it is possible to obtain these parameters by competition of the ligand with a reference one of the same binding site that shows such change. Nevertheless, although the experimental setup of the competition measurements is easier, the treatment of the data is complex because simultaneous equilibrium/kinetic equations have to be solved. In this chapter, the taxoid-binding site of the microtubules will be used as an example to describe experimental competition and data analysis methods to determine the binding constants and kinetic rates of association and dissociation of ligands for microtubulesPeer reviewe

Cooperative stabilization of microtubule dynamics by EB1 and CLIP-170 involves displacement of stably bound P i at microtubule ends

End binding protein 1 (EB1) and cytoplasmic linker protein of 170 kDa (CLIP-170) are two well-studied microtubule plus-end-tracking proteins (+TIPs) that target growing microtubule plus ends in the form of comet tails and regulate microtubule dynamics. However, the mechanism by which they regulate microtubule dynamics is not well understood. Using full-length EB1 and a minimal functional fragment of CLIP-170 (ClipCG12), we found that EB1 and CLIP-170 cooperatively regulate microtubule dynamic instability at concentrations below which neither protein is effective. By use of small-angle X-ray scattering and analytical ultracentrifugation, we found that ClipCG12 adopts a largely extended conformation with two noninteracting CAP-Gly domains and that it formed a complex in solution with EB1. Using a reconstituted steady-state mammalian microtubule system, we found that at a low concentration of 250 nM, neither EB1 nor ClipCG12 individually modulated plus-end dynamic instability. Higher concentrations (up to 2 μM) of the two proteins individually did modulate dynamic instability, perhaps by a combination of effects at the tips and along the microtubule lengths. However, when low concentrations (250 nM) of EB1 and ClipCG12 were present together, the mixture modulated dynamic instability considerably. Using a pulsing strategy with [γ 32P]GTP, we further found that unlike EB1 or ClipCG12 alone, the EB1-ClipCG12 mixture partially depleted the microtubule ends of stably bound 32P i. Together, our results suggest that EB1 and ClipCG12 act cooperatively to regulate microtubule dynamics. They further indicate that stabilization of microtubule plus ends by the EB1-ClipCG12 mixture may involve modification of an aspect of the stabilizing cap.Supported by USPHS NS13560 (L.W.), by a FEBS Fellowship, Juan de la Cierva postdoctoral contracts, and a Marie Curie Career Integration Grant EB-SxIP: 293831 (R.M.B), and by grants from the Swiss National Science Foundation (M.O.S.).Peer Reviewe

Structure of the plakin domain of plectin

Resumen del póster presentado al 22nd IUBMB y al 37th FEBS, celebrados en Sevilla (España) del 4 al 9 de septiembre de 2012.Plectin is a member of the plakin family of proteins that cross-links components of the cytoskeleton and link them to membrane-associated structures, such as hemidesmosomes. Plectin has a multi-domain structure. The N-terminal region contains a conserved domain terme the plakin domain that consists of an array of 9 Spectrin Repeats (SR1 to SR9) arranged in tandem and a Src-homology 3 (SH3) domain inserted in the central SR5. We have combined x-ray crystallography and SAXS to elucidate the structure of the plakin domain of plectin. Here, we present the crystal structure of several fragments of the central (SR3-SR6) and C-terminal region (SR7-SR9) of the plakin domain, that together cover the region SR3-SR9. Each SR consists on 3 helices (A,B y C) connected by short loops and packed in a helical bundle with a up-down-up topology. Adjacent SRs are linked by a continuos helix formed by the fusion of the helix-C of the N-terminal repeat and the helix-A of the C-terminal repeat. Yet there is no conservation in the relative orientation of adjacent SRs. The SH3 domain of plectin shows the canonical SH3 fold, but exhibits alterations in its putative Pro-rich binding-site suggesting that this domain does not bind to Pro-rich motifs. Moreover, the SH3 binding-site is occluded by intramolecular contacts with the SR4. Residues that participate in the SR4-SH3 interaction are conserved in other members of the plakin family. The structure of the plakin domain of plectin serves as a structural model for other plakins.Peer Reviewe