Vrije Universiteit Brussel

About: Vrije Universiteit Brussel is a education organization based out in Brussels, Belgium. It is known for research contribution in the topics: Population & Context (language use). The organization has 14295 authors who have published 38258 publications receiving 1203970 citations. The organization is also known as: VUB.

Government Weakness and Local Public Debt Development in Flemish Municipalities

Abstract: The Weak Government Hypothesis states that government fragmentation leads to higher public deficits and debt. This relation can be explained by government inaction, common pool problems or the strategic use of debt that arise in coalition governments. Importantly, whereas government inaction models concentrate on the short-term effects of government fragmentation on indebtedness, common pool and strategic debt models imply that such effects will persist in the long term. We test these hypotheses using a large panel of data on municipal debt in 298 Flemish municipalities (1977–2000). We find that there is no long-run effect from weak governments. However, there is general support for the fact that the number of parties in a coalition has a positive effect on the municipality’s short-term debt levels–in line with government inaction models.

Multi actor multi criteria analysis (MAMCA) as a tool to support sustainable decisions: State of use

Abstract: In this contribution, the multi actor multi criteria analysis (MAMCA) to evaluate transport projects is presented. This evaluation methodology specifically focuses on the inclusion of the different actors that are involved in a project, the so-called stakeholders. Like the traditional multi criteria decision analysis (MCDA), it allows including qualitative as well as quantitative criteria with their relative importance, but within the MAMCA they represent the goals and objectives of the multiple stakeholders. As such, the stakeholders are incorporated in the decision process. The theoretical foundation of the MAMCA method is shown, together with several applications in the field of transport appraisal.

Allosteric coupling from G protein to the agonist-binding pocket in GPCRs

Abstract: G-protein-coupled receptors (GPCRs) remain the primary conduit by which cells detect environmental stimuli and communicate with each other. Upon activation by extracellular agonists, these seven-transmembrane-domain-containing receptors interact with heterotrimeric G proteins to regulate downstream second messenger and/or protein kinase cascades. Crystallographic evidence from a prototypic GPCR, the β2-adrenergic receptor (β2AR), in complex with its cognate G protein, Gs, has provided a model for how agonist binding promotes conformational changes that propagate through the GPCR and into the nucleotide-binding pocket of the G protein α-subunit to catalyse GDP release, the key step required for GTP binding and activation of G proteins. The structure also offers hints about how G-protein binding may, in turn, allosterically influence ligand binding. Here we provide functional evidence that G-protein coupling to the β2AR stabilizes a ‘closed’ receptor conformation characterized by restricted access to and egress from the hormone-binding site. Surprisingly, the effects of G protein on the hormone-binding site can be observed in the absence of a bound agonist, where G-protein coupling driven by basal receptor activity impedes the association of agonists, partial agonists, antagonists and inverse agonists. The ability of bound ligands to dissociate from the receptor is also hindered, providing a structural explanation for the G-protein-mediated enhancement of agonist affinity, which has been observed for many GPCR–G-protein pairs. Our data also indicate that, in contrast to agonist binding alone, coupling of a G protein in the absence of an agonist stabilizes large structural changes in a GPCR. The effects of nucleotide-free G protein on ligand-binding kinetics are shared by other members of the superfamily of GPCRs, suggesting that a common mechanism may underlie G-protein-mediated enhancement of agonist affinity.