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1.
Phys Rev Lett ; 117(19): 192001, 2016 Nov 04.
Artículo en Inglés | MEDLINE | ID: mdl-27858429

RESUMEN

Ultrahigh energy cosmic ray air showers probe particle physics at energies beyond the reach of accelerators. Here we introduce a new method to test hadronic interaction models without relying on the absolute energy calibration, and apply it to events with primary energy 6-16 EeV (E_{CM}=110-170 TeV), whose longitudinal development and lateral distribution were simultaneously measured by the Pierre Auger Observatory. The average hadronic shower is 1.33±0.16 (1.61±0.21) times larger than predicted using the leading LHC-tuned models EPOS-LHC (QGSJetII-04), with a corresponding excess of muons.

2.
Phys Rev Lett ; 116(24): 241101, 2016 Jun 17.
Artículo en Inglés | MEDLINE | ID: mdl-27367377

RESUMEN

We measure the energy emitted by extensive air showers in the form of radio emission in the frequency range from 30 to 80 MHz. Exploiting the accurate energy scale of the Pierre Auger Observatory, we obtain a radiation energy of 15.8±0.7(stat)±6.7(syst) MeV for cosmic rays with an energy of 1 EeV arriving perpendicularly to a geomagnetic field of 0.24 G, scaling quadratically with the cosmic-ray energy. A comparison with predictions from state-of-the-art first-principles calculations shows agreement with our measurement. The radiation energy provides direct access to the calorimetric energy in the electromagnetic cascade of extensive air showers. Comparison with our result thus allows the direct calibration of any cosmic-ray radio detector against the well-established energy scale of the Pierre Auger Observatory.

3.
Eur Phys J C Part Fields ; 75(6): 269, 2015.
Artículo en Inglés | MEDLINE | ID: mdl-26120280

RESUMEN

Energy-dependent patterns in the arrival directions of cosmic rays are searched for using data of the Pierre Auger Observatory. We investigate local regions around the highest-energy cosmic rays with [Formula: see text] eV by analyzing cosmic rays with energies above [Formula: see text] eV arriving within an angular separation of approximately 15[Formula: see text]. We characterize the energy distributions inside these regions by two independent methods, one searching for angular dependence of energy-energy correlations and one searching for collimation of energy along the local system of principal axes of the energy distribution. No significant patterns are found with this analysis. The comparison of these measurements with astrophysical scenarios can therefore be used to obtain constraints on related model parameters such as strength of cosmic-ray deflection and density of point sources.

4.
Neuron ; 31(3): 367-79, 2001 Aug 16.
Artículo en Inglés | MEDLINE | ID: mdl-11516395

RESUMEN

Mice that lack all beta1-class integrins in neurons and glia die prematurely after birth with severe brain malformations. Cortical hemispheres and cerebellar folia fuse, and cortical laminae are perturbed. These defects result from disorganization of the cortical marginal zone, where beta1-class integrins regulate glial endfeet anchorage, meningeal basement membrane remodeling, and formation of the Cajal-Retzius cell layer. Surprisingly, beta1-class integrins are not essential for neuron-glia interactions and neuronal migration during corticogenesis. The phenotype of the beta1-deficient mice resembles pathological changes observed in human cortical dysplasias, suggesting that defective integrin-mediated signal transduction contributes to the development of some of these diseases.


Asunto(s)
Encéfalo/anomalías , Corteza Cerebelosa/anomalías , Corteza Cerebelosa/embriología , Corteza Cerebral/anomalías , Corteza Cerebral/embriología , Integrina beta1/fisiología , Neuronas/fisiología , Animales , Moléculas de Adhesión Celular Neuronal/análisis , Células Cultivadas , Corteza Cerebelosa/patología , Corteza Cerebral/patología , Modelos Animales de Enfermedad , Desarrollo Embrionario y Fetal , Matriz Extracelular/patología , Matriz Extracelular/fisiología , Proteínas de la Matriz Extracelular/análisis , Integrina beta1/genética , Proteínas de Filamentos Intermediarios/genética , Proteínas de Filamentos Intermediarios/metabolismo , Ratones , Ratones Noqueados , Ratones Transgénicos , Proteínas del Tejido Nervioso/análisis , Nestina , Neuroglía/patología , Neuroglía/fisiología , Neuronas/patología , Neuronas/ultraestructura , Proteína Reelina , Serina Endopeptidasas , Transducción de Señal , beta-Galactosidasa/genética
5.
J Neurochem ; 71(6): 2615-25, 1998 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-9832163

RESUMEN

Previous experiments suggested that the human cell adhesion molecule L1 interacts with different integrins via its sixth immunoglobulin-like domain in an RGD-dependent manner. Here we have described the expression of this domain from early postnatal mouse brain, analyzed the structure of the recombinant protein by circular dichroism and fluorescence spectroscopy, and performed solid-phase binding studies to alpha(v)beta3, alpha(IIb)beta3, and alpha5beta1 integrins. The domain was found to have the expected beta-sheet organization, which was lost in the presence of guanidine hydrochloride. The midpoint of the single-step transition occurred at 1.5 M guanidine hydrochloride. The sixth immunoglobulin-like domain of mouse brain L1 contains two RGD motifs and was found to bind in a concentration-dependent and saturable way to alpha(v)beta3, alpha(IIb)beta3, and alpha5beta1 integrins, suggesting specific interactions with these ligands. However, only the interaction to alpha(v)beta3 could be inhibited in a concentration-dependent manner by an RGD-containing peptide, and the IC50 was determined to be approximately 20 nM. Mutants of the domain, which lack either one or both of the RGD sites, demonstrated that the RGD site comprising residues 562-564 is involved in the interaction to alpha(v)beta3. Our findings indicate an RGD-independent mechanism for the interactions to alpha(IIb)beta3 and alpha5beta1, as no involvement of any RGD motif could be demonstrated.


Asunto(s)
Inmunoglobulinas/genética , Moléculas de Adhesión de Célula Nerviosa/genética , Moléculas de Adhesión de Célula Nerviosa/fisiología , Complejo GPIIb-IIIa de Glicoproteína Plaquetaria/fisiología , Receptores de Fibronectina/fisiología , Receptores de Vitronectina/fisiología , Secuencia de Aminoácidos , Animales , Interacciones Farmacológicas , Ratones , Ratones Endogámicos , Moléculas de Adhesión de Célula Nerviosa/metabolismo , Oligopéptidos/genética , Oligopéptidos/fisiología , Complejo GPIIb-IIIa de Glicoproteína Plaquetaria/metabolismo , Receptores de Fibronectina/metabolismo , Receptores de Vitronectina/metabolismo , Proteínas Recombinantes
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