University of Alcalá

About: University of Alcalá is a education organization based out in Alcalá de Henares, Spain. It is known for research contribution in the topics: Population & Context (language use). The organization has 10795 authors who have published 20718 publications receiving 410089 citations. The organization is also known as: University of Alcala & University of Alcala de Henares.

Constraints on the origin of cosmic rays above 10(18) eV from large-scale anisotropy searches in data of the Pierre Auger Observatory

Abstract: A thorough search for large-scale anisotropies in the distribution of arrival directions of cosmic rays detected above 10(18) eV at the Pierre Auger Observatory is reported. For the first time, these large-scale anisotropy searches are performed as a function of both the right ascension and the declination and expressed in terms of dipole and quadrupole moments. Within the systematic uncertainties, no significant deviation from isotropy is revealed. Upper limits on dipole and quadrupole amplitudes are derived under the hypothesis that any cosmic ray anisotropy is dominated by such moments in this energy range. These upper limits provide constraints on the production of cosmic rays above 10(18) eV, since they allow us to challenge an origin from stationary galactic sources densely distributed in the galactic disk and emitting predominantly light particles in all directions.

Rejecting and resisting Nobel class discoveries: accounts by Nobel Laureates

Abstract: I review and discuss instances in which 19 future Nobel Laureates encountered resistance on the part of the scientific community towards their discoveries, and instances in which 24 future Nobel Laureates encountered resistance on the part of scientific journal editors or referees to manuscripts that dealt with discoveries that later would earn them the Nobel Prize.

Mutational pathways, resistance profile, and side effects of cyanovirin relative to human immunodeficiency virus type 1 strains with N-glycan deletions in their gp120 envelopes

Abstract: Limited data are available on the genotypic and phenotypic resistance profile of the -(1-2)mannose oligomer-specific prokaryotic lectin cyanovirin (CV-N). Therefore, a more systematic investigation was carried out to obtain a better view of the interaction between CV-N and human immunodeficiency virus type 1 (HIV-1) gp120. When HIV-1-infected CEM cell cultures were exposed to CV-N in a dose-escalating manner, a total of eight different amino acid mutations exclusively located at N-glycosylation sites in the envelope surface gp120 were observed. Six of the eight mutations resulted in the deletion of high-mannose type N-glycans (i.e., at amino acid positions 230, 332, 339, 386, 392, and 448). Two mutations (i.e., at position 136 and 160) deleted a complex type N-glycan in the variable V1/V2 domain of gp120. The level of phenotypic resistance of the mutated virus strains against CV-N generally correlated with the number of glycan deletions in gp120, although deletion of the glycans at N-230, N-392, and N-448 generally afforded a more pronounced CV-N resistance than other N-glycan deletions. However, the extent of the decrease of antiviral activity of CV-N against the mutated virus strains was markedly less pronounced than observed for (1-3)- and (1-6)-mannose-specific plant lectins Hippeastrum hybrid agglutinin (HHA) and Galanthus nivalis agglutinin (GNA), which points to the existence of a higher genetic barrier for CV-N. This is in agreement with a more consistent suppression of a wider variety of HIV-1 clades by CV-N than by HHA and GNA. Whereas the antiviral and in vitro antiproliferative activity of CV-N can be efficiently reversed by mannan, the pronounced mitogenic activity of CV-N on peripheral blood mononuclear cells was unaffected by mannan, indicating that some of the observed side effects of CV-N are unrelated to its carbohydrate specificity/activity.