University of Trento

About: University of Trento is a education organization based out in Trento, Italy. It is known for research contribution in the topics: Population & Large Hadron Collider. The organization has 10527 authors who have published 30978 publications receiving 896614 citations. The organization is also known as: Universitá degli Studi di Trento & Universita degli Studi di Trento.

Improving zero-shot learning by mitigating the hubness problem

Abstract: The zero-shot paradigm exploits vector-based word representations extracted from text corpora with unsupervised methods to learn general mapping functions from other feature spaces onto word space, where the words associated to the nearest neighbours of the mapped vectors are used as their linguistic labels. We show that the neighbourhoods of the mapped elements are strongly polluted by hubs, vectors that tend to be near a high proportion of items, pushing their correct labels down the neighbour list. After illustrating the problem empirically, we propose a simple method to correct it by taking the proximity distribution of potential neighbours across many mapped vectors into account. We show that this correction leads to consistent improvements in realistic zero-shot experiments in the cross-lingual, image labeling and image retrieval domains.

Ionic channels formed by Staphylococcus aureus alpha-toxin: Voltage-dependent inhibition by divalent and trivalent cations

Abstract: The interaction of Staphylococcus aureus alpha-toxin with planar lipid membranes results in the formation of ionic channels whose conductance can be directly measured in voltage-clamp experiments. Single-channel conductance depends linearly on the solution conductivity suggesting that the pores are filled with aqueous solution; a rough diameter of 11.4 +/- 0.4 A can be estimated for the pore. The conductance depends asymmetrically on voltage and it is slightly anion selective at pH 7.0, which implies that the channels are asymmetrically oriented into the bilayer and that ion motion is restricted at least in a region of the pore. The pores are usually open in a KCl solution but undergo a dose- and voltage-dependent inactivation in the presence of di- and trivalent cations, which is mediated by open-closed fluctuations at the single-channel level. Hill plots indicate that each channel can bind two to three inactivating cations. The inhibiting efficiency follows the sequence Zn2+ greater than Tb3+ greater than Ca2+ greater than Mg2+ greater than Ba2+, suggesting that carboxyl groups of the protein may be involved in the binding step. A voltage-gated inactivation mechanism is proposed which involves the binding of two polyvalent cations to the channel, one in the open and one in the closed configuration, and which can explain voltage, dose and time dependence of the inactivation.