The high activity of fluorohydroxybenzylbenzimidazoles against some small RNA-viruses

Zusammenfassung Fluorierte Derivate des 2-(-Oxybenzyl)-benzimidazol hemmen die Vermehrung des Poliovirus, 1, 2 und 3, sowie diejenige des Coxsackievirus A9 und A21.     

Prospects for detecting supersymmetric dark matter in the Galactic halo

Dark matter is the dominant form of matter in the Universe, but its nature is unknown. It is plausibly an elementary particle, perhaps the lightest supersymmetric partner of known particle species. In this case, annihilation of dark matter in the halo of the Milky Way should produce gamma-rays at a level that may soon be observable. Previous work has argued that the annihilation signal will be dominated by emission from very small clumps (perhaps smaller even than the Earth), which would be most easily detected where they cluster together in the dark matter haloes of dwarf satellite galaxies. Here we report that such small-scale structure will, in fact, have a negligible impact on dark matter detectability. Rather, the dominant and probably most easily detectable signal will be produced by diffuse dark matter in the main halo of the Milky Way. If the main halo is strongly detected, then small dark matter clumps should also be visible, but may well contain no stars, thereby confirming a key prediction of the cold dark matter model.     

Antiviral properties of 1-allyl and 1-crotyl derivatives of 2-(α-hydroxybenzyl) benzimidazole

Zusammenfassung 1-Allylund 1-Crotyl-2-(oxy-benzyl)-Benzimidazol hemmen die Vermehrung von Poliovirus 1, 2 und 3, sowie diejenige der Coxsackieviren A 9 und A 21 und diejenige des ECHO-Virus 11.     

Mutant dynactin in motor neuron disease

Impaired axonal transport in motor neurons has been proposed as a mechanism for neuronal degeneration in motor neuron disease. Here we show linkage of a lower motor neuron disease to a region of 4 Mb at chromosome 2p13. Mutation analysis of a gene in this interval that encodes the largest subunit of the axonal transport protein dynactin showed a single base-pair change resulting in an amino-acid substitution that is predicted to distort the folding of dynactin's microtubule-binding domain. Binding assays show decreased binding of the mutant protein to microtubules. Our results show that dysfunction of dynactin-mediated transport can lead to human motor neuron disease.