Author: Nati Infante

Abstract The success of viruses in the delivery of the viral genome to target cells relies on the evolutionary selection of protein-based domains able to hijack the intermolecular interactions through which cells respond to intra- and extracellular stimuli. In an effort to mimic viral infection capabilities during non-viral gene delivery, a modular recombinant protein named T-Rp3 was recently developed, containing a DNA binding domain, a dynein molecular motor interacting domain, and a TAT-derived transduction domain. Here, we analyzed at the microscopic level the mechanisms behind the cell internalization and intracellular trafficking of this highly efficient modular protein vector. We found that the protein has the ability to self-assemble in discrete protein nanoparticles resemblin...

Engineering multifunctional protein nanoparticles by in vitro disassembling and reassembling of heterologous building blocks Ugutz Unzueta1, Naroa Serna2, Laura Sánchez-García3, Mónica Roldan4, Alejandro Sánchez-Chardi5, Ramon Mangues6, Antonio Villaverde Villaverde7 and Esther Vázquez8   http://iopscience.iop.org/article/10.1088/1361-6528/aa963e#top

El 4 d'octubre, entitats de la societat civil catalana, amb la participació de la UAB i la UB, van constituir una Comissió Independent per a la mediació, el diàleg i la conciliació. Ara, totes les universitats catalanes han donat suport a aquesta iniciativa. Totes les universitats catalanes donem suport a la iniciativa de creació d'una comissió independent de mediació, diàleg i conciliació promoguda pel Col·legi de l'Advocacia de Barcelona i altres entitats de la societat civil. Universitat de Barcelona, Universitat Autònoma de Barcelona, Universitat Politècnica de Catalunya, Universitat Pompeu Fabra, Universitat de Lleida, Universitat de Girona, Universitat Rovira i Virgili, Universitat Ramon Llull, Universitat Oberta de Catalunya, Universitat de Vic - Universitat Central de Catalunya

  Perfecting prediction of mutational impact on the aggregation propensity of the ALS-associated hnRNPA2 prion-like protein Cristina Batlle, María rosario Fernández, Valentín Iglesias, Salvador Ventura http://onlinelibrary.wiley.com/doi/10.1002/1873-3468.12698/full   Abstract  An increasing number of human proteins are being found to bear a prion-like domain (PrLD) driving the formation of membraneless compartments through liquid–liquid phase separation. Point mutations in these PrLDs promote the transition to an amyloid-like state. There has been much debate on whether this aberrant aggregation is caused by compositional or sequential changes. A recent extensive mutational study of the ALS-associated prion-like hnRNPA2 protein provides a framework to discriminate t